ID 6PGL_THEMA Reviewed; 220 AA. AC Q9X0N8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=6-phosphogluconolactonase; DE Short=6PGL; DE EC=3.1.1.31; GN Name=pgl; Synonyms=devB; OrderedLocusNames=TM_1154; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2/3. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36230.1; -; Genomic_DNA. DR PIR; F72289; F72289. DR RefSeq; NP_228960.1; NC_000853.1. DR RefSeq; WP_008195599.1; NZ_CP011107.1. DR PDB; 1PBT; X-ray; 1.70 A; A=1-220. DR PDB; 1VL1; X-ray; 1.55 A; A=1-220. DR PDBsum; 1PBT; -. DR PDBsum; 1VL1; -. DR ProteinModelPortal; Q9X0N8; -. DR SMR; Q9X0N8; 1-220. DR STRING; 243274.TM1154; -. DR DrugBank; DB03754; Tris. DR PRIDE; Q9X0N8; -. DR EnsemblBacteria; AAD36230; AAD36230; TM_1154. DR GeneID; 898332; -. DR KEGG; tma:TM1154; -. DR PATRIC; 23937245; VBITheMar51294_1171. DR eggNOG; ENOG4108Q79; Bacteria. DR eggNOG; COG0363; LUCA. DR InParanoid; Q9X0N8; -. DR KO; K01057; -. DR OMA; PEANIHG; -. DR OrthoDB; EOG63FW46; -. DR BioCyc; TMAR243274:GC6P-1183-MONOMER; -. DR UniPathway; UPA00115; UER00409. DR EvolutionaryTrace; Q9X0N8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB. DR InterPro; IPR006148; Glc/Gal-6P_isomerase. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 220 6-phosphogluconolactonase. FT /FTId=PRO_0000090108. FT STRAND 4 11 {ECO:0000244|PDB:1VL1}. FT HELIX 13 31 {ECO:0000244|PDB:1VL1}. FT STRAND 35 39 {ECO:0000244|PDB:1VL1}. FT HELIX 45 52 {ECO:0000244|PDB:1VL1}. FT HELIX 59 61 {ECO:0000244|PDB:1VL1}. FT STRAND 62 72 {ECO:0000244|PDB:1VL1}. FT HELIX 80 87 {ECO:0000244|PDB:1VL1}. FT TURN 88 91 {ECO:0000244|PDB:1VL1}. FT HELIX 96 98 {ECO:0000244|PDB:1VL1}. FT HELIX 108 122 {ECO:0000244|PDB:1VL1}. FT STRAND 127 131 {ECO:0000244|PDB:1VL1}. FT HELIX 145 148 {ECO:0000244|PDB:1VL1}. FT STRAND 151 156 {ECO:0000244|PDB:1VL1}. FT STRAND 158 160 {ECO:0000244|PDB:1VL1}. FT TURN 161 164 {ECO:0000244|PDB:1VL1}. FT STRAND 167 170 {ECO:0000244|PDB:1VL1}. FT HELIX 172 175 {ECO:0000244|PDB:1VL1}. FT STRAND 179 187 {ECO:0000244|PDB:1VL1}. FT HELIX 188 198 {ECO:0000244|PDB:1VL1}. FT HELIX 204 207 {ECO:0000244|PDB:1VL1}. FT STRAND 211 219 {ECO:0000244|PDB:1VL1}. SQ SEQUENCE 220 AA; 25325 MW; 9B0FD07EE01E60C3 CRC64; MEKTVIYLLE DGYVDFVVEK IRTKMEKLLE EKDKIFVVLA GGRTPLPVYE KLAEQKFPWN RIHFFLSDER YVPLDSDQSN FRNINEVLFS RAKIPSGNVH YVDTSLPIEK ACEKYEREIR SATDQFDLAI LGMGPDGHVA SIFDLETGNK DNLVTFTDPS GDPKVPRVTL TFRALNTSLY VLFLIRGKEK INRLTEILKD TPLPAYFVRG KEKTVWFVGK // ID 1A1D_THEMA Reviewed; 312 AA. AC Q9WY68; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=Putative 1-aminocyclopropane-1-carboxylate deaminase; DE Short=ACC deaminase; DE EC=3.5.99.7; GN OrderedLocusNames=TM_0225; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: 1-aminocyclopropane-1-carboxylate + H(2)O = 2- CC oxobutanoate + NH(3). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35317.1; -; Genomic_DNA. DR PIR; D72401; D72401. DR RefSeq; NP_228040.1; NC_000853.1. DR RefSeq; WP_004082912.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY68; -. DR STRING; 243274.TM0225; -. DR EnsemblBacteria; AAD35317; AAD35317; TM_0225. DR GeneID; 897123; -. DR KEGG; tma:TM0225; -. DR PATRIC; 23935322; VBITheMar51294_0227. DR eggNOG; ENOG4105K6H; Bacteria. DR eggNOG; COG2515; LUCA. DR InParanoid; Q9WY68; -. DR KO; K05396; -. DR OMA; TLWDDYF; -. DR OrthoDB; EOG6FBX0P; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR InterPro; IPR027278; ACCD_DCysDesulf. DR InterPro; IPR005966; D-Cys_desShydrase. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF00291; PALP; 1. DR PIRSF; PIRSF006278; ACCD_DCysDesulf; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR01275; ACC_deam_rel; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Pyridoxal phosphate; Reference proteome. FT CHAIN 1 312 Putative 1-aminocyclopropane-1- FT carboxylate deaminase. FT /FTId=PRO_0000184520. FT MOD_RES 42 42 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 312 AA; 34756 MW; 6BE2A4A0BFC1E15F CRC64; MRIDLSLKPT PVQFLKRLSE KYGFNIYVKR DDLTELVGSG NKIRKLEYLL WEALKKGATT VFTCGGLQSN HARATAYVSR RYGLKPVLFL RKGEKVLNGN LLLDILLGAE IVEVSPEEYE RIDEIFDVHK KMREKKGEKV YVIPEGGSNS LGAFGYFNAV LEMKDQLNLE SFDAIVCAVG SGGTIAGLSA GISFLEYHVP VVGVNVTTKN SDYFVGKVKR IISGMEEYGL RVNETVFEVV DDYRGPGYAI PSSEDVEILK EVASIEGIIL DPVYTAKAFR GMIEMFRNSE KNVLFIHTGG IFGLFAQSRR LV // ID AAT_THEMA Reviewed; 377 AA. AC Q9X0Y2; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=Aspartate aminotransferase; DE Short=AspAT; DE EC=2.6.1.1; DE AltName: Full=Transaminase A; GN Name=aspC; OrderedLocusNames=TM_1255; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL RP PHOSPHATE, AND SUBUNIT. RX PubMed=15103638; DOI=10.1002/prot.10646; RA Schwarzenbacher R., Jaroszewski L., von Delft F., Abdubek P., RA Ambing E., Biorac T., Brinen L.S., Canaves J.M., Cambell J., RA Chiu H.-J., Dai X., Deacon A.M., DiDonato M., Elsliger M.-A., RA Eshagi S., Floyd R., Godzik A., Grittini C., Grzechnik S.K., RA Hampton E., Karlak C., Klock H.E., Koesema E., Kovarik J.S., RA Kreusch A., Kuhn P., Lesley S.A., Levin I., McMullan D., RA McPhillips T.M., Miller M.D., Morse A., Moy K., Ouyang J., Page R., RA Quijano K., Robb A., Spraggon G., Stevens R.C., van den Bedem H., RA Velasquez J., Vincent J., Wang X., West B., Wolf G., Xu Q., RA Hodgson K.O., Wooley J., Wilson I.A.; RT "Crystal structure of an aspartate aminotransferase (TM1255) from RT Thermotoga maritima at 1.90 A resolution."; RL Proteins 55:759-763(2004). CC -!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate + CC L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15103638}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36330.1; -; Genomic_DNA. DR PIR; B72275; B72275. DR RefSeq; NP_229060.1; NC_000853.1. DR RefSeq; WP_004080007.1; NZ_CP011107.1. DR PDB; 1O4S; X-ray; 1.90 A; A/B=1-377. DR PDBsum; 1O4S; -. DR ProteinModelPortal; Q9X0Y2; -. DR SMR; Q9X0Y2; 1-376. DR STRING; 243274.TM1255; -. DR EnsemblBacteria; AAD36330; AAD36330; TM_1255. DR GeneID; 898228; -. DR KEGG; tma:TM1255; -. DR PATRIC; 23937450; VBITheMar51294_1271. DR eggNOG; ENOG4105CHM; Bacteria. DR eggNOG; COG0436; LUCA. DR InParanoid; Q9X0Y2; -. DR KO; K00812; -. DR OMA; WALEHGI; -. DR OrthoDB; EOG6RRKNS; -. DR EvolutionaryTrace; Q9X0Y2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminotransferase; Complete proteome; Cytoplasm; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 377 Aspartate aminotransferase. FT /FTId=PRO_0000123857. FT BINDING 37 37 Aspartate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 123 123 Aspartate. {ECO:0000250}. FT BINDING 173 173 Aspartate. {ECO:0000250}. FT BINDING 353 353 Aspartate. {ECO:0000250}. FT MOD_RES 234 234 N6-(pyridoxal phosphate)lysine. FT HELIX 4 8 {ECO:0000244|PDB:1O4S}. FT HELIX 15 26 {ECO:0000244|PDB:1O4S}. FT HELIX 45 55 {ECO:0000244|PDB:1O4S}. FT HELIX 69 83 {ECO:0000244|PDB:1O4S}. FT HELIX 89 91 {ECO:0000244|PDB:1O4S}. FT STRAND 92 96 {ECO:0000244|PDB:1O4S}. FT HELIX 97 109 {ECO:0000244|PDB:1O4S}. FT STRAND 115 121 {ECO:0000244|PDB:1O4S}. FT HELIX 126 132 {ECO:0000244|PDB:1O4S}. FT STRAND 136 141 {ECO:0000244|PDB:1O4S}. FT HELIX 144 146 {ECO:0000244|PDB:1O4S}. FT HELIX 152 157 {ECO:0000244|PDB:1O4S}. FT STRAND 163 171 {ECO:0000244|PDB:1O4S}. FT TURN 173 175 {ECO:0000244|PDB:1O4S}. FT HELIX 181 194 {ECO:0000244|PDB:1O4S}. FT STRAND 197 201 {ECO:0000244|PDB:1O4S}. FT TURN 203 206 {ECO:0000244|PDB:1O4S}. FT HELIX 216 219 {ECO:0000244|PDB:1O4S}. FT STRAND 221 223 {ECO:0000244|PDB:1O4S}. FT STRAND 226 232 {ECO:0000244|PDB:1O4S}. FT TURN 233 237 {ECO:0000244|PDB:1O4S}. FT HELIX 239 241 {ECO:0000244|PDB:1O4S}. FT STRAND 244 247 {ECO:0000244|PDB:1O4S}. FT HELIX 250 263 {ECO:0000244|PDB:1O4S}. FT HELIX 269 278 {ECO:0000244|PDB:1O4S}. FT HELIX 284 303 {ECO:0000244|PDB:1O4S}. FT STRAND 312 320 {ECO:0000244|PDB:1O4S}. FT HELIX 325 336 {ECO:0000244|PDB:1O4S}. FT HELIX 343 346 {ECO:0000244|PDB:1O4S}. FT STRAND 351 355 {ECO:0000244|PDB:1O4S}. FT HELIX 360 374 {ECO:0000244|PDB:1O4S}. SQ SEQUENCE 377 AA; 42421 MW; 4EB507704C45E221 CRC64; MVSRRISEIP ISKTMELDAK AKALIKKGED VINLTAGEPD FPTPEPVVEE AVRFLQKGEV KYTDPRGIYE LREGIAKRIG ERYKKDISPD QVVVTNGAKQ ALFNAFMALL DPGDEVIVFS PVWVSYIPQI ILAGGTVNVV ETFMSKNFQP SLEEVEGLLV GKTKAVLINS PNNPTGVVYR REFLEGLVRL AKKRNFYIIS DEVYDSLVYT DEFTSILDVS EGFDRIVYIN GFSKSHSMTG WRVGYLISSE KVATAVSKIQ SHTTSCINTV AQYAALKALE VDNSYMVQTF KERKNFVVER LKKMGVKFVE PEGAFYLFFK VRGDDVKFCE RLLEEKKVAL VPGSAFLKPG FVRLSFATSI ERLTEALDRI EDFLNSR // ID ACYP_THEMA Reviewed; 90 AA. AC Q9X1Q0; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 92. DE RecName: Full=Acylphosphatase; DE EC=3.6.1.7; DE AltName: Full=Acylphosphate phosphohydrolase; GN Name=acyP; OrderedLocusNames=TM_1564; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: An acylphosphate + H(2)O = a carboxylate + CC phosphate. CC -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 acylphosphatase-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00520}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36630.1; -; Genomic_DNA. DR PIR; G72240; G72240. DR RefSeq; NP_229364.1; NC_000853.1. DR RefSeq; WP_004081975.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1Q0; -. DR STRING; 243274.TM1564; -. DR EnsemblBacteria; AAD36630; AAD36630; TM_1564. DR GeneID; 897410; -. DR KEGG; tma:TM1564; -. DR PATRIC; 23938090; VBITheMar51294_1582. DR eggNOG; ENOG4105VSY; Bacteria. DR eggNOG; COG1254; LUCA. DR InParanoid; Q9X1Q0; -. DR KO; K01512; -. DR OMA; FTVTQAR; -. DR OrthoDB; EOG6ND0QX; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central. DR InterPro; IPR001792; Acylphosphatase-like_dom. DR InterPro; IPR017968; Acylphosphatase_CS. DR Pfam; PF00708; Acylphosphatase; 1. DR SUPFAM; SSF54975; SSF54975; 1. DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1. DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1. DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 90 Acylphosphatase. FT /FTId=PRO_0000326833. FT DOMAIN 3 89 Acylphosphatase-like. FT {ECO:0000255|PROSITE-ProRule:PRU00520}. FT ACT_SITE 18 18 {ECO:0000255|PROSITE-ProRule:PRU00520}. FT ACT_SITE 36 36 {ECO:0000255|PROSITE-ProRule:PRU00520}. SQ SEQUENCE 90 AA; 10048 MW; 9A1C09DEAD44C6BE CRC64; MKALKIRVEG IVQGVGFRYF TRRVAKSLGV KGYVMNMDDG SVFIHAEGDE NALRRFLNEV AKGPPAAVVT NVSVEETTPE GYEDFTIKYY // ID ACKA_THEMA Reviewed; 403 AA. AC Q9WYB1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=Acetate kinase {ECO:0000255|HAMAP-Rule:MF_00020}; DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020}; DE AltName: Full=Acetokinase {ECO:0000255|HAMAP-Rule:MF_00020}; GN Name=ackA {ECO:0000255|HAMAP-Rule:MF_00020}; GN OrderedLocusNames=TM_0274; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF 1-12, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT. RX PubMed=10074080; RA Bock A.-K., Glasemacher J., Schmidt R., Schoenheit P.; RT "Purification and characterization of two extremely thermostable RT enzymes, phosphate acetyltransferase and acetate kinase, from the RT hyperthermophilic eubacterium Thermotoga maritima."; RL J. Bacteriol. 181:1861-1867(1999). CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate CC and ATP. Can also catalyze the reverse reaction. Phosphorylates CC propionate (54%) in addition to acetate (100%). Uses GTP (100%), CC ITP (163%), UTP (56%), and CTP (21%) as phosphoryl donors in CC addition to ATP (100%). {ECO:0000255|HAMAP-Rule:MF_00020, CC ECO:0000269|PubMed:10074080}. CC -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00020, ECO:0000269|PubMed:10074080}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020, CC ECO:0000269|PubMed:10074080}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020, CC ECO:0000269|PubMed:10074080}; CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP- CC Rule:MF_00020, ECO:0000269|PubMed:10074080}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.0. {ECO:0000269|PubMed:10074080}; CC Temperature dependence: CC Optimum temperature is 90 degrees Celsius. CC {ECO:0000269|PubMed:10074080}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA CC biosynthesis; acetyl-CoA from acetate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00020, ECO:0000269|PubMed:10074080}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020, CC ECO:0000269|PubMed:10074080}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}. CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP- CC Rule:MF_00020}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35363.1; -; Genomic_DNA. DR PIR; H72397; H72397. DR RefSeq; NP_228087.1; NC_000853.1. DR RefSeq; WP_004082978.1; NZ_CP011107.1. DR PDB; 2IIR; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J=1-403. DR PDBsum; 2IIR; -. DR ProteinModelPortal; Q9WYB1; -. DR SMR; Q9WYB1; 1-400. DR DIP; DIP-2899N; -. DR STRING; 243274.TM0274; -. DR EnsemblBacteria; AAD35363; AAD35363; TM_0274. DR GeneID; 897189; -. DR KEGG; tma:TM0274; -. DR PATRIC; 23935425; VBITheMar51294_0278. DR eggNOG; ENOG4105C6H; Bacteria. DR eggNOG; COG0282; LUCA. DR InParanoid; Q9WYB1; -. DR KO; K00925; -. DR OMA; HRLKKYI; -. DR OrthoDB; EOG69975F; -. DR BioCyc; MetaCyc:MONOMER-428; -. DR BRENDA; 2.7.2.1; 6331. DR UniPathway; UPA00340; UER00458. DR EvolutionaryTrace; Q9WYB1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro. DR HAMAP; MF_00020; Acetate_kinase; 1. DR InterPro; IPR004372; Ac/propionate_kinase. DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain. DR InterPro; IPR023865; Aliphatic_acid_kinase_CS. DR PANTHER; PTHR21060; PTHR21060; 1. DR Pfam; PF00871; Acetate_kinase; 1. DR PIRSF; PIRSF000722; Acetate_prop_kin; 1. DR PRINTS; PR00471; ACETATEKNASE. DR TIGRFAMs; TIGR00016; ackA; 1. DR PROSITE; PS01075; ACETATE_KINASE_1; 1. DR PROSITE; PS01076; ACETATE_KINASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; KW Direct protein sequencing; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 403 Acetate kinase. FT /FTId=PRO_0000107631. FT NP_BIND 207 211 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 283 285 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 331 335 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT ACT_SITE 147 147 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT METAL 7 7 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT METAL 386 386 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT BINDING 14 14 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT BINDING 90 90 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT SITE 179 179 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT SITE 240 240 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT STRAND 2 9 {ECO:0000244|PDB:2IIR}. FT STRAND 12 19 {ECO:0000244|PDB:2IIR}. FT TURN 20 23 {ECO:0000244|PDB:2IIR}. FT STRAND 24 32 {ECO:0000244|PDB:2IIR}. FT STRAND 40 45 {ECO:0000244|PDB:2IIR}. FT STRAND 48 53 {ECO:0000244|PDB:2IIR}. FT HELIX 59 71 {ECO:0000244|PDB:2IIR}. FT TURN 73 75 {ECO:0000244|PDB:2IIR}. FT STRAND 86 92 {ECO:0000244|PDB:2IIR}. FT TURN 95 97 {ECO:0000244|PDB:2IIR}. FT HELIX 106 115 {ECO:0000244|PDB:2IIR}. FT HELIX 116 118 {ECO:0000244|PDB:2IIR}. FT TURN 120 122 {ECO:0000244|PDB:2IIR}. FT HELIX 123 136 {ECO:0000244|PDB:2IIR}. FT STRAND 142 146 {ECO:0000244|PDB:2IIR}. FT HELIX 149 153 {ECO:0000244|PDB:2IIR}. FT HELIX 156 159 {ECO:0000244|PDB:2IIR}. FT HELIX 166 171 {ECO:0000244|PDB:2IIR}. FT HELIX 180 193 {ECO:0000244|PDB:2IIR}. FT HELIX 198 200 {ECO:0000244|PDB:2IIR}. FT STRAND 202 218 {ECO:0000244|PDB:2IIR}. FT STRAND 221 226 {ECO:0000244|PDB:2IIR}. FT STRAND 233 235 {ECO:0000244|PDB:2IIR}. FT HELIX 248 256 {ECO:0000244|PDB:2IIR}. FT HELIX 260 269 {ECO:0000244|PDB:2IIR}. FT HELIX 272 276 {ECO:0000244|PDB:2IIR}. FT TURN 277 279 {ECO:0000244|PDB:2IIR}. FT HELIX 284 292 {ECO:0000244|PDB:2IIR}. FT HELIX 296 320 {ECO:0000244|PDB:2IIR}. FT STRAND 324 329 {ECO:0000244|PDB:2IIR}. FT HELIX 330 333 {ECO:0000244|PDB:2IIR}. FT HELIX 337 345 {ECO:0000244|PDB:2IIR}. FT HELIX 346 350 {ECO:0000244|PDB:2IIR}. FT HELIX 356 361 {ECO:0000244|PDB:2IIR}. FT STRAND 376 381 {ECO:0000244|PDB:2IIR}. FT HELIX 386 398 {ECO:0000244|PDB:2IIR}. SQ SEQUENCE 403 AA; 44804 MW; 98340ACB2AC04A7E CRC64; MRVLVINSGS SSIKYQLIEM EGEKVLCKGI AERIGIEGSR LVHRVGDEKH VIERELPDHE EALKLILNTL VDEKLGVIKD LKEIDAVGHR VVHGGERFKE SVLVDEEVLK AIEEVSPLAP LHNPANLMGI KAAMKLLPGV PNVAVFDTAF HQTIPQKAYL YAIPYEYYEK YKIRRYGFHG TSHRYVSKRA AEILGKKLEE LKIITCHIGN GASVAAVKYG KCVDTSMGFT PLEGLVMGTR SGDLDPAIPF FIMEKEGISP QEMYDILNKK SGVYGLSKGF SSDMRDIEEA ALKGDEWCKL VLEIYDYRIA KYIGAYAAAM NGVDAIVFTA GVGENSPITR EDVCSYLEFL GVKLDKQKNE ETIRGKEGII STPDSRVKVL VVPTNEELMI ARDTKEIVEK IGR // ID ACPS_THEMA Reviewed; 169 AA. AC Q9WZF6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=Holo-[acyl-carrier-protein] synthase {ECO:0000255|HAMAP-Rule:MF_00101}; DE Short=Holo-ACP synthase {ECO:0000255|HAMAP-Rule:MF_00101}; DE EC=2.7.8.7 {ECO:0000255|HAMAP-Rule:MF_00101}; DE AltName: Full=4'-phosphopantetheinyl transferase AcpS {ECO:0000255|HAMAP-Rule:MF_00101}; GN Name=acpS {ECO:0000255|HAMAP-Rule:MF_00101}; GN OrderedLocusNames=TM_0692; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme CC A to a Ser of acyl-carrier-protein. {ECO:0000255|HAMAP- CC Rule:MF_00101}. CC -!- CATALYTIC ACTIVITY: CoA-(4'-phosphopantetheine) + apo-[acyl- CC carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl- CC carrier-protein]. {ECO:0000255|HAMAP-Rule:MF_00101}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00101}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00101}. CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS CC family. {ECO:0000255|HAMAP-Rule:MF_00101}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35774.1; -; Genomic_DNA. DR PIR; B72345; B72345. DR RefSeq; NP_228501.1; NC_000853.1. DR RefSeq; WP_004081065.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZF6; -. DR STRING; 243274.TM0692; -. DR EnsemblBacteria; AAD35774; AAD35774; TM_0692. DR GeneID; 898359; -. DR KEGG; tma:TM0692; -. DR PATRIC; 23936302; VBITheMar51294_0704. DR eggNOG; ENOG41082V8; Bacteria. DR eggNOG; COG0736; LUCA. DR InParanoid; Q9WZF6; -. DR KO; K00997; -. DR OMA; KDMEVVN; -. DR OrthoDB; EOG6384R9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.470.20; -; 1. DR HAMAP; MF_00101; AcpS; 1. DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_SF. DR InterPro; IPR002582; ACPS. DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom. DR Pfam; PF01648; ACPS; 1. DR ProDom; PD004282; PPantethiene-prot_Trfase; 1. DR SUPFAM; SSF56214; SSF56214; 1. DR TIGRFAMs; TIGR00516; acpS; 1. DR TIGRFAMs; TIGR00556; pantethn_trn; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Magnesium; Metal-binding; Reference proteome; Transferase. FT CHAIN 1 169 Holo-[acyl-carrier-protein] synthase. FT /FTId=PRO_0000175720. FT METAL 8 8 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00101}. FT METAL 50 50 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00101}. SQ SEQUENCE 169 AA; 19291 MW; 5B83A60B76027778 CRC64; MIVGVGIDVL EVERVPEKFA ERILGESEKR LFLTRKRRRE FIAGRFALKE AFFKALGTGL NGHSFTDVEF LESNGKPVLC VHKDFGFFNY AHVSLSHDRF AVALVVLEKR KGDIIVEGDE SFLRKRFEVL ERSVEGWEIE TSLPPFTLKK LLESSGCRLV RYGNILIGE // ID AEEP_THEMA Reviewed; 345 AA. AC Q9WXM1; DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=L-Ala-D/L-Glu epimerase; DE Short=AE epimerase; DE Short=AEE; DE EC=5.1.1.20 {ECO:0000269|PubMed:11747447, ECO:0000269|PubMed:19000819}; GN OrderedLocusNames=TM_0006; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP CATALYTIC ACTIVITY. RX PubMed=11747447; DOI=10.1021/bi011640x; RA Schmidt D.M.Z., Hubbard B.K., Gerlt J.A.; RT "Evolution of enzymatic activities in the enolase superfamily: RT functional assignment of unknown proteins in Bacillus subtilis and RT Escherichia coli as L-Ala-D/L-Glu epimerases."; RL Biochemistry 40:15707-15715(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEXES RP WITH SUBSTRATE AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=19000819; DOI=10.1016/j.str.2008.08.015; RA Kalyanaraman C., Imker H.J., Fedorov A.A., Fedorov E.V., Glasner M.E., RA Babbitt P.C., Almo S.C., Gerlt J.A., Jacobson M.P.; RT "Discovery of a dipeptide epimerase enzymatic function guided by RT homology modeling and virtual screening."; RL Structure 16:1668-1677(2008). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of muconate cycloisomerase from Thermotoga maritima RT MSB8."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L- CC Glu and has probably a role in the metabolism of the murein CC peptide, of which L-Ala-D-Glu is a component. Is also able to CC catalyze the reverse reaction and the epimerization of a broad CC range of other dipeptides; is most efficient with L-Ala-D/L-Phe, CC L-Ala-D/L-Tyr, and L-Ala-D/L-His. {ECO:0000269|PubMed:19000819}. CC -!- CATALYTIC ACTIVITY: L-alanyl-D-glutamate = L-alanyl-L-glutamate. CC {ECO:0000269|PubMed:11747447, ECO:0000269|PubMed:19000819}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.8 mM for L-Ala-L-Glu (at pH 7.5 and 28 degrees Celsius) CC {ECO:0000269|PubMed:19000819}; CC KM=1.3 mM for L-Ala-L-Phe (at pH 7.5 and 28 degrees Celsius) CC {ECO:0000269|PubMed:19000819}; CC KM=0.71 mM for L-Ala-L-Tyr (at pH 7.5 and 28 degrees Celsius) CC {ECO:0000269|PubMed:19000819}; CC KM=5.3 mM for L-Ala-L-His (at pH 7.5 and 28 degrees Celsius) CC {ECO:0000269|PubMed:19000819}; CC KM=2.9 mM for L-Ala-L-Leu (at pH 7.5 and 28 degrees Celsius) CC {ECO:0000269|PubMed:19000819}; CC KM=4.7 mM for L-Ile-L-Phe (at pH 7.5 and 28 degrees Celsius) CC {ECO:0000269|PubMed:19000819}; CC KM=3.9 mM for L-Lys-L-Phe (at pH 7.5 and 28 degrees Celsius) CC {ECO:0000269|PubMed:19000819}; CC -!- PATHWAY: Cell wall degradation; peptidoglycan degradation. CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing CC enzyme family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35100.1; -; Genomic_DNA. DR PIR; H72429; H72429. DR RefSeq; NP_227822.1; NC_000853.1. DR RefSeq; WP_004082436.1; NZ_CP011107.1. DR PDB; 2ZAD; X-ray; 1.60 A; A/B/C/D=1-345. DR PDB; 3DEQ; X-ray; 2.10 A; A/B/C/D=1-345. DR PDB; 3DER; X-ray; 1.90 A; A/B/C/D=1-345. DR PDB; 3DES; X-ray; 2.30 A; A/B/C/D=1-345. DR PDB; 3DFY; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-345. DR PDBsum; 2ZAD; -. DR PDBsum; 3DEQ; -. DR PDBsum; 3DER; -. DR PDBsum; 3DES; -. DR PDBsum; 3DFY; -. DR ProteinModelPortal; Q9WXM1; -. DR SMR; Q9WXM1; 2-345. DR STRING; 243274.TM0006; -. DR DNASU; 896814; -. DR EnsemblBacteria; AAD35100; AAD35100; TM_0006. DR GeneID; 896814; -. DR KEGG; tma:TM0006; -. DR PATRIC; 23934852; VBITheMar51294_0004. DR eggNOG; ENOG4105DTQ; Bacteria. DR eggNOG; COG4948; LUCA. DR InParanoid; Q9WXM1; -. DR OMA; DFDAPLM; -. DR OrthoDB; EOG6S52NQ; -. DR SABIO-RK; Q9WXM1; -. DR UniPathway; UPA00549; -. DR EvolutionaryTrace; Q9WXM1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IDA:CACAO. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.120; -; 1. DR Gene3D; 3.30.390.10; -; 1. DR InterPro; IPR029065; Enolase_C-like. DR InterPro; IPR029017; Enolase_N-like. DR InterPro; IPR013342; Mandelate_racemase_C. DR InterPro; IPR013341; Mandelate_racemase_N_dom. DR InterPro; IPR001354; MR/MLE/MAL. DR PANTHER; PTHR13794; PTHR13794; 1. DR Pfam; PF13378; MR_MLE_C; 1. DR Pfam; PF02746; MR_MLE_N; 1. DR SMART; SM00922; MR_MLE; 1. DR SUPFAM; SSF51604; SSF51604; 1. DR SUPFAM; SSF54826; SSF54826; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell wall biogenesis/degradation; Complete proteome; KW Isomerase; Magnesium; Metal-binding; Reference proteome. FT CHAIN 1 345 L-Ala-D/L-Glu epimerase. FT /FTId=PRO_0000388972. FT ACT_SITE 161 161 Proton acceptor; specific for (R)- FT substrate epimerization. {ECO:0000250}. FT ACT_SITE 265 265 Proton acceptor; specific for (S)- FT substrate epimerization. {ECO:0000250}. FT METAL 188 188 Magnesium. FT METAL 216 216 Magnesium. FT METAL 241 241 Magnesium. FT BINDING 134 134 Substrate. FT BINDING 159 159 Substrate. FT BINDING 190 190 Substrate. FT BINDING 292 292 Substrate; via carbonyl oxygen. FT BINDING 317 317 Substrate. FT BINDING 319 319 Substrate. FT STRAND 3 22 {ECO:0000244|PDB:2ZAD}. FT STRAND 25 39 {ECO:0000244|PDB:2ZAD}. FT STRAND 44 49 {ECO:0000244|PDB:2ZAD}. FT HELIX 53 56 {ECO:0000244|PDB:2ZAD}. FT HELIX 60 65 {ECO:0000244|PDB:2ZAD}. FT HELIX 67 74 {ECO:0000244|PDB:2ZAD}. FT HELIX 79 81 {ECO:0000244|PDB:2ZAD}. FT HELIX 82 89 {ECO:0000244|PDB:2ZAD}. FT HELIX 96 114 {ECO:0000244|PDB:2ZAD}. FT HELIX 118 121 {ECO:0000244|PDB:2ZAD}. FT STRAND 127 131 {ECO:0000244|PDB:2ZAD}. FT STRAND 133 135 {ECO:0000244|PDB:2ZAD}. FT HELIX 140 152 {ECO:0000244|PDB:2ZAD}. FT STRAND 156 161 {ECO:0000244|PDB:2ZAD}. FT HELIX 166 179 {ECO:0000244|PDB:2ZAD}. FT STRAND 184 188 {ECO:0000244|PDB:2ZAD}. FT HELIX 195 207 {ECO:0000244|PDB:2ZAD}. FT STRAND 213 216 {ECO:0000244|PDB:2ZAD}. FT HELIX 224 233 {ECO:0000244|PDB:2ZAD}. FT STRAND 234 236 {ECO:0000244|PDB:2ZAD}. FT STRAND 238 241 {ECO:0000244|PDB:2ZAD}. FT HELIX 247 256 {ECO:0000244|PDB:2ZAD}. FT STRAND 260 264 {ECO:0000244|PDB:2ZAD}. FT HELIX 266 282 {ECO:0000244|PDB:2ZAD}. FT TURN 283 285 {ECO:0000244|PDB:2ZAD}. FT STRAND 287 290 {ECO:0000244|PDB:2ZAD}. FT HELIX 297 310 {ECO:0000244|PDB:2ZAD}. FT STRAND 314 316 {ECO:0000244|PDB:2ZAD}. FT HELIX 320 323 {ECO:0000244|PDB:2ZAD}. FT STRAND 324 326 {ECO:0000244|PDB:2ZAD}. FT STRAND 332 336 {ECO:0000244|PDB:2ZAD}. FT STRAND 339 341 {ECO:0000244|PDB:2ZAD}. SQ SEQUENCE 345 AA; 38664 MW; 587BDE71BB1E777B CRC64; MSRIVNVKLS LKRYEYEKPF HITGSVSSES RNVEVEIVLE SGVKGYGEAS PSFRVNGERV EALLAIENAV REMITGIDVR NYARIFEITD RLFGFPSLKA AVQFATLDAL SQELGTQVCY LLGGKRDEIE TDKTVGIDTV ENRVKEAKKI FEEGFRVIKI KVGENLKEDI EAVEEIAKVT RGAKYIVDAN MGYTQKEAVE FARAVYQKGI DIAVYEQPVR REDIEGLKFV RFHSPFPVAA DESARTKFDV MRLVKEEAVD YVNIKLMKSG ISDALAIVEI AESSGLKLMI GCMGESSLGI NQSVHFALGT GAFEFHDLDS HLMLKEEVFR GKFIQDGPRM RVKDQ // ID ACP_THEMA Reviewed; 81 AA. AC Q9WZD0; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Acyl carrier protein {ECO:0000255|HAMAP-Rule:MF_01217}; DE Short=ACP {ECO:0000255|HAMAP-Rule:MF_01217}; GN Name=acpP {ECO:0000255|HAMAP-Rule:MF_01217}; GN OrderedLocusNames=TM_0662; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01217}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01217}. CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific CC serine of apo-ACP by AcpS. This modification is essential for CC activity because fatty acids are bound in thioester linkage to the CC sulfhydryl of the prosthetic group. {ECO:0000255|HAMAP- CC Rule:MF_01217}. CC -!- SIMILARITY: Contains 1 acyl carrier domain. {ECO:0000255|HAMAP- CC Rule:MF_01217}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35746.1; -; Genomic_DNA. DR PIR; C72349; C72349. DR RefSeq; NP_228471.1; NC_000853.1. DR RefSeq; WP_004081111.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZD0; -. DR STRING; 243274.TM0662; -. DR EnsemblBacteria; AAD35746; AAD35746; TM_0662. DR GeneID; 897775; -. DR KEGG; tma:TM0662; -. DR PATRIC; 23936238; VBITheMar51294_0672. DR eggNOG; ENOG4105VNB; Bacteria. DR eggNOG; COG0236; LUCA. DR InParanoid; Q9WZD0; -. DR KO; K02078; -. DR OMA; ENEFGVQ; -. DR OrthoDB; EOG6MWNJM; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000036; F:ACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1200.10; -; 1. DR HAMAP; MF_01217; Acyl_carrier; 1. DR InterPro; IPR003231; Acyl_carrier. DR InterPro; IPR009081; PP-bd_ACP. DR InterPro; IPR006162; Ppantetheine_attach_site. DR Pfam; PF00550; PP-binding; 1. DR ProDom; PD000887; PD000887; 1. DR SUPFAM; SSF47336; SSF47336; 1. DR TIGRFAMs; TIGR00517; acyl_carrier; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Phosphopantetheine; Phosphoprotein; Reference proteome. FT CHAIN 1 81 Acyl carrier protein. FT /FTId=PRO_0000180208. FT MOD_RES 40 40 O-(pantetheine 4'-phosphoryl)serine. FT {ECO:0000255|HAMAP-Rule:MF_01217}. SQ SEQUENCE 81 AA; 8897 MW; 3C437DE0BF758781 CRC64; MASREEIFSK VKSIISEKLG VDESQVTEEA KLIDDLGADS LDLVDLVMDF ESEFGVKVDD ADLEKISTVG DIVSYIEKKL G // ID AGLUS_THEMA Reviewed; 507 AA. AC Q9WYM8; G4FHV6; DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Archaeal-type glutamate synthase [NADPH] {ECO:0000303|PubMed:11230537}; DE EC=1.4.1.13 {ECO:0000250|UniProtKB:Q58746}; DE AltName: Full=Archaeal-type NADPH-GOGAT {ECO:0000250|UniProtKB:Q58746}; GN Name=gltB {ECO:0000303|PubMed:11230537}; OrderedLocusNames=TM_0397; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] {ECO:0000312|EMBL:AAD35482.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000305} RP PHYLOGENETIC STUDY. RX PubMed=11230537; DOI=10.1093/oxfordjournals.molbev.a003812; RA Nesbo C.L., L'Haridon S., Stetter K.O., Doolittle W.F.; RT "Phylogenetic analyses of two 'archaeal' genes in thermotoga maritima RT reveal multiple transfers between archaea and bacteria."; RL Mol. Biol. Evol. 18:362-375(2001). CC -!- CATALYTIC ACTIVITY: 2 L-glutamate + NADP(+) = L-glutamine + 2- CC oxoglutarate + NADPH. {ECO:0000250|UniProtKB:Q58746}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000250|UniProtKB:Q58746}; CC -!- SIMILARITY: Belongs to the glutamate synthase family. CC {ECO:0000255}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35482.1; -; Genomic_DNA. DR PIR; F72382; F72382. DR RefSeq; NP_228207.1; NC_000853.1. DR RefSeq; WP_004083229.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYM8; -. DR STRING; 243274.TM0397; -. DR EnsemblBacteria; AAD35482; AAD35482; TM_0397. DR GeneID; 897389; -. DR KEGG; tma:TM0397; -. DR PATRIC; 23935675; VBITheMar51294_0402. DR eggNOG; ENOG4105CBC; Bacteria. DR eggNOG; COG0069; LUCA. DR eggNOG; COG1145; LUCA. DR InParanoid; Q9WYM8; -. DR OMA; DACQVTN; -. DR OrthoDB; EOG60W7PX; -. DR BioCyc; TMAR243274:GC6P-411-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR024188; GltB. DR InterPro; IPR002932; Glu_synthdom. DR Pfam; PF12838; Fer4_7; 1. DR Pfam; PF01645; Glu_synthase; 1. DR PIRSF; PIRSF006429; GOGAT_lg_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; Complete proteome; Flavoprotein; FMN; KW Glutamate biosynthesis; Iron; Iron-sulfur; Metal-binding; NADP; KW Oxidoreductase; Reference proteome; Repeat. FT CHAIN 1 507 Archaeal-type glutamate synthase [NADPH]. FT /FTId=PRO_0000420608. FT DOMAIN 10 39 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 41 70 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 19 19 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:Q58746}. FT METAL 22 22 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:Q58746}. FT METAL 25 25 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:Q58746}. FT METAL 29 29 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:Q58746}. FT METAL 50 50 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:Q58746}. FT METAL 53 53 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:Q58746}. FT METAL 56 56 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:Q58746}. FT METAL 60 60 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:Q58746}. SQ SEQUENCE 507 AA; 55199 MW; C59B631742EDB9C9 CRC64; MAKRKVPPEF VVERDDYKCI RCLACVRVCS YGANFYDENA NRVYTENTKC VGCHFCEAIC PTEAITVRKN DFDIRPLAHW TPEHLIGIMK QAETGGVLLT SMGNDRPYFS YFDRIVLNAS QVTNPSIDPL REPMEIRTYI GRKEEKLEIE EDEDGTVKLK TEIAPQLKLE VPVMFTAMSY GSISLNAILS LARAARTVGT FFNTGEGGLP KELREFKDNM IVQVASGRFG VSADYLNAGS AVEIKIGQGA KPGIGGHLPG EKVTEPISET RMIPVGTDAL SPAPHHDIYS IEDLRQLIYA IKEATRYEKP VGVKIAAVHN VAPIAAGAVR AGADYIVIDG IRGGTGAAPK ITRDHVGIPI EFAVAVVDQR LREEGIRHMA SIVVAGGIRN SADVIKAIAL GADAVYIGTA ALISLGCHLC QTCYLGKCNW GIATQDPKLT KRLNPEIGAR RAANLLRAWA HEIKEILGGM GINAIESLRG NREVLRGVGL HEYELKLLGI KPAGEAW // ID AGLA_THEMA Reviewed; 480 AA. AC O33830; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 131. DE RecName: Full=Alpha-glucosidase; DE EC=3.2.1.20; DE AltName: Full=Maltase; GN Name=aglA; OrderedLocusNames=TM_1834; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9453151; DOI=10.1111/j.1574-6968.1998.tb12793.x; RA Bibel M., Brettl C., Gosslar U., Kriegshaeuser G., Liebl W.; RT "Isolation and analysis of genes for amylolytic enzymes of the RT hyperthermophilic bacterium Thermotoga maritima."; RL FEMS Microbiol. Lett. 158:9-15(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP CHARACTERIZATION, SUBUNIT, COFACTOR, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10972187; DOI=10.1007/PL00010711; RA Raasch C., Streit W., Schanzer J., Bibel M., Gosslar U., Liebl W.; RT "Thermotoga maritima AglA, an extremely thermostable NAD+-, Mn2+-, and RT thiol-dependent alpha-glucosidase."; RL Extremophiles 4:189-200(2000). RN [4] RP MUTAGENESIS OF GLY-10; GLY-12 AND SER-13, AND KINETIC PARAMETERS. RX PubMed=12062450; DOI=10.1016/S0014-5793(02)02641-8; RA Raasch C., Armbrecht M., Streit W., Hoecker B., Straeter N., Liebl W.; RT "Identification of residues important for NAD+ binding by the RT Thermotoga maritima alpha-glucosidase AglA, a member of glycoside RT hydrolase family 4."; RL FEBS Lett. 517:267-271(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH NAD(+) AND RP MALTOSE. RX PubMed=12588867; DOI=10.1074/jbc.M211626200; RA Lodge J.A., Maier T., Liebl W., Hoffmann V., Straeter N.; RT "Crystal structure of Thermotoga maritima alpha-glucosidase AglA RT defines a new clan of NAD+-dependent glycosidases."; RL J. Biol. Chem. 278:19151-19158(2003). CC -!- FUNCTION: Alpha-glycosidase with a very broad specificity. CC Hydrolyzes maltose and other small maltooligosaccharides but is CC inactive against the polymeric substrate starch. AglA is not CC specific with respect to the configuration at the C-4 position of CC its substrates because glycosidic derivatives of D-galactose are CC also hydrolyzed. Does not cleave beta-glycosidic bonds. CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing (1->4)- CC linked alpha-D-glucose residues with release of alpha-D-glucose. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000269|PubMed:10972187}; CC Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:10972187}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:10972187}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:10972187}; CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000269|PubMed:10972187}; CC Note=Binds 1 Mn(2+) ion per subunit. Can also use Co(2+) and CC Ni(2+) ions, albeit less efficiently than manganese ion. CC {ECO:0000269|PubMed:10972187}; CC -!- ENZYME REGULATION: Inhibited by Hg(2+) ion and EDTA. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.23 mM for p-nitrophenyl-alpha-D-glucopyranoside CC {ECO:0000269|PubMed:10972187, ECO:0000269|PubMed:12062450}; CC KM=0.53 mM for p-nitrophenyl-alpha-D-galactopyranoside CC {ECO:0000269|PubMed:10972187, ECO:0000269|PubMed:12062450}; CC Vmax=9.94 umol/min/mg enzyme with p-nitrophenyl-alpha-D- CC glucopyranoside as substrate {ECO:0000269|PubMed:10972187, CC ECO:0000269|PubMed:12062450}; CC Vmax=11.42 umol/min/mg enzyme with p-nitrophenyl-alpha-D- CC galactopyranoside as substrate {ECO:0000269|PubMed:10972187, CC ECO:0000269|PubMed:12062450}; CC pH dependence: CC Optimum pH is 7.5. Active from pH 6.5 to 9. CC {ECO:0000269|PubMed:10972187}; CC Temperature dependence: CC Optimum temperature is 90 degrees Celsius. Active from 60 to 105 CC degrees Celsius. Highly thermostable. CC {ECO:0000269|PubMed:10972187}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10972187}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. CC {ECO:0000305}. CC -!- CAUTION: In the crystal structure (PubMed:12588867), the metal ion CC is absent, probably due to the oxidation of the active site Cys- CC 174 to sulfinic acid. In the absence of metal, positions of the CC coenzyme and the substrate and their interactions are all CC significantly altered, presumably accounting for the inactivity of CC this form. {ECO:0000305|PubMed:12588867}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ001089; CAA04524.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36897.1; -; Genomic_DNA. DR PIR; F72205; F72205. DR RefSeq; NP_229631.1; NC_000853.1. DR RefSeq; WP_010865414.1; NZ_CP011107.1. DR PDB; 1OBB; X-ray; 1.90 A; A/B=1-480. DR PDBsum; 1OBB; -. DR ProteinModelPortal; O33830; -. DR SMR; O33830; 2-479. DR STRING; 243274.TM1834; -. DR CAZy; GH4; Glycoside Hydrolase Family 4. DR EnsemblBacteria; AAD36897; AAD36897; TM_1834. DR GeneID; 897356; -. DR KEGG; tma:TM1834; -. DR PATRIC; 23938655; VBITheMar51294_1854. DR eggNOG; ENOG4107V4V; Bacteria. DR eggNOG; COG1486; LUCA. DR InParanoid; O33830; -. DR KO; K07406; -. DR OMA; QMPREEI; -. DR OrthoDB; EOG6TJ7TJ; -. DR BioCyc; TMAR243274:GC6P-1885-MONOMER; -. DR BRENDA; 3.2.1.20; 6331. DR EvolutionaryTrace; O33830; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 2. DR InterPro; IPR019802; GlycHydrolase_4_CS. DR InterPro; IPR001088; Glyco_hydro_4. DR InterPro; IPR022616; Glyco_hydro_4_C. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF02056; Glyco_hydro_4; 1. DR Pfam; PF11975; Glyco_hydro_4C; 1. DR PRINTS; PR00732; GLHYDRLASE4. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF56327; SSF56327; 1. DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cobalt; Complete proteome; KW Glycosidase; Hydrolase; Manganese; Metal-binding; NAD; Nickel; KW Reference proteome. FT CHAIN 1 480 Alpha-glucosidase. FT /FTId=PRO_0000169855. FT NP_BIND 4 70 NAD. FT ACT_SITE 175 175 Proton donor. {ECO:0000305}. FT ACT_SITE 260 260 Proton acceptor. {ECO:0000305}. FT METAL 174 174 Manganese. {ECO:0000250}. FT METAL 203 203 Manganese. {ECO:0000250}. FT BINDING 119 119 Substrate. FT BINDING 153 153 Substrate. FT MUTAGEN 10 10 G->A: Reduced activity. 300-fold FT reduction of the binding affinity for FT NAD(+). No change in substrate affinity. FT {ECO:0000269|PubMed:12062450}. FT MUTAGEN 12 12 G->A: No change in activity and substrate FT affinity. 5-fold reduction of the binding FT affinity for NAD(+). FT {ECO:0000269|PubMed:12062450}. FT MUTAGEN 13 13 S->A: Highly reduced activity. 10-fold FT reduction of the binding affinity for FT NAD(+). No change in substrate affinity. FT {ECO:0000269|PubMed:12062450}. FT CONFLICT 459 479 Missing (in Ref. 1). {ECO:0000305}. FT STRAND 5 9 {ECO:0000244|PDB:1OBB}. FT TURN 10 12 {ECO:0000244|PDB:1OBB}. FT HELIX 14 25 {ECO:0000244|PDB:1OBB}. FT HELIX 28 30 {ECO:0000244|PDB:1OBB}. FT STRAND 34 38 {ECO:0000244|PDB:1OBB}. FT HELIX 42 58 {ECO:0000244|PDB:1OBB}. FT STRAND 64 69 {ECO:0000244|PDB:1OBB}. FT HELIX 71 75 {ECO:0000244|PDB:1OBB}. FT STRAND 79 83 {ECO:0000244|PDB:1OBB}. FT HELIX 89 102 {ECO:0000244|PDB:1OBB}. FT STRAND 122 124 {ECO:0000244|PDB:1OBB}. FT HELIX 126 142 {ECO:0000244|PDB:1OBB}. FT STRAND 147 150 {ECO:0000244|PDB:1OBB}. FT HELIX 155 165 {ECO:0000244|PDB:1OBB}. FT STRAND 168 173 {ECO:0000244|PDB:1OBB}. FT HELIX 176 178 {ECO:0000244|PDB:1OBB}. FT HELIX 179 186 {ECO:0000244|PDB:1OBB}. FT HELIX 191 193 {ECO:0000244|PDB:1OBB}. FT STRAND 194 201 {ECO:0000244|PDB:1OBB}. FT STRAND 204 212 {ECO:0000244|PDB:1OBB}. FT HELIX 218 227 {ECO:0000244|PDB:1OBB}. FT HELIX 229 231 {ECO:0000244|PDB:1OBB}. FT HELIX 244 253 {ECO:0000244|PDB:1OBB}. FT HELIX 259 261 {ECO:0000244|PDB:1OBB}. FT HELIX 267 270 {ECO:0000244|PDB:1OBB}. FT HELIX 273 280 {ECO:0000244|PDB:1OBB}. FT TURN 282 285 {ECO:0000244|PDB:1OBB}. FT HELIX 290 316 {ECO:0000244|PDB:1OBB}. FT HELIX 322 324 {ECO:0000244|PDB:1OBB}. FT STRAND 326 329 {ECO:0000244|PDB:1OBB}. FT HELIX 333 346 {ECO:0000244|PDB:1OBB}. FT HELIX 356 365 {ECO:0000244|PDB:1OBB}. FT STRAND 369 376 {ECO:0000244|PDB:1OBB}. FT STRAND 388 397 {ECO:0000244|PDB:1OBB}. FT STRAND 400 403 {ECO:0000244|PDB:1OBB}. FT HELIX 412 417 {ECO:0000244|PDB:1OBB}. FT HELIX 419 435 {ECO:0000244|PDB:1OBB}. FT HELIX 438 446 {ECO:0000244|PDB:1OBB}. FT HELIX 454 465 {ECO:0000244|PDB:1OBB}. FT HELIX 468 470 {ECO:0000244|PDB:1OBB}. FT HELIX 471 477 {ECO:0000244|PDB:1OBB}. SQ SEQUENCE 480 AA; 55047 MW; 4CA5DB3B155CE5A1 CRC64; MPSVKIGIIG AGSAVFSLRL VSDLCKTPGL SGSTVTLMDI DEERLDAILT IAKKYVEEVG ADLKFEKTMN LDDVIIDADF VINTAMVGGH TYLEKVRQIG EKYGYYRGID AQEFNMVSDY YTFSNYNQLK YFVDIARKIE KLSPKAWYLQ AANPIFEGTT LVTRTVPIKA VGFCHGHYGV MEIVEKLGLE EEKVDWQVAG VNHGIWLNRF RYNGGNAYPL LDKWIEEKSK DWKPENPFND QLSPAAIDMY RFYGVMPIGD TVRNSSWRYH RDLETKKKWY GEPWGGADSE IGWKWYQDTL GKVTEITKKV AKFIKENPSV RLSDLGSVLG KDLSEKQFVL EVEKILDPER KSGEQHIPFI DALLNDNKAR FVVNIPNKGI IHGIDDDVVV EVPALVDKNG IHPEKIEPPL PDRVVKYYLR PRIMRMEMAL EAFLTGDIRI IKELLYRDPR TKSDEQVEKV IEEILALPEN EEMRKHYLKR // ID AGLB_THEMA Reviewed; 473 AA. AC Q9X2F4; DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Cyclomaltodextrinase; DE EC=3.2.1.54; DE AltName: Full=Maltodextrin glucosidase; DE AltName: Full=TMG; GN Name=aglB; OrderedLocusNames=TM_1835; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=12127967; DOI=10.1016/S0006-291X(02)00748-9; RA Lee M.H., Kim Y.W., Kim T.J., Park C.S., Kim J.W., Moon T.W., RA Park K.H.; RT "A novel amylolytic enzyme from Thermotoga maritima, resembling RT cyclodextrinase and alpha-glucosidase, that liberates glucose from the RT reducing end of the substrates."; RL Biochem. Biophys. Res. Commun. 295:818-825(2002). CC -!- FUNCTION: Is able to hydrolyze various linear CC maltooligosaccharides (maltotriose to maltoheptaose) and CC cyclomaltodextrins (CDs), to mainly glucose and maltose, by CC liberating glucose from the reducing end of the molecules. Shows a CC very weak activity on starch. Can neither hydrolyze maltose nor CC degrade pullulan, but rapidly hydrolyzes acarbose, a strong CC amylase and glucosidase inhibitor, to acarviosine and glucose. CC {ECO:0000269|PubMed:12127967}. CC -!- CATALYTIC ACTIVITY: Cyclomaltodextrin + H(2)O = linear CC maltodextrin. {ECO:0000269|PubMed:12127967}. CC -!- ENZYME REGULATION: Mn(2+), Co(2+), Zn(2+), Fe(2+), Mg(2+), and CC Ca(2+) inhibit the hydrolysis activity of the enzyme whereas EGTA CC and EDTA do not affect the activity. CC {ECO:0000269|PubMed:12127967}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=20.64 mM for maltotriose (at pH 6.5 and 85 degrees Celsius) CC {ECO:0000269|PubMed:12127967}; CC KM=11.84 mM for maltotetraose (at pH 6.5 and 85 degrees Celsius) CC {ECO:0000269|PubMed:12127967}; CC KM=9.95 mM for maltopentaose (at pH 6.5 and 85 degrees Celsius) CC {ECO:0000269|PubMed:12127967}; CC KM=7.77 mM for maltohexaose (at pH 6.5 and 85 degrees Celsius) CC {ECO:0000269|PubMed:12127967}; CC KM=7.41 mM for maltoheptaose (at pH 6.5 and 85 degrees Celsius) CC {ECO:0000269|PubMed:12127967}; CC KM=2.26 mM for pNP-maltopentaose (at pH 6.5 and 85 degrees CC Celsius) {ECO:0000269|PubMed:12127967}; CC KM=14.53 mM for beta-cyclodextrin (at pH 6.5 and 85 degrees CC Celsius) {ECO:0000269|PubMed:12127967}; CC pH dependence: CC Optimum pH is 6.5 with beta-cyclodextrin as substrate. CC {ECO:0000269|PubMed:12127967}; CC Temperature dependence: CC Optimum temperature is 85 degrees Celsius with beta-cyclodextrin CC as substrate. Retains 80% of its activity at 90 degrees Celsius. CC The half-lives of the enzyme examined at 80, 85, and 90 degrees CC Celsius are 147, 108, and 23 minutes, respectively. CC {ECO:0000269|PubMed:12127967}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36898.1; -; Genomic_DNA. DR PIR; G72205; G72205. DR RefSeq; NP_229632.1; NC_000853.1. DR RefSeq; WP_004082380.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2F4; -. DR STRING; 243274.TM1835; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblBacteria; AAD36898; AAD36898; TM_1835. DR GeneID; 897817; -. DR KEGG; tma:TM1835; -. DR PATRIC; 23938657; VBITheMar51294_1855. DR eggNOG; ENOG4108IUK; Bacteria. DR eggNOG; COG0366; LUCA. DR InParanoid; Q9X2F4; -. DR OMA; GNNDPFC; -. DR OrthoDB; EOG6TFCNV; -. DR BioCyc; TMAR243274:GC6P-1886-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0047798; F:cyclomaltodextrinase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR015902; Glyco_hydro_13. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10357; PTHR10357; 2. DR Pfam; PF00128; Alpha-amylase; 2. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Complete proteome; Glycosidase; Hydrolase; KW Reference proteome. FT CHAIN 1 473 Cyclomaltodextrinase. FT /FTId=PRO_0000415271. FT ACT_SITE 210 210 Nucleophile. {ECO:0000250}. FT ACT_SITE 239 239 Proton donor. {ECO:0000250}. FT SITE 298 298 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 473 AA; 55181 MW; E1CC229BAE5FA6CE CRC64; MMYPMPSWVY DSVVYQIFPD RFFIGKGKTV EDKKDLYLKR GGVIEKWGVP PRKLPGAQHV KIFYGGDLWG IAEKVDYFEE LGINVLYLTP IFLSDTNHKY DTIDYFRVDP QFGGKRAFLH LLRVLHERSM KLILDGVFNH VGSQHPWFKK AKKNDPEYVN RFFLYKDRHR SWFDVGSLPE LNVEVEEVKE YILKVVEHYL KLGIDGWRLD CGHDLGPTVN LWINMKVKEF SAEKYLVSEI WTYPAGWDMV DGLMNYNFRN LVLSYVNGET DSIGFHLERA YRETKNIFGC WNMLDSHDTP RLATMVPDRD LRKLAVVLQF TYPGVPLVYY GTEIGLTGGE DPECRATMEW NREKWDVDLF EFYKKMIRLR RTDPGLRFGE FVLLNDSPLA FLRKAPHPLQ NTIVVVNPGE EKVLVLSIPD GKIMNTTPLV DVFSGERFHV DGGVVKLPLL ARSFRILKPE DLRVGKYRLY KRV // ID AGUA_THEMA Reviewed; 674 AA. AC P96105; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 2. DT 13-APR-2016, entry version 112. DE RecName: Full=Xylan alpha-(1->2)-glucuronosidase; DE EC=3.2.1.131; DE AltName: Full=Alpha-glucuronidase; GN Name=aguA; OrderedLocusNames=TM_0055; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, FUNCTION, RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9044261; DOI=10.1046/j.1365-2958.1997.2011568.x; RA Ruile P., Winterhalter C., Liebl W.; RT "Isolation and analysis of a gene encoding alpha-glucuronidase, an RT enzyme with a novel primary structure involved in the breakdown of RT xylan."; RL Mol. Microbiol. 23:267-279(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Alpha-glucuronidase involved in the hydrolysis of xylan, CC a major structural heterogeneous polysaccharide found in plant CC biomass representing the second most abundant polysaccharide in CC the biosphere, after cellulose. It catalyzes the cleavage of CC alpha-(1->2)-glycosidic bond of the 4-O-methyl-D-glucuronic acid CC side chain of xylan and releases 4-O-methylglucuronic acid from CC xylan. {ECO:0000269|PubMed:9044261}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of (1->2)-alpha-D-(4-O- CC methyl)glucuronosyl links in the main chain of hardwood xylans. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.95 mM for 2-O-(4-O-methyl-alpha-D-glucopyranosyluronic CC acid)-D-xylobiose (MeGlcAX2) (at 75 degrees Celsius) CC {ECO:0000269|PubMed:9044261}; CC Vmax=31 umol/min/mg enzyme with MeGlcAX2 as substrate (at 75 CC degrees Celsius) {ECO:0000269|PubMed:9044261}; CC pH dependence: CC Optimum pH is 6.3 with more than 50% activity occurring between CC pH 5.2 and 7.9. {ECO:0000269|PubMed:9044261}; CC Temperature dependence: CC Optimum temperature is 85 degrees Celsius. CC {ECO:0000269|PubMed:9044261}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9044261}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y09510; CAA70702.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35149.1; -; Genomic_DNA. DR PIR; H72423; H72423. DR RefSeq; NP_227871.1; NC_000853.1. DR RefSeq; WP_004082543.1; NZ_CP011107.1. DR ProteinModelPortal; P96105; -. DR SMR; P96105; 3-674. DR STRING; 243274.TM0055; -. DR CAZy; GH67; Glycoside Hydrolase Family 67. DR EnsemblBacteria; AAD35149; AAD35149; TM_0055. DR GeneID; 896879; -. DR KEGG; tma:TM0055; -. DR PATRIC; 23934950; VBITheMar51294_0053. DR eggNOG; ENOG4105D0H; Bacteria. DR eggNOG; COG3661; LUCA. DR InParanoid; P96105; -. DR KO; K01235; -. DR OMA; MVNPGHH; -. DR OrthoDB; EOG6J48K3; -. DR BRENDA; 3.2.1.139; 6331. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0046559; F:alpha-glucuronidase activity; IEA:InterPro. DR GO; GO:0033939; F:xylan alpha-1,2-glucuronosidase activity; IDA:UniProtKB. DR GO; GO:2000886; P:glucuronoxylan catabolic process; IDA:UniProtKB. DR Gene3D; 3.20.20.80; -; 1. DR Gene3D; 3.30.379.10; -; 1. DR Gene3D; 3.90.1330.10; -; 1. DR InterPro; IPR029018; Chitobiase/Hex_dom_2-like. DR InterPro; IPR011395; Glyco_hydro_67_aGlcAse. DR InterPro; IPR005154; Glyco_hydro_67_aGlcAse_N. DR InterPro; IPR011099; Glyco_hydro_67_C. DR InterPro; IPR011100; Glyco_hydro_67_cat. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF07477; Glyco_hydro_67C; 1. DR Pfam; PF07488; Glyco_hydro_67M; 1. DR Pfam; PF03648; Glyco_hydro_67N; 1. DR PIRSF; PIRSF029900; Alpha-glucuronds; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR SUPFAM; SSF55545; SSF55545; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Complete proteome; Direct protein sequencing; KW Glycosidase; Hydrolase; Polysaccharide degradation; KW Reference proteome; Xylan degradation. FT CHAIN 1 674 Xylan alpha-(1->2)-glucuronosidase. FT /FTId=PRO_0000057716. FT REGION 155 156 Substrate binding. {ECO:0000250}. FT ACT_SITE 281 281 Proton donor. {ECO:0000250}. FT ACT_SITE 360 360 Proton acceptor. {ECO:0000250}. FT ACT_SITE 388 388 Proton acceptor. {ECO:0000250}. FT BINDING 197 197 beta-D-glucuronic acid. {ECO:0000250}. FT BINDING 277 277 Substrate. {ECO:0000250}. FT BINDING 314 314 Substrate. {ECO:0000250}. FT BINDING 331 331 Substrate. {ECO:0000250}. FT BINDING 355 355 Substrate. {ECO:0000250}. FT BINDING 382 382 Substrate. {ECO:0000250}. FT BINDING 506 506 Substrate. {ECO:0000250}. FT BINDING 536 536 Substrate. {ECO:0000250}. FT SITE 147 147 Participates in a stacking interactions FT with the sugar rings of 4-O-MeGlcA. FT {ECO:0000250}. FT SITE 536 536 Participates in a stacking interactions FT with the sugar rings of 4-O-MeGlcA. FT {ECO:0000250}. SQ SEQUENCE 674 AA; 78629 MW; 350F1CBEDE452761 CRC64; MDYRMCWLEY RGLPADVAGK LKDWFSSVSI LEPGSSVLKD EIRRFSERSI GITPRFYSRP LKKEKYIMVG RLESLPIKLD VNLGEEGFML RTIEWNGSKI LLVTGETKKA LVYGIFDLMK RIRLGEDIEK MNVLAKPKAK FRMLNHWDNL DGTIERGYAG NSIFFKDNRI IINQRTKDYA RLLASIGING VVINNVNVKK REVYLIDSIY LKKLKKLADI FREYGIKIYL SINFASPVYL GGLDTADPLD ERVARWWREK ARGIYDYIPD FGGFLVKADS EFNPGPHMFG RTHAEGANML ARALAPFGGV VIWRAFVYNC LQDWRDYKTD RAKAAYDNFK PLDGQFDDNV IIQIKYGPMD FQVREPVNPL FGGMEKTNQI LELQITQEYT GQQIHLCFLG TLWKEILEFD TFAKGEGSYV KRIVDGTLFD RENNGFAGVS NVGDSVNWTG HDLAQANLYA FGRLAWNPDE EIERIVEEWI KLTFGDDEKV LENVSYMLMK SHRTYEKYTT PFGLGWMVNP GHHYGPNPEG YEYSKWGTYH RANWEAIGVD RTSRGTGYTL QYHSPWKEIY DDINTCPEDL LLFFHRVRYD HRLKSGKTLL QTMYDLHFEG VEEVEEFIKK WEELKDRVSP DIFERVKERL HMQLEHAKEW RDVINTYFYR RTGIPDEKGR KIYP // ID APEA_THEMA Reviewed; 451 AA. AC Q9WYJ9; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 24-OCT-2001, sequence version 2. DT 13-APR-2016, entry version 103. DE RecName: Full=Probable M18 family aminopeptidase 1; DE EC=3.4.11.-; GN Name=apeA; OrderedLocusNames=TM_0365; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35452.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35452.1; ALT_INIT; Genomic_DNA. DR PIR; E72387; E72387. DR RefSeq; NP_228176.1; NC_000853.1. DR RefSeq; WP_004083171.1; NZ_CP011107.1. DR RefSeq; WP_010865103.1; NC_000853.1. DR PDB; 2GLF; X-ray; 2.80 A; A/B/C/D=2-451. DR PDBsum; 2GLF; -. DR ProteinModelPortal; Q9WYJ9; -. DR SMR; Q9WYJ9; 2-451. DR STRING; 243274.TM0365; -. DR MEROPS; M18.004; -. DR EnsemblBacteria; AAD35452; AAD35452; TM_0365. DR GeneID; 897324; -. DR KEGG; tma:TM0365; -. DR PATRIC; 23935611; VBITheMar51294_0370. DR eggNOG; ENOG4105DFM; Bacteria. DR eggNOG; COG1362; LUCA. DR InParanoid; Q9WYJ9; -. DR OMA; ENPTIFH; -. DR OrthoDB; EOG6BW4VB; -. DR BioCyc; TMAR243274:GC6P-379-MONOMER; -. DR EvolutionaryTrace; Q9WYJ9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.250.10; -; 1. DR HAMAP; MF_00466; Aminopeptidase_M18_1; 1. DR InterPro; IPR022983; M18_aminopeptidase_1. DR InterPro; IPR001948; Peptidase_M18. DR InterPro; IPR023358; Peptidase_M18_dom2. DR Pfam; PF02127; Peptidase_M18; 1. DR PRINTS; PR00932; AMINO1PTASE. PE 1: Evidence at protein level; KW 3D-structure; Aminopeptidase; Complete proteome; Hydrolase; KW Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc. FT CHAIN 1 451 Probable M18 family aminopeptidase 1. FT /FTId=PRO_0000173458. FT METAL 93 93 Zinc. {ECO:0000255}. FT METAL 168 168 Zinc. {ECO:0000255}. FT METAL 426 426 Zinc. {ECO:0000255}. FT HELIX 8 10 {ECO:0000244|PDB:2GLF}. FT HELIX 14 30 {ECO:0000244|PDB:2GLF}. FT HELIX 34 46 {ECO:0000244|PDB:2GLF}. FT TURN 47 49 {ECO:0000244|PDB:2GLF}. FT STRAND 65 72 {ECO:0000244|PDB:2GLF}. FT STRAND 74 79 {ECO:0000244|PDB:2GLF}. FT HELIX 83 85 {ECO:0000244|PDB:2GLF}. FT STRAND 88 93 {ECO:0000244|PDB:2GLF}. FT STRAND 98 109 {ECO:0000244|PDB:2GLF}. FT STRAND 112 122 {ECO:0000244|PDB:2GLF}. FT HELIX 126 128 {ECO:0000244|PDB:2GLF}. FT STRAND 129 131 {ECO:0000244|PDB:2GLF}. FT STRAND 133 140 {ECO:0000244|PDB:2GLF}. FT STRAND 146 157 {ECO:0000244|PDB:2GLF}. FT HELIX 167 169 {ECO:0000244|PDB:2GLF}. FT TURN 176 179 {ECO:0000244|PDB:2GLF}. FT HELIX 182 184 {ECO:0000244|PDB:2GLF}. FT STRAND 186 190 {ECO:0000244|PDB:2GLF}. FT HELIX 201 214 {ECO:0000244|PDB:2GLF}. FT HELIX 218 221 {ECO:0000244|PDB:2GLF}. FT STRAND 224 230 {ECO:0000244|PDB:2GLF}. FT STRAND 235 238 {ECO:0000244|PDB:2GLF}. FT STRAND 243 246 {ECO:0000244|PDB:2GLF}. FT HELIX 249 264 {ECO:0000244|PDB:2GLF}. FT STRAND 271 277 {ECO:0000244|PDB:2GLF}. FT HELIX 279 281 {ECO:0000244|PDB:2GLF}. FT STRAND 285 292 {ECO:0000244|PDB:2GLF}. FT HELIX 293 304 {ECO:0000244|PDB:2GLF}. FT STRAND 308 310 {ECO:0000244|PDB:2GLF}. FT HELIX 311 319 {ECO:0000244|PDB:2GLF}. FT STRAND 322 326 {ECO:0000244|PDB:2GLF}. FT HELIX 334 339 {ECO:0000244|PDB:2GLF}. FT HELIX 342 344 {ECO:0000244|PDB:2GLF}. FT STRAND 352 357 {ECO:0000244|PDB:2GLF}. FT HELIX 371 383 {ECO:0000244|PDB:2GLF}. FT STRAND 388 390 {ECO:0000244|PDB:2GLF}. FT STRAND 393 395 {ECO:0000244|PDB:2GLF}. FT HELIX 405 409 {ECO:0000244|PDB:2GLF}. FT TURN 410 412 {ECO:0000244|PDB:2GLF}. FT STRAND 415 419 {ECO:0000244|PDB:2GLF}. FT STRAND 421 424 {ECO:0000244|PDB:2GLF}. FT STRAND 427 433 {ECO:0000244|PDB:2GLF}. FT HELIX 434 450 {ECO:0000244|PDB:2GLF}. SQ SEQUENCE 451 AA; 50381 MW; C2310E30DA36BCD8 CRC64; MKMERKNVWH HRKKEEIEAF SKEYMEFMSK AKTERMTVKE IKRILDESGF VPLEDFAGDP MNMTVYAVNR GKAIAAFRVV DDLKRGLNLV VAHIDSPRLD FKPNPLIEDE QIALFKTHYY GGIKKYHWLS IPLEIHGVLF KNDGTEIEIH IGDKPEDPVF TIPDLLPHLD KEDAKISEKF KGENLMLIAG TIPLSGEEKE AVKTNVLKIL NEMYGITEED FVSGEIEVVP AFSPREVGMD RSLIGAYGQD DRICAYTALR ALLSANPEKS IGVIFFDKEE IGSDGNTGAK ARFYLKALRQ ILKMQGAKDS EFVLDEVLEN TSVISGDVCA AVNPPYKDVH DLHNAPKLGY GVALVKYTGA RGKYSTNDAH AEFVARVRKV LNEQGVIWQV ATLGKVDQGG GGTIAKFFAE RGSDVIDMGP ALLGMHSPFE ISSKADLFET YVAYRSLMEK L // ID ARGB_THEMA Reviewed; 282 AA. AC Q9X2A4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 126. DE RecName: Full=Acetylglutamate kinase; DE EC=2.7.2.8; DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase; DE AltName: Full=NAG kinase; DE Short=AGK; GN Name=argB; OrderedLocusNames=TM_1784; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF 1-35, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, PATHWAY, AND MASS SPECTROMETRY. RX PubMed=15342584; DOI=10.1128/JB.186.18.6142-6149.2004; RA Fernandez-Murga M.L., Gil-Ortiz F., Llacer J.L., Rubio V.; RT "Arginine biosynthesis in Thermotoga maritima: characterization of the RT arginine-sensitive N-acetyl-L-glutamate kinase."; RL J. Bacteriol. 186:6142-6149(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND RP ARGININE, MASS SPECTROMETRY, ENZYME REGULATION, AND SUBUNIT. RX PubMed=16376937; DOI=10.1016/j.jmb.2005.11.079; RA Ramon-Maiques S., Fernandez-Murga M.L., Gil-Ortiz F., Vagin A., RA Fita I., Rubio V.; RT "Structural bases of feed-back control of arginine biosynthesis, RT revealed by the structures of two hexameric N-acetylglutamate kinases, RT from Thermotoga maritima and Pseudomonas aeruginosa."; RL J. Mol. Biol. 356:695-713(2006). CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L- CC glutamate 5-phosphate. {ECO:0000269|PubMed:15342584}. CC -!- ENZYME REGULATION: Allosterically inhibited by arginine. CC {ECO:0000269|PubMed:16376937}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Active from 25 to 80 degrees Celsius. CC {ECO:0000269|PubMed:15342584}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 2/4. CC {ECO:0000269|PubMed:15342584}. CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:16376937}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MASS SPECTROMETRY: Mass=30341; Method=MALDI; Range=1-282; CC Evidence={ECO:0000269|PubMed:15342584}; CC -!- MASS SPECTROMETRY: Mass=30352; Method=Electrospray; Range=1-282; CC Evidence={ECO:0000269|PubMed:16376937}; CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36847.1; -; Genomic_DNA. DR PIR; C72211; C72211. DR RefSeq; NP_229581.1; NC_000853.1. DR RefSeq; WP_004082330.1; NZ_CP011107.1. DR PDB; 2BTY; X-ray; 2.75 A; A/B/C=1-282. DR PDBsum; 2BTY; -. DR ProteinModelPortal; Q9X2A4; -. DR SMR; Q9X2A4; 1-282. DR STRING; 243274.TM1784; -. DR EnsemblBacteria; AAD36847; AAD36847; TM_1784. DR GeneID; 897763; -. DR KEGG; tma:TM1784; -. DR PATRIC; 23938553; VBITheMar51294_1804. DR eggNOG; ENOG4105CAS; Bacteria. DR eggNOG; COG0548; LUCA. DR InParanoid; Q9X2A4; -. DR KO; K00930; -. DR OMA; PKTECCI; -. DR OrthoDB; EOG6T1WVF; -. DR BRENDA; 2.7.2.8; 6331. DR UniPathway; UPA00068; UER00107. DR EvolutionaryTrace; Q9X2A4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003991; F:acetylglutamate kinase activity; IBA:GO_Central. DR GO; GO:0034618; F:arginine binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_00082_A; ArgB_A; 1. DR HAMAP; MF_00082_B; ArgB_B; 1. DR InterPro; IPR004662; AcgluKinase. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF000728; NAGK; 1. DR PRINTS; PR00474; GLU5KINASE. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR00761; argB; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis; KW Arginine biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Direct protein sequencing; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 282 Acetylglutamate kinase. FT /FTId=PRO_0000112678. FT REGION 62 63 Substrate binding. {ECO:0000250}. FT REGION 266 269 Allosteric inhibitor binding. FT BINDING 84 84 Substrate. {ECO:0000250}. FT BINDING 178 178 Substrate. {ECO:0000269|PubMed:16376937}. FT BINDING 196 196 Allosteric inhibitor. FT BINDING 214 214 Allosteric inhibitor. FT SITE 27 27 Transition state stabilizer. FT {ECO:0000250}. FT SITE 237 237 Transition state stabilizer. FT {ECO:0000250}. FT HELIX 2 19 {ECO:0000244|PDB:2BTY}. FT STRAND 23 28 {ECO:0000244|PDB:2BTY}. FT HELIX 31 34 {ECO:0000244|PDB:2BTY}. FT HELIX 36 51 {ECO:0000244|PDB:2BTY}. FT STRAND 55 60 {ECO:0000244|PDB:2BTY}. FT HELIX 64 72 {ECO:0000244|PDB:2BTY}. FT STRAND 79 84 {ECO:0000244|PDB:2BTY}. FT HELIX 88 100 {ECO:0000244|PDB:2BTY}. FT HELIX 102 111 {ECO:0000244|PDB:2BTY}. FT TURN 112 114 {ECO:0000244|PDB:2BTY}. FT STRAND 117 121 {ECO:0000244|PDB:2BTY}. FT HELIX 124 126 {ECO:0000244|PDB:2BTY}. FT STRAND 127 132 {ECO:0000244|PDB:2BTY}. FT STRAND 140 148 {ECO:0000244|PDB:2BTY}. FT HELIX 151 158 {ECO:0000244|PDB:2BTY}. FT STRAND 162 170 {ECO:0000244|PDB:2BTY}. FT STRAND 172 174 {ECO:0000244|PDB:2BTY}. FT STRAND 176 178 {ECO:0000244|PDB:2BTY}. FT HELIX 181 192 {ECO:0000244|PDB:2BTY}. FT STRAND 195 205 {ECO:0000244|PDB:2BTY}. FT HELIX 218 225 {ECO:0000244|PDB:2BTY}. FT TURN 226 228 {ECO:0000244|PDB:2BTY}. FT HELIX 234 246 {ECO:0000244|PDB:2BTY}. FT STRAND 252 256 {ECO:0000244|PDB:2BTY}. FT HELIX 262 267 {ECO:0000244|PDB:2BTY}. FT STRAND 268 271 {ECO:0000244|PDB:2BTY}. FT STRAND 273 277 {ECO:0000244|PDB:2BTY}. SQ SEQUENCE 282 AA; 30345 MW; A140CE3899BFA40A CRC64; MRIDTVNVLL EALPYIKEFY GKTFVIKFGG SAMKQENAKK AFIQDIILLK YTGIKPIIVH GGGPAISQMM KDLGIEPVFK NGHRVTDEKT MEIVEMVLVG KINKEIVMNL NLHGGRAVGI CGKDSKLIVA EKETKHGDIG YVGKVKKVNP EILHALIEND YIPVIAPVGI GEDGHSYNIN ADTAAAEIAK SLMAEKLILL TDVDGVLKDG KLISTLTPDE AEELIRDGTV TGGMIPKVEC AVSAVRGGVG AVHIINGGLE HAILLEIFSR KGIGTMIKEL EG // ID ARGD_THEMA Reviewed; 385 AA. AC Q9X2A5; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 126. DE RecName: Full=Acetylornithine aminotransferase; DE Short=ACOAT; DE EC=2.6.1.11; GN Name=argD; OrderedLocusNames=TM_1785; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH PLP. RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of acetylornithine aminotransferase from Thermotoga RT maritima."; RL Submitted (FEB-2009) to the PDB data bank. RN [3] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PLP. RG Joint center for structural genomics (JCSG); RT "Crystal structure of acetylornithine aminotransferase (EC 2.6.1.11) RT (acoat) (tm1785) from Thermotoga maritima at 1.40 a resolution."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N- CC acetyl-L-glutamate 5-semialdehyde + L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Note=Binds 1 pyridoxal phosphate per subunit.; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 4/4. CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.2, ECO:0000305|Ref.3}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate CC aminotransferase activity, thus carrying out the corresponding CC step in lysine biosynthesis. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. ArgD subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36848.1; -; Genomic_DNA. DR PIR; D72211; D72211. DR RefSeq; NP_229582.1; NC_000853.1. DR RefSeq; WP_004082331.1; NZ_CP011107.1. DR PDB; 2E54; X-ray; 1.50 A; A=1-385. DR PDB; 2ORD; X-ray; 1.40 A; A/B=1-385. DR PDBsum; 2E54; -. DR PDBsum; 2ORD; -. DR ProteinModelPortal; Q9X2A5; -. DR SMR; Q9X2A5; 1-385. DR STRING; 243274.TM1785; -. DR EnsemblBacteria; AAD36848; AAD36848; TM_1785. DR GeneID; 897842; -. DR KEGG; tma:TM1785; -. DR PATRIC; 23938555; VBITheMar51294_1805. DR eggNOG; ENOG4105C8Y; Bacteria. DR eggNOG; COG4992; LUCA. DR InParanoid; Q9X2A5; -. DR KO; K00821; -. DR OMA; TGKMWGY; -. DR OrthoDB; EOG6QVRHN; -. DR UniPathway; UPA00068; UER00109. DR EvolutionaryTrace; Q9X2A5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR HAMAP; MF_01107; ArgD_aminotrans_3; 1. DR InterPro; IPR004636; AcOrn/SuccOrn_fam. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11986; PTHR11986; 1. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00707; argD; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aminotransferase; KW Arginine biosynthesis; Complete proteome; Cytoplasm; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 385 Acetylornithine aminotransferase. FT /FTId=PRO_0000112805. FT REGION 94 95 Pyridoxal phosphate binding. FT REGION 211 214 Pyridoxal phosphate binding. FT BINDING 126 126 Pyridoxal phosphate; via carbonyl oxygen. FT BINDING 129 129 N2-acetyl-L-ornithine. {ECO:0000250}. FT BINDING 267 267 N2-acetyl-L-ornithine. {ECO:0000250}. FT BINDING 268 268 Pyridoxal phosphate. {ECO:0000250}. FT MOD_RES 240 240 N6-(pyridoxal phosphate)lysine. FT STRAND 13 19 {ECO:0000244|PDB:2ORD}. FT STRAND 21 24 {ECO:0000244|PDB:2ORD}. FT STRAND 29 34 {ECO:0000244|PDB:2ORD}. FT HELIX 35 38 {ECO:0000244|PDB:2ORD}. FT HELIX 47 59 {ECO:0000244|PDB:2ORD}. FT STRAND 67 69 {ECO:0000244|PDB:2ORD}. FT HELIX 70 81 {ECO:0000244|PDB:2ORD}. FT TURN 82 84 {ECO:0000244|PDB:2ORD}. FT STRAND 87 93 {ECO:0000244|PDB:2ORD}. FT HELIX 94 112 {ECO:0000244|PDB:2ORD}. FT STRAND 118 123 {ECO:0000244|PDB:2ORD}. FT HELIX 131 136 {ECO:0000244|PDB:2ORD}. FT HELIX 140 143 {ECO:0000244|PDB:2ORD}. FT HELIX 144 146 {ECO:0000244|PDB:2ORD}. FT STRAND 153 156 {ECO:0000244|PDB:2ORD}. FT HELIX 161 167 {ECO:0000244|PDB:2ORD}. FT STRAND 172 177 {ECO:0000244|PDB:2ORD}. FT STRAND 179 181 {ECO:0000244|PDB:2ORD}. FT TURN 183 185 {ECO:0000244|PDB:2ORD}. FT HELIX 191 204 {ECO:0000244|PDB:2ORD}. FT STRAND 207 211 {ECO:0000244|PDB:2ORD}. FT TURN 213 220 {ECO:0000244|PDB:2ORD}. FT STRAND 221 224 {ECO:0000244|PDB:2ORD}. FT HELIX 225 229 {ECO:0000244|PDB:2ORD}. FT STRAND 234 238 {ECO:0000244|PDB:2ORD}. FT HELIX 240 243 {ECO:0000244|PDB:2ORD}. FT STRAND 249 253 {ECO:0000244|PDB:2ORD}. FT TURN 255 257 {ECO:0000244|PDB:2E54}. FT HELIX 273 286 {ECO:0000244|PDB:2ORD}. FT HELIX 291 312 {ECO:0000244|PDB:2ORD}. FT STRAND 316 322 {ECO:0000244|PDB:2ORD}. FT STRAND 325 330 {ECO:0000244|PDB:2ORD}. FT HELIX 336 345 {ECO:0000244|PDB:2ORD}. FT STRAND 351 353 {ECO:0000244|PDB:2ORD}. FT TURN 354 356 {ECO:0000244|PDB:2ORD}. FT STRAND 357 360 {ECO:0000244|PDB:2ORD}. FT HELIX 368 383 {ECO:0000244|PDB:2ORD}. SQ SEQUENCE 385 AA; 42884 MW; 4018F87FCBEBFFE0 CRC64; MYLMNTYSRF PATFVYGKGS WIYDEKGNAY LDFTSGIAVN VLGHSHPRLV EAIKDQAEKL IHCSNLFWNR PQMELAELLS KNTFGGKVFF ANTGTEANEA AIKIARKYGK KKSEKKYRIL SAHNSFHGRT LGSLTATGQP KYQKPFEPLV PGFEYFEFNN VEDLRRKMSE DVCAVFLEPI QGESGIVPAT KEFLEEARKL CDEYDALLVF DEVQCGMGRT GKLFAYQKYG VVPDVLTTAK GLGGGVPIGA VIVNERANVL EPGDHGTTFG GNPLACRAGV TVIKELTKEG FLEEVEEKGN YLMKKLQEMK EEYDVVADVR GMGLMIGIQF REEVSNREVA TKCFENKLLV VPAGNNTIRF LPPLTVEYGE IDLAVETLKK VLQGI // ID ARGJ_THEMA Reviewed; 397 AA. AC Q9X2A3; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000255|HAMAP-Rule:MF_01106}; DE Includes: DE RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106}; DE EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_01106}; DE AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Short=OATase {ECO:0000255|HAMAP-Rule:MF_01106}; DE AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Includes: DE RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106}; DE EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01106}; DE AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Short=AGSase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Contains: DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_01106}; DE Contains: DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_01106}; GN Name=argJ {ECO:0000255|HAMAP-Rule:MF_01106}; GN OrderedLocusNames=TM_1783; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes two activities which are involved in the CC cyclic version of arginine biosynthesis: the synthesis of N- CC acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, CC and of ornithine by transacetylation between N(2)-acetylornithine CC and glutamate. {ECO:0000255|HAMAP-Rule:MF_01106}. CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L- CC ornithine + N-acetyl-L-glutamate. {ECO:0000255|HAMAP- CC Rule:MF_01106}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L- CC glutamate. {ECO:0000255|HAMAP-Rule:MF_01106}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)- CC acetyl-L-ornithine (cyclic): step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01106}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 1/4. {ECO:0000255|HAMAP- CC Rule:MF_01106}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. CC {ECO:0000255|HAMAP-Rule:MF_01106}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01106}. CC -!- MISCELLANEOUS: Some bacteria possess a monofunctional ArgJ, i.e. CC capable of catalyzing only the fifth step of the arginine CC biosynthetic pathway. CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP- CC Rule:MF_01106}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36846.1; -; Genomic_DNA. DR PIR; B72211; B72211. DR RefSeq; NP_229580.1; NC_000853.1. DR RefSeq; WP_004082329.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2A3; -. DR STRING; 243274.TM1783; -. DR MEROPS; T05.001; -. DR EnsemblBacteria; AAD36846; AAD36846; TM_1783. DR GeneID; 897843; -. DR KEGG; tma:TM1783; -. DR PATRIC; 23938551; VBITheMar51294_1803. DR eggNOG; ENOG4105C5V; Bacteria. DR eggNOG; COG1364; LUCA. DR InParanoid; Q9X2A3; -. DR KO; K00620; -. DR OMA; WTCDLTH; -. DR OrthoDB; EOG6P8TQQ; -. DR UniPathway; UPA00068; UER00106. DR UniPathway; UPA00068; UER00111. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0004358; F:glutamate N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0006592; P:ornithine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.60.70.12; -; 1. DR HAMAP; MF_01106; ArgJ; 1. DR InterPro; IPR002813; Arg_biosynth_ArgJ. DR InterPro; IPR016117; ArgJ-like_dom. DR PANTHER; PTHR23100; PTHR23100; 1. DR Pfam; PF01960; ArgJ; 1. DR SUPFAM; SSF56266; SSF56266; 1. DR TIGRFAMs; TIGR00120; ArgJ; 1. PE 3: Inferred from homology; KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; KW Autocatalytic cleavage; Complete proteome; Cytoplasm; KW Multifunctional enzyme; Reference proteome; Transferase. FT CHAIN 1 179 Arginine biosynthesis bifunctional FT protein ArgJ alpha chain. FT {ECO:0000255|HAMAP-Rule:MF_01106}. FT /FTId=PRO_0000002257. FT CHAIN 180 397 Arginine biosynthesis bifunctional FT protein ArgJ beta chain. FT {ECO:0000255|HAMAP-Rule:MF_01106}. FT /FTId=PRO_0000002258. FT ACT_SITE 180 180 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 143 143 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 169 169 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 180 180 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 266 266 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 392 392 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT BINDING 397 397 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT SITE 107 107 Involved in the stabilization of negative FT charge on the oxyanion by the formation FT of the oxyanion hole. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT SITE 108 108 Involved in the stabilization of negative FT charge on the oxyanion by the formation FT of the oxyanion hole. {ECO:0000255|HAMAP- FT Rule:MF_01106}. FT SITE 179 180 Cleavage; by autolysis. FT {ECO:0000255|HAMAP-Rule:MF_01106}. SQ SEQUENCE 397 AA; 43049 MW; 72F3396B1506EAF2 CRC64; MFTPRGFKFA GVHCKIKRKR KDLGIIFSEV PCVAAGVFTT NVVKAAPVIY DMEILKKNPN GIKAVVVNSG VANACTGEQG MINARRMAEK TAEELGVPVE SVLVSSTGVI GVQLPMDKVE NGIEEAARVL SNDPLPFAEA IMTTDTKVKM HSTKVMIDGK EITVLGIAKG SGMIHPNMAT MLSFITTDAK ISEEALKKLL KLSVDDSYNM IDVDGDTSTN DMVIVLANGL AGNTTIQPET DGFWKLYEAV HEVNQVLAEK IVEDGEGATK VMEVHVINAP DIKSARLIAR SIVSSNLVKT AIYGEDANWG RVIAAAGYSG ATFDPEKLDL FFESEAGRIK VAENGQGVSF DEEEAKKILS EKKIRIILDM KQGKETAKAW GCDLTEKYVE INGRYRT // ID APGM_THEMA Reviewed; 401 AA. AC Q9X295; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01402}; DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01402}; DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01402}; DE Short=aPGAM {ECO:0000255|HAMAP-Rule:MF_01402}; DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01402}; GN Name=apgM {ECO:0000255|HAMAP-Rule:MF_01402}; GN OrderedLocusNames=TM_1774; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and CC 3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01402}. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate. CC {ECO:0000255|HAMAP-Rule:MF_01402}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP- CC Rule:MF_01402}. CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase CC family. A-PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01402}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36837.1; -; Genomic_DNA. DR PIR; E72213; E72213. DR RefSeq; NP_229571.1; NC_000853.1. DR RefSeq; WP_004082320.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X295; -. DR STRING; 243274.TM1774; -. DR EnsemblBacteria; AAD36837; AAD36837; TM_1774. DR GeneID; 897849; -. DR KEGG; tma:TM1774; -. DR PATRIC; 23938530; VBITheMar51294_1794. DR eggNOG; ENOG4105E3H; Bacteria. DR eggNOG; COG3635; LUCA. DR InParanoid; Q9X295; -. DR KO; K15635; -. DR OMA; KKTDSYG; -. DR OrthoDB; EOG6GXTSN; -. DR BioCyc; MetaCyc:MONOMER-402; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.720.10; -; 2. DR HAMAP; MF_01402_B; ApgM_B; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR023665; ApgAM_prokaryotes. DR InterPro; IPR006124; Metalloenzyme. DR InterPro; IPR004456; Phosphoglycerate_mutase_apgM. DR Pfam; PF01676; Metalloenzyme; 1. DR Pfam; PF10143; PhosphMutase; 1. DR PIRSF; PIRSF006392; IPGAM_arch; 1. DR SUPFAM; SSF53649; SSF53649; 2. DR TIGRFAMs; TIGR00306; apgM; 1. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Isomerase; Reference proteome. FT CHAIN 1 401 Probable 2,3-bisphosphoglycerate- FT independent phosphoglycerate mutase. FT /FTId=PRO_0000138155. SQ SEQUENCE 401 AA; 44275 MW; 9B2FB45F1C154411 CRC64; MFDKQEFVSK LVTEEKAKIV LLVMDGLGDI PVNGKTPLQA ANTPNLDNLA KESDLGQTIP VLPGITPGSG PGHLSLFGYD PIKYQIGRGI LEALGIGVEV GEKDVVARAN FATWDGKVVL DRRAGRPATE ESAKVVQLLS EKIKKIEDVE ITFYPGKEHR FVVKFTGEGL GDKVTDADPQ KEGHPMVWAE GLDEPSKKTA RIVNELIKKI AEVLKDNPKI NFALIRGFSK YPDLPKFPQV YKMKAGAIAT YPMYRGLAKL VGMEIIETGQ TVADEIKTLK EKWNDYDFFY VHVKKTDSYG EDGKFEEKVK VIEEVDAIIP EIVSLNPDVL VITGDHSTPV PLKAHSWHPV PLLIWSKYTR RGLSQAFNEF ECARGTLGTI HASDVMTLAL AYAGKLEKFG A // ID APT_THEMA Reviewed; 173 AA. AC Q9X1A4; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=TM_1384; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36454.1; -; Genomic_DNA. DR PIR; A72262; A72262. DR RefSeq; NP_229185.1; NC_000853.1. DR RefSeq; WP_010865328.1; NC_000853.1. DR ProteinModelPortal; Q9X1A4; -. DR STRING; 243274.TM1384; -. DR EnsemblBacteria; AAD36454; AAD36454; TM_1384. DR GeneID; 898094; -. DR KEGG; tma:TM1384; -. DR PATRIC; 23937710; VBITheMar51294_1396. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR InParanoid; Q9X1A4; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; TMAR243274:GC6P-1419-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 173 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149478. SQ SEQUENCE 173 AA; 19766 MW; 1C065FFFD0BB1DC8 CRC64; MFKLDLKRFI RDIPDFPQKG IVFRDITPLL RNQEAFKEAI DRMCELVFDR EFDLVVAPEA RGFILGAAMA YKLGKGFVPV RKPGKLPYKT VYEEYQLEYG TEQLHIHEDA IEKGQKVLIV DDVLATGGTA EALIRLVKKL GGEVVSLAFL VELSYLEPRK RLEGYDVKTL IVY // ID ARAA_THEMA Reviewed; 496 AA. AC Q9WYB3; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=L-arabinose isomerase {ECO:0000255|HAMAP-Rule:MF_00519}; DE EC=5.3.1.4 {ECO:0000255|HAMAP-Rule:MF_00519}; GN Name=araA {ECO:0000255|HAMAP-Rule:MF_00519}; GN OrderedLocusNames=TM_0276; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose. CC {ECO:0000255|HAMAP-Rule:MF_00519}. CC -!- CATALYTIC ACTIVITY: L-arabinose = L-ribulose. {ECO:0000255|HAMAP- CC Rule:MF_00519}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00519}; CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00519}; CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L- CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial CC route): step 1/3. {ECO:0000255|HAMAP-Rule:MF_00519}. CC -!- SIMILARITY: Belongs to the arabinose isomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00519}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35365.1; -; Genomic_DNA. DR PIR; B72398; B72398. DR RefSeq; NP_228089.1; NC_000853.1. DR RefSeq; WP_004082981.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYB3; -. DR SMR; Q9WYB3; 1-493. DR STRING; 243274.TM0276; -. DR EnsemblBacteria; AAD35365; AAD35365; TM_0276. DR GeneID; 897191; -. DR KEGG; tma:TM0276; -. DR PATRIC; 23935429; VBITheMar51294_0280. DR eggNOG; ENOG4105CAC; Bacteria. DR eggNOG; COG2160; LUCA. DR InParanoid; Q9WYB3; -. DR KO; K01804; -. DR OMA; HMLEICP; -. DR OrthoDB; EOG6SZ1H3; -. DR BRENDA; 5.3.1.4; 6331. DR SABIO-RK; Q9WYB3; -. DR UniPathway; UPA00145; UER00565. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0008733; F:L-arabinose isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00519; Arabinose_Isome; 1. DR InterPro; IPR024664; Ara_Isoase_C. DR InterPro; IPR004216; Fuc/Ara_isomerase_C. DR InterPro; IPR009015; Fucose_isomerase_N/cen. DR InterPro; IPR003762; Lara_isomerase. DR Pfam; PF11762; Arabinose_Iso_C; 1. DR Pfam; PF02610; Arabinose_Isome; 1. DR PIRSF; PIRSF001478; L-ara_isomerase; 1. DR ProDom; PD018364; Lara_isomerase; 1. DR SUPFAM; SSF50443; SSF50443; 1. DR SUPFAM; SSF53743; SSF53743; 1. PE 3: Inferred from homology; KW Arabinose catabolism; Carbohydrate metabolism; Complete proteome; KW Isomerase; Manganese; Metal-binding; Reference proteome. FT CHAIN 1 496 L-arabinose isomerase. FT /FTId=PRO_0000198394. FT METAL 302 302 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_00519}. FT METAL 329 329 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_00519}. FT METAL 346 346 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_00519}. FT METAL 445 445 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_00519}. SQ SEQUENCE 496 AA; 56658 MW; D6AA88752A183DE0 CRC64; MIDLKQYEFW FLVGSQYLYG LETLKKVEQQ ASKIVDSLND DPIFPSKIVL KPVLKSSSEI TEIFEKANAD PKCAGVIVWM HTFSPSKMWI RGLSINKKPL LHLHTQYNRE IPWDTIDMDY MNLNQSAHGD REHGFIHARM RLPRKVVVGH WEEKEVREKI AKWMRVACAI QDGRMGQIVR FGDNMREVAS TEGDKVEAQI KLGWSINTWG VGELAERVKA VPEREVEELL KEYREKYIMP EDEYSLKAIR EQAKIEIALR EFLKEKNAVG FTTTFEDLHD LPQLPGLAVQ RLMEEGYGFG AEGDWKAAGL VRAIKVMGTS LPGGTSFMED YTYHLTPGNE LVLGAHMLEV CPTIAKEKPR IEVHPLSIGG KADPARLVFD GQEGPAVNAS IVDMGNRFRL VVNKVLSVPI ERKMPKLPTA RVLWKPLPDF KRATTAWILA GGSHHTAFST AIDVEYLIDW AEALEIEYVV IDENLDLEDF KKELRWNELY WGLLKR // ID AROA_THEMA Reviewed; 410 AA. AC Q9WYI0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210}; DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210}; DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210}; DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210}; GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210}; GN OrderedLocusNames=TM_0345; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of CC phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3- CC phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and CC inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. CC {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35431.1; -; Genomic_DNA. DR PIR; G72388; G72388. DR RefSeq; NP_228156.2; NC_000853.1. DR ProteinModelPortal; Q9WYI0; -. DR STRING; 243274.TM0345; -. DR DNASU; 897301; -. DR EnsemblBacteria; AAD35431; AAD35431; TM_0345. DR GeneID; 897301; -. DR KEGG; tma:TM0345; -. DR PATRIC; 23935571; VBITheMar51294_0350. DR eggNOG; ENOG4105CMY; Bacteria. DR eggNOG; COG0128; LUCA. DR InParanoid; Q9WYI0; -. DR KO; K00800; -. DR OMA; GDDCLST; -. DR OrthoDB; EOG6Z6FZ4; -. DR UniPathway; UPA00053; UER00089. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central. DR Gene3D; 3.65.10.10; -; 2. DR HAMAP; MF_00210; EPSP_synth; 1. DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom. DR InterPro; IPR006264; EPSP_synthase. DR InterPro; IPR023193; EPSP_synthase_CS. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR Pfam; PF00275; EPSP_synthase; 1. DR PIRSF; PIRSF000505; EPSPS; 1. DR SUPFAM; SSF55205; SSF55205; 1. DR TIGRFAMs; TIGR01356; aroA; 1. DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1. DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 410 3-phosphoshikimate 1- FT carboxyvinyltransferase. FT /FTId=PRO_0000088312. FT REGION 8 9 Shikimate-3-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT REGION 75 78 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT ACT_SITE 296 296 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT ACT_SITE 324 324 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 13 13 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 105 105 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 323 323 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 327 327 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 369 369 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. SQ SEQUENCE 410 AA; 45342 MW; DC9F7D44792CA69F CRC64; MLSVPPDKSI THRALILSAL AETESTLYNL LRCLDTERTH DILEKLGTRF EGDWEKMKVF PKPFAEPIEP LFCGNSGTTT RLMSGVLASY EMFTVLYGDP SLSRRPMRRV IEPLEMMGAR FMARQNNYLP MAIKGNHLSG ISYKTPVASA QVKSAVLLAG LRASGRTIVI EPAKSRDHTE RMLKNLGVPV EVEGTRVVLE PATFRGFTMK VPGDISSAAF FVVLGAIHPN ARITVTDVGL NPTRTGLLEV MKLMGANLEW EITEENLEPI GTVRVETSPN LKGVVVPEHL VPLMIDELPL VALLGVFAEG ETVVRNAEEL RKKESDRIRV LVENFKRLGV EIEEFKDGFK IVGKQSIKGG SVDPEGDHRM AMLFSIAGLV SEEGVDVKDH ECVAVSFPNF YELLERVVIS // ID ARGC_THEMA Reviewed; 339 AA. AC Q9X2A2; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 125. DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase; DE Short=AGPR; DE EC=1.2.1.38; DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase; DE Short=NAGSA dehydrogenase; GN Name=argC; OrderedLocusNames=TM_1782; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) CC + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 3/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1 CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36845.1; -; Genomic_DNA. DR PIR; A72211; A72211. DR RefSeq; NP_229579.1; NC_000853.1. DR RefSeq; WP_004082328.1; NZ_CP011107.1. DR PDB; 1VKN; X-ray; 1.80 A; A/B/C/D=1-339. DR PDBsum; 1VKN; -. DR ProteinModelPortal; Q9X2A2; -. DR SMR; Q9X2A2; 1-339. DR STRING; 243274.TM1782; -. DR EnsemblBacteria; AAD36845; AAD36845; TM_1782. DR GeneID; 897760; -. DR KEGG; tma:TM1782; -. DR PATRIC; 23938549; VBITheMar51294_1802. DR eggNOG; ENOG4105C0N; Bacteria. DR eggNOG; COG0002; LUCA. DR InParanoid; Q9X2A2; -. DR KO; K00145; -. DR OMA; TFVPHLT; -. DR OrthoDB; EOG6XSZS3; -. DR UniPathway; UPA00068; UER00108. DR EvolutionaryTrace; Q9X2A2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00150; ArgC_type1; 1. DR InterPro; IPR023013; AGPR_AS. DR InterPro; IPR000706; AGPR_type-1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01850; argC; 1. DR PROSITE; PS01224; ARGC; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 339 N-acetyl-gamma-glutamyl-phosphate FT reductase. FT /FTId=PRO_0000112466. FT ACT_SITE 145 145 {ECO:0000250}. FT STRAND 2 8 {ECO:0000244|PDB:1VKN}. FT HELIX 12 23 {ECO:0000244|PDB:1VKN}. FT STRAND 27 33 {ECO:0000244|PDB:1VKN}. FT TURN 36 39 {ECO:0000244|PDB:1VKN}. FT HELIX 42 45 {ECO:0000244|PDB:1VKN}. FT HELIX 47 49 {ECO:0000244|PDB:1VKN}. FT HELIX 60 66 {ECO:0000244|PDB:1VKN}. FT STRAND 68 72 {ECO:0000244|PDB:1VKN}. FT HELIX 78 83 {ECO:0000244|PDB:1VKN}. FT STRAND 90 96 {ECO:0000244|PDB:1VKN}. FT TURN 97 99 {ECO:0000244|PDB:1VKN}. FT HELIX 103 110 {ECO:0000244|PDB:1VKN}. FT HELIX 117 119 {ECO:0000244|PDB:1VKN}. FT STRAND 122 124 {ECO:0000244|PDB:1VKN}. FT HELIX 127 134 {ECO:0000244|PDB:1VKN}. FT STRAND 138 141 {ECO:0000244|PDB:1VKN}. FT HELIX 145 159 {ECO:0000244|PDB:1VKN}. FT STRAND 166 175 {ECO:0000244|PDB:1VKN}. FT HELIX 176 179 {ECO:0000244|PDB:1VKN}. FT HELIX 185 187 {ECO:0000244|PDB:1VKN}. FT HELIX 189 192 {ECO:0000244|PDB:1VKN}. FT HELIX 206 218 {ECO:0000244|PDB:1VKN}. FT STRAND 223 235 {ECO:0000244|PDB:1VKN}. FT STRAND 237 244 {ECO:0000244|PDB:1VKN}. FT HELIX 249 260 {ECO:0000244|PDB:1VKN}. FT STRAND 266 268 {ECO:0000244|PDB:1VKN}. FT HELIX 277 280 {ECO:0000244|PDB:1VKN}. FT STRAND 286 293 {ECO:0000244|PDB:1VKN}. FT TURN 294 297 {ECO:0000244|PDB:1VKN}. FT STRAND 298 305 {ECO:0000244|PDB:1VKN}. FT TURN 307 312 {ECO:0000244|PDB:1VKN}. FT HELIX 313 323 {ECO:0000244|PDB:1VKN}. FT TURN 328 331 {ECO:0000244|PDB:1VKN}. SQ SEQUENCE 339 AA; 37936 MW; E3152D5D4E4EA116 CRC64; MIRAGIIGAT GYTGLELVRL LKNHPEAKIT YLSSRTYAGK KLEEIFPSTL ENSILSEFDP EKVSKNCDVL FTALPAGASY DLVRELKGVK IIDLGADFRF DDPGVYREWY GKELSGYENI KRVYGLPELH REEIKNAQVV GNPGCYPTSV ILALAPALKH NLVDPETILV DAKSGVSGAG RKEKVDYLFS EVNESLRPYN VAKHRHVPEM EQELGKISGK KVNVVFTPHL VPMTRGILST IYVKTDKSLE EIHEAYLEFY KNEPFVHVLP MGIYPSTKWC YGSNHVFIGM QMEERTNTLI LMSAIDNLVK GASGQAVQNM NIMFGLDETK GLEFTPIYP // ID ARGR_THEMA Reviewed; 152 AA. AC Q9WW19; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=Arginine repressor; GN Name=argR; OrderedLocusNames=TM_0371; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10732680; DOI=10.1007/s004380050038; RA Dimova D., Weigel P., Takahashi M., Marc F., Van Duyne G.D., RA Sakanyan V.; RT "Thermostability, oligomerization and DNA-binding properties of the RT regulatory protein ArgR from the hyperthermophilic bacterium RT Thermotoga neapolitana."; RL Mol. Gen. Genet. 263:119-130(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Regulates arginine biosynthesis genes. {ECO:0000250}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis CC [regulation]. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ132286; CAB45262.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35458.1; -; Genomic_DNA. DR PIR; A72385; A72385. DR RefSeq; NP_228182.1; NC_000853.1. DR RefSeq; WP_004083185.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WW19; -. DR STRING; 243274.TM0371; -. DR EnsemblBacteria; AAD35458; AAD35458; TM_0371. DR GeneID; 897330; -. DR KEGG; tma:TM0371; -. DR PATRIC; 23935623; VBITheMar51294_0376. DR eggNOG; ENOG4105XBY; Bacteria. DR eggNOG; COG1438; LUCA. DR InParanoid; Q9WW19; -. DR KO; K03402; -. DR OMA; DILNRQP; -. DR OrthoDB; EOG6Z9B6J; -. DR UniPathway; UPA00068; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0034618; F:arginine binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0051259; P:protein oligomerization; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.1360.40; -; 1. DR HAMAP; MF_00173; Arg_repressor; 1. DR InterPro; IPR001669; Arg_repress. DR InterPro; IPR020899; Arg_repress_C. DR InterPro; IPR024946; Arg_repress_C-like. DR InterPro; IPR020900; Arg_repress_DNA-bd. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01316; Arg_repressor; 1. DR Pfam; PF02863; Arg_repressor_C; 1. DR PRINTS; PR01467; ARGREPRESSOR. DR ProDom; PD007402; Arg_repress; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF55252; SSF55252; 1. DR TIGRFAMs; TIGR01529; argR_whole; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; KW Cytoplasm; DNA-binding; Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 152 Arginine repressor. FT /FTId=PRO_0000205136. SQ SEQUENCE 152 AA; 17222 MW; BCD5384934D490E9 CRC64; MKISKKRRQE LIRKIIHEKK ISNQFQIVEE LKKYGIKAVQ PTVARDLKEI GAVKIMDESG NYVYKLLDET PVIDPWKELK RNFKSFVESI DRAGNLIVIK TIPGTASGIA RVIDRLDIDE IVGTLAGDDT IFVAVRDPES CEKIVEKLSS IL // ID AROC_THEMA Reviewed; 376 AA. AC Q9WYI2; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 104. DE RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300}; DE Short=CS {ECO:0000255|HAMAP-Rule:MF_00300}; DE EC=4.2.3.5 {ECO:0000255|HAMAP-Rule:MF_00300}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000255|HAMAP-Rule:MF_00300}; GN Name=aroC {ECO:0000255|HAMAP-Rule:MF_00300}; GN OrderedLocusNames=TM_0347; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate CC and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate CC (EPSP) to yield chorismate, which is the branch point compound CC that serves as the starting substrate for the three terminal CC pathways of aromatic amino acid biosynthesis. This reaction CC introduces a second double bond into the aromatic ring system. CC {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- CATALYTIC ACTIVITY: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = CC chorismate + phosphate. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- COFACTOR: CC Name=FMNH2; Xref=ChEBI:CHEBI:57618; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300}; CC Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 7/7. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- SIMILARITY: Belongs to the chorismate synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00300}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35433.1; -; Genomic_DNA. DR PIR; A72389; A72389. DR RefSeq; NP_228158.1; NC_000853.1. DR RefSeq; WP_004083133.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYI2; -. DR STRING; 243274.TM0347; -. DR EnsemblBacteria; AAD35433; AAD35433; TM_0347. DR GeneID; 897303; -. DR KEGG; tma:TM0347; -. DR PATRIC; 23935575; VBITheMar51294_0352. DR eggNOG; ENOG4105D10; Bacteria. DR eggNOG; COG0082; LUCA. DR InParanoid; Q9WYI2; -. DR KO; K01736; -. DR OMA; MLSINAV; -. DR OrthoDB; EOG6WDSHT; -. DR UniPathway; UPA00053; UER00090. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.60.150.10; -; 1. DR HAMAP; MF_00300; Chorismate_synth; 1. DR InterPro; IPR000453; Chorismate_synth. DR InterPro; IPR020541; Chorismate_synthase_CS. DR PANTHER; PTHR21085; PTHR21085; 1. DR Pfam; PF01264; Chorismate_synt; 1. DR PIRSF; PIRSF001456; Chorismate_synth; 1. DR SUPFAM; SSF103263; SSF103263; 1. DR TIGRFAMs; TIGR00033; aroC; 1. DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1. DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1. DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; FAD; Flavoprotein; FMN; Lyase; NADP; KW Reference proteome. FT CHAIN 1 376 Chorismate synthase. FT /FTId=PRO_0000140668. FT NP_BIND 115 117 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT NP_BIND 291 295 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 39 39 NADP. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 45 45 NADP. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 276 276 FMN; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 317 317 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. SQ SEQUENCE 376 AA; 41750 MW; 2353443592578C02 CRC64; MKLTIAGDSH GKYMVAILEG LPSGIRVDEE LIRRDLFRRR NCYGRGKRMK MEEDAFEIVS GLWKGITTGA PVTILIPNRA GNPVKDVRSV PRPGHIDYAA WVKYKLPDLN IYVERSSARW TVALTAAGSL LKSLLKEFGI EVLGFVTRLG NVEARDIPGD FEELKRRRDE SVVFCPDPEA TKEMVAEIDR AKEEGNTLGG KVKVIARGVP AGIGSYSDLF KKLDSKIGSL FFAIPAVKGV VIGSEEMWYG FDYLDEFELE DGKIKRKTNN LGGIEGGITN GEDVWVNVSV KPIPTTGKPL KSVDLRTMEP AKTPYVRSDV TAVPPASVVC EAALAVVISD ALLEHLGDGN IDDLKRRFEN ENLPRWNDGF WKEHYR // ID ARCH_THEMA Reviewed; 124 AA. AC Q9X0H1; DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=Protein archease; GN OrderedLocusNames=TM_1083; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PRELIMINARY FUNCTION. RX PubMed=15162483; DOI=10.1002/prot.20141; RA Canaves J.M.; RT "Predicted role for the archease protein family based on structural RT and sequence analysis of TM1083 and MTH1598, two proteins structurally RT characterized through structural genomics efforts."; RL Proteins 56:19-27(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CALCIUM. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of archease, possible chaperone (TM1083) from RT Thermotoga maritima at 2.0 A resolution."; RL Submitted (JUL-2002) to the PDB data bank. CC -!- FUNCTION: Activates the tRNA-splicing ligase complex by CC facilitating the enzymatic turnover of catalytic subunit RtcB. CC Acts by promoting the guanylylation of RtcB, a key intermediate CC step in tRNA ligation. Can also alter the NTP specificity of RtcB CC such that ATP, dGTP or ITP is used efficiently (By similarity). CC May also act as a chaperone or modulator of proteins involved in CC DNA or RNA processing. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the archease family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36160.1; -; Genomic_DNA. DR PIR; C72297; C72297. DR RefSeq; NP_228889.1; NC_000853.1. DR RefSeq; WP_004080400.1; NZ_CP011107.1. DR PDB; 1J5U; X-ray; 2.00 A; A=1-124. DR PDBsum; 1J5U; -. DR ProteinModelPortal; Q9X0H1; -. DR SMR; Q9X0H1; 1-124. DR STRING; 243274.TM1083; -. DR EnsemblBacteria; AAD36160; AAD36160; TM_1083. DR GeneID; 897569; -. DR KEGG; tma:TM1083; -. DR PATRIC; 23937095; VBITheMar51294_1096. DR eggNOG; ENOG4106FU4; Bacteria. DR eggNOG; COG1371; LUCA. DR InParanoid; Q9X0H1; -. DR OMA; WILEISK; -. DR OrthoDB; EOG6R5C88; -. DR EvolutionaryTrace; Q9X0H1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.55.10.10; -; 1. DR InterPro; IPR002804; Archease. DR InterPro; IPR023572; Archease_dom. DR PANTHER; PTHR12682; PTHR12682; 1. DR Pfam; PF01951; Archease; 1. DR ProDom; PD012969; PD012969; 1. DR SUPFAM; SSF69819; SSF69819; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Complete proteome; Metal-binding; KW Reference proteome; tRNA processing. FT CHAIN 1 124 Protein archease. FT /FTId=PRO_0000407063. FT METAL 7 7 Calcium; via carbonyl oxygen. FT {ECO:0000269|Ref.3}. FT METAL 10 10 Calcium. {ECO:0000269|Ref.3}. FT METAL 123 123 Calcium. {ECO:0000269|Ref.3}. FT METAL 124 124 Calcium. {ECO:0000269|Ref.3}. FT STRAND 11 19 {ECO:0000244|PDB:1J5U}. FT HELIX 20 35 {ECO:0000244|PDB:1J5U}. FT STRAND 38 49 {ECO:0000244|PDB:1J5U}. FT HELIX 54 69 {ECO:0000244|PDB:1J5U}. FT STRAND 72 80 {ECO:0000244|PDB:1J5U}. FT STRAND 83 93 {ECO:0000244|PDB:1J5U}. FT STRAND 110 112 {ECO:0000244|PDB:1J5U}. FT STRAND 115 123 {ECO:0000244|PDB:1J5U}. SQ SEQUENCE 124 AA; 14666 MW; 637DF1E707B61AC1 CRC64; MRKPIEHTAD IAYEISGNSY EELLEEARNI LLEEEGIVLD TEEKEKMYPL EETEDAFFDT VNDWILEISK GWAPWRIKRE GNELKVTFRK IRKKEGTEIK ALTYHLLKFE RDGDVLKTKV VFDT // ID AROF_THEMA Reviewed; 338 AA. AC Q9WYH8; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase; DE EC=2.5.1.54; DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase; DE AltName: Full=DAHP synthase; DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase; GN Name=aroF; OrderedLocusNames=TM_0343; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP CHARACTERIZATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=12743122; DOI=10.1074/jbc.M304631200; RA Wu J., Howe D.L., Woodard R.W.; RT "Thermotoga maritima 3-deoxy-D-arabino-heptulosonate 7-phosphate RT (DAHP) synthase: the ancestral eubacterial DAHP synthase?"; RL J. Biol. Chem. 278:27525-27531(2003). CC -!- FUNCTION: Catalyzes the condensation of phosphoenolpyruvate (PEP) CC and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D- CC arabino-heptulosonate-7-phosphate (DAHP). CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + D-erythrose 4-phosphate CC + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + CC phosphate. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Note=Divalent metal ions.; CC -!- ENZYME REGULATION: Inhibited by L-phenylalanine and L-tyrosine. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6.3 at 60 degrees Celsius.; CC Temperature dependence: CC Optimum temperature is 90 degrees Celsius. Extremely CC thermostable.; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 1/7. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35429.1; -; Genomic_DNA. DR PIR; E72388; E72388. DR RefSeq; NP_228154.1; NC_000853.1. DR RefSeq; WP_004083125.1; NZ_CP011107.1. DR PDB; 1RZM; X-ray; 2.20 A; A/B=1-338. DR PDB; 1VR6; X-ray; 1.92 A; A/B/C/D=1-338. DR PDB; 3PG8; X-ray; 2.00 A; A/B=71-338. DR PDB; 3PG9; X-ray; 2.35 A; A/B/C/D/E/F/G/H=1-338. DR PDB; 4GRS; X-ray; 3.00 A; A/B/C/D=1-103. DR PDBsum; 1RZM; -. DR PDBsum; 1VR6; -. DR PDBsum; 3PG8; -. DR PDBsum; 3PG9; -. DR PDBsum; 4GRS; -. DR ProteinModelPortal; Q9WYH8; -. DR SMR; Q9WYH8; 1-338. DR STRING; 243274.TM0343; -. DR EnsemblBacteria; AAD35429; AAD35429; TM_0343. DR GeneID; 897299; -. DR KEGG; tma:TM0343; -. DR PATRIC; 23935567; VBITheMar51294_0348. DR eggNOG; ENOG4108JPM; Bacteria. DR eggNOG; COG2876; LUCA. DR InParanoid; Q9WYH8; -. DR KO; K03856; -. DR OMA; GVIVEIH; -. DR OrthoDB; EOG657JFQ; -. DR UniPathway; UPA00053; UER00084. DR EvolutionaryTrace; Q9WYH8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006218; DAHP1/KDSA. DR InterPro; IPR006268; DAHP_syn_2. DR Pfam; PF00793; DAHP_synth_1; 1. DR TIGRFAMs; TIGR01361; DAHP_synth_Bsub; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Complete proteome; KW Reference proteome; Transferase. FT CHAIN 1 338 Phospho-2-dehydro-3-deoxyheptonate FT aldolase. FT /FTId=PRO_0000140847. FT STRAND 1 5 {ECO:0000244|PDB:1VR6}. FT HELIX 11 23 {ECO:0000244|PDB:1VR6}. FT STRAND 26 32 {ECO:0000244|PDB:1VR6}. FT STRAND 37 47 {ECO:0000244|PDB:1VR6}. FT HELIX 50 54 {ECO:0000244|PDB:1VR6}. FT STRAND 59 64 {ECO:0000244|PDB:1VR6}. FT TURN 74 76 {ECO:0000244|PDB:1VR6}. FT STRAND 82 84 {ECO:0000244|PDB:3PG8}. FT STRAND 89 91 {ECO:0000244|PDB:1VR6}. FT STRAND 94 100 {ECO:0000244|PDB:1VR6}. FT HELIX 107 119 {ECO:0000244|PDB:1VR6}. FT STRAND 124 126 {ECO:0000244|PDB:1VR6}. FT STRAND 128 130 {ECO:0000244|PDB:1RZM}. FT HELIX 144 157 {ECO:0000244|PDB:1VR6}. FT STRAND 160 164 {ECO:0000244|PDB:1VR6}. FT HELIX 168 170 {ECO:0000244|PDB:1VR6}. FT HELIX 171 177 {ECO:0000244|PDB:1VR6}. FT STRAND 179 183 {ECO:0000244|PDB:1VR6}. FT HELIX 185 187 {ECO:0000244|PDB:1VR6}. FT HELIX 191 198 {ECO:0000244|PDB:1VR6}. FT STRAND 204 207 {ECO:0000244|PDB:1VR6}. FT HELIX 214 226 {ECO:0000244|PDB:1VR6}. FT STRAND 232 236 {ECO:0000244|PDB:1VR6}. FT STRAND 245 249 {ECO:0000244|PDB:1VR6}. FT HELIX 254 261 {ECO:0000244|PDB:1VR6}. FT STRAND 262 264 {ECO:0000244|PDB:1VR6}. FT STRAND 266 268 {ECO:0000244|PDB:1VR6}. FT HELIX 270 274 {ECO:0000244|PDB:1VR6}. FT HELIX 277 279 {ECO:0000244|PDB:1VR6}. FT HELIX 280 290 {ECO:0000244|PDB:1VR6}. FT STRAND 293 299 {ECO:0000244|PDB:1VR6}. FT HELIX 303 305 {ECO:0000244|PDB:1VR6}. FT HELIX 310 312 {ECO:0000244|PDB:1VR6}. FT HELIX 316 333 {ECO:0000244|PDB:1VR6}. FT STRAND 336 338 {ECO:0000244|PDB:1VR6}. SQ SEQUENCE 338 AA; 37378 MW; E9634B6704D3DF4D CRC64; MIVVLKPGST EEDIRKVVKL AESYNLKCHI SKGQERTVIG IIGDDRYVVA DKFESLDCVE SVVRVLKPYK LVSREFHPED TVIDLGDVKI GNGYFTIIAG PCSVEGREML METAHFLSEL GVKVLRGGAY KPRTSPYSFQ GLGEKGLEYL REAADKYGMY VVTEALGEDD LPKVAEYADI IQIGARNAQN FRLLSKAGSY NKPVLLKRGF MNTIEEFLLS AEYIANSGNT KIILCERGIR TFEKATRNTL DISAVPIIRK ESHLPILVDP SHSGGRRDLV IPLSRAAIAV GAHGIIVEVH PEPEKALSDG KQSLDFELFK ELVQEMKKLA DALGVKVN // ID ASSY_THEMA Reviewed; 409 AA. AC Q9X2A1; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00005}; DE EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00005}; DE AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00005}; GN Name=argG {ECO:0000255|HAMAP-Rule:MF_00005}; GN OrderedLocusNames=TM_1780; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND SUBUNIT. RG Joint center for structural genomics (JCSG); RT "Crystal structure of argininosuccinate synthase (TM1780) from RT Thermotoga maritima at 1.65 A resolution."; RL Submitted (MAR-2006) to the PDB data bank. CC -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP + CC diphosphate + N(omega)-(L-arginino)succinate. {ECO:0000255|HAMAP- CC Rule:MF_00005}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 2/3. CC {ECO:0000255|HAMAP-Rule:MF_00005}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00005, CC ECO:0000269|Ref.2}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type CC 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00005}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36844.1; -; Genomic_DNA. DR PIR; H72210; H72210. DR RefSeq; NP_229577.1; NC_000853.1. DR RefSeq; WP_004082326.1; NZ_CP011107.1. DR PDB; 1VL2; X-ray; 1.65 A; A/B/C/D=1-409. DR PDBsum; 1VL2; -. DR ProteinModelPortal; Q9X2A1; -. DR SMR; Q9X2A1; 2-409. DR STRING; 243274.TM1780; -. DR EnsemblBacteria; AAD36844; AAD36844; TM_1780. DR GeneID; 897844; -. DR KEGG; tma:TM1780; -. DR PATRIC; 23938542; VBITheMar51294_1799. DR eggNOG; ENOG4105CDH; Bacteria. DR eggNOG; COG0137; LUCA. DR InParanoid; Q9X2A1; -. DR KO; K01940; -. DR OMA; PAREWGM; -. DR OrthoDB; EOG6K9QCV; -. DR UniPathway; UPA00068; UER00113. DR EvolutionaryTrace; Q9X2A1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004055; F:argininosuccinate synthase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0000053; P:argininosuccinate metabolic process; IBA:GO_Central. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.90.1260.10; -; 1. DR HAMAP; MF_00005; Arg_succ_synth_type1; 1. DR InterPro; IPR001518; Arginosuc_synth. DR InterPro; IPR018223; Arginosuc_synth_CS. DR InterPro; IPR023434; Arginosuc_synth_type_1_subfam. DR InterPro; IPR024074; AS_cat/multimer_dom_body. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00764; Arginosuc_synth; 1. DR TIGRFAMs; TIGR00032; argG; 1. DR PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1. DR PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 409 Argininosuccinate synthase. FT /FTId=PRO_0000148656. FT NP_BIND 8 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00005}. FT BINDING 34 34 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 85 85 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 115 115 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00005}. FT BINDING 117 117 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 121 121 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 121 121 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 122 122 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 125 125 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 178 178 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 187 187 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 268 268 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 280 280 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT STRAND 4 8 {ECO:0000244|PDB:1VL2}. FT HELIX 13 24 {ECO:0000244|PDB:1VL2}. FT STRAND 28 37 {ECO:0000244|PDB:1VL2}. FT HELIX 42 52 {ECO:0000244|PDB:1VL2}. FT STRAND 55 61 {ECO:0000244|PDB:1VL2}. FT HELIX 63 69 {ECO:0000244|PDB:1VL2}. FT HELIX 71 75 {ECO:0000244|PDB:1VL2}. FT TURN 76 78 {ECO:0000244|PDB:1VL2}. FT TURN 82 84 {ECO:0000244|PDB:1VL2}. FT HELIX 88 107 {ECO:0000244|PDB:1VL2}. FT STRAND 110 113 {ECO:0000244|PDB:1VL2}. FT HELIX 122 133 {ECO:0000244|PDB:1VL2}. FT STRAND 137 140 {ECO:0000244|PDB:1VL2}. FT HELIX 142 144 {ECO:0000244|PDB:1VL2}. FT HELIX 146 151 {ECO:0000244|PDB:1VL2}. FT HELIX 157 165 {ECO:0000244|PDB:1VL2}. FT STRAND 176 181 {ECO:0000244|PDB:1VL2}. FT STRAND 186 190 {ECO:0000244|PDB:1VL2}. FT HELIX 191 194 {ECO:0000244|PDB:1VL2}. FT HELIX 202 204 {ECO:0000244|PDB:1VL2}. FT TURN 211 213 {ECO:0000244|PDB:1VL2}. FT STRAND 219 226 {ECO:0000244|PDB:1VL2}. FT STRAND 229 235 {ECO:0000244|PDB:1VL2}. FT TURN 236 238 {ECO:0000244|PDB:1VL2}. FT HELIX 245 258 {ECO:0000244|PDB:1VL2}. FT STRAND 263 269 {ECO:0000244|PDB:1VL2}. FT STRAND 271 281 {ECO:0000244|PDB:1VL2}. FT HELIX 283 299 {ECO:0000244|PDB:1VL2}. FT HELIX 302 321 {ECO:0000244|PDB:1VL2}. FT HELIX 327 340 {ECO:0000244|PDB:1VL2}. FT STRAND 345 352 {ECO:0000244|PDB:1VL2}. FT STRAND 355 362 {ECO:0000244|PDB:1VL2}. FT STRAND 364 366 {ECO:0000244|PDB:1VL2}. FT HELIX 383 404 {ECO:0000244|PDB:1VL2}. SQ SEQUENCE 409 AA; 46054 MW; ECCDC8575E962482 CRC64; MKEKVVLAYS GGLDTSVILK WLCEKGFDVI AYVANVGQKD DFVAIKEKAL KTGASKVYVE DLRREFVTDY IFTALLGNAM YEGRYLLGTA IARPLIAKRQ VEIAEKEGAQ YVAHGATGKG NDQVRFELTY AALNPNLKVI SPWKDPEFLA KFKGRTDLIN YAMEKGIPIK VSKKRPYSED ENLMHISHEA GKLEDPAHIP DEDVFTWTVS PKDAPDEETL LEIHFENGIP VKVVNLKDGT EKTDPLELFE YLNEVGAKNG VGRLDMVENR FIGIKSRGVY ETPGATILWI AHRDLEGITM DKEVMHLRDM LAPKFAELIY NGFWFSPEME FLLAAFRKAQ ENVTGKVTVS IYKGNVMPVA RYSPYSLYNP ELSSMDVEGG FDATDSKGFI NIHALRLKVH QLVKKGYQR // ID AROE_THEMA Reviewed; 253 AA. AC Q9WYI1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00222}; DE Short=SDH {ECO:0000255|HAMAP-Rule:MF_00222}; DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_00222}; GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222}; GN OrderedLocusNames=TM_0346; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in the biosynthesis of the chorismate, which CC leads to the biosynthesis of aromatic amino acids. Catalyzes the CC reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to CC yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate + CC NADPH. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_00222}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35432.1; -; Genomic_DNA. DR PIR; H72388; H72388. DR RefSeq; NP_228157.1; NC_000853.1. DR RefSeq; WP_004083132.1; NZ_CP011107.1. DR PDB; 3U62; X-ray; 1.45 A; A=1-253. DR PDBsum; 3U62; -. DR ProteinModelPortal; Q9WYI1; -. DR STRING; 243274.TM0346; -. DR EnsemblBacteria; AAD35432; AAD35432; TM_0346. DR GeneID; 897302; -. DR KEGG; tma:TM0346; -. DR PATRIC; 23935573; VBITheMar51294_0351. DR eggNOG; ENOG4108237; Bacteria. DR eggNOG; COG0169; LUCA. DR InParanoid; Q9WYI1; -. DR KO; K00014; -. DR OMA; KVAIMEH; -. DR OrthoDB; EOG64R67G; -. DR BRENDA; 1.1.1.25; 6331. DR UniPathway; UPA00053; UER00087. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00222; Shikimate_DH_AroE; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR013708; Shikimate_DH-bd_N. DR InterPro; IPR022893; Shikimate_DH_fam. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. DR Pfam; PF01488; Shikimate_DH; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Complete proteome; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 253 Shikimate dehydrogenase (NADP(+)). FT /FTId=PRO_0000136046. FT NP_BIND 115 119 NADP. {ECO:0000255|HAMAP-Rule:MF_00222}. FT NP_BIND 139 144 NADP. {ECO:0000255|HAMAP-Rule:MF_00222}. FT REGION 13 15 Shikimate binding. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT ACT_SITE 63 63 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 59 59 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 74 74 NADP. {ECO:0000255|HAMAP-Rule:MF_00222}. FT BINDING 83 83 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 94 94 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 199 199 NADP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00222}. FT BINDING 201 201 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 221 221 NADP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00222}. FT STRAND 2 9 {ECO:0000244|PDB:3U62}. FT HELIX 15 26 {ECO:0000244|PDB:3U62}. FT STRAND 31 36 {ECO:0000244|PDB:3U62}. FT HELIX 39 41 {ECO:0000244|PDB:3U62}. FT HELIX 42 52 {ECO:0000244|PDB:3U62}. FT STRAND 54 58 {ECO:0000244|PDB:3U62}. FT HELIX 65 69 {ECO:0000244|PDB:3U62}. FT STRAND 70 72 {ECO:0000244|PDB:3U62}. FT HELIX 74 79 {ECO:0000244|PDB:3U62}. FT STRAND 84 86 {ECO:0000244|PDB:3U62}. FT STRAND 89 91 {ECO:0000244|PDB:3U62}. FT HELIX 94 101 {ECO:0000244|PDB:3U62}. FT TURN 102 104 {ECO:0000244|PDB:3U62}. FT STRAND 109 114 {ECO:0000244|PDB:3U62}. FT HELIX 118 129 {ECO:0000244|PDB:3U62}. FT STRAND 135 140 {ECO:0000244|PDB:3U62}. FT HELIX 142 146 {ECO:0000244|PDB:3U62}. FT STRAND 153 156 {ECO:0000244|PDB:3U62}. FT HELIX 157 159 {ECO:0000244|PDB:3U62}. FT HELIX 160 165 {ECO:0000244|PDB:3U62}. FT STRAND 168 172 {ECO:0000244|PDB:3U62}. FT TURN 176 179 {ECO:0000244|PDB:3U62}. FT HELIX 187 190 {ECO:0000244|PDB:3U62}. FT STRAND 194 198 {ECO:0000244|PDB:3U62}. FT STRAND 200 202 {ECO:0000244|PDB:3U62}. FT HELIX 205 213 {ECO:0000244|PDB:3U62}. FT STRAND 216 219 {ECO:0000244|PDB:3U62}. FT HELIX 222 235 {ECO:0000244|PDB:3U62}. FT HELIX 241 248 {ECO:0000244|PDB:3U62}. FT HELIX 249 252 {ECO:0000244|PDB:3U62}. SQ SEQUENCE 253 AA; 28889 MW; 64778D10CB07CE0E CRC64; MKFCIIGYPV RHSISPRLYN EYFKRAGMNH SYGMEEIPPE SFDTEIRRIL EEYDGFNATI PHKERVMRYV EPSEDAQRIK AVNCVFRGKG YNTDWVGVVK SLEGVEVKEP VVVVGAGGAA RAVIYALLQM GVKDIWVVNR TIERAKALDF PVKIFSLDQL DEVVKKAKSL FNTTSVGMKG EELPVSDDSL KNLSLVYDVI YFDTPLVVKA RKLGVKHIIK GNLMFYYQAM ENLKIWGIYD EEVFKEVFGE VLK // ID AROQ_THEMA Reviewed; 144 AA. AC Q9WYI4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=3-dehydroquinate dehydratase; DE Short=3-dehydroquinase; DE EC=4.2.1.10; DE AltName: Full=Type II DHQase; GN Name=aroQ; OrderedLocusNames=TM_0349; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate CC intermediate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 3/7. CC -!- SUBUNIT: Homododecamer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35435.1; -; Genomic_DNA. DR PIR; C72389; C72389. DR RefSeq; NP_228160.1; NC_000853.1. DR RefSeq; WP_004083137.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYI4; -. DR STRING; 243274.TM0349; -. DR EnsemblBacteria; AAD35435; AAD35435; TM_0349. DR GeneID; 897305; -. DR KEGG; tma:TM0349; -. DR PATRIC; 23935579; VBITheMar51294_0354. DR eggNOG; ENOG4108Z38; Bacteria. DR eggNOG; COG0757; LUCA. DR InParanoid; Q9WYI4; -. DR KO; K03786; -. DR OMA; RCAGIVI; -. DR OrthoDB; EOG66MQVT; -. DR UniPathway; UPA00053; UER00086. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.9100; -; 1. DR HAMAP; MF_00169; AroQ; 1. DR InterPro; IPR001874; DHquinase_II. DR InterPro; IPR018509; DHquinase_II_CS. DR PANTHER; PTHR21272; PTHR21272; 1. DR Pfam; PF01220; DHquinase_II; 1. DR PIRSF; PIRSF001399; DHquinase_II; 1. DR ProDom; PD004527; DHquinase_II; 1. DR SUPFAM; SSF52304; SSF52304; 1. DR TIGRFAMs; TIGR01088; aroQ; 1. DR PROSITE; PS01029; DEHYDROQUINASE_II; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Reference proteome. FT CHAIN 1 144 3-dehydroquinate dehydratase. FT /FTId=PRO_0000159934. FT REGION 98 99 Substrate binding. {ECO:0000250}. FT ACT_SITE 22 22 Proton acceptor. {ECO:0000250}. FT ACT_SITE 97 97 Proton donor. {ECO:0000250}. FT BINDING 71 71 Substrate. {ECO:0000250}. FT BINDING 77 77 Substrate. {ECO:0000250}. FT BINDING 84 84 Substrate. {ECO:0000250}. FT BINDING 108 108 Substrate. {ECO:0000250}. FT SITE 17 17 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 144 AA; 16566 MW; 0CD0053918257FB7 CRC64; MKVLVVNGPN LNMLGKRDKN IYGNFSHEDL VKMIEDWGRK NGVEVEVFQS NHEGKILDRL HRLDFDGLVI NPGAFTHYSY AIRDALEIVK VPKVEVHISN IHRREEFRRR SVTAEVCDGQ ISGLGVYGYL LALEYIKKKL EELT // ID ASPD_THEMA Reviewed; 241 AA. AC Q9X1X6; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=L-aspartate dehydrogenase; DE EC=1.4.1.21; GN Name=nadX; OrderedLocusNames=TM_1643; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH NAD. RG Joint center for structural genomics (JCSG); RT "Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga RT maritima at 1.9 A resolution."; RL Submitted (JUL-2002) to the PDB data bank. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-241 IN COMPLEX WITH NAD, RP FUNCTION, CHARACTERIZATION, AND KINETIC PARAMETERS. RX PubMed=12496312; DOI=10.1074/jbc.M211892200; RA Yang Z., Savchenko A., Yakunin A.F., Zhang R., Edwards A.M., RA Arrowsmith C.H., Tong L.; RT "Aspartate dehydrogenase, a novel enzyme identified from structural RT and functional studies of TM1643."; RL J. Biol. Chem. 278:8804-8808(2003). CC -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent CC dehydrogenation of L-aspartate to iminoaspartate. Does not show CC aspartate oxidase activity. Is also able to catalyze the reverse CC reaction, i.e. the reductive amination of oxaloacetate. CC {ECO:0000269|PubMed:12496312}. CC -!- CATALYTIC ACTIVITY: L-aspartate + H(2)O + NAD(P)(+) = oxaloacetate CC + NH(3) + NAD(P)H. CC -!- ENZYME REGULATION: Competitively inhibited by L-malate and CC NH(4)(+). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.067 mM for L-aspartate (in the presence of NAD) CC {ECO:0000269|PubMed:12496312}; CC KM=1.20 mM for L-aspartate (in the presence of NADP) CC {ECO:0000269|PubMed:12496312}; CC KM=0.25 mM for NAD {ECO:0000269|PubMed:12496312}; CC KM=0.72 mM for NADP {ECO:0000269|PubMed:12496312}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; CC iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:12496312}. CC -!- MISCELLANEOUS: The iminoaspartate product is unstable in aqueous CC solution and can decompose to oxaloacetate and ammonia. CC -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36710.1; -; Genomic_DNA. DR PIR; H72226; H72226. DR RefSeq; NP_229443.1; NC_000853.1. DR RefSeq; WP_004082138.1; NZ_CP011107.1. DR PDB; 1H2H; X-ray; 2.60 A; A=1-241. DR PDB; 1J5P; X-ray; 1.90 A; A=1-241. DR PDBsum; 1H2H; -. DR PDBsum; 1J5P; -. DR ProteinModelPortal; Q9X1X6; -. DR SMR; Q9X1X6; 1-241. DR STRING; 243274.TM1643; -. DR EnsemblBacteria; AAD36710; AAD36710; TM_1643. DR GeneID; 897714; -. DR KEGG; tma:TM1643; -. DR PATRIC; 23938260; VBITheMar51294_1662. DR eggNOG; ENOG4108Q27; Bacteria. DR eggNOG; COG1712; LUCA. DR InParanoid; Q9X1X6; -. DR KO; K06989; -. DR OMA; MIMSVGA; -. DR OrthoDB; EOG6ND0JC; -. DR BRENDA; 1.4.1.21; 6331. DR SABIO-RK; Q9X1X6; -. DR UniPathway; UPA00253; UER00456. DR EvolutionaryTrace; Q9X1X6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006742; P:NADP catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01265; NadX; 1. DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd. DR InterPro; IPR002811; Asp_DH. DR InterPro; IPR022487; Asp_DH_arc. DR InterPro; IPR020626; Asp_DH_prok. DR InterPro; IPR011182; L-Asp_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01958; DUF108; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR03855; NAD_NadX; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; NAD; NADP; Oxidoreductase; KW Pyridine nucleotide biosynthesis; Reference proteome. FT CHAIN 1 241 L-aspartate dehydrogenase. FT /FTId=PRO_0000144893. FT ACT_SITE 193 193 {ECO:0000305}. FT BINDING 11 11 NAD; via amide nitrogen. FT {ECO:0000269|PubMed:12496312}. FT BINDING 28 28 NAD. {ECO:0000269|PubMed:12496312}. FT BINDING 57 57 NAD. {ECO:0000269|PubMed:12496312}. FT BINDING 63 63 NAD. {ECO:0000269|PubMed:12496312}. FT BINDING 64 64 NAD. {ECO:0000269|PubMed:12496312}. FT BINDING 78 78 NAD; via carbonyl oxygen. FT {ECO:0000269|PubMed:12496312}. FT BINDING 79 79 NAD. {ECO:0000269|PubMed:12496312}. FT BINDING 109 109 NAD; via amide nitrogen. FT {ECO:0000269|PubMed:12496312}. FT BINDING 164 164 NAD. {ECO:0000269|PubMed:12496312}. FT STRAND 2 6 {ECO:0000244|PDB:1J5P}. FT HELIX 10 18 {ECO:0000244|PDB:1J5P}. FT STRAND 22 27 {ECO:0000244|PDB:1J5P}. FT STRAND 35 39 {ECO:0000244|PDB:1J5P}. FT STRAND 51 54 {ECO:0000244|PDB:1J5P}. FT HELIX 58 68 {ECO:0000244|PDB:1J5P}. FT STRAND 71 77 {ECO:0000244|PDB:1J5P}. FT HELIX 80 84 {ECO:0000244|PDB:1J5P}. FT HELIX 86 97 {ECO:0000244|PDB:1J5P}. FT STRAND 102 104 {ECO:0000244|PDB:1J5P}. FT HELIX 113 119 {ECO:0000244|PDB:1J5P}. FT HELIX 120 122 {ECO:0000244|PDB:1J5P}. FT STRAND 123 132 {ECO:0000244|PDB:1J5P}. FT HELIX 134 137 {ECO:0000244|PDB:1J5P}. FT STRAND 145 150 {ECO:0000244|PDB:1J5P}. FT HELIX 152 158 {ECO:0000244|PDB:1J5P}. FT STRAND 160 162 {ECO:0000244|PDB:1J5P}. FT HELIX 164 173 {ECO:0000244|PDB:1J5P}. FT HELIX 175 177 {ECO:0000244|PDB:1J5P}. FT STRAND 178 184 {ECO:0000244|PDB:1J5P}. FT STRAND 192 201 {ECO:0000244|PDB:1J5P}. FT STRAND 203 208 {ECO:0000244|PDB:1J5P}. FT HELIX 221 235 {ECO:0000244|PDB:1J5P}. SQ SEQUENCE 241 AA; 26640 MW; AF52221512C3DE2E CRC64; MTVLIIGMGN IGKKLVELGN FEKIYAYDRI SKDIPGVVRL DEFQVPSDVS TVVECASPEA VKEYSLQILK NPVNYIIIST SAFADEVFRE RFFSELKNSP ARVFFPSGAI GGLDVLSSIK DFVKNVRIET IKPPKSLGLD LKGKTVVFEG SVEEASKLFP RNINVASTIG LIVGFEKVKV TIVADPAMDH NIHIVRISSA IGNYEFKIEN IPSPENPKTS MLTVYSILRT LRNLESKIIF G // ID ATPB_THEMA Reviewed; 468 AA. AC O50550; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 11-MAY-2016, entry version 130. DE RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347}; DE EC=3.6.3.14 {ECO:0000255|HAMAP-Rule:MF_01347}; DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347}; DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347}; GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; GN OrderedLocusNames=TM_1610; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9588802; DOI=10.1002/elps.1150190416; RA Ludwig W., Strunk O., Klugbauer S., Klugbauer N., Weizenegger M., RA Neumaier J., Bachleitner M., Schleifer K.H.; RT "Bacterial phylogeny based on comparative sequence analysis."; RL Electrophoresis 19:554-568(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The catalytic sites are hosted CC primarily by the beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). {ECO:0000255|HAMAP-Rule:MF_01347}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a(1), b(2) and c(9-12). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. CF(1) is attached to CF(0) by a central stalk formed CC by the gamma and epsilon chains, while a peripheral stalk is CC formed by the delta and b chains. {ECO:0000255|HAMAP- CC Rule:MF_01347}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01347}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000255|HAMAP-Rule:MF_01347}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y15792; CAA75784.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36677.1; -; Genomic_DNA. DR PIR; D72231; D72231. DR RefSeq; NP_229410.1; NC_000853.1. DR RefSeq; WP_004082059.1; NZ_CP011107.1. DR ProteinModelPortal; O50550; -. DR SMR; O50550; 5-466. DR STRING; 243274.TM1610; -. DR PRIDE; O50550; -. DR EnsemblBacteria; AAD36677; AAD36677; TM_1610. DR GeneID; 897936; -. DR KEGG; tma:TM1610; -. DR PATRIC; 23938194; VBITheMar51294_1629. DR eggNOG; ENOG4105C4J; Bacteria. DR eggNOG; COG0055; LUCA. DR InParanoid; O50550; -. DR KO; K02112; -. DR OMA; FKESGVI; -. DR OrthoDB; EOG6HQSP3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1140.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01347; ATP_synth_beta_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR005722; ATPase_F1-cplx_bsu. DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR004100; ATPase_F1_a/bsu_N. DR InterPro; IPR024034; ATPase_F1_bsu/V1_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF47917; SSF47917; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01039; atpD; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Hydrolase; Ion transport; KW Membrane; Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 468 ATP synthase subunit beta. FT /FTId=PRO_0000144484. FT NP_BIND 155 162 ATP. {ECO:0000255|HAMAP-Rule:MF_01347}. SQ SEQUENCE 468 AA; 51241 MW; F9D6E85F86A42F69 CRC64; MAKGSKGFIV SIMGPVVDVK FPEEELPDIY NALEVVNPQT GQKVVLEVEQ LIGDGVVRTV AMDSTDGLTK GLEVVDTGAP ITAPVGKEVL GRILNVIGEP VDEAGEIKAK ERWPIHRPAP ELVEQSTEIE ILETGIKVID LLAPFPKGGK IGFFGGAGVG KTVLVMELIR NIAIEHKGFS VFAGVGERTR EGNELWLEMQ ESGVLGNTVL VFGQMNEPPG ARFRVALTAL TIAEYFRDVE GRDVLLFIDN IFRFVQAGSE VSALLGRMPS AVGYQPTLAT DMGELQERIT STRRGSITSV QAIYVPADDI TDPAPATTFA HLDATVVLSR RIAELGLYPA VDPLDSSSKI LDPAIVGREH YEVARGVQEV LQRYKDLQDI IAILGVEELS PEDKLVVHRA RRIQRFLSQP FHVAERFTGR PGRYVPIEET IRGFKEILDG KLDDVPEQAF LMAGNIDEVK ERAKEMRS // ID AROKB_THEMA Reviewed; 492 AA. AC Q9WYI3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 121. DE RecName: Full=Bifunctional shikimate kinase/3-dehydroquinate synthase; DE Includes: DE RecName: Full=Shikimate kinase; DE Short=SK; DE EC=2.7.1.71; DE Includes: DE RecName: Full=3-dehydroquinate synthase; DE EC=4.2.3.4; GN Name=aroKB; OrderedLocusNames=TM_0348; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl CC group of shikimic acid using ATP as a cosubstrate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate CC = 3-dehydroquinate + phosphate. CC -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 2/7. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 5/7. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the shikimate CC kinase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC dehydroquinate synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35434.1; -; Genomic_DNA. DR PIR; B72389; B72389. DR RefSeq; NP_228159.1; NC_000853.1. DR RefSeq; WP_004083135.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYI3; -. DR STRING; 243274.TM0348; -. DR EnsemblBacteria; AAD35434; AAD35434; TM_0348. DR GeneID; 897304; -. DR KEGG; tma:TM0348; -. DR PATRIC; 23935577; VBITheMar51294_0353. DR eggNOG; ENOG4105D49; Bacteria. DR eggNOG; COG0337; LUCA. DR eggNOG; COG0703; LUCA. DR InParanoid; Q9WYI3; -. DR KO; K13829; -. DR OMA; ERIREIW; -. DR OrthoDB; EOG6SJJGD; -. DR UniPathway; UPA00053; UER00085. DR UniPathway; UPA00053; UER00088. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central. DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00109; Shikimate_kinase; 1. DR InterPro; IPR016037; DHQ_synth_AroB. DR InterPro; IPR030960; DHQS/DOIS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR031322; Shikimate/glucono_kinase. DR InterPro; IPR000623; Shikimate_kinase/TSH1. DR InterPro; IPR023000; Shikimate_kinase_CS. DR Pfam; PF01761; DHQ_synthase; 1. DR Pfam; PF01202; SKI; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01357; aroB; 1. DR PROSITE; PS01128; SHIKIMATE_KINASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Lyase; Magnesium; KW Metal-binding; Multifunctional enzyme; NAD; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 492 Bifunctional shikimate kinase/3- FT dehydroquinate synthase. FT /FTId=PRO_0000192432. FT NP_BIND 10 15 ATP. {ECO:0000250}. FT REGION 1 161 Shikimate kinase. FT REGION 162 492 3-dehydroquinate synthase. FT METAL 14 14 Magnesium. {ECO:0000250}. FT BINDING 32 32 Substrate. {ECO:0000250}. FT BINDING 56 56 Substrate. {ECO:0000250}. FT BINDING 78 78 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 114 114 ATP. {ECO:0000250}. FT BINDING 131 131 Substrate. {ECO:0000250}. SQ SEQUENCE 492 AA; 56385 MW; F04C7058237C1C1A CRC64; MRIFLVGMMG SGKSTIGKRI SEVLDLQFID MDEEIERREG RSVRRIFEED GEEYFRLKEK ELLKELVERD NVVVATGGGV VVDPENRELL KKEKTLFLYA PPEVLMERVT TENRPLLSEG KERIREIWEK RKQFYAEFRR IDTSRLNEWE TTALVVLEAL DEKEISTIEK PHLVKIILGG FKRVRNEELV FTTERVEKIY GRYLPENRLL FPDGEEVKTL EHVSRAYYEL IRMDFPRGKT IAGVGGGALT DFTGFVASTF KRGVGLSFYP TTLLAQVDAS VGGKNAIDFA GVKNVVGTFR MPDYVIIDPT VTLSMDEGRF EEGVVEAFKM TILSGRGVEL FDEPEKIEKR NLRVLSEMVK ISVEEKARIV MEDPYDMGLR HALNLGHTLG HVYEMLEGVP HGIAVAWGIE KETMYLYRKG IVPKETMRWI VEKVKQIVPI PVPSVDVEKA RNLILNDKKI LKGSRVRLPY VKEIGKIEFL EVDPLELLEV VD // ID ATPA_THEMA Reviewed; 503 AA. AC Q9X1U7; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; DE EC=3.6.3.14 {ECO:0000255|HAMAP-Rule:MF_01346}; DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; GN OrderedLocusNames=TM_1612; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The alpha chain is a regulatory CC subunit. {ECO:0000255|HAMAP-Rule:MF_01346}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). {ECO:0000255|HAMAP-Rule:MF_01346}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a(1), b(2) and c(9-12). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. CF(1) is attached to CF(0) by a central stalk formed CC by the gamma and epsilon chains, while a peripheral stalk is CC formed by the delta and b chains. {ECO:0000255|HAMAP- CC Rule:MF_01346}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01346}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000255|HAMAP-Rule:MF_01346}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36679.1; -; Genomic_DNA. DR PIR; F72231; F72231. DR RefSeq; NP_229412.1; NC_000853.1. DR RefSeq; WP_004082064.1; NZ_CP011107.1. DR PDB; 2R9V; X-ray; 2.10 A; A=2-503. DR PDBsum; 2R9V; -. DR ProteinModelPortal; Q9X1U7; -. DR SMR; Q9X1U7; 17-503. DR STRING; 243274.TM1612; -. DR PRIDE; Q9X1U7; -. DR DNASU; 897935; -. DR EnsemblBacteria; AAD36679; AAD36679; TM_1612. DR GeneID; 897935; -. DR KEGG; tma:TM1612; -. DR PATRIC; 23938198; VBITheMar51294_1631. DR eggNOG; ENOG4105CDG; Bacteria. DR eggNOG; COG0056; LUCA. DR InParanoid; Q9X1U7; -. DR KO; K02111; -. DR OMA; QVVSIWA; -. DR OrthoDB; EOG67X1S1; -. DR EvolutionaryTrace; Q9X1U7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.30.20; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR023366; ATPase_asu-like. DR InterPro; IPR005294; ATPase_F1-cplx_asu. DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR004100; ATPase_F1_a/bsu_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR15184:SF3; PTHR15184:SF3; 1. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1. DR SUPFAM; SSF47917; SSF47917; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00962; atpA; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP synthesis; ATP-binding; Cell inner membrane; KW Cell membrane; CF(1); Complete proteome; Hydrogen ion transport; KW Hydrolase; Ion transport; Membrane; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 503 ATP synthase subunit alpha. FT /FTId=PRO_0000238387. FT NP_BIND 170 177 ATP. {ECO:0000255|HAMAP-Rule:MF_01346}. FT SITE 363 363 Required for activity. FT {ECO:0000255|HAMAP-Rule:MF_01346}. FT TURN 25 27 {ECO:0000244|PDB:2R9V}. FT STRAND 28 35 {ECO:0000244|PDB:2R9V}. FT STRAND 38 43 {ECO:0000244|PDB:2R9V}. FT STRAND 51 55 {ECO:0000244|PDB:2R9V}. FT TURN 56 58 {ECO:0000244|PDB:2R9V}. FT STRAND 61 66 {ECO:0000244|PDB:2R9V}. FT STRAND 72 78 {ECO:0000244|PDB:2R9V}. FT STRAND 88 95 {ECO:0000244|PDB:2R9V}. FT STRAND 97 101 {ECO:0000244|PDB:2R9V}. FT HELIX 102 104 {ECO:0000244|PDB:2R9V}. FT STRAND 117 119 {ECO:0000244|PDB:2R9V}. FT STRAND 125 130 {ECO:0000244|PDB:2R9V}. FT HELIX 137 139 {ECO:0000244|PDB:2R9V}. FT STRAND 145 147 {ECO:0000244|PDB:2R9V}. FT HELIX 152 157 {ECO:0000244|PDB:2R9V}. FT STRAND 165 171 {ECO:0000244|PDB:2R9V}. FT HELIX 176 185 {ECO:0000244|PDB:2R9V}. FT TURN 186 191 {ECO:0000244|PDB:2R9V}. FT STRAND 192 200 {ECO:0000244|PDB:2R9V}. FT HELIX 203 215 {ECO:0000244|PDB:2R9V}. FT HELIX 218 221 {ECO:0000244|PDB:2R9V}. FT STRAND 222 227 {ECO:0000244|PDB:2R9V}. FT HELIX 233 251 {ECO:0000244|PDB:2R9V}. FT TURN 252 254 {ECO:0000244|PDB:2R9V}. FT STRAND 256 262 {ECO:0000244|PDB:2R9V}. FT HELIX 264 276 {ECO:0000244|PDB:2R9V}. FT HELIX 291 299 {ECO:0000244|PDB:2R9V}. FT STRAND 303 305 {ECO:0000244|PDB:2R9V}. FT TURN 307 310 {ECO:0000244|PDB:2R9V}. FT STRAND 313 323 {ECO:0000244|PDB:2R9V}. FT HELIX 330 337 {ECO:0000244|PDB:2R9V}. FT STRAND 339 345 {ECO:0000244|PDB:2R9V}. FT HELIX 347 352 {ECO:0000244|PDB:2R9V}. FT TURN 360 362 {ECO:0000244|PDB:2R9V}. FT HELIX 366 368 {ECO:0000244|PDB:2R9V}. FT TURN 369 371 {ECO:0000244|PDB:2R9V}. FT HELIX 374 394 {ECO:0000244|PDB:2R9V}. FT HELIX 397 399 {ECO:0000244|PDB:2R9V}. FT HELIX 405 420 {ECO:0000244|PDB:2R9V}. FT HELIX 431 442 {ECO:0000244|PDB:2R9V}. FT TURN 443 448 {ECO:0000244|PDB:2R9V}. FT HELIX 451 453 {ECO:0000244|PDB:2R9V}. FT HELIX 454 468 {ECO:0000244|PDB:2R9V}. FT HELIX 470 479 {ECO:0000244|PDB:2R9V}. FT HELIX 484 500 {ECO:0000244|PDB:2R9V}. SQ SEQUENCE 503 AA; 56062 MW; 886C9736F16BF149 CRC64; MRINPGEITK VLEEKIKSFE EKIDLEDTGK VIQVGDGIAR AYGLNKVMVS ELVEFVETGV KGVAFNLEED NVGIIILGEY KDIKEGHTVR RLKRIIEVPV GEELLGRVVN PLGEPLDGKG PINAKNFRPI EIKAPGVIYR KPVDTPLQTG IKAIDSMIPI GRGQRELIIG DRQTGKTAIA IDTIINQKGQ GVYCIYVAIG QKKSAIARII DKLRQYGAME YTTVVVASAS DPASLQYIAP YAGCAMGEYF AYSGRDALVV YDDLSKHAVA YRQLSLLMRR PPGREAYPGD IFYLHSRLLE RAVRLNDKLG GGSLTALPIV ETQANDISAY IPTNVISITD GQIYLEPGLF YAGQRPAINV GLSVSRVGGS AQIKAMKQVA GMLRIDLAQY RELETFAQFA TELDPATRAQ IIRGQRLMEL LKQEQYSPMP VEEQVVVLFA GVRGYLDDLP VEEVRRFEKE FLRFMHEKHQ DILDDIKTKK ELTSETEEKL KKAIEEFKTT FRV // ID ATPE_THEMA Reviewed; 108 AA. AC Q9X1U5; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=ATP synthase epsilon chain {ECO:0000255|HAMAP-Rule:MF_00530}; DE AltName: Full=ATP synthase F1 sector epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530}; DE AltName: Full=F-ATPase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530}; GN Name=atpC {ECO:0000255|HAMAP-Rule:MF_00530}; GN OrderedLocusNames=TM_1609; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. {ECO:0000255|HAMAP-Rule:MF_00530}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00530}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00530}. CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family. CC {ECO:0000255|HAMAP-Rule:MF_00530}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36676.1; -; Genomic_DNA. DR PIR; C72231; C72231. DR RefSeq; NP_229409.1; NC_000853.1. DR RefSeq; WP_004082057.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1U5; -. DR STRING; 243274.TM1609; -. DR EnsemblBacteria; AAD36676; AAD36676; TM_1609. DR GeneID; 897603; -. DR KEGG; tma:TM1609; -. DR PATRIC; 23938192; VBITheMar51294_1628. DR eggNOG; ENOG41082J0; Bacteria. DR eggNOG; COG0355; LUCA. DR InParanoid; Q9X1U5; -. DR KO; K02114; -. DR OMA; DGFLHCD; -. DR OrthoDB; EOG6ZSPD8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.15.10; -; 1. DR HAMAP; MF_00530; ATP_synth_epsil_bac; 1. DR InterPro; IPR001469; ATPase_F1-cplx_dsu/esu. DR InterPro; IPR020546; ATPase_F1-cplx_dsu/esu_N. DR PANTHER; PTHR13822; PTHR13822; 1. DR Pfam; PF02823; ATP-synt_DE_N; 1. DR ProDom; PD000944; ATPase_F1-cplx_dsu/esu; 1. DR SUPFAM; SSF51344; SSF51344; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transport. FT CHAIN 1 108 ATP synthase epsilon chain. FT /FTId=PRO_0000188231. SQ SEQUENCE 108 AA; 12329 MW; 4C6CBFCDA1CA623D CRC64; MKVKIVTPYG IVYDRESDFI SFRTVEGSMG ILPRRAPIVT QLSVCDVKIK SGDDEYHLKV AGGFLLCDGK DVIIITEEAG REEDISPDRF MEARERVERV RRFFQSSL // ID ATPF_THEMA Reviewed; 164 AA. AC Q9X1U9; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=ATP synthase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=F-type ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE Short=F-ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; GN OrderedLocusNames=TM_1614; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the CC presence of a proton or sodium gradient. F-type ATPases consist of CC two structural domains, F(1) containing the extramembraneous CC catalytic core and F(0) containing the membrane proton channel, CC linked together by a central stalk and a peripheral stalk. During CC catalysis, ATP synthesis in the catalytic domain of F(1) is CC coupled via a rotary mechanism of the central stalk subunits to CC proton translocation. {ECO:0000255|HAMAP-Rule:MF_01398}. CC -!- FUNCTION: Component of the F(0) channel, it forms part of the CC peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP- CC Rule:MF_01398}. CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic CC core - and F(0) - the membrane proton channel. F(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) CC has three main subunits: a(1), b(2) and c(10-14). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. F(1) is attached to F(0) by a central stalk formed by CC the gamma and epsilon chains, while a peripheral stalk is formed CC by the delta and b chains. {ECO:0000255|HAMAP-Rule:MF_01398}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01398}. CC -!- SIMILARITY: Belongs to the ATPase B chain family. CC {ECO:0000255|HAMAP-Rule:MF_01398}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36681.1; -; Genomic_DNA. DR PIR; H72231; H72231. DR RefSeq; NP_229414.1; NC_000853.1. DR RefSeq; WP_004082072.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1U9; -. DR STRING; 243274.TM1614; -. DR EnsemblBacteria; AAD36681; AAD36681; TM_1614. DR GeneID; 897934; -. DR KEGG; tma:TM1614; -. DR PATRIC; 23938202; VBITheMar51294_1633. DR eggNOG; ENOG41084Y9; Bacteria. DR eggNOG; COG0711; LUCA. DR InParanoid; Q9X1U9; -. DR KO; K02109; -. DR OMA; SMIQDLS; -. DR OrthoDB; EOG6DNTDK; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.5.620; -; 1. DR HAMAP; MF_01398; ATP_synth_b_bact; 1. DR InterPro; IPR028987; ATPase_B-like_membr. DR InterPro; IPR002146; ATPase_F0-cplx_b/b'su_bac. DR InterPro; IPR005864; ATPase_F0-cplx_bsu_bac. DR Pfam; PF00430; ATP-synt_B; 1. DR SUPFAM; SSF81573; SSF81573; 1. DR TIGRFAMs; TIGR01144; ATP_synt_b; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 164 ATP synthase subunit b. FT /FTId=PRO_0000368843. FT TRANSMEM 10 32 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01398}. SQ SEQUENCE 164 AA; 19295 MW; 7B0F14F285A88CE0 CRC64; MGFLEINWTS AAMLMLFVLM VYFLNKFLYT PFIEMAEKRR KKVEEDLKSA EQLKEEAEKM RSEAERFLSE ARQRADEIVE SARKEAEAIV EEAREKAKKE AQNIVESAKT QIEVEYKKAL EQVQERAAEL SVILATKLLQ KVFQDERARR EYLVKILKEE IEKS // ID ATPD_THEMA Reviewed; 183 AA. AC Q9X1U8; DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=ATP synthase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; GN Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416}; GN OrderedLocusNames=TM_1613; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the CC presence of a proton or sodium gradient. F-type ATPases consist of CC two structural domains, F(1) containing the extramembraneous CC catalytic core and F(0) containing the membrane proton channel, CC linked together by a central stalk and a peripheral stalk. During CC catalysis, ATP synthesis in the catalytic domain of F(1) is CC coupled via a rotary mechanism of the central stalk subunits to CC proton translocation. {ECO:0000255|HAMAP-Rule:MF_01416}. CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CC CF(1). It either transmits conformational changes from CF(0) to CC CF(1) or is implicated in proton conduction. {ECO:0000255|HAMAP- CC Rule:MF_01416}. CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic CC core - and F(0) - the membrane proton channel. F(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) CC has three main subunits: a(1), b(2) and c(10-14). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. F(1) is attached to F(0) by a central stalk formed by CC the gamma and epsilon chains, while a peripheral stalk is formed CC by the delta and b chains. {ECO:0000255|HAMAP-Rule:MF_01416}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01416}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01416}. CC -!- SIMILARITY: Belongs to the ATPase delta chain family. CC {ECO:0000255|HAMAP-Rule:MF_01416}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36680.1; -; Genomic_DNA. DR PIR; G72231; G72231. DR RefSeq; NP_229413.1; NC_000853.1. DR RefSeq; WP_004082066.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1U8; -. DR STRING; 243274.TM1613; -. DR EnsemblBacteria; AAD36680; AAD36680; TM_1613. DR GeneID; 897372; -. DR KEGG; tma:TM1613; -. DR PATRIC; 23938200; VBITheMar51294_1632. DR eggNOG; ENOG41085KK; Bacteria. DR eggNOG; COG0712; LUCA. DR InParanoid; Q9X1U8; -. DR KO; K02113; -. DR OMA; IWFDLEM; -. DR OrthoDB; EOG6DNTDK; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.520.20; -; 1. DR HAMAP; MF_01416; ATP_synth_delta_bact; 1. DR InterPro; IPR026015; ATPase_OSCP/delta_N. DR InterPro; IPR000711; ATPase_OSCP/dsu. DR PANTHER; PTHR11910; PTHR11910; 1. DR Pfam; PF00213; OSCP; 1. DR PRINTS; PR00125; ATPASEDELTA. DR SUPFAM; SSF47928; SSF47928; 1. DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transport. FT CHAIN 1 183 ATP synthase subunit delta. FT /FTId=PRO_0000382161. SQ SEQUENCE 183 AA; 21539 MW; 7484D266A32E9F9E CRC64; MRFSAVAGRY ARALLNVAIE KEKEEEYLRF LDLVCQIYES SRELFDNPIL KPEKKISLIK EIMKSFGQEM DEFQERFLTL VFERKRQKLL RNIRDLFEYE KILSEQKVPA NLSIAHSPED EELSLLRKFV RKYALKDPVF DISIDESLIA GALVEFEGFR LDTTVQGRLK RIAREALKRG EMS // ID BGAL_THEMA Reviewed; 1084 AA. AC Q56307; O33834; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 118. DE RecName: Full=Beta-galactosidase; DE Short=Beta-gal; DE EC=3.2.1.23; DE AltName: Full=Lactase; GN Name=lacZ; OrderedLocusNames=TM_1193; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8088532; DOI=10.1016/0378-1119(94)90046-9; RA Moore J.B., Markiewicz P., Miller J.H.; RT "Identification and sequencing of the Thermotoga maritima lacZ gene, RT part of a divergently transcribed operon."; RL Gene 147:101-106(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 554-1084. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9741105; RA Liebl W., Wagner B., Schellhase J.; RT "Properties of an alpha-galactosidase, and structure of its gene galA, RT within an alpha- and beta-galactoside utilization gene cluster of the RT hyperthermophilic bacterium Thermotoga maritima."; RL Syst. Appl. Microbiol. 21:1-11(1998). CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D- CC galactose residues in beta-D-galactosides. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD36268.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U08186; AAA50597.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36268.1; ALT_INIT; Genomic_DNA. DR EMBL; AJ001072; CAA04513.1; -; Genomic_DNA. DR PIR; F72283; F72283. DR RefSeq; NP_228998.1; NC_000853.1. DR RefSeq; WP_004080135.1; NZ_CP011107.1. DR ProteinModelPortal; Q56307; -. DR STRING; 243274.TM1193; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR EnsemblBacteria; AAD36268; AAD36268; TM_1193. DR GeneID; 898291; -. DR KEGG; tma:TM1193; -. DR PATRIC; 23937328; VBITheMar51294_1211. DR eggNOG; ENOG4105CNT; Bacteria. DR eggNOG; COG3250; LUCA. DR InParanoid; Q56307; -. DR KO; K01190; -. DR OMA; WHERRNV; -. DR OrthoDB; EOG6XWV0T; -. DR BioCyc; TMAR243274:GC6P-1223-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro. DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 2.60.40.320; -; 2. DR Gene3D; 2.70.98.10; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR004199; B-gal_small/dom_5. DR InterPro; IPR011013; Gal_mutarotase_SF_dom. DR InterPro; IPR008979; Galactose-bd-like. DR InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub. DR InterPro; IPR006101; Glyco_hydro_2. DR InterPro; IPR013812; Glyco_hydro_2/20_Ig-like. DR InterPro; IPR023232; Glyco_hydro_2_AS. DR InterPro; IPR006103; Glyco_hydro_2_cat. DR InterPro; IPR023230; Glyco_hydro_2_CS. DR InterPro; IPR006102; Glyco_hydro_2_Ig-like. DR InterPro; IPR006104; Glyco_hydro_2_N. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR032312; LacZ_4. DR Pfam; PF02929; Bgal_small_N; 1. DR Pfam; PF16353; DUF4981; 1. DR Pfam; PF00703; Glyco_hydro_2; 1. DR Pfam; PF02836; Glyco_hydro_2_C; 1. DR Pfam; PF02837; Glyco_hydro_2_N; 1. DR PRINTS; PR00132; GLHYDRLASE2. DR SMART; SM01038; Bgal_small_N; 1. DR SUPFAM; SSF49303; SSF49303; 2. DR SUPFAM; SSF49785; SSF49785; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR SUPFAM; SSF74650; SSF74650; 1. DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1. DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosidase; Hydrolase; Reference proteome. FT CHAIN 1 1084 Beta-galactosidase. FT /FTId=PRO_0000057678. FT ACT_SITE 441 441 Proton donor. {ECO:0000250}. FT ACT_SITE 507 507 Nucleophile. {ECO:0000250}. FT CONFLICT 152 175 SKDSCTPAEFRLTDVLRPGKNLIT -> RQRQLHARRIQTH FT RCSKTREESDH (in Ref. 1; AAA50597). FT {ECO:0000305}. FT CONFLICT 1028 1084 SKEKQVVLFVDGNEYSVRRVVIPPFKKEELVFKVEGLKKGE FT HLIHTNLNTRKTIYVR -> RQGKTGGSLC (in Ref. FT 1). {ECO:0000305}. SQ SEQUENCE 1084 AA; 127608 MW; D52E3B762B53DDFC CRC64; MPYEWENPQL VSEGTEKSHA SFIPYLDPFS GEWEYPEEFI SLNGNWRFLF AKNPFEVPED FFSEKFDDSN WDEIEVPSNW EMKGYGKPIY TNVVYPFEPN PPFVPKDDNP TGVYRRWIEI PEDWFKKEIF LHFEGVRSFF YLWVNGKKIG FSKDSCTPAE FRLTDVLRPG KNLITVEVLK WSDGSYLEDQ DMWWFAGIYR DVYLYALPKF HIRDVFVRTD LDENYRNGKI FLDVEMRNLG EEEEKDLEVT LITPDGDEKT LVKETVKPED RVLSFAFDVK DPKKWSAETP HLYVLKLKLG EDEKKVNFGF RKIEIKDGTL LFNGKPLYIK GVNRHEFDPD RGHAVTVERM IQDIKLMKQH NINTVRTSHY PNQTKWYDLC DYFGLYVIDE ANIESHGIDW DPEVTLANRW EWEKAHFDRI KRMVERDKNH PSIIFWSLGN EAGDGVNFEK AALWIKKRDN TRLIHYEGTT RRGESYYVDV FSLMYPKMDI LLEYASKKRE KPFIMCEYAH AMGNSVGNLK DYWDVIEKYP YLHGGCIWDW VDQGIRKKDE NGREFWAYGG DFGDTPNDGN FCINGVVLPD RTPEPELYEV KKVYQNVKIR QVSKDTYEVE NRYLFTNLEM FDGAWKIRKD GEVIEEKTFK IFAEPGEKRL LKIPLPEMDD SEYFLEISFS LSEDTPWAEK GHVVAWEQFL LKAPAFEKKS ISDGVSLRED GKHLTVEAKD TVYVFSKLTG LLEQILHRRK KILKSPVVPN FWRVPTDNDI GNRMPQRLAI WKRASKERKL FKMHWKKEEN RVSVHSVFQL PGNSWVYTTY TVFGNGDVLV DLSLIPAEDV PEIPRIGFQF TVPEEFGTVE WYGRGPHETY WDRKESGLFA RYRKAVGEMM HRYVRPQETG NRSDVRWFAL SDGETKLFVS GMPQIDFSVW PFSMEDLERV QHISELPERD FVTVNVDFRQ MGLGGDDSWG AMPHLEYRLL PKPYRFSFRM RISEEIPSWR VLAAIPETLH VEMSSEDVIR EGDTLRVKFS LLNDTPLSKE KQVVLFVDGN EYSVRRVVIP PFKKEELVFK VEGLKKGEHL IHTNLNTRKT IYVR // ID BFRA_THEMA Reviewed; 432 AA. AC O33833; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 11-MAY-2016, entry version 117. DE RecName: Full=Beta-fructosidase; DE EC=3.2.1.26; DE AltName: Full=Invertase; DE AltName: Full=Sucrase; GN Name=bfrA; OrderedLocusNames=TM_1414; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9720201; DOI=10.1007/s002530051256; RA Liebl W., Brem D., Gotschlich A.; RT "Analysis of the gene for beta-fructosidase (invertase, inulinase) of RT the hyperthermophilic bacterium Thermotoga maritima, and RT characterisation of the enzyme expressed in Escherichia coli."; RL Appl. Microbiol. Biotechnol. 50:55-64(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-432. RX PubMed=14973124; DOI=10.1074/jbc.M313911200; RA Alberto F., Bignon C., Sulzenbacher G., Henrissat B., Czjzek M.; RT "The three-dimensional structure of invertase (beta-fructosidase) from RT Thermotoga maritima reveals a bimodular arrangement and an RT evolutionary relationship between retaining and inverting RT glycosidases."; RL J. Biol. Chem. 279:18903-18910(2004). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 2-432 IN COMPLEX WITH RP SUBSTRATES, AND MUTAGENESIS OF GLU-190. RX PubMed=16411890; DOI=10.1042/BJ20051936; RA Alberto F., Jordi E., Henrissat B., Czjzek M.; RT "Crystal structure of inactivated Thermotoga maritima invertase in RT complex with the trisaccharide substrate raffinose."; RL Biochem. J. 395:457-462(2006). CC -!- FUNCTION: Hydrolysis of sucrose, raffinose, inulin and levan. CC Specific for the fructose moiety and the beta-anomeric CC configuration of the glycosidic linkages of its substrates. The CC enzyme released fructose from sucrose and raffinose, and the CC fructose polymer inulin is hydrolyzed quantitatively in an exo- CC type fashion. CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D- CC fructofuranoside residues in beta-D-fructofuranosides. CC {ECO:0000255|PROSITE-ProRule:PRU10067}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 90-95 degrees Celsius. Highly CC thermostable.; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ001073; CAA04518.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36485.1; -; Genomic_DNA. DR PIR; D72255; D72255. DR RefSeq; NP_229215.1; NC_000853.1. DR RefSeq; WP_004081649.1; NZ_CP011107.1. DR PDB; 1UYP; X-ray; 1.90 A; A/B/C/D/E/F=2-432. DR PDB; 1W2T; X-ray; 1.87 A; A/B/C/D/E/F=2-432. DR PDBsum; 1UYP; -. DR PDBsum; 1W2T; -. DR ProteinModelPortal; O33833; -. DR SMR; O33833; 1-432. DR STRING; 243274.TM1414; -. DR CAZy; GH32; Glycoside Hydrolase Family 32. DR EnsemblBacteria; AAD36485; AAD36485; TM_1414. DR GeneID; 898062; -. DR KEGG; tma:TM1414; -. DR PATRIC; 23937772; VBITheMar51294_1425. DR eggNOG; ENOG4108HKT; Bacteria. DR eggNOG; COG1621; LUCA. DR InParanoid; O33833; -. DR KO; K01193; -. DR OMA; ARQSKWR; -. DR OrthoDB; EOG6KDKMP; -. DR BRENDA; 3.2.1.26; 6331. DR EvolutionaryTrace; O33833; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IBA:GO_Central. DR GO; GO:0005987; P:sucrose catabolic process; IBA:GO_Central. DR Gene3D; 2.115.10.20; -; 1. DR Gene3D; 2.60.120.560; -; 1. DR InterPro; IPR013320; ConA-like_dom. DR InterPro; IPR001362; Glyco_hydro_32. DR InterPro; IPR018053; Glyco_hydro_32_AS. DR InterPro; IPR013189; Glyco_hydro_32_C. DR InterPro; IPR013148; Glyco_hydro_32_N. DR InterPro; IPR023296; Glyco_hydro_beta-prop. DR Pfam; PF00251; Glyco_hydro_32N; 1. DR SMART; SM00640; Glyco_32; 1. DR SUPFAM; SSF49899; SSF49899; 1. DR SUPFAM; SSF75005; SSF75005; 1. DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Glycosidase; Hydrolase; KW Reference proteome. FT CHAIN 1 432 Beta-fructosidase. FT /FTId=PRO_0000169881. FT REGION 14 17 Substrate binding. FT REGION 74 75 Substrate binding. FT REGION 137 138 Substrate binding. FT REGION 188 190 Substrate binding. FT ACT_SITE 17 17 FT BINDING 33 33 Substrate. FT BINDING 41 41 Substrate. FT BINDING 92 92 Substrate. FT BINDING 208 208 Substrate. FT BINDING 260 260 Substrate. FT MUTAGEN 190 190 E->A: Loss of activity. FT {ECO:0000269|PubMed:16411890}. FT MUTAGEN 190 190 E->D: Reduced activity. FT {ECO:0000269|PubMed:16411890}. FT STRAND 5 7 {ECO:0000244|PDB:1W2T}. FT STRAND 11 24 {ECO:0000244|PDB:1W2T}. FT STRAND 27 35 {ECO:0000244|PDB:1W2T}. FT STRAND 38 40 {ECO:0000244|PDB:1W2T}. FT STRAND 45 56 {ECO:0000244|PDB:1W2T}. FT STRAND 58 64 {ECO:0000244|PDB:1W2T}. FT STRAND 71 81 {ECO:0000244|PDB:1W2T}. FT STRAND 84 93 {ECO:0000244|PDB:1W2T}. FT STRAND 102 114 {ECO:0000244|PDB:1W2T}. FT STRAND 133 143 {ECO:0000244|PDB:1W2T}. FT STRAND 145 156 {ECO:0000244|PDB:1W2T}. FT TURN 157 159 {ECO:0000244|PDB:1W2T}. FT STRAND 160 173 {ECO:0000244|PDB:1W2T}. FT STRAND 175 183 {ECO:0000244|PDB:1W2T}. FT STRAND 190 197 {ECO:0000244|PDB:1W2T}. FT STRAND 200 207 {ECO:0000244|PDB:1W2T}. FT TURN 208 211 {ECO:0000244|PDB:1W2T}. FT STRAND 212 221 {ECO:0000244|PDB:1W2T}. FT STRAND 224 233 {ECO:0000244|PDB:1W2T}. FT STRAND 236 238 {ECO:0000244|PDB:1W2T}. FT STRAND 240 244 {ECO:0000244|PDB:1W2T}. FT STRAND 249 258 {ECO:0000244|PDB:1W2T}. FT TURN 260 262 {ECO:0000244|PDB:1W2T}. FT HELIX 263 265 {ECO:0000244|PDB:1W2T}. FT HELIX 268 271 {ECO:0000244|PDB:1W2T}. FT STRAND 281 286 {ECO:0000244|PDB:1W2T}. FT STRAND 289 294 {ECO:0000244|PDB:1W2T}. FT HELIX 296 301 {ECO:0000244|PDB:1W2T}. FT STRAND 302 311 {ECO:0000244|PDB:1W2T}. FT STRAND 313 316 {ECO:0000244|PDB:1W2T}. FT STRAND 320 322 {ECO:0000244|PDB:1W2T}. FT STRAND 324 339 {ECO:0000244|PDB:1W2T}. FT STRAND 344 350 {ECO:0000244|PDB:1W2T}. FT STRAND 353 357 {ECO:0000244|PDB:1W2T}. FT STRAND 368 372 {ECO:0000244|PDB:1W2T}. FT STRAND 377 386 {ECO:0000244|PDB:1W2T}. FT STRAND 389 394 {ECO:0000244|PDB:1W2T}. FT TURN 395 397 {ECO:0000244|PDB:1W2T}. FT STRAND 398 403 {ECO:0000244|PDB:1W2T}. FT STRAND 412 427 {ECO:0000244|PDB:1W2T}. SQ SEQUENCE 432 AA; 49841 MW; 39F61B2E1BC462B9 CRC64; MFKPNYHFFP ITGWMNDPNG LIFWKGKYHM FYQYNPRKPE WGNICWGHAV SDDLVHWRHL PVALYPDDET HGVFSGSAVE KDGKMFLVYT YYRDPTHNKG EKETQCVAMS ENGLDFVKYD GNPVISKPPE EGTHAFRDPK VNRSNGEWRM VLGSGKDEKI GRVLLYTSDD LFHWKYEGVI FEDETTKEIE CPDLVRIGEK DILIYSITST NSVLFSMGEL KEGKLNVEKR GLLDHGTDFY AAQTFFGTDR VVVIGWLQSW LRTGLYPTKR EGWNGVMSLP RELYVENNEL KVKPVDELLA LRKRKVFETA KSGTFLLDVK ENSYEIVCEF SGEIELRMGN ESEEVVITKS RDELIVDTTR SGVSGGEVRK STVEDEATNR IRAFLDSCSV EFFFNDSIAF SFRIHPENVY NILSVKSNQV KLEVFELENI WL // ID ATPL_THEMA Reviewed; 85 AA. AC Q9X1V0; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=ATP synthase subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE AltName: Full=F-type ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE Short=F-ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE AltName: Full=Lipid-binding protein {ECO:0000255|HAMAP-Rule:MF_01396}; GN Name=atpE {ECO:0000255|HAMAP-Rule:MF_01396}; GN OrderedLocusNames=TM_1615; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the CC presence of a proton or sodium gradient. F-type ATPases consist of CC two structural domains, F(1) containing the extramembraneous CC catalytic core and F(0) containing the membrane proton channel, CC linked together by a central stalk and a peripheral stalk. During CC catalysis, ATP synthesis in the catalytic domain of F(1) is CC coupled via a rotary mechanism of the central stalk subunits to CC proton translocation. {ECO:0000255|HAMAP-Rule:MF_01396}. CC -!- FUNCTION: Key component of the F(0) channel; it plays a direct CC role in translocation across the membrane. A homomeric c-ring of CC between 10-14 subunits forms the central stalk rotor element with CC the F(1) delta and epsilon subunits. {ECO:0000255|HAMAP- CC Rule:MF_01396}. CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic CC core - and F(0) - the membrane proton channel. F(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) CC has three main subunits: a(1), b(2) and c(10-14). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. F(1) is attached to F(0) by a central stalk formed by CC the gamma and epsilon chains, while a peripheral stalk is formed CC by the delta and b chains. {ECO:0000255|HAMAP-Rule:MF_01396}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01396}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01396}. CC -!- SIMILARITY: Belongs to the ATPase C chain family. CC {ECO:0000255|HAMAP-Rule:MF_01396}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36682.1; -; Genomic_DNA. DR PIR; A72232; A72232. DR RefSeq; NP_229415.1; NC_000853.1. DR RefSeq; WP_004082074.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1V0; -. DR STRING; 243274.TM1615; -. DR EnsemblBacteria; AAD36682; AAD36682; TM_1615. DR GeneID; 897622; -. DR KEGG; tma:TM1615; -. DR PATRIC; 23938204; VBITheMar51294_1634. DR eggNOG; ENOG410855G; Bacteria. DR eggNOG; COG0636; LUCA. DR InParanoid; Q9X1V0; -. DR KO; K02110; -. DR OMA; VRGTQEG; -. DR OrthoDB; EOG68H8G3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. DR Gene3D; 1.20.20.10; -; 1. DR HAMAP; MF_01396; ATP_synth_c_bact; 1. DR InterPro; IPR000454; ATPase_F0-cplx_csu. DR InterPro; IPR005953; ATPase_F0-cplx_csu_bac/chlpt. DR InterPro; IPR020537; ATPase_F0-cplx_csu_DDCD_BS. DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom. DR Pfam; PF00137; ATP-synt_C; 1. DR PRINTS; PR00124; ATPASEC. DR SUPFAM; SSF81333; SSF81333; 1. DR TIGRFAMs; TIGR01260; ATP_synt_c; 1. DR PROSITE; PS00605; ATPASE_C; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0); KW Complete proteome; Hydrogen ion transport; Ion transport; KW Lipid-binding; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 85 ATP synthase subunit c. FT /FTId=PRO_0000365935. FT TRANSMEM 10 30 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01396}. FT TRANSMEM 65 85 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01396}. FT SITE 68 68 Reversibly protonated during proton FT transport. {ECO:0000255|HAMAP- FT Rule:MF_01396}. SQ SEQUENCE 85 AA; 8648 MW; B861616C2C403174 CRC64; MENLGDLAQG LALLGKYLGA GLCMGIGAIG PGIGEGNIGA HAMDAMARQP EMVGTITTRM LLADAVAETT GIYSLLIAFM ILLVV // ID BUK1_THEMA Reviewed; 357 AA. AC Q9X276; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Probable butyrate kinase 1 {ECO:0000255|HAMAP-Rule:MF_00542}; DE Short=BK 1 {ECO:0000255|HAMAP-Rule:MF_00542}; DE EC=2.7.2.7 {ECO:0000255|HAMAP-Rule:MF_00542}; DE AltName: Full=Branched-chain carboxylic acid kinase 1 {ECO:0000255|HAMAP-Rule:MF_00542}; GN Name=buk1 {ECO:0000255|HAMAP-Rule:MF_00542}; GN OrderedLocusNames=TM_1754; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + butanoate = ADP + butanoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00542}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00542}. CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP- CC Rule:MF_00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36819.1; -; Genomic_DNA. DR PIR; C72214; C72214. DR RefSeq; NP_229552.1; NC_000853.1. DR RefSeq; WP_004082288.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X276; -. DR STRING; 243274.TM1754; -. DR EnsemblBacteria; AAD36819; AAD36819; TM_1754. DR GeneID; 897730; -. DR KEGG; tma:TM1754; -. DR PATRIC; 23938484; VBITheMar51294_1772. DR eggNOG; ENOG4105CKM; Bacteria. DR eggNOG; COG3426; LUCA. DR InParanoid; Q9X276; -. DR KO; K00929; -. DR OMA; CDEARFS; -. DR OrthoDB; EOG6KHG1Q; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0047761; F:butyrate kinase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00542; Butyrate_kinase; 1. DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain. DR InterPro; IPR023865; Aliphatic_acid_kinase_CS. DR InterPro; IPR011245; Butyrate_kin. DR PANTHER; PTHR21060; PTHR21060; 1. DR Pfam; PF00871; Acetate_kinase; 1. DR PIRSF; PIRSF036458; Butyrate_kin; 1. DR PRINTS; PR00471; ACETATEKNASE. DR TIGRFAMs; TIGR02707; butyr_kinase; 1. DR PROSITE; PS01075; ACETATE_KINASE_1; 1. DR PROSITE; PS01076; ACETATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 357 Probable butyrate kinase 1. FT /FTId=PRO_0000107674. SQ SEQUENCE 357 AA; 39283 MW; 826F1AC844DAEAEE CRC64; MYRILVINPG SSSTKVAVFE DEKKIAEKNV SHSVEELKKF KRSMDQEPLR RKAVEDFIDE VGYRIEDFSA IAARGGVLEP VPGGTYVVNE YMVDYLINRS PVDHVSNLAA VIGYKLGKPH GIPCFVVDPV SVDEMCDEAR FSGIPEIERK SYSHALNIKA VLRKVSREMG KTPEEVKIVV AHLGSGISVC ACKNGKIIDV NNANDEGPFS IERTGELPVG DVVKTAYSSK HSAAELKEEF TRKGGLLAYL GTKNLKKALD SMETSRKAKL VVEAMAYQIA KEIGGMCAVL GEKPDAIVIT GGMAHEIRFV RMITDYIEKF GKVEVIPGEL EMEALALGVL RVLRGEEKAM DYRSVVE // ID BUK2_THEMA Reviewed; 375 AA. AC Q9X278; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=Probable butyrate kinase 2 {ECO:0000255|HAMAP-Rule:MF_00542}; DE Short=BK 2 {ECO:0000255|HAMAP-Rule:MF_00542}; DE EC=2.7.2.7 {ECO:0000255|HAMAP-Rule:MF_00542}; DE AltName: Full=Branched-chain carboxylic acid kinase 2 {ECO:0000255|HAMAP-Rule:MF_00542}; GN Name=buk2 {ECO:0000255|HAMAP-Rule:MF_00542}; GN OrderedLocusNames=TM_1756; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + butanoate = ADP + butanoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00542}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00542}. CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP- CC Rule:MF_00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36821.1; -; Genomic_DNA. DR PIR; E72214; E72214. DR RefSeq; NP_229554.1; NC_000853.1. DR RefSeq; WP_004082291.1; NZ_CP011107.1. DR PDB; 1SAZ; X-ray; 2.50 A; A=1-375. DR PDB; 1X9J; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-375. DR PDBsum; 1SAZ; -. DR PDBsum; 1X9J; -. DR ProteinModelPortal; Q9X278; -. DR SMR; Q9X278; 1-375. DR STRING; 243274.TM1756; -. DR EnsemblBacteria; AAD36821; AAD36821; TM_1756. DR GeneID; 897722; -. DR KEGG; tma:TM1756; -. DR PATRIC; 23938488; VBITheMar51294_1774. DR eggNOG; ENOG4105CKM; Bacteria. DR eggNOG; COG3426; LUCA. DR InParanoid; Q9X278; -. DR KO; K00929; -. DR OMA; FRILTIN; -. DR OrthoDB; EOG6KHG1Q; -. DR BRENDA; 2.7.2.7; 6331. DR EvolutionaryTrace; Q9X278; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0047761; F:butyrate kinase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00542; Butyrate_kinase; 1. DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain. DR InterPro; IPR023865; Aliphatic_acid_kinase_CS. DR InterPro; IPR011245; Butyrate_kin. DR PANTHER; PTHR21060; PTHR21060; 1. DR PANTHER; PTHR21060:SF3; PTHR21060:SF3; 1. DR Pfam; PF00871; Acetate_kinase; 1. DR PIRSF; PIRSF036458; Butyrate_kin; 1. DR PRINTS; PR00471; ACETATEKNASE. DR TIGRFAMs; TIGR02707; butyr_kinase; 1. DR PROSITE; PS01075; ACETATE_KINASE_1; 1. DR PROSITE; PS01076; ACETATE_KINASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 375 Probable butyrate kinase 2. FT /FTId=PRO_0000107675. FT STRAND 3 9 {ECO:0000244|PDB:1SAZ}. FT STRAND 11 20 {ECO:0000244|PDB:1SAZ}. FT STRAND 23 31 {ECO:0000244|PDB:1SAZ}. FT HELIX 34 38 {ECO:0000244|PDB:1SAZ}. FT HELIX 43 46 {ECO:0000244|PDB:1SAZ}. FT HELIX 47 59 {ECO:0000244|PDB:1SAZ}. FT TURN 60 62 {ECO:0000244|PDB:1SAZ}. FT HELIX 65 67 {ECO:0000244|PDB:1SAZ}. FT STRAND 69 74 {ECO:0000244|PDB:1SAZ}. FT STRAND 83 87 {ECO:0000244|PDB:1SAZ}. FT HELIX 90 98 {ECO:0000244|PDB:1SAZ}. FT TURN 99 101 {ECO:0000244|PDB:1SAZ}. FT HELIX 107 120 {ECO:0000244|PDB:1SAZ}. FT STRAND 124 128 {ECO:0000244|PDB:1SAZ}. FT HELIX 137 139 {ECO:0000244|PDB:1SAZ}. FT STRAND 143 146 {ECO:0000244|PDB:1X9J}. FT HELIX 155 168 {ECO:0000244|PDB:1SAZ}. FT HELIX 173 175 {ECO:0000244|PDB:1SAZ}. FT STRAND 177 193 {ECO:0000244|PDB:1SAZ}. FT STRAND 196 200 {ECO:0000244|PDB:1SAZ}. FT HELIX 203 205 {ECO:0000244|PDB:1SAZ}. FT HELIX 220 227 {ECO:0000244|PDB:1SAZ}. FT HELIX 236 238 {ECO:0000244|PDB:1SAZ}. FT TURN 240 243 {ECO:0000244|PDB:1SAZ}. FT HELIX 247 251 {ECO:0000244|PDB:1SAZ}. FT HELIX 256 264 {ECO:0000244|PDB:1SAZ}. FT HELIX 268 291 {ECO:0000244|PDB:1SAZ}. FT TURN 292 294 {ECO:0000244|PDB:1SAZ}. FT STRAND 297 303 {ECO:0000244|PDB:1SAZ}. FT HELIX 304 307 {ECO:0000244|PDB:1SAZ}. FT TURN 309 311 {ECO:0000244|PDB:1SAZ}. FT HELIX 312 320 {ECO:0000244|PDB:1SAZ}. FT TURN 321 323 {ECO:0000244|PDB:1SAZ}. FT STRAND 326 331 {ECO:0000244|PDB:1SAZ}. FT HELIX 334 346 {ECO:0000244|PDB:1SAZ}. FT HELIX 355 369 {ECO:0000244|PDB:1SAZ}. FT HELIX 371 373 {ECO:0000244|PDB:1SAZ}. SQ SEQUENCE 375 AA; 42022 MW; E42C4887071D008D CRC64; MFRILTINPG STSTKLSIFE DERMVKMQNF SHSPDELGRF QKILDQLEFR EKIARQFVEE TGYSLSSFSA FVSRGGLLDP IPGGVYLVDG LMIKTLKSGK NGEHASNLGA IIAHRFSSET GVPAYVVDPV VVDEMEDVAR VSGHPNYQRK SIFHALNQKT VAKEVARMMN KRYEEMNLVV AHMGGGISIA AHRKGRVIDV NNALDGDGPF TPERSGTLPL TQLVDLCFSG KFTYEEMKKR IVGNGGLVAY LGTSDAREVV RRIKQGDEWA KRVYRAMAYQ IAKWIGKMAA VLKGEVDFIV LTGGLAHEKE FLVPWITKRV SFIAPVLVFP GSNEEKALAL SALRVLRGEE KPKNYSEESR RWRERYDSYL DGILR // ID BGLT_THEMA Reviewed; 415 AA. AC Q9X108; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=6-phospho-beta-glucosidase BglT; DE EC=3.2.1.86; GN Name=bglT; OrderedLocusNames=TM_1281; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP CHARACTERIZATION, AND REACTION MECHANISM. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=15237973; DOI=10.1021/ja047632w; RA Yip V.L.Y., Varrot A., Davies G.J., Rajan S.S., Yang X., Thompson J., RA Anderson W.F., Withers S.G.; RT "An unusual mechanism of glycoside hydrolysis involving redox and RT elimination steps by a family 4 beta-glycosidase from Thermotoga RT maritima."; RL J. Am. Chem. Soc. 126:8354-8355(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX RP WITH NAD(+) AND GLUCOSE-6-PHOSPHATE. RX PubMed=15670594; DOI=10.1016/j.jmb.2004.11.058; RA Varrot A., Yip V.L.Y., Li Y., Rajan S.S., Yang X., Anderson W.F., RA Thompson J., Withers S.G., Davies G.J.; RT "NAD(+) and metal-ion dependent hydrolysis by family 4 glycosidases: RT structural insight into specificity for phospho-beta-D-glucosides."; RL J. Mol. Biol. 346:423-435(2005). CC -!- FUNCTION: Hydrolyzes cellobiose 6'-phosphate into glucose 6- CC phosphate (Glc6P) and glucose. CC -!- CATALYTIC ACTIVITY: 6-phospho-beta-D-glucosyl-(1,4)-D-glucose + CC H(2)O = D-glucose + D-glucose 6-phosphate. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Note=Binds 1 NAD(+) per subunit.; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 1 Mn(2+) ion per subunit.; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=41 uM for p-nitrophenyl-beta-D-glucopyranoside 6-phosphate; CC pH dependence: CC Optimum pH is 8.0. Active from pH 6.5 to 10.; CC -!- SUBUNIT: Homodimer or homotetramer. Exists in a CC homodimer/homotetramer equilibrium state in solution. CC -!- MISCELLANEOUS: Is a retaining glucosidase as it hydrolyzes CC glycosidic bond with retention of anomeric configuration. Reaction CC mechanism includes redox steps involving NAD and stabilization of CC intermediates by Mn(2+). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36356.1; -; Genomic_DNA. DR PIR; E72273; E72273. DR RefSeq; NP_229086.1; NC_000853.1. DR RefSeq; WP_004079953.1; NZ_CP011107.1. DR PDB; 1UP4; X-ray; 2.85 A; A/B/C/D/E/F/G/H=1-415. DR PDB; 1UP6; X-ray; 2.55 A; A/B/C/D/E/F/G/H=1-415. DR PDB; 1UP7; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-415. DR PDBsum; 1UP4; -. DR PDBsum; 1UP6; -. DR PDBsum; 1UP7; -. DR ProteinModelPortal; Q9X108; -. DR SMR; Q9X108; 1-415. DR STRING; 243274.TM1281; -. DR CAZy; GH4; Glycoside Hydrolase Family 4. DR EnsemblBacteria; AAD36356; AAD36356; TM_1281. DR GeneID; 898202; -. DR KEGG; tma:TM1281; -. DR PATRIC; 23937500; VBITheMar51294_1296. DR eggNOG; ENOG4105F8D; Bacteria. DR eggNOG; COG1486; LUCA. DR InParanoid; Q9X108; -. DR KO; K01222; -. DR OMA; WINEYLY; -. DR OrthoDB; EOG6CP3SG; -. DR BRENDA; 3.2.1.86; 6331. DR SABIO-RK; Q9X108; -. DR EvolutionaryTrace; Q9X108; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR InterPro; IPR019802; GlycHydrolase_4_CS. DR InterPro; IPR001088; Glyco_hydro_4. DR InterPro; IPR022616; Glyco_hydro_4_C. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF02056; Glyco_hydro_4; 1. DR Pfam; PF11975; Glyco_hydro_4C; 1. DR PRINTS; PR00732; GLHYDRLASE4. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF56327; SSF56327; 1. DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Complete proteome; Glycosidase; KW Hydrolase; Manganese; Metal-binding; NAD; Reference proteome. FT CHAIN 1 415 6-phospho-beta-glucosidase BglT. FT /FTId=PRO_0000169857. FT NP_BIND 1 64 NAD. FT ACT_SITE 241 241 Proton acceptor. FT METAL 162 162 Manganese. FT METAL 192 192 Manganese. FT BINDING 87 87 Substrate. FT BINDING 140 140 Substrate. FT BINDING 163 163 Substrate. FT BINDING 261 261 Substrate. FT SITE 103 103 Increases basicity of active site Tyr. FT {ECO:0000250}. FT STRAND 2 7 {ECO:0000244|PDB:1UP7}. FT HELIX 13 23 {ECO:0000244|PDB:1UP7}. FT TURN 24 26 {ECO:0000244|PDB:1UP7}. FT STRAND 31 35 {ECO:0000244|PDB:1UP7}. FT HELIX 39 53 {ECO:0000244|PDB:1UP7}. FT STRAND 56 61 {ECO:0000244|PDB:1UP7}. FT HELIX 65 69 {ECO:0000244|PDB:1UP7}. FT STRAND 73 77 {ECO:0000244|PDB:1UP7}. FT HELIX 83 92 {ECO:0000244|PDB:1UP7}. FT HELIX 93 97 {ECO:0000244|PDB:1UP7}. FT STRAND 103 105 {ECO:0000244|PDB:1UP7}. FT HELIX 107 129 {ECO:0000244|PDB:1UP7}. FT STRAND 134 137 {ECO:0000244|PDB:1UP7}. FT STRAND 139 141 {ECO:0000244|PDB:1UP7}. FT HELIX 142 151 {ECO:0000244|PDB:1UP7}. FT STRAND 156 160 {ECO:0000244|PDB:1UP7}. FT HELIX 164 175 {ECO:0000244|PDB:1UP7}. FT HELIX 180 182 {ECO:0000244|PDB:1UP7}. FT STRAND 183 190 {ECO:0000244|PDB:1UP7}. FT STRAND 193 201 {ECO:0000244|PDB:1UP7}. FT HELIX 207 214 {ECO:0000244|PDB:1UP7}. FT HELIX 228 234 {ECO:0000244|PDB:1UP7}. FT STRAND 236 238 {ECO:0000244|PDB:1UP7}. FT HELIX 240 242 {ECO:0000244|PDB:1UP7}. FT HELIX 243 246 {ECO:0000244|PDB:1UP7}. FT HELIX 248 256 {ECO:0000244|PDB:1UP7}. FT HELIX 261 276 {ECO:0000244|PDB:1UP7}. FT HELIX 284 288 {ECO:0000244|PDB:1UP7}. FT TURN 290 293 {ECO:0000244|PDB:1UP7}. FT HELIX 294 306 {ECO:0000244|PDB:1UP7}. FT STRAND 307 309 {ECO:0000244|PDB:1UP7}. FT STRAND 311 318 {ECO:0000244|PDB:1UP7}. FT STRAND 331 339 {ECO:0000244|PDB:1UP7}. FT STRAND 342 346 {ECO:0000244|PDB:1UP7}. FT HELIX 353 374 {ECO:0000244|PDB:1UP7}. FT HELIX 378 387 {ECO:0000244|PDB:1UP7}. FT HELIX 394 407 {ECO:0000244|PDB:1UP7}. FT TURN 408 411 {ECO:0000244|PDB:1UP7}. SQ SEQUENCE 415 AA; 47627 MW; FB4E3B358245BFEE CRC64; MRIAVIGGGS SYTPELVKGL LDISEDVRID EVIFYDIDEE KQKIVVDFVK RLVKDRFKVL ISDTFEGAVV DAKYVIFQFR PGGLKGREND EGIPLKYGLI GQETTGVGGF SAALRAFPIV EEYVDTVRKT SNATIVNFTN PSGHITEFVR NYLEYEKFIG LCNVPINFIR EIAEMFSARL EDVFLKYYGL NHLSFIEKVF VKGEDVTEKV FENLKLKLSN IPDEDFPTWF YDSVRLIVNP YLRYYLMEKK MFKKISTHEL RAREVMKIEK ELFEKYRTAV EIPEELTKRG GSMYSTAAAH LIRDLETDEG KIHIVNTRNN GSIENLPDDY VLEIPCYVRS GRVHTLSQGK GDHFALSFIH AVKMYERLTI EAYLKRSKKL ALKALLSHPL GPDVEDAKDL LEEILEANRE YVKLG // ID CAH_THEMA Reviewed; 325 AA. AC Q9WXT2; G4FGZ2; DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Cephalosporin-C deacetylase {ECO:0000305}; DE EC=3.1.1.41 {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095}; DE AltName: Full=Acetylxylan esterase; DE EC=3.1.1.72 {ECO:0000269|PubMed:21255309}; GN Name=axeA {ECO:0000303|PubMed:21255309}; OrderedLocusNames=TM_0077; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000269|PubMed:21255309}; RX PubMed=21255309; DOI=10.1111/j.1751-7915.2009.00150.x; RA Drzewiecki K., Angelov A., Ballschmiter M., Tiefenbach K.J., RA Sterner R., Liebl W.; RT "Hyperthermostable acetyl xylan esterase."; RL Microb. Biotechnol. 3:84-92(2010). RN [3] {ECO:0000305} RP FUNCTION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF GLN-88; TYR-92; TRP-102; TRP-105; TRP-124; SER-188; RP PHE-213; PRO-228 AND ILE-276. RX PubMed=22659119; DOI=10.1016/j.bbapap.2012.05.009; RA Hedge M.K., Gehring A.M., Adkins C.T., Weston L.A., Lavis L.D., RA Johnson R.J.; RT "The structural basis for the narrow substrate specificity of an RT acetyl esterase from Thermotoga maritima."; RL Biochim. Biophys. Acta 1824:1024-1030(2012). RN [4] {ECO:0000305, ECO:0000312|PDB:3M83} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH PMSF AND RP DIETHYL PHOSPHONATE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000269|PubMed:22411095}; RX PubMed=22411095; DOI=10.1002/prot.24041; RA Levisson M., Han G.W., Deller M.C., Xu Q., Biely P., Hendriks S., RA Ten Eyck L.F., Flensburg C., Roversi P., Miller M.D., McMullan D., RA von Delft F., Kreusch A., Deacon A.M., van der Oost J., Lesley S.A., RA Elsliger M.A., Kengen S.W., Wilson I.A.; RT "Functional and structural characterization of a thermostable acetyl RT esterase from Thermotoga maritima."; RL Proteins 80:1545-1559(2012). CC -!- FUNCTION: Esterase that removes acetyl groups from a number of O- CC acetylated small substrates, such as acetylated xylose, short CC xylo-oligosaccharides and cephalosporin C. Has no activity towards CC polymeric acetylated xylan, 4-methylumbelliferyl acetate or alpha- CC naphthyl acetate. Able to catalyze rapid hydrolysis of a range of CC substrates preferably with acetate groups, independent of the CC alcohol moiety. Exhibits a narrow selectivity for short chain acyl CC esters (C2-C3). Displays broad substrate specificity by CC hydrolyzing acetate at 2, 3, and 4 positions of 4-nitrophenyl- CC beta-D-xylopyranoside (pNP-Xyl) with similar efficiency. Cannot CC cleave amide linkages. {ECO:0000269|PubMed:21255309, CC ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}. CC -!- CATALYTIC ACTIVITY: Deacetylation of xylans and xylo- CC oligosaccharides. {ECO:0000269|PubMed:21255309, CC ECO:0000269|PubMed:22411095}. CC -!- CATALYTIC ACTIVITY: Cephalosporin C + H(2)O = CC deacetylcephalosporin C + acetate. {ECO:0000269|PubMed:21255309, CC ECO:0000269|PubMed:22411095}. CC -!- ENZYME REGULATION: Activity stimulated by up to 40% in the CC presence of divalent cations such as BaCl(2), CaCl(2), MgCl(2) and CC MnCl(2) at 3 mM concentration, but inhibited by 82-85% in the CC presence of CdCl(2) and ZnCl(2) at 3 mM concentration. CC {ECO:0000269|PubMed:21255309}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.12 mM for p-nitrophenyl-acetate CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=6.05 mM for glucose penta-acetate CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=4.18 mM for cephalosporin-C {ECO:0000269|PubMed:21255309, CC ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; CC KM=20.8 mM for 7-aminocephalosporonic acid (7-ACA) CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=760 uM for p-nitrophenyl acetate CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=3.7 uM for fluoroscein di(acetoxymethyl) ether CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=0.97 uM for fluoroscein dipropyloxymethyl ether CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=0.41 uM for fluoroscein dibutyloxymethyl ether CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=1.0 uM for fluoroscein divaleryloxymethyl ether CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=2.6 uM for fluoroscein dicaproyloxymethyl ether CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=0.51 uM for fluoroscein dimethacryloxymethyl ether CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=0.96 uM for fluoroscein dicyclobutylcarboxymethyl ether CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=0.54 uM for fluoroscein dimethylcyclopropanecarboxymethyl CC ether {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=0.185 mM for p-nitrophenyl-acetate CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=0.137 mM for p-nitrophenyl-propionate CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC KM=3.6 mM for 2-O-acetyl-pNP-Xyl {ECO:0000269|PubMed:21255309, CC ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; CC KM=4.2 mM for 3-O-acetyl-pNP-Xyl {ECO:0000269|PubMed:21255309, CC ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; CC KM=4.0 mM for 4-O-acetyl-pNP-Xyl {ECO:0000269|PubMed:21255309, CC ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; CC Vmax=113.5 umol/min/mg enzyme with pNP-acetate as substrate CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC Vmax=366.8 umol/min/mg enzyme with glucose penta-acetate as CC substrate {ECO:0000269|PubMed:21255309, CC ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; CC Vmax=19.2 umol/min/mg enzyme with cephalosporin-C as substrate CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC pH dependence: CC Optimum pH is 6.5. Half-maximal activity between pH 5.0-7.5. CC {ECO:0000269|PubMed:21255309, ECO:0000269|PubMed:22411095, CC ECO:0000269|PubMed:22659119}; CC Temperature dependence: CC Optimum temperature is 90 degrees Celsius. Activity drops CC sharply above 90 degrees Celsius. Stable up to 100-104 degrees CC Celsius. {ECO:0000269|PubMed:21255309, CC ECO:0000269|PubMed:22411095, ECO:0000269|PubMed:22659119}; CC -!- SUBUNIT: Homohexamer, formed by a trimer of dimers. Also exists as CC a homodimer. {ECO:0000269|PubMed:21255309, CC ECO:0000269|PubMed:22411095}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P94388}. CC -!- SIMILARITY: Belongs to the carbohydrate esterase 7 family. CC {ECO:0000255}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35171.1; -; Genomic_DNA. DR PIR; E72421; E72421. DR RefSeq; NP_227893.1; NC_000853.1. DR RefSeq; WP_004082599.1; NZ_CP011107.1. DR PDB; 1VLQ; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-325. DR PDB; 3M81; X-ray; 2.50 A; A/B/C/D/E/F=1-325. DR PDB; 3M82; X-ray; 2.40 A; A/B/C/D/E/F=1-325. DR PDB; 3M83; X-ray; 2.12 A; A/B/C/D/E/F=1-325. DR PDBsum; 1VLQ; -. DR PDBsum; 3M81; -. DR PDBsum; 3M82; -. DR PDBsum; 3M83; -. DR ProteinModelPortal; Q9WXT2; -. DR SMR; Q9WXT2; 2-323. DR STRING; 243274.TM0077; -. DR ESTHER; thema-TM0077; Acetyl-esterase_deacetylase. DR EnsemblBacteria; AAD35171; AAD35171; TM_0077. DR GeneID; 896903; -. DR KEGG; tma:TM0077; -. DR PATRIC; 23934994; VBITheMar51294_0075. DR eggNOG; ENOG4105I82; Bacteria. DR eggNOG; COG3458; LUCA. DR InParanoid; Q9WXT2; -. DR KO; K01060; -. DR OMA; NWALHGY; -. DR OrthoDB; EOG6CZQPN; -. DR BioCyc; TMAR243274:GC6P-77-MONOMER; -. DR EvolutionaryTrace; Q9WXT2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046555; F:acetylxylan esterase activity; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0047739; F:cephalosporin-C deacetylase activity; IDA:UniProtKB. DR GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR GO; GO:0008152; P:metabolic process; IDA:UniProtKB. DR GO; GO:0005976; P:polysaccharide metabolic process; IDA:UniProtKB. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR008391; AXE1_dom. DR Pfam; PF05448; AXE1; 1. DR SUPFAM; SSF53474; SSF53474; 2. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Carbohydrate metabolism; Cellulose degradation; KW Complete proteome; Cytoplasm; Hydrolase; Metal-binding; KW Polysaccharide degradation; Reference proteome; Serine esterase. FT CHAIN 1 325 Cephalosporin-C deacetylase. FT /FTId=PRO_0000419766. FT ACT_SITE 188 188 Nucleophile. FT {ECO:0000269|PubMed:22411095}. FT ACT_SITE 274 274 Charge relay system. FT {ECO:0000250|UniProtKB:P94388}. FT ACT_SITE 303 303 Charge relay system. FT {ECO:0000250|UniProtKB:P94388}. FT BINDING 92 92 Substrate; via amide nitrogen. FT {ECO:0000250|UniProtKB:P94388}. FT BINDING 188 188 Inhibitor. {ECO:0000269|PubMed:22411095}. FT BINDING 188 188 Inhibitor (covalent). FT {ECO:0000269|PubMed:22411095}. FT MUTAGEN 88 88 Q->A: Minimal change in catalytic FT efficiency toward acetate substrates. FT {ECO:0000269|PubMed:22659119}. FT MUTAGEN 92 92 Y->A: Reduction in catalytic efficiency FT towards fluoroscein diacetoxymethyl FT ether; when associated with A-228. FT {ECO:0000269|PubMed:22659119}. FT MUTAGEN 102 102 W->A: Minimal change in catalytic FT efficiency toward the acetate substrates. FT {ECO:0000269|PubMed:22659119}. FT MUTAGEN 105 105 W->A: Minimal change in catalytic FT efficiency toward the acetate substrates. FT {ECO:0000269|PubMed:22659119}. FT MUTAGEN 124 124 W->A: Minimal change in catalytic FT efficiency toward the acetate substrates. FT {ECO:0000269|PubMed:22659119}. FT MUTAGEN 188 188 S->A: Activity abolished towards FT fluoroscein diacetoxymethyl ether. FT {ECO:0000269|PubMed:22659119}. FT MUTAGEN 213 213 F->A: Reduction in catalytic efficiency FT towards fluoroscein diacetoxymethyl FT ether; when associated with A-228. FT {ECO:0000269|PubMed:22659119}. FT MUTAGEN 228 228 P->A: Reduces catalytic activity by 33- FT fold against fluoroscein diacetoxymethyl FT ether; 8-fold decrease in activity FT against dimethacryloxymethyl ether; 4- FT fold increase in catalytic efficiency FT toward dicyclobutylcarboxymethyl ether. FT Reduction in catalytic efficiency towards FT fluoroscein diacetoxymethyl ether; when FT associated with A-92; A-213 or A-276. FT {ECO:0000269|PubMed:22659119}. FT MUTAGEN 276 276 I->A: Greater than 10-fold reduction in FT catalytic efficiency toward the acetate FT substrates. Reduction in catalytic FT efficiency towards fluoroscein FT diacetoxymethyl ether; when associated FT with A-228. FT {ECO:0000269|PubMed:22659119}. FT HELIX 8 11 {ECO:0000244|PDB:1VLQ}. FT HELIX 24 36 {ECO:0000244|PDB:1VLQ}. FT STRAND 43 46 {ECO:0000244|PDB:1VLQ}. FT STRAND 52 62 {ECO:0000244|PDB:1VLQ}. FT HELIX 64 66 {ECO:0000244|PDB:1VLQ}. FT STRAND 68 76 {ECO:0000244|PDB:1VLQ}. FT STRAND 81 88 {ECO:0000244|PDB:1VLQ}. FT HELIX 99 102 {ECO:0000244|PDB:1VLQ}. FT HELIX 104 107 {ECO:0000244|PDB:1VLQ}. FT STRAND 111 115 {ECO:0000244|PDB:1VLQ}. FT STRAND 123 125 {ECO:0000244|PDB:1VLQ}. FT STRAND 134 137 {ECO:0000244|PDB:1VLQ}. FT STRAND 142 144 {ECO:0000244|PDB:1VLQ}. FT TURN 145 150 {ECO:0000244|PDB:1VLQ}. FT TURN 152 154 {ECO:0000244|PDB:1VLQ}. FT HELIX 156 172 {ECO:0000244|PDB:1VLQ}. FT STRAND 177 187 {ECO:0000244|PDB:1VLQ}. FT HELIX 189 200 {ECO:0000244|PDB:1VLQ}. FT STRAND 206 211 {ECO:0000244|PDB:1VLQ}. FT HELIX 217 223 {ECO:0000244|PDB:1VLQ}. FT HELIX 229 238 {ECO:0000244|PDB:1VLQ}. FT HELIX 243 251 {ECO:0000244|PDB:1VLQ}. FT HELIX 255 259 {ECO:0000244|PDB:1VLQ}. FT STRAND 266 271 {ECO:0000244|PDB:1VLQ}. FT STRAND 275 277 {ECO:0000244|PDB:1VLQ}. FT HELIX 279 288 {ECO:0000244|PDB:1VLQ}. FT STRAND 291 298 {ECO:0000244|PDB:1VLQ}. FT TURN 303 306 {ECO:0000244|PDB:1VLQ}. FT HELIX 307 322 {ECO:0000244|PDB:1VLQ}. SQ SEQUENCE 325 AA; 37156 MW; AF2879D86680A3C4 CRC64; MAFFDLPLEE LKKYRPERYE EKDFDEFWEE TLAESEKFPL DPVFERMESH LKTVEAYDVT FSGYRGQRIK GWLLVPKLEE EKLPCVVQYI GYNGGRGFPH DWLFWPSMGY ICFVMDTRGQ GSGWLKGDTP DYPEGPVDPQ YPGFMTRGIL DPRTYYYRRV FTDAVRAVEA AASFPQVDQE RIVIAGGSQG GGIALAVSAL SKKAKALLCD VPFLCHFRRA VQLVDTHPYA EITNFLKTHR DKEEIVFRTL SYFDGVNFAA RAKIPALFSV GLMDNICPPS TVFAAYNYYA GPKEIRIYPY NNHEGGGSFQ AVEQVKFLKK LFEKG // ID BIOY_THEMA Reviewed; 169 AA. AC Q9WZQ6; G4FD25; DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 73. DE RecName: Full=Biotin transporter BioY; DE AltName: Full=Biotin ECF transporter S component BioY; GN Name=bioY; OrderedLocusNames=TM_0799; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROBABLE FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR RP LOCATION, AND EXPRESSION IN E.COLI. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23359690; DOI=10.1073/pnas.1217361110; RA Karpowich N.K., Wang D.N.; RT "Assembly and mechanism of a group II ECF transporter."; RL Proc. Natl. Acad. Sci. U.S.A. 110:2534-2539(2013). CC -!- FUNCTION: Substrate-binding (S) component of an energy-coupling CC factor (ECF) ABC-transporter complex. Probably a biotin-binding CC protein that interacts with the energy-coupling factor (ECF) ABC- CC transporter complex. Unlike classic ABC transporters this ECF CC transporter provides the energy necessary to transport a number of CC different substrates. The substrates themselves are bound by CC transmembrane, not extracytoplasmic soluble proteins (Probable). CC {ECO:0000305}. CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter CC complex composed of 2 membrane-embedded substrate-binding proteins CC (S component, RibU, BioY), 2 ATP-binding proteins (A component) CC and 2 transmembrane proteins (T component) upon coexpression in CC E.coli. A stable subcomplex with both A and T components are also CC isolated. This complex interacts with at least 2 substrate- CC specific components, BioY and RibU. {ECO:0000269|PubMed:23359690}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000305|PubMed:23359690}; Multi-pass membrane protein CC {ECO:0000305|PubMed:23359690}. CC -!- SIMILARITY: Belongs to the BioY family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35881.1; -; Genomic_DNA. DR PIR; H72334; H72334. DR RefSeq; NP_228608.1; NC_000853.1. DR RefSeq; WP_004080866.1; NZ_CP011107.1. DR STRING; 243274.TM0799; -. DR TCDB; 3.A.1.25.5; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35881; AAD35881; TM_0799. DR GeneID; 898467; -. DR KEGG; tma:TM0799; -. DR PATRIC; 23936518; VBITheMar51294_0811. DR eggNOG; ENOG4105VKD; Bacteria. DR eggNOG; COG1268; LUCA. DR InParanoid; Q9WZQ6; -. DR KO; K03523; -. DR OMA; LMWLASA; -. DR OrthoDB; EOG6PKFJK; -. DR BioCyc; TMAR243274:GC6P-826-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015225; F:biotin transporter activity; IEA:InterPro. DR InterPro; IPR003784; BioY. DR Pfam; PF02632; BioY; 1. DR PIRSF; PIRSF016661; BioY; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 169 Biotin transporter BioY. FT /FTId=PRO_0000422263. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 47 67 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT TRANSMEM 106 126 Helical. {ECO:0000255}. FT TRANSMEM 139 159 Helical. {ECO:0000255}. SQ SEQUENCE 169 AA; 18235 MW; C99E94F178266729 CRC64; MRQLIKAGIF TALIVVGAWI SIPLGPVPFT LQVFFVFLSA YVLGKKYGTL AVATYVLLGA MGLPVFANFK GGAQVLVGPT GGYLFGFILG AFVIGLLAEK KESFAWYLAS GVAGLGIIYA LGVFVLNFYV HDIRKAISVG FVPFVWFDLI KLVVAALIAL RLKKLEVER // ID CAS1_THEMA Reviewed; 319 AA. AC Q9X2B7; G4FGI5; DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=CRISPR-associated endonuclease Cas1; DE EC=3.1.-.-; GN Name=cas1; OrderedLocusNames=TM_1797; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), AND SUBUNIT. RA Beloglazova N., Skarina T., Petit P., Flick R., Brown G., RA Savchenko A., Yakunin A.F.; RT "Crystal structure and nuclease activity of TM1797, a Cas1 protein RT from Thermotoga maritima."; RL Submitted (JAN-2010) to the PDB data bank. CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat), is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC sequences complementary to antecedent mobile elements and target CC invading nucleic acids. CRISPR clusters are transcribed and CC processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. CC Involved in the integration of spacer DNA into the CRISPR cassette CC (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer (Probable). Forms a heterotetramer with a Cas2 CC homodimer (By similarity). {ECO:0000250, ECO:0000305}. CC -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36860.1; -; Genomic_DNA. DR PIR; B72210; B72210. DR RefSeq; NP_229594.1; NC_000853.1. DR RefSeq; WP_004082344.1; NZ_CP011107.1. DR PDB; 4XTK; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-319. DR PDBsum; 4XTK; -. DR ProteinModelPortal; Q9X2B7; -. DR STRING; 243274.TM1797; -. DR EnsemblBacteria; AAD36860; AAD36860; TM_1797. DR GeneID; 897836; -. DR KEGG; tma:TM1797; -. DR PATRIC; 23938583; VBITheMar51294_1818. DR eggNOG; ENOG4105DYN; Bacteria. DR eggNOG; COG1518; LUCA. DR InParanoid; Q9X2B7; -. DR KO; K15342; -. DR OMA; IMFETDE; -. DR OrthoDB; EOG66MQRM; -. DR BioCyc; TMAR243274:GC6P-1848-MONOMER; -. DR EvolutionaryTrace; Q9X2B7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-HAMAP. DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01470; Cas1; 1. DR InterPro; IPR002729; CRISPR-assoc_Cas1. DR InterPro; IPR019858; CRISPR-assoc_Cas1_HMARI/TNEAP. DR Pfam; PF01867; Cas_Cas1; 1. DR TIGRFAMs; TIGR00287; cas1; 1. DR TIGRFAMs; TIGR03641; cas1_HMARI; 1. PE 1: Evidence at protein level; KW 3D-structure; Antiviral defense; Complete proteome; DNA-binding; KW Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding; KW Nuclease; Reference proteome. FT CHAIN 1 319 CRISPR-associated endonuclease Cas1. FT /FTId=PRO_0000417089. FT METAL 148 148 Manganese or magnesium. {ECO:0000250}. FT METAL 214 214 Manganese or magnesium. {ECO:0000250}. FT METAL 229 229 Manganese or magnesium. {ECO:0000250}. FT STRAND 2 6 {ECO:0000244|PDB:4XTK}. FT STRAND 10 14 {ECO:0000244|PDB:4XTK}. FT STRAND 16 22 {ECO:0000244|PDB:4XTK}. FT STRAND 27 30 {ECO:0000244|PDB:4XTK}. FT STRAND 35 40 {ECO:0000244|PDB:4XTK}. FT STRAND 44 47 {ECO:0000244|PDB:4XTK}. FT HELIX 48 56 {ECO:0000244|PDB:4XTK}. FT STRAND 61 64 {ECO:0000244|PDB:4XTK}. FT STRAND 70 76 {ECO:0000244|PDB:4XTK}. FT HELIX 83 94 {ECO:0000244|PDB:4XTK}. FT HELIX 96 120 {ECO:0000244|PDB:4XTK}. FT HELIX 129 137 {ECO:0000244|PDB:4XTK}. FT HELIX 141 160 {ECO:0000244|PDB:4XTK}. FT HELIX 166 168 {ECO:0000244|PDB:4XTK}. FT HELIX 181 201 {ECO:0000244|PDB:4XTK}. FT STRAND 212 214 {ECO:0000244|PDB:4XTK}. FT HELIX 223 231 {ECO:0000244|PDB:4XTK}. FT TURN 232 235 {ECO:0000244|PDB:4XTK}. FT HELIX 236 245 {ECO:0000244|PDB:4XTK}. FT HELIX 251 253 {ECO:0000244|PDB:4XTK}. FT HELIX 265 279 {ECO:0000244|PDB:4XTK}. FT TURN 286 289 {ECO:0000244|PDB:4XTK}. FT HELIX 294 309 {ECO:0000244|PDB:4XTK}. SQ SEQUENCE 319 AA; 37705 MW; 8507C7996A0B4CA7 CRC64; MESVYLFSSG TLKRKANTIC LETESGRKYI PVENVMDIKV FGEVDLNKRF LEFLSQKRIP IHFFNREGYY VGTFYPREYL NSGFLILKQA EHYINQEKRM LIAREIVSRS FQNMVDFLKK RKVRADSLTR YKKKAEEASN VSELMGIEGN AREEYYSMID SLVSDERFRI EKRTRRPPKN FANTLISFGN SLLYTTVLSL IYQTHLDPRI GYLHETNFRR FSLNLDIAEL FKPAVVDRLF LNLVNTRQIN EKHFDEISEG LMLNDEGKSL FVKNYEQALR ETVFHKKLNR YVSMRSLIKM ELHKLEKHLI GEQVFGSEE // ID BSUHB_THEMA Reviewed; 256 AA. AC O33832; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 11-MAY-2016, entry version 117. DE RecName: Full=Fructose-1,6-bisphosphatase/inositol-1-monophosphatase; DE Short=FBPase/IMPase; DE EC=3.1.3.11 {ECO:0000269|PubMed:11062561}; DE EC=3.1.3.25 {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}; DE AltName: Full=Inositol-1-phosphatase; DE Short=I-1-Pase; GN Name=suhB; OrderedLocusNames=TM_1415; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9720201; DOI=10.1007/s002530051256; RA Liebl W., Brem D., Gotschlich A.; RT "Analysis of the gene for beta-fructosidase (invertase, inulinase) of RT the hyperthermophilic bacterium Thermotoga maritima, and RT characterisation of the enzyme expressed in Escherichia coli."; RL Appl. Microbiol. Biotechnol. 50:55-64(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP FUNCTION AS IMPASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT. RX PubMed=10508089; RA Chen L., Roberts M.F.; RT "Characterization of a tetrameric inositol monophosphatase from the RT hyperthermophilic bacterium Thermotoga maritima."; RL Appl. Environ. Microbiol. 65:4559-4567(1999). RN [4] RP FUNCTION AS BOTH FBPASE AND IMPASE, CATALYTIC ACTIVITY, AND KINETIC RP PARAMETERS. RX PubMed=11062561; DOI=10.1038/80968; RA Stec B., Yang H., Johnson K.A., Chen L., Roberts M.F.; RT "MJ0109 is an enzyme that is both an inositol monophosphatase and the RT 'missing' archaeal fructose-1,6-bisphosphatase."; RL Nat. Struct. Biol. 7:1046-1050(2000). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MAGNESIUM. RX PubMed=17419729; DOI=10.1111/j.0014-2956.2007.05779.x; RA Stieglitz K.A., Roberts M.F., Li W., Stec B.; RT "Crystal structure of the tetrameric inositol 1-phosphate phosphatase RT (TM1415) from the hyperthermophile, Thermotoga maritima."; RL FEBS J. 274:2461-2469(2007). CC -!- FUNCTION: Phosphatase with broad specificity; it can CC dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of CC inositol-1-phosphate (I-1-P) but displaying a 20-fold higher rate CC of hydrolysis of D-I-1-P than of the L isomer, 2'-AMP, pNPP, CC inositol-2-phosphate, beta-glycerol phosphate, and alpha-D- CC glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, CC fructose-6-phosphate, 5'-AMP and NAD(+). May be involved in the CC biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate. CC {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}. CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D- CC fructose 6-phosphate + phosphate. {ECO:0000269|PubMed:11062561}. CC -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol CC + phosphate. {ECO:0000269|PubMed:10508089, CC ECO:0000269|PubMed:11062561}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:10508089}; CC -!- ENZYME REGULATION: In contrast to mammalian I-1-P phosphatases, is CC only weakly inhibited by Li(+), since 50% inhibitory concentration CC for Li(+) is about 100 mM, and the Li(+) concentration required to CC totally abolish I-1-Pase activity is 1 M. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.145 mM for DL-inositol-1-phosphate (at 95 degrees Celsius) CC {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}; CC KM=0.126 mM for D-inositol-1-phosphate (at 95 degrees Celsius) CC {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}; CC KM=0.460 mM for inositol-2-phosphate (at 95 degrees Celsius) CC {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}; CC Vmax=443 umol/min/mg enzyme with D-inositol-1-phosphate as CC substrate (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089, CC ECO:0000269|PubMed:11062561}; CC Vmax=23 umol/min/mg enzyme with L-inositol-1-phosphate as CC substrate (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089, CC ECO:0000269|PubMed:11062561}; CC Vmax=5.8 umol/min/mg enzyme with inositol-2-phosphate as CC substrate (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089, CC ECO:0000269|PubMed:11062561}; CC Note=kcat is 207 sec(-1) for IMPase activity (at 95 degrees CC Celsius) and 268 sec(-1) for FBPase activity (at 95 degrees CC Celsius). {ECO:0000269|PubMed:11062561}; CC Temperature dependence: CC Thermostable. No loss of IMPase activity after incubation at 85 CC degrees Celsius for 30 minutes. Heating at 100 degrees Celsius CC for 10 minutes results in a loss of about 20 to 25% of the CC activity, and 30 minutes at this temperature inactivate about CC 70% of the activity. {ECO:0000269|PubMed:10508089}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10508089, CC ECO:0000269|PubMed:17419729}. CC -!- SIMILARITY: Belongs to the inositol monophosphatase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD36486.1; Type=Frameshift; Positions=22; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ001073; CAA04517.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36486.1; ALT_FRAME; Genomic_DNA. DR PIR; E72255; E72255. DR PIR; T50642; T50642. DR RefSeq; NP_229216.1; NC_000853.1. DR RefSeq; WP_004081652.1; NZ_CP011107.1. DR PDB; 2P3N; X-ray; 2.20 A; A/B/C/D=1-256. DR PDB; 2P3V; X-ray; 2.40 A; A/B/C/D=1-256. DR PDBsum; 2P3N; -. DR PDBsum; 2P3V; -. DR ProteinModelPortal; O33832; -. DR SMR; O33832; 1-256. DR STRING; 243274.TM1415; -. DR EnsemblBacteria; AAD36486; AAD36486; TM_1415. DR GeneID; 898061; -. DR KEGG; tma:TM1415; -. DR PATRIC; 23937774; VBITheMar51294_1426. DR eggNOG; ENOG4105ECY; Bacteria. DR eggNOG; COG0483; LUCA. DR InParanoid; O33832; -. DR KO; K01092; -. DR OMA; HGYPFFA; -. DR OrthoDB; EOG6QK4W4; -. DR BioCyc; MetaCyc:MONOMER-5063; -. DR BioCyc; TMAR243274:GC6P-1452-MONOMER; -. DR BRENDA; 3.1.3.25; 6331. DR UniPathway; UPA00138; -. DR EvolutionaryTrace; O33832; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central. DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central. DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central. DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR InterPro; IPR020583; Inositol_monoP_metal-BS. DR InterPro; IPR000760; Inositol_monophosphatase. DR InterPro; IPR020550; Inositol_monophosphatase_CS. DR PANTHER; PTHR20854; PTHR20854; 1. DR Pfam; PF00459; Inositol_P; 1. DR PRINTS; PR00377; IMPHPHTASES. DR PROSITE; PS00629; IMP_1; 1. DR PROSITE; PS00630; IMP_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Complete proteome; KW Gluconeogenesis; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 256 Fructose-1,6-bisphosphatase/inositol-1- FT monophosphatase. FT /FTId=PRO_0000142574. FT REGION 82 84 Substrate binding. {ECO:0000250}. FT METAL 65 65 Magnesium 1. FT {ECO:0000269|PubMed:17419729}. FT METAL 79 79 Magnesium 1. FT {ECO:0000269|PubMed:17419729}. FT METAL 79 79 Magnesium 2. {ECO:0000250}. FT METAL 81 81 Magnesium 1; via carbonyl oxygen. FT {ECO:0000269|PubMed:17419729}. FT METAL 82 82 Magnesium 2. {ECO:0000250}. FT METAL 201 201 Magnesium 2. {ECO:0000250}. FT BINDING 172 172 Substrate. {ECO:0000250}. FT BINDING 177 177 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 196 196 Substrate. {ECO:0000250}. FT HELIX 2 21 {ECO:0000244|PDB:2P3N}. FT STRAND 29 38 {ECO:0000244|PDB:2P3N}. FT HELIX 40 56 {ECO:0000244|PDB:2P3N}. FT STRAND 61 67 {ECO:0000244|PDB:2P3N}. FT STRAND 73 82 {ECO:0000244|PDB:2P3N}. FT HELIX 84 89 {ECO:0000244|PDB:2P3N}. FT STRAND 95 102 {ECO:0000244|PDB:2P3N}. FT STRAND 105 113 {ECO:0000244|PDB:2P3N}. FT TURN 114 117 {ECO:0000244|PDB:2P3N}. FT STRAND 118 123 {ECO:0000244|PDB:2P3N}. FT TURN 124 126 {ECO:0000244|PDB:2P3N}. FT STRAND 127 130 {ECO:0000244|PDB:2P3N}. FT STRAND 133 135 {ECO:0000244|PDB:2P3V}. FT HELIX 143 145 {ECO:0000244|PDB:2P3N}. FT STRAND 147 150 {ECO:0000244|PDB:2P3N}. FT HELIX 156 164 {ECO:0000244|PDB:2P3N}. FT TURN 165 167 {ECO:0000244|PDB:2P3N}. FT STRAND 168 173 {ECO:0000244|PDB:2P3N}. FT HELIX 177 185 {ECO:0000244|PDB:2P3N}. FT STRAND 190 196 {ECO:0000244|PDB:2P3N}. FT HELIX 199 211 {ECO:0000244|PDB:2P3N}. FT STRAND 215 217 {ECO:0000244|PDB:2P3N}. FT STRAND 221 223 {ECO:0000244|PDB:2P3N}. FT STRAND 229 234 {ECO:0000244|PDB:2P3N}. FT STRAND 236 238 {ECO:0000244|PDB:2P3N}. FT HELIX 239 253 {ECO:0000244|PDB:2P3N}. SQ SEQUENCE 256 AA; 28647 MW; 550C15FEEA50B8DC CRC64; MDRLDFSIKL LRKVGHLLMI HWGRVDNVEK KTGFKDIVTE IDREAQRMIV DEIRKFFPDE NIMAEEGIFE KGDRLWIIDP IDGTINFVHG LPNFSISLAY VENGEVKLGV VHAPALNETL YAEEGSGAFF NGERIRVSEN ASLEECVGST GSYVDFTGKF IERMEKRTRR IRILGSAALN AAYVGAGRVD FFVTWRINPW DIAAGLIIVK EAGGMVTDFS GKEANAFSKN FIFSNGLIHD EVVKVVNEVV EEIGGK // ID CAS2_THEMA Reviewed; 87 AA. AC Q9X2B6; DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=CRISPR-associated endoribonuclease Cas2; DE EC=3.1.-.-; GN Name=cas2; OrderedLocusNames=TM_1796; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION AS A SSRNA-SPECIFIC ENDORIBONUCLEASE. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=18482976; DOI=10.1074/jbc.M803225200; RA Beloglazova N., Brown G., Zimmerman M.D., Proudfoot M., Makarova K.S., RA Kudritska M., Kochinyan S., Wang S., Chruszcz M., Minor W., RA Koonin E.V., Edwards A.M., Savchenko A., Yakunin A.F.; RT "A novel family of sequence-specific endoribonucleases associated with RT the clustered regularly interspaced short palindromic repeats."; RL J. Biol. Chem. 283:20361-20371(2008). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat), is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC sequences complementary to antecedent mobile elements and target CC invading nucleic acids. CRISPR clusters are transcribed and CC processed into CRISPR RNA (crRNA). Involved in the integration of CC spacer DNA into the CRISPR cassette (By similarity). Functions as CC a ssRNA-specific endoribonuclease. {ECO:0000250, CC ECO:0000269|PubMed:18482976}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas1 homodimer. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2 CC protein family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36859.1; -; Genomic_DNA. DR PIR; A72210; A72210. DR RefSeq; NP_229593.1; NC_000853.1. DR RefSeq; WP_004082343.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2B6; -. DR STRING; 243274.TM1796; -. DR EnsemblBacteria; AAD36859; AAD36859; TM_1796. DR GeneID; 897473; -. DR KEGG; tma:TM1796; -. DR PATRIC; 23938581; VBITheMar51294_1817. DR eggNOG; ENOG4105ZHF; Bacteria. DR eggNOG; COG1343; LUCA. DR InParanoid; Q9X2B6; -. DR KO; K09951; -. DR OMA; KGGESLF; -. DR OrthoDB; EOG6R2H64; -. DR BioCyc; TMAR243274:GC6P-1847-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-HAMAP. DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.240; -; 1. DR HAMAP; MF_01471; Cas2; 1. DR InterPro; IPR021127; CRISPR_associated_Cas2. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR019199; Virulence_VapD/CRISPR_Cas2. DR Pfam; PF09827; CRISPR_Cas2; 1. DR TIGRFAMs; TIGR01573; cas2; 1. PE 1: Evidence at protein level; KW Antiviral defense; Complete proteome; Endonuclease; Hydrolase; KW Magnesium; Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 87 CRISPR-associated endoribonuclease Cas2. FT /FTId=PRO_0000416947. FT METAL 8 8 Magnesium; catalytic. {ECO:0000255}. SQ SEQUENCE 87 AA; 10238 MW; 393705D9485F556B CRC64; MYVIMVYDVN EKRVAKILKI ARKYLKWVQN SVLEGELSPG KYEKLKLEVS RLIDEKEDSV RFYVMDSQKV FNLETLGVEK GEDGFIF // ID CARB_THEMA Reviewed; 1099 AA. AC Q9WZ27; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 123. DE RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210}; DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210}; DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210}; GN Name=carB {ECO:0000255|HAMAP-Rule:MF_01210}; GN OrderedLocusNames=TM_0557; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01210}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01210}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000255|HAMAP-Rule:MF_01210}. CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain CC promotes the hydrolysis of glutamine to ammonia, which is used by CC the large (or ammonia) chain to synthesize carbamoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01210}. CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP- CC Rule:MF_01210}. CC -!- SIMILARITY: Contains 2 ATP-grasp domains. {ECO:0000255|HAMAP- CC Rule:MF_01210}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35642.1; -; Genomic_DNA. DR PIR; C72363; C72363. DR RefSeq; NP_228367.1; NC_000853.1. DR RefSeq; WP_004081324.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ27; -. DR STRING; 243274.TM0557; -. DR PRIDE; Q9WZ27; -. DR EnsemblBacteria; AAD35642; AAD35642; TM_0557. DR GeneID; 897615; -. DR KEGG; tma:TM0557; -. DR PATRIC; 23936021; VBITheMar51294_0565. DR eggNOG; ENOG4105CU6; Bacteria. DR eggNOG; COG0458; LUCA. DR InParanoid; Q9WZ27; -. DR KO; K01955; -. DR OMA; AVFPFNK; -. DR OrthoDB; EOG6J1DC6; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IBA:GO_Central. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR Gene3D; 1.10.1030.10; -; 1. DR Gene3D; 3.30.1490.20; -; 2. DR Gene3D; 3.30.470.20; -; 2. DR Gene3D; 3.40.50.1380; -; 1. DR Gene3D; 3.40.50.20; -; 2. DR HAMAP; MF_01210_A; CPSase_L_chain_A; 1. DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR006275; CarbamoylP_synth_lsu. DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR016185; PreATP-grasp_dom. DR Pfam; PF02786; CPSase_L_D2; 2. DR Pfam; PF02787; CPSase_L_D3; 1. DR Pfam; PF02142; MGS; 1. DR PRINTS; PR00098; CPSASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF48108; SSF48108; 1. DR SUPFAM; SSF52335; SSF52335; 1. DR SUPFAM; SSF52440; SSF52440; 2. DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00866; CPSASE_1; 2. DR PROSITE; PS00867; CPSASE_2; 2. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Ligase; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome; KW Repeat. FT CHAIN 1 1099 Carbamoyl-phosphate synthase large chain. FT /FTId=PRO_0000145058. FT DOMAIN 133 328 ATP-grasp 1. {ECO:0000255|HAMAP- FT Rule:MF_01210}. FT DOMAIN 666 857 ATP-grasp 2. {ECO:0000255|HAMAP- FT Rule:MF_01210}. FT NP_BIND 159 216 ATP. {ECO:0000255|HAMAP-Rule:MF_01210}. FT NP_BIND 692 749 ATP. {ECO:0000255|HAMAP-Rule:MF_01210}. FT REGION 1 402 Carboxyphosphate synthetic domain. FT REGION 403 541 Oligomerization domain. FT REGION 542 944 Carbamoyl phosphate synthetic domain. FT REGION 945 1099 Allosteric domain. FT METAL 285 285 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 299 299 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 299 299 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 301 301 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 816 816 Magnesium or manganese 3. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 828 828 Magnesium or manganese 3. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 828 828 Magnesium or manganese 4. FT {ECO:0000255|HAMAP-Rule:MF_01210}. FT METAL 830 830 Magnesium or manganese 4. FT {ECO:0000255|HAMAP-Rule:MF_01210}. SQ SEQUENCE 1099 AA; 121317 MW; C2D51E7F649BBAE5 CRC64; MPKREDIKRI LVIGSGPITI GQAAEFDYSG TQALKALKSA GYEVIIVNSN SATIMTDPEF SDAVYIEPLT VEFLEKIIEK ERPDALLPTL GGQTALNLAV ELAERGILDK YGVQLIGAKL ESIKKAEDRE LFKETMEKAG LEVLRSRLVN NLADALETAR EFGYPVIIRP SFTLGGTGGG IAFNEEELRD IVTKGLIESP VHTVLIEESV LGWKEYELEV VRDGAGNFIV VCSIENLDPM GIHTGDSITV APAQTLTDVE YQRMRDAAYK VIDAIGIETG GSNIQFALDP ETGRMVVIEM NPRVSRSSAL ASKATGYPIA KVAALLAVGF TLDEIPNYIT GKTMAAFEPS IDYVVVKIPR FQLEKFPGAD PRLNTQMKSV GEVMAIGRTF KEALGKALRS LELDAAPKLD LEHIREHLAN PTPERISYVF AAFRNGMDVE EVHELTKIDR WFLREMKACI ELEEELKLKK FDVEILKKAK QWGYSDREIA EIWGVSEKEI RKMREDNRIF PVYKMVDTCA AEFEAQTPYY YSTYNGVENE AVPSDREKIM ILGSGPNRIG QGIEFDYTNV HGVWSFQEEG YETIMVNSNP ETVSTDYDTS DRLYFEPLTV EDVLEIVRNE KPKGVVVAFG GQTPLKIAKY LVEERVNIIG TSFESIEIAE DREKFAKLLK QIGLKCPPFG TASSVEEALR VAENLGYPVL VRPSYVLGGR AMAIVDTPQE LEMYVKEAAV VSPGYPVLID KFLEDAIELD VDVVSDGKYV WIAGLMEQIE EAGVHSGDSA CVLPPVSLSE KLVEEIEETV YKLVKALKVV GVANIQLAVK DEEIYIIEAN PRASRTVPFV SKAIGIPVAR IAAKIMVGRN LPELLSEYFP YPTRPGVKVD KLGESEILPT PWPKMFSVKE VVIPFHKFPG TDVLLGPEMR STGEVMGIGE DFAEAFAKAQ IAAGNPLPTT GAILATVADK DKREAVPLLA HLADMGFEIY ATRGTAKALQ SHGVEVKVVP KVGEGRPDVI DLLEQGKISL VVITQSSDEP ALVAVSHGKE PFKVEGRRTV GYMIRTTALK RKIPYLTTVE SLRAAVAAIR KMKKGSIVKV RRLTDTWKM // ID CARA_THEMA Reviewed; 392 AA. AC Q9WZ28; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 119. DE RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000255|HAMAP-Rule:MF_01209}; DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01209}; DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000255|HAMAP-Rule:MF_01209}; GN Name=carA {ECO:0000255|HAMAP-Rule:MF_01209}; GN OrderedLocusNames=TM_0558; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01209}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01209}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000255|HAMAP-Rule:MF_01209}. CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain CC promotes the hydrolysis of glutamine to ammonia, which is used by CC the large (or ammonia) chain to synthesize carbamoyl phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01209}. CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000255|HAMAP- CC Rule:MF_01209}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_01209}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35643.1; -; Genomic_DNA. DR PIR; D72363; D72363. DR RefSeq; NP_228368.1; NC_000853.1. DR RefSeq; WP_004081322.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ28; -. DR STRING; 243274.TM0558; -. DR MEROPS; C26.A33; -. DR EnsemblBacteria; AAD35643; AAD35643; TM_0558. DR GeneID; 897616; -. DR KEGG; tma:TM0558; -. DR PATRIC; 23936023; VBITheMar51294_0566. DR eggNOG; ENOG4105C1M; Bacteria. DR eggNOG; COG0505; LUCA. DR InParanoid; Q9WZ28; -. DR KO; K01956; -. DR OMA; TNAHIGN; -. DR OrthoDB; EOG61ZTH6; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR Gene3D; 3.40.50.880; -; 2. DR Gene3D; 3.50.30.20; -; 1. DR HAMAP; MF_01209; CPSase_S_chain; 1. DR InterPro; IPR006274; CarbamoylP_synth_ssu. DR InterPro; IPR002474; CarbamoylP_synth_ssu_N. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR Pfam; PF00988; CPSase_sm_chain; 1. DR Pfam; PF00117; GATase; 1. DR SMART; SM01097; CPSase_sm_chain; 1. DR SUPFAM; SSF52021; SSF52021; 1. DR SUPFAM; SSF52317; SSF52317; 2. DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 392 Carbamoyl-phosphate synthase small chain. FT /FTId=PRO_0000112340. FT DOMAIN 176 392 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_01209}. FT REGION 1 172 CPSase. FT ACT_SITE 252 252 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01209}. FT ACT_SITE 367 367 {ECO:0000255|HAMAP-Rule:MF_01209}. FT ACT_SITE 369 369 {ECO:0000255|HAMAP-Rule:MF_01209}. SQ SEQUENCE 392 AA; 42930 MW; B5312FBB07B181FC CRC64; MSKKALLALE DGSFFFGQSL GAEGETFGEL VFNTGMTGYQ EVLTDPSYTG QIVVMTYPEI GIYGVNDEDV ESDGIKVAGF VVYRSVDTPS NWRATMSFPD YLKKYNIVAI EGVDTRALTR KIRVKGAMKG AISTVDLDPD SLVKRVKESP SIVGRDLAGL VSPKEVIVEN PEGDFSVVVL DSGVKWGILR DLKRVGAKVM RVPYSVDIDD IKKLNPDGVL ISNGPGDPAA LLKTIRLIKD LLKEEIPLAG ICLGHQLLGL AVGGRTYKMK FGHRGINHPV KDLRTGRVLI TTHNHGFAVD PKSFGLPELG SEDQDANVLT KNLQKISVLE GISPQGIKVE ITHISLNDGT MEGMRLVDYP AFSVQYHPEA SPGPHDAKYF FEEFKRLIKE VR // ID CDSA_THEMA Reviewed; 270 AA. AC Q9X1B7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Phosphatidate cytidylyltransferase; DE EC=2.7.7.41; DE AltName: Full=CDP-DAG synthase; DE AltName: Full=CDP-DG synthase; DE AltName: Full=CDP-diacylglycerol synthase; DE Short=CDS; DE AltName: Full=CDP-diglyceride pyrophosphorylase; DE AltName: Full=CDP-diglyceride synthase; DE AltName: Full=CTP:phosphatidate cytidylyltransferase; GN Name=cdsA; OrderedLocusNames=TM_1397; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: CTP + phosphatidate = diphosphate + CDP- CC diacylglycerol. CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36468.1; -; Genomic_DNA. DR PIR; F72259; F72259. DR RefSeq; NP_229198.1; NC_000853.1. DR RefSeq; WP_004081613.1; NZ_CP011107.1. DR PDB; 4Q2E; X-ray; 3.40 A; A/B=1-270. DR PDB; 4Q2G; X-ray; 3.40 A; A/B=1-270. DR PDBsum; 4Q2E; -. DR PDBsum; 4Q2G; -. DR STRING; 243274.TM1397; -. DR EnsemblBacteria; AAD36468; AAD36468; TM_1397. DR GeneID; 898079; -. DR KEGG; tma:TM1397; -. DR PATRIC; 23937740; VBITheMar51294_1409. DR eggNOG; ENOG4105KNE; Bacteria. DR eggNOG; COG0575; LUCA. DR InParanoid; Q9X1B7; -. DR KO; K00981; -. DR OMA; FDSFAYF; -. DR OrthoDB; EOG6TBHJT; -. DR UniPathway; UPA00557; UER00614. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IBA:GO_Central. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IBA:GO_Central. DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IBA:GO_Central. DR InterPro; IPR000374; PC_trans. DR PROSITE; PS01315; CDS; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Membrane; Nucleotidyltransferase; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 270 Phosphatidate cytidylyltransferase. FT /FTId=PRO_0000090758. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 55 75 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TRANSMEM 104 124 Helical. {ECO:0000255}. FT TRANSMEM 129 149 Helical. {ECO:0000255}. FT TRANSMEM 170 190 Helical. {ECO:0000255}. FT TRANSMEM 193 213 Helical. {ECO:0000255}. FT TRANSMEM 248 268 Helical. {ECO:0000255}. FT HELIX 5 9 {ECO:0000244|PDB:4Q2G}. FT HELIX 10 20 {ECO:0000244|PDB:4Q2E}. FT HELIX 25 45 {ECO:0000244|PDB:4Q2E}. FT HELIX 51 69 {ECO:0000244|PDB:4Q2E}. FT TURN 70 72 {ECO:0000244|PDB:4Q2E}. FT STRAND 73 75 {ECO:0000244|PDB:4Q2E}. FT HELIX 76 93 {ECO:0000244|PDB:4Q2E}. FT HELIX 97 113 {ECO:0000244|PDB:4Q2E}. FT HELIX 115 118 {ECO:0000244|PDB:4Q2E}. FT HELIX 121 154 {ECO:0000244|PDB:4Q2E}. FT STRAND 162 164 {ECO:0000244|PDB:4Q2E}. FT HELIX 169 191 {ECO:0000244|PDB:4Q2E}. FT STRAND 193 195 {ECO:0000244|PDB:4Q2G}. FT STRAND 201 203 {ECO:0000244|PDB:4Q2G}. FT HELIX 204 229 {ECO:0000244|PDB:4Q2E}. FT STRAND 232 234 {ECO:0000244|PDB:4Q2E}. FT STRAND 239 242 {ECO:0000244|PDB:4Q2E}. FT HELIX 244 265 {ECO:0000244|PDB:4Q2E}. SQ SEQUENCE 270 AA; 30099 MW; BDAAF664120D7D3E CRC64; MDDLKTRVIT ASVVAPFVVL CFVSYESLIG LVSAILILAG YELITLEMKE RDARFFYVIL LALYPVLYGL VFEEPTQPLS ILFITGVVFS LITDKDPSQV FKTVAAFSIA LIYVTFFLSF FLPIYRDFGA ANALLVLTST WVFDSFAYFT GLKFGRTRIS PRYSPRKSLE GVIGGFLGVV IYTFLYRLVV NDLLSVNVIS FRTFLPFAAT VAIMDTFGDI FESALKRHYG VKDSGKTLPG HGGMLDRIDG LLFVAPVSYI VFKILEGVVR // ID CH60_THEMA Reviewed; 538 AA. AC Q9WYX6; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=GroEL protein {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=Protein Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600}; GN Name=groL {ECO:0000255|HAMAP-Rule:MF_00600}; GN Synonyms=groEL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA; GN OrderedLocusNames=TM_0506; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Prevents misfolding and promotes the refolding and CC proper assembly of unfolded polypeptides generated under stress CC conditions. {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of CC 7 subunits. {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000255|HAMAP-Rule:MF_00600}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35591.1; -; Genomic_DNA. DR PIR; H72367; H72367. DR RefSeq; NP_228316.1; NC_000853.1. DR RefSeq; WP_004081434.1; NC_023151.1. DR ProteinModelPortal; Q9WYX6; -. DR SMR; Q9WYX6; 3-526. DR STRING; 243274.TM0506; -. DR PRIDE; Q9WYX6; -. DR EnsemblBacteria; AAD35591; AAD35591; TM_0506. DR GeneID; 897549; -. DR KEGG; tma:TM0506; -. DR PATRIC; 23935917; VBITheMar51294_0513. DR eggNOG; ENOG4105CJ9; Bacteria. DR eggNOG; COG0459; LUCA. DR InParanoid; Q9WYX6; -. DR KO; K04077; -. DR OMA; KKQMDET; -. DR OrthoDB; EOG6JDWBZ; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.560.10; -; 2. DR Gene3D; 3.50.7.10; -; 1. DR HAMAP; MF_00600; CH60; 1. DR InterPro; IPR018370; Chaperonin_Cpn60_CS. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom. DR InterPro; IPR027413; GROEL-like_equatorial. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF52029; SSF52029; 1. DR TIGRFAMs; TIGR02348; GroEL; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 538 60 kDa chaperonin. FT /FTId=PRO_0000063579. SQ SEQUENCE 538 AA; 58066 MW; 193F1ACCCE45F813 CRC64; MPKILKFNEE ARRALERGVD KVANAVKVTL GPKGRNVVIE KSWGSPTITN DGVSIAKEIE LEDKFENLGA QLVKEVASKT NDVAGDGTTT ATVLAQAMIK EGLKNVAAGA NPILLKRGID KAVEKAVEEI KKVSKKLSGR EDIAHVAAIS ANSAEIGELI AEAMDKVGED GVITVEDSKT LETYVEFTEG MQFDRGYISP YFVTDAEKME VVLKEPFILI TDRKLSAVKP LIPILEKVAQ TGKPLLVIAE DVEGEVLTTL VLNKLKGTLQ SCAVKAPGFG ERRKAMLQDI AILTGGQVAS EELGINLEDL TLEDLGRADL VRVKKDETII IGGKGDPEAI KKRIAQIKAQ IEETTSEYEK ETLQERMAKL AGGVAVIKVG AATETELKEK KHRIEDALSA TRAAVEEGIV PGGGVTLLRA RKAVEKVIEE LEGDEKIGAQ IVYKALSAPI KQIAENAGYD GAVIIEKILS NDDPAYGFDA LRGEYCNMFE RGIIDPAKVT RSALQNAASI AGMLLTTEVL IVEKPEEKKE TPSMPEEF // ID CHED_THEMA Reviewed; 157 AA. AC Q9X005; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=Chemoreceptor glutamine deamidase CheD; DE EC=3.5.1.44; DE AltName: Full=Chemoreceptor glutamate methylesterase CheD; DE EC=3.1.1.61; GN Name=cheD; OrderedLocusNames=TM_0903; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CHEC, AND RP MUTAGENESIS OF THR-21; SER-26; CYS-27 AND HIS-44. RX PubMed=16469702; DOI=10.1016/j.cell.2005.11.046; RA Chao X., Muff T.J., Park S.-Y., Zhang S., Pollard A.M., Ordal G.W., RA Bilwes A.M., Crane B.R.; RT "A receptor-modifying deamidase in complex with a signaling RT phosphatase reveals reciprocal regulation."; RL Cell 124:561-571(2006). CC -!- FUNCTION: Deamidates glutamine residues on chemoreceptors (MCPs). CC CheD-mediated MCP deamidation is required for productive CC communication of the conformational signals of the chemoreceptors CC to the CheA kinase. In addition, demethylates methylated glutamate CC residues on chemoreceptors Mcp2 and Mcp4. Enhances the activity of CC CheC. CC -!- CATALYTIC ACTIVITY: Protein L-glutamine + H(2)O = protein L- CC glutamate + NH(3). CC -!- CATALYTIC ACTIVITY: Protein L-glutamate O(5)-methyl ester + H(2)O CC = protein L-glutamate + methanol. CC -!- SUBUNIT: Heterodimer with CheC. The CheC-CheD heterodimer CC interacts with phosphorylated CheY. {ECO:0000269|PubMed:16469702}. CC -!- SIMILARITY: Belongs to the CheD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35984.1; -; Genomic_DNA. DR PIR; F72318; F72318. DR RefSeq; NP_228711.1; NC_000853.1. DR RefSeq; WP_004080666.1; NZ_CP011107.1. DR PDB; 2F9Z; X-ray; 2.40 A; C/D=1-157. DR PDBsum; 2F9Z; -. DR ProteinModelPortal; Q9X005; -. DR SMR; Q9X005; 1-157. DR STRING; 243274.TM0903; -. DR EnsemblBacteria; AAD35984; AAD35984; TM_0903. DR GeneID; 898577; -. DR KEGG; tma:TM0903; -. DR PATRIC; 23936737; VBITheMar51294_0917. DR eggNOG; ENOG4108Z4W; Bacteria. DR eggNOG; COG1871; LUCA. DR InParanoid; Q9X005; -. DR KO; K03411; -. DR OMA; AGGSDML; -. DR OrthoDB; EOG6WHNQB; -. DR EvolutionaryTrace; Q9X005; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-EC. DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01440; CheD; 1. DR InterPro; IPR005659; Chemorcpt_Glu_NH3ase_CheD. DR InterPro; IPR011324; Cytotoxic_necrot_fac-like_cat. DR Pfam; PF03975; CheD; 1. DR SUPFAM; SSF64438; SSF64438; 1. PE 1: Evidence at protein level; KW 3D-structure; Chemotaxis; Complete proteome; Hydrolase; KW Reference proteome. FT CHAIN 1 157 Chemoreceptor glutamine deamidase CheD. FT /FTId=PRO_0000251072. FT ACT_SITE 27 27 Nucleophile. FT MUTAGEN 21 21 T->A: 6-fold reduction in activity. FT {ECO:0000269|PubMed:16469702}. FT MUTAGEN 26 26 S->A,H: Loss of activity. FT {ECO:0000269|PubMed:16469702}. FT MUTAGEN 26 26 S->N: Reduced activity. FT {ECO:0000269|PubMed:16469702}. FT MUTAGEN 27 27 C->A: Loss of activity. Does not prevent FT binding to mcp2. FT {ECO:0000269|PubMed:16469702}. FT MUTAGEN 27 27 C->H,N: Loss of activity. FT {ECO:0000269|PubMed:16469702}. FT MUTAGEN 44 44 H->A: Loss of activity. FT {ECO:0000269|PubMed:16469702}. FT STRAND 2 4 {ECO:0000244|PDB:2F9Z}. FT STRAND 10 14 {ECO:0000244|PDB:2F9Z}. FT STRAND 18 26 {ECO:0000244|PDB:2F9Z}. FT STRAND 28 34 {ECO:0000244|PDB:2F9Z}. FT TURN 35 38 {ECO:0000244|PDB:2F9Z}. FT STRAND 39 45 {ECO:0000244|PDB:2F9Z}. FT HELIX 57 59 {ECO:0000244|PDB:2F9Z}. FT HELIX 61 73 {ECO:0000244|PDB:2F9Z}. FT TURN 74 76 {ECO:0000244|PDB:2F9Z}. FT HELIX 79 81 {ECO:0000244|PDB:2F9Z}. FT STRAND 83 88 {ECO:0000244|PDB:2F9Z}. FT HELIX 100 114 {ECO:0000244|PDB:2F9Z}. FT STRAND 119 124 {ECO:0000244|PDB:2F9Z}. FT STRAND 130 135 {ECO:0000244|PDB:2F9Z}. FT TURN 136 139 {ECO:0000244|PDB:2F9Z}. FT STRAND 140 144 {ECO:0000244|PDB:2F9Z}. FT STRAND 154 157 {ECO:0000244|PDB:2F9Z}. SQ SEQUENCE 157 AA; 16657 MW; E5B03D96D2DDEDBE CRC64; MKKVIGIGEY AVMKNPGVIV TLGLGSCVAV CMRDPVAKVG AMAHVMLPDS GGKTDKPGKY ADTAVKTLVE ELKKMGAKVE RLEAKIAGGA SMFESKGMNI GARNVEAVKK HLKDFGIKLL AEDTGGNRAR SVEYNIETGK LLVRKVGGGE QLEIKEI // ID CHEA_THEMA Reviewed; 671 AA. AC Q56310; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 137. DE RecName: Full=Chemotaxis protein CheA; DE EC=2.7.13.3; GN Name=cheA; OrderedLocusNames=TM_0702; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8550470; RA Swanson R.V., Sanna M.G., Simon M.I.; RT "Thermostable chemotaxis proteins from the hyperthermophilic bacterium RT Thermotoga maritima."; RL J. Bacteriol. 178:484-489(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 293-671. RX PubMed=9989504; DOI=10.1016/S0092-8674(00)80966-6; RA Bilwes A.M., Alex L.A., Crane B.R., Simon M.I.; RT "Structure of CheA, a signal-transducing histidine kinase."; RL Cell 96:131-141(1999). CC -!- FUNCTION: Involved in the transmission of sensory signals from the CC chemoreceptors to the flagellar motors. CheA is CC autophosphorylated; it can transfer its phosphate group to either CC CheB or CheY (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Contains 1 cheW-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00052}. CC -!- SIMILARITY: Contains 1 histidine kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00107}. CC -!- SIMILARITY: Contains 1 HPt domain. {ECO:0000255|PROSITE- CC ProRule:PRU00110}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U30501; AAA96387.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35784.1; -; Genomic_DNA. DR PIR; D72346; D72346. DR RefSeq; NP_228511.1; NC_000853.1. DR RefSeq; WP_004081040.1; NZ_CP011107.1. DR PDB; 1B3Q; X-ray; 2.60 A; A/B=293-671. DR PDB; 1I58; X-ray; 1.60 A; A/B=352-540. DR PDB; 1I59; X-ray; 1.80 A; A/B=352-540. DR PDB; 1I5A; X-ray; 1.90 A; A/B=352-540. DR PDB; 1I5B; X-ray; 1.94 A; A/B=352-540. DR PDB; 1I5C; X-ray; 1.90 A; A/B=352-540. DR PDB; 1I5D; X-ray; 2.90 A; A=350-540. DR PDB; 1TQG; X-ray; 0.98 A; A=4-104. DR PDB; 1U0S; X-ray; 1.90 A; A=175-260. DR PDB; 2CH4; X-ray; 3.50 A; A/B=355-671. DR PDB; 2LD6; NMR; -; A=1-131. DR PDB; 3JA6; EM; 12.70 A; C/E=293-671. DR PDB; 3UR1; X-ray; 4.50 A; A=355-671. DR PDB; 4JPB; X-ray; 3.19 A; A=355-671. DR PDB; 4XIV; X-ray; 3.00 A; A/B=289-540. DR PDBsum; 1B3Q; -. DR PDBsum; 1I58; -. DR PDBsum; 1I59; -. DR PDBsum; 1I5A; -. DR PDBsum; 1I5B; -. DR PDBsum; 1I5C; -. DR PDBsum; 1I5D; -. DR PDBsum; 1TQG; -. DR PDBsum; 1U0S; -. DR PDBsum; 2CH4; -. DR PDBsum; 2LD6; -. DR PDBsum; 3JA6; -. DR PDBsum; 3UR1; -. DR PDBsum; 4JPB; -. DR PDBsum; 4XIV; -. DR ProteinModelPortal; Q56310; -. DR SMR; Q56310; 4-104, 175-260, 293-671. DR DIP; DIP-29071N; -. DR IntAct; Q56310; 1. DR STRING; 243274.TM0702; -. DR DNASU; 898369; -. DR EnsemblBacteria; AAD35784; AAD35784; TM_0702. DR GeneID; 898369; -. DR KEGG; tma:TM0702; -. DR PATRIC; 23936322; VBITheMar51294_0714. DR eggNOG; ENOG4105CBS; Bacteria. DR eggNOG; COG0643; LUCA. DR InParanoid; Q56310; -. DR KO; K03407; -. DR OMA; YHSGNHV; -. DR OrthoDB; EOG62RS8P; -. DR BRENDA; 2.7.13.3; 6331. DR EvolutionaryTrace; Q56310; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.560; -; 1. DR Gene3D; 1.20.120.160; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR Gene3D; 3.30.70.1110; -; 1. DR InterPro; IPR004105; CheA-like_dim. DR InterPro; IPR002545; CheW. DR InterPro; IPR015162; CheY-binding. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom. DR InterPro; IPR010808; Sig_transdc_His_kinase_P2-bd. DR Pfam; PF01584; CheW; 1. DR Pfam; PF02895; H-kinase_dim; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF01627; Hpt; 1. DR Pfam; PF07194; P2; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00260; CheW; 1. DR SMART; SM01231; H-kinase_dim; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00073; HPT; 1. DR SUPFAM; SSF47226; SSF47226; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF50341; SSF50341; 1. DR SUPFAM; SSF55052; SSF55052; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50851; CHEW; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50894; HPT; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Chemotaxis; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; KW Transferase; Two-component regulatory system. FT CHAIN 1 671 Chemotaxis protein CheA. FT /FTId=PRO_0000074718. FT DOMAIN 1 102 HPt. {ECO:0000255|PROSITE- FT ProRule:PRU00110}. FT DOMAIN 291 541 Histidine kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00107}. FT DOMAIN 543 671 CheW-like. {ECO:0000255|PROSITE- FT ProRule:PRU00052}. FT MOD_RES 45 45 Phosphohistidine; by autocatalysis. FT {ECO:0000255|PROSITE-ProRule:PRU00107}. FT CONFLICT 304 304 D -> G (in Ref. 1; AAA96387). FT {ECO:0000305}. FT HELIX 4 29 {ECO:0000244|PDB:1TQG}. FT HELIX 34 53 {ECO:0000244|PDB:1TQG}. FT HELIX 57 74 {ECO:0000244|PDB:1TQG}. FT HELIX 82 102 {ECO:0000244|PDB:1TQG}. FT HELIX 114 123 {ECO:0000244|PDB:2LD6}. FT STRAND 177 184 {ECO:0000244|PDB:1U0S}. FT HELIX 192 205 {ECO:0000244|PDB:1U0S}. FT STRAND 209 215 {ECO:0000244|PDB:1U0S}. FT HELIX 217 221 {ECO:0000244|PDB:1U0S}. FT STRAND 225 237 {ECO:0000244|PDB:1U0S}. FT HELIX 239 247 {ECO:0000244|PDB:1U0S}. FT STRAND 249 251 {ECO:0000244|PDB:1U0S}. FT STRAND 253 260 {ECO:0000244|PDB:1U0S}. FT STRAND 295 299 {ECO:0000244|PDB:1B3Q}. FT HELIX 300 322 {ECO:0000244|PDB:1B3Q}. FT HELIX 324 326 {ECO:0000244|PDB:4XIV}. FT STRAND 354 357 {ECO:0000244|PDB:1I58}. FT HELIX 359 362 {ECO:0000244|PDB:1I58}. FT HELIX 365 375 {ECO:0000244|PDB:1I58}. FT STRAND 380 385 {ECO:0000244|PDB:1I58}. FT STRAND 390 392 {ECO:0000244|PDB:1I58}. FT HELIX 393 413 {ECO:0000244|PDB:1I58}. FT HELIX 418 424 {ECO:0000244|PDB:1I58}. FT STRAND 428 439 {ECO:0000244|PDB:1I58}. FT STRAND 442 449 {ECO:0000244|PDB:1I58}. FT HELIX 456 465 {ECO:0000244|PDB:1I58}. FT STRAND 466 468 {ECO:0000244|PDB:1B3Q}. FT HELIX 471 474 {ECO:0000244|PDB:1I58}. FT HELIX 479 483 {ECO:0000244|PDB:1I58}. FT HELIX 484 487 {ECO:0000244|PDB:1I58}. FT TURN 489 492 {ECO:0000244|PDB:2CH4}. FT HELIX 493 498 {ECO:0000244|PDB:1I58}. FT HELIX 499 501 {ECO:0000244|PDB:1I58}. FT HELIX 506 516 {ECO:0000244|PDB:1I58}. FT STRAND 520 526 {ECO:0000244|PDB:1I58}. FT TURN 527 529 {ECO:0000244|PDB:1I58}. FT STRAND 530 538 {ECO:0000244|PDB:1I58}. FT STRAND 542 551 {ECO:0000244|PDB:1B3Q}. FT STRAND 554 559 {ECO:0000244|PDB:1B3Q}. FT HELIX 560 562 {ECO:0000244|PDB:1B3Q}. FT STRAND 563 567 {ECO:0000244|PDB:1B3Q}. FT HELIX 571 573 {ECO:0000244|PDB:4JPB}. FT STRAND 575 577 {ECO:0000244|PDB:1B3Q}. FT STRAND 580 585 {ECO:0000244|PDB:1B3Q}. FT STRAND 588 594 {ECO:0000244|PDB:1B3Q}. FT HELIX 595 598 {ECO:0000244|PDB:1B3Q}. FT STRAND 611 617 {ECO:0000244|PDB:1B3Q}. FT STRAND 620 637 {ECO:0000244|PDB:1B3Q}. FT HELIX 641 644 {ECO:0000244|PDB:1B3Q}. FT STRAND 648 655 {ECO:0000244|PDB:1B3Q}. FT STRAND 657 659 {ECO:0000244|PDB:1B3Q}. FT STRAND 661 665 {ECO:0000244|PDB:1B3Q}. FT HELIX 667 669 {ECO:0000244|PDB:1B3Q}. SQ SEQUENCE 671 AA; 75556 MW; F264398B88DA34E1 CRC64; MMEEYLGVFV DETKEYLQNL NDTLLELEKN PEDMELINEA FRALHTLKGM AGTMGFSSMA KLCHTLENIL DKARNSEIKI TSDLLDKIFA GVDMITRMVD KIVSEGSDDI GENIDVFSDT IKSFASSGKE KPSEIKNETE TKGEEEHKGE STSNEEVVVL PEEVAHVLQE ARNKGFKTFY IKVILKEGTQ LKSARIYLVF HKLEELKCEV VRTIPSVEEI EEEKFENEVE LFVISPVDLE KLSEALSSIA DIERVIIKEV TAVTEESGAE KRTEKEEKTE KTEEKAERKK VISQTVRVDI EKLDNLMDLM GELVIARSRI LETLKKYNIK ELDESLSHLS RITLDLQNVV MKIRMVPISF VFNRFPRMVR DLAKKMNKEV NFIMRGEDTE LDRTFVEEIG EPLLHLLRNA IDHGIEPKEE RIAKGKPPIG TLILSARHEG NNVVIEVEDD GRGIDKEKII RKAIEKGLID ESKAATLSDQ EILNFLFVPG FSTKEKVSEV SGRGVGMDVV KNVVESLNGS ISIESEKDKG TKVTIRLPLT LAIIQALLVK VNNLVYAIPI ANIDTILSIS KEDIQRVQDR DVIVIRGEVI PVYRLWEVLQ IEHKEELEEM EAVIVRVGNR KYGIVVDDLL GQDDIVIKSL GKVFSEVKEF SGAAILGDGS IALIINVSGI V // ID CHER_THEMA Reviewed; 282 AA. AC Q9WYT5; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=Chemotaxis protein methyltransferase; DE EC=2.1.1.80; GN Name=cheR; OrderedLocusNames=TM_0464; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Methylation of the membrane-bound methyl-accepting CC chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester CC residues in MCP. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-glutamate CC = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester. CC -!- SIMILARITY: Contains 1 cheR-type methyltransferase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00051}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35548.1; -; Genomic_DNA. DR PIR; H72373; H72373. DR RefSeq; NP_228274.1; NC_000853.1. DR RefSeq; WP_004081502.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYT5; -. DR STRING; 243274.TM0464; -. DR DNASU; 897495; -. DR EnsemblBacteria; AAD35548; AAD35548; TM_0464. DR GeneID; 897495; -. DR KEGG; tma:TM0464; -. DR PATRIC; 23935825; VBITheMar51294_0471. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR InParanoid; Q9WYT5; -. DR KO; K00575; -. DR OMA; TEQIIMP; -. DR OrthoDB; EOG615VHS; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR Gene3D; 1.10.155.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR022642; CheR_C. DR InterPro; IPR000780; CheR_MeTrfase. DR InterPro; IPR022641; CheR_N. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01739; CheR; 1. DR Pfam; PF03705; CheR_N; 1. DR PRINTS; PR00996; CHERMTFRASE. DR SMART; SM00138; MeTrc; 1. DR SUPFAM; SSF47757; SSF47757; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS50123; CHER; 1. PE 3: Inferred from homology; KW Chemotaxis; Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 282 Chemotaxis protein methyltransferase. FT /FTId=PRO_0000176040. FT DOMAIN 17 282 CheR-type methyltransferase. FT {ECO:0000255|PROSITE-ProRule:PRU00051}. FT REGION 210 211 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT REGION 226 227 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 91 91 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 93 93 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 97 97 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 132 132 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 155 155 S-adenosyl-L-methionine. {ECO:0000250}. SQ SEQUENCE 282 AA; 34225 MW; F3D5910026E9E0B0 CRC64; MQEERSEKKI GPFKFQSNFE WKEFPQEEFE WFVKEVEKRF GLNLSSYKPQ RVKRRTELLL RKYNVGYREY LNMLIKDKKY LDEFMDKMTI NVTEFFRNPE KWWELRDEII PLIAKNSLRM KFWSAGCSSG EEPYSLAILV HELNLSYKTR ILATDIDIGV LRRAQEGIYE ERAFVSTPKE YLEKYFEKLP DGRYRIKDSV KKIVEFKRHD LLKDPFEKNF DLIVCRNVVI YFEPEAKNEL YRKFAESLKP GGFLFVGNTE RIFNYKELGF EIYKPFIYRK VK // ID CHEW_THEMA Reviewed; 151 AA. AC Q56311; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 105. DE RecName: Full=Chemotaxis protein CheW; GN Name=cheW; OrderedLocusNames=TM_0701; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8550470; RA Swanson R.V., Sanna M.G., Simon M.I.; RT "Thermostable chemotaxis proteins from the hyperthermophilic bacterium RT Thermotoga maritima."; RL J. Bacteriol. 178:484-489(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in the transmission of sensory signals from the CC chemoreceptors to the flagellar motors. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 cheW-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00052}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U30501; AAA96388.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35783.1; -; Genomic_DNA. DR PIR; C72346; C72346. DR RefSeq; NP_228510.1; NC_000853.1. DR RefSeq; WP_010865187.1; NC_000853.1. DR PDB; 1K0S; NMR; -; A=1-151. DR PDB; 2CH4; X-ray; 3.50 A; W/Y=1-151. DR PDB; 3JA6; EM; 12.70 A; A/B/D/F=9-147. DR PDB; 3UR1; X-ray; 4.50 A; B=9-147. DR PDB; 4JPB; X-ray; 3.19 A; W=1-147. DR PDBsum; 1K0S; -. DR PDBsum; 2CH4; -. DR PDBsum; 3JA6; -. DR PDBsum; 3UR1; -. DR PDBsum; 4JPB; -. DR DisProt; DP00350; -. DR ProteinModelPortal; Q56311; -. DR SMR; Q56311; 1-151. DR DIP; DIP-29073N; -. DR STRING; 243274.TM0701; -. DR EnsemblBacteria; AAD35783; AAD35783; TM_0701. DR GeneID; 898368; -. DR KEGG; tma:TM0701; -. DR KEGG; tmi:THEMA_01160; -. DR PATRIC; 23936320; VBITheMar51294_0713. DR eggNOG; ENOG4105YVF; Bacteria. DR eggNOG; COG0835; LUCA. DR InParanoid; Q56311; -. DR KO; K03408; -. DR OMA; ILMLFDI; -. DR OrthoDB; EOG60CWQ7; -. DR BioCyc; TMAR243274:GC6P-727-MONOMER; -. DR EvolutionaryTrace; Q56311; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR InterPro; IPR002545; CheW. DR Pfam; PF01584; CheW; 1. DR SMART; SM00260; CheW; 1. DR SUPFAM; SSF50341; SSF50341; 1. DR PROSITE; PS50851; CHEW; 1. PE 1: Evidence at protein level; KW 3D-structure; Chemotaxis; Complete proteome; Cytoplasm; KW Reference proteome. FT CHAIN 1 151 Chemotaxis protein CheW. FT /FTId=PRO_0000198349. FT DOMAIN 10 147 CheW-like. {ECO:0000255|PROSITE- FT ProRule:PRU00052}. FT STRAND 10 20 {ECO:0000244|PDB:4JPB}. FT STRAND 22 26 {ECO:0000244|PDB:4JPB}. FT HELIX 27 29 {ECO:0000244|PDB:4JPB}. FT STRAND 30 35 {ECO:0000244|PDB:4JPB}. FT STRAND 46 48 {ECO:0000244|PDB:1K0S}. FT STRAND 49 55 {ECO:0000244|PDB:4JPB}. FT STRAND 58 64 {ECO:0000244|PDB:4JPB}. FT HELIX 65 69 {ECO:0000244|PDB:4JPB}. FT HELIX 75 77 {ECO:0000244|PDB:4JPB}. FT STRAND 80 86 {ECO:0000244|PDB:4JPB}. FT STRAND 89 105 {ECO:0000244|PDB:4JPB}. FT STRAND 108 110 {ECO:0000244|PDB:4JPB}. FT TURN 113 115 {ECO:0000244|PDB:2CH4}. FT STRAND 116 118 {ECO:0000244|PDB:2CH4}. FT HELIX 119 121 {ECO:0000244|PDB:4JPB}. FT STRAND 122 128 {ECO:0000244|PDB:4JPB}. FT STRAND 131 136 {ECO:0000244|PDB:4JPB}. FT HELIX 138 145 {ECO:0000244|PDB:4JPB}. FT TURN 148 150 {ECO:0000244|PDB:1K0S}. SQ SEQUENCE 151 AA; 16955 MW; 122A5EFEDFA3D561 CRC64; MKTLADALKE FEVLSFEIDE QALAFDVDNI EMVIEKSDIT PVPKSRHFVE GVINLRGRII PVVNLAKILG ISFDEQKMKS IIVARTKDVE VGFLVDRVLG VLRITENQLD LTNVSDKFGK KSKGLVKTDG RLIIYLDIDK IIEEITVKEG V // ID CH10_THEMA Reviewed; 92 AA. AC Q9WYX5; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=10 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00580}; DE AltName: Full=GroES protein {ECO:0000255|HAMAP-Rule:MF_00580}; DE AltName: Full=Protein Cpn10 {ECO:0000255|HAMAP-Rule:MF_00580}; GN Name=groS {ECO:0000255|HAMAP-Rule:MF_00580}; GN Synonyms=groES {ECO:0000255|HAMAP-Rule:MF_00580}; GN OrderedLocusNames=TM_0505; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds to Cpn60 in the presence of Mg-ATP and suppresses CC the ATPase activity of the latter. {ECO:0000255|HAMAP- CC Rule:MF_00580}. CC -!- SUBUNIT: Heptamer of 7 subunits arranged in a ring. CC {ECO:0000255|HAMAP-Rule:MF_00580}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00580}. CC -!- SIMILARITY: Belongs to the GroES chaperonin family. CC {ECO:0000255|HAMAP-Rule:MF_00580}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35590.1; -; Genomic_DNA. DR PIR; G72367; G72367. DR RefSeq; NP_228315.1; NC_000853.1. DR RefSeq; WP_004081435.1; NC_000853.1. DR ProteinModelPortal; Q9WYX5; -. DR STRING; 243274.TM0505; -. DR EnsemblBacteria; AAD35590; AAD35590; TM_0505. DR GeneID; 897548; -. DR KEGG; tma:TM0505; -. DR PATRIC; 23935915; VBITheMar51294_0512. DR eggNOG; ENOG41083C3; Bacteria. DR eggNOG; COG0234; LUCA. DR InParanoid; Q9WYX5; -. DR KO; K04078; -. DR OMA; DTGKEKP; -. DR OrthoDB; EOG6GFGSD; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.33.40; -; 1. DR HAMAP; MF_00580; CH10; 1. DR InterPro; IPR020818; Chaperonin_GroES. DR InterPro; IPR018369; Chaprnonin_Cpn10_CS. DR InterPro; IPR011032; GroES-like. DR PANTHER; PTHR10772; PTHR10772; 1. DR Pfam; PF00166; Cpn10; 1. DR PRINTS; PR00297; CHAPERONIN10. DR SMART; SM00883; Cpn10; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR PROSITE; PS00681; CHAPERONINS_CPN10; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 92 10 kDa chaperonin. FT /FTId=PRO_0000174883. SQ SEQUENCE 92 AA; 10333 MW; 6E07AAEEDB92800D CRC64; MMKVIPLGER LLIKPIKEEK KTEGGIVLPD SAKEKPMKAE VVAVGKIDDD EKFDIKVGDK VIYSKYAGTE IKIDDEDYII IDVNDILAKI EE // ID CHEB_THEMA Reviewed; 344 AA. AC Q9WYN9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 122. DE RecName: Full=Chemotaxis response regulator protein-glutamate methylesterase; DE EC=3.1.1.61; GN Name=cheB; OrderedLocusNames=TM_0408; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in the modulation of the chemotaxis system; CC catalyzes the demethylation of specific methylglutamate residues CC introduced into the chemoreceptors (methyl-accepting chemotaxis CC proteins) by CheR. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein L-glutamate O(5)-methyl ester + H(2)O CC = protein L-glutamate + methanol. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: The N-terminal regulatory domain inhibits the activity of CC the C-terminal effector domain. {ECO:0000250}. CC -!- PTM: Phosphorylated by CheA. Phosphorylation suppresses the CC inhibitory activity of the N-terminal domain (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Contains 1 cheB-type methylesterase domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 response regulatory domain. CC {ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35493.1; -; Genomic_DNA. DR PIR; F72380; F72380. DR RefSeq; NP_228218.1; NC_000853.1. DR RefSeq; WP_004083251.1; NZ_CP011107.1. DR PDB; 3SFT; X-ray; 2.15 A; A=156-344. DR PDB; 3T8Y; X-ray; 1.90 A; A/B=1-144. DR PDBsum; 3SFT; -. DR PDBsum; 3T8Y; -. DR ProteinModelPortal; Q9WYN9; -. DR STRING; 243274.TM0408; -. DR EnsemblBacteria; AAD35493; AAD35493; TM_0408. DR GeneID; 897407; -. DR KEGG; tma:TM0408; -. DR PATRIC; 23935699; VBITheMar51294_0413. DR eggNOG; ENOG4105CMP; Bacteria. DR eggNOG; COG2201; LUCA. DR InParanoid; Q9WYN9; -. DR KO; K03412; -. DR OMA; MLEMHRA; -. DR OrthoDB; EOG6PKFC7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro. DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.180; -; 1. DR HAMAP; MF_00099; CheB_methylest; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR008248; Sig_transdc_resp-reg_CheB. DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR Pfam; PF01339; CheB_methylest; 1. DR Pfam; PF00072; Response_reg; 1. DR PIRSF; PIRSF000876; RR_chemtxs_CheB; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR SUPFAM; SSF52738; SSF52738; 1. DR PROSITE; PS50122; CHEB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 1: Evidence at protein level; KW 3D-structure; Chemotaxis; Complete proteome; Cytoplasm; Hydrolase; KW Phosphoprotein; Reference proteome. FT CHAIN 1 344 Chemotaxis response regulator protein- FT glutamate methylesterase. FT /FTId=PRO_0000158032. FT DOMAIN 7 124 Response regulatory. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. FT DOMAIN 154 344 CheB-type methylesterase. FT ACT_SITE 166 166 {ECO:0000250}. FT ACT_SITE 193 193 {ECO:0000250}. FT ACT_SITE 289 289 {ECO:0000250}. FT MOD_RES 58 58 4-aspartylphosphate. {ECO:0000250}. FT STRAND 6 11 {ECO:0000244|PDB:3T8Y}. FT HELIX 15 26 {ECO:0000244|PDB:3T8Y}. FT STRAND 31 39 {ECO:0000244|PDB:3T8Y}. FT HELIX 40 50 {ECO:0000244|PDB:3T8Y}. FT STRAND 53 57 {ECO:0000244|PDB:3T8Y}. FT STRAND 62 64 {ECO:0000244|PDB:3T8Y}. FT HELIX 66 76 {ECO:0000244|PDB:3T8Y}. FT STRAND 80 87 {ECO:0000244|PDB:3T8Y}. FT HELIX 93 100 {ECO:0000244|PDB:3T8Y}. FT STRAND 105 108 {ECO:0000244|PDB:3T8Y}. FT STRAND 110 114 {ECO:0000244|PDB:3T8Y}. FT HELIX 116 121 {ECO:0000244|PDB:3T8Y}. FT HELIX 122 132 {ECO:0000244|PDB:3T8Y}. FT STRAND 160 165 {ECO:0000244|PDB:3SFT}. FT HELIX 169 173 {ECO:0000244|PDB:3SFT}. FT TURN 174 176 {ECO:0000244|PDB:3SFT}. FT HELIX 177 179 {ECO:0000244|PDB:3SFT}. FT STRAND 188 192 {ECO:0000244|PDB:3SFT}. FT HELIX 199 209 {ECO:0000244|PDB:3SFT}. FT STRAND 211 216 {ECO:0000244|PDB:3SFT}. FT STRAND 227 230 {ECO:0000244|PDB:3SFT}. FT STRAND 235 242 {ECO:0000244|PDB:3SFT}. FT STRAND 245 251 {ECO:0000244|PDB:3SFT}. FT STRAND 256 258 {ECO:0000244|PDB:3SFT}. FT HELIX 263 274 {ECO:0000244|PDB:3SFT}. FT HELIX 275 277 {ECO:0000244|PDB:3SFT}. FT STRAND 278 282 {ECO:0000244|PDB:3SFT}. FT STRAND 284 287 {ECO:0000244|PDB:3SFT}. FT HELIX 291 299 {ECO:0000244|PDB:3SFT}. FT STRAND 303 307 {ECO:0000244|PDB:3SFT}. FT HELIX 309 311 {ECO:0000244|PDB:3SFT}. FT STRAND 313 316 {ECO:0000244|PDB:3SFT}. FT HELIX 317 323 {ECO:0000244|PDB:3SFT}. FT STRAND 328 331 {ECO:0000244|PDB:3SFT}. FT HELIX 333 335 {ECO:0000244|PDB:3SFT}. FT HELIX 336 343 {ECO:0000244|PDB:3SFT}. SQ SEQUENCE 344 AA; 37623 MW; 419C1E09B2267E55 CRC64; MTDRVIRVLV VDDSAFMRMV LKDIIDSQPD MKVVGFAKDG LEAVEKAIEL KPDVITMDIE MPNLNGIEAL KLIMKKAPTR VIMVSSLTEE GAAITIEALR NGAVDFITKP HGSISLTFRQ VAPELLEKIR QAMNVDPRTL LFKPKVSRLT ITKPAVSGKI VVIGSSTGGP RSLDMIIPNL PKNFPAPIVV VQHMPPGFTK SLAMRLDSTS ELTVKEAEDG EEVKPGFVYI APGDFHLGLK AQNGKVFFFL DKSDKINNVR PAVDFTLDKA AEIYKSKTIA VILTGMGKDG TKGAFKVKFY GGTVIAEDKE TCVVFGMPKS VIEEGYADYV LPAYKIPEKL IELV // ID CINAL_THEMA Reviewed; 408 AA. AC Q9S5X1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=CinA-like protein {ECO:0000255|HAMAP-Rule:MF_00226}; GN OrderedLocusNames=TM_0703; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the CinA family. {ECO:0000255|HAMAP- CC Rule:MF_00226}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35785.1; -; Genomic_DNA. DR PIR; E72346; E72346. DR RefSeq; NP_228512.1; NC_000853.1. DR RefSeq; WP_004081038.1; NZ_CP011107.1. DR ProteinModelPortal; Q9S5X1; -. DR STRING; 243274.TM0703; -. DR EnsemblBacteria; AAD35785; AAD35785; TM_0703. DR GeneID; 898370; -. DR KEGG; tma:TM0703; -. DR PATRIC; 23936324; VBITheMar51294_0715. DR eggNOG; ENOG4105CEV; Bacteria. DR eggNOG; COG1058; LUCA. DR eggNOG; COG1546; LUCA. DR InParanoid; Q9S5X1; -. DR KO; K03742; -. DR OMA; GTAPGMI; -. DR OrthoDB; EOG61S359; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.40.980.10; -; 1. DR Gene3D; 3.90.950.20; -; 1. DR HAMAP; MF_00226_B; CinA_B; 1. DR InterPro; IPR008136; CinA_C. DR InterPro; IPR008135; Competence-induced_CinA. DR InterPro; IPR001453; MoaB/Mog_dom. DR Pfam; PF02464; CinA; 1. DR Pfam; PF00994; MoCF_biosynth; 1. DR PIRSF; PIRSF006728; CinA; 1. DR SMART; SM00852; MoCF_biosynth; 1. DR SUPFAM; SSF142433; SSF142433; 1. DR SUPFAM; SSF53218; SSF53218; 1. DR TIGRFAMs; TIGR00200; cinA_nterm; 1. DR TIGRFAMs; TIGR00177; molyb_syn; 1. DR TIGRFAMs; TIGR00199; PncC_domain; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 408 CinA-like protein. FT /FTId=PRO_0000156786. SQ SEQUENCE 408 AA; 45181 MW; F198A086614C76E7 CRC64; MKKAAIITIG SELLEGLILN KNAQFLCQEL KNLGYRVVKV STVGDDLISI SEEVKTLLLK VDLLILTGGL GPTQDDLTRD AVAKVLNRSL KLNEELLSKI KEKIKKYHSE IPQNIERQAL VIDGAEVLDN PVGSAPGQLL TVDGKIVILL PGPPRELIPM FNALKDRLRT PDALYQVVLK YYSIPEAVLE DLLKDILYSQ NIVEVATMAD HVEGVRLRLT THMKNKEYLD EMVKKILDKT GEHLYGVNDE KMEEVVVRLL KDRKKTLAVA ESCTGGMLSS LVVNVPGASE VFIGGVVAYS NDLKKHILGV REDTLKKHGA VSEECVQEMT EGLKKLTGAD ICVSISGIAG PSGGTPEKPV GTVFIDIFEH EHITMRYNFT GDRNMIRTRS AMMALENLRK YLKGRERV // ID CLPP_THEMA Reviewed; 203 AA. AC Q9WZF9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444}; DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444}; DE AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444}; GN Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; GN OrderedLocusNames=TM_0695; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Cleaves peptides in various proteins in a process that CC requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a CC major role in the degradation of misfolded proteins. CC {ECO:0000255|HAMAP-Rule:MF_00444}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in CC the presence of ATP and magnesium. Alpha-casein is the usual test CC substrate. In the absence of ATP, only oligopeptides shorter than CC five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; CC and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- CC and -Tyr-|-Trp bonds also occurs). {ECO:0000255|HAMAP- CC Rule:MF_00444}. CC -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings CC which stack back to back to give a disk-like structure with a CC central cavity, resembling the structure of eukaryotic CC proteasomes. {ECO:0000255|HAMAP-Rule:MF_00444}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}. CC -!- SIMILARITY: Belongs to the peptidase S14 family. CC {ECO:0000255|HAMAP-Rule:MF_00444}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35777.1; -; Genomic_DNA. DR PIR; E72345; E72345. DR RefSeq; NP_228504.1; NC_000853.1. DR RefSeq; WP_004081059.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZF9; -. DR SMR; Q9WZF9; 13-202. DR STRING; 243274.TM0695; -. DR MEROPS; S14.001; -. DR EnsemblBacteria; AAD35777; AAD35777; TM_0695. DR GeneID; 898362; -. DR KEGG; tma:TM0695; -. DR PATRIC; 23936308; VBITheMar51294_0707. DR eggNOG; ENOG4105CCQ; Bacteria. DR eggNOG; COG0740; LUCA. DR InParanoid; Q9WZF9; -. DR KO; K01358; -. DR OMA; ARMNELM; -. DR OrthoDB; EOG6Z3KQ0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.226.10; -; 1. DR HAMAP; MF_00444; ClpP; 1. DR InterPro; IPR001907; ClpP. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR023562; ClpP/TepA. DR InterPro; IPR033135; ClpP_His_AS. DR InterPro; IPR018215; ClpP_Ser_AS. DR PANTHER; PTHR10381; PTHR10381; 1. DR Pfam; PF00574; CLP_protease; 1. DR PRINTS; PR00127; CLPPROTEASEP. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR00493; clpP; 1. DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1. DR PROSITE; PS00381; CLP_PROTEASE_SER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Protease; Reference proteome; KW Serine protease. FT CHAIN 1 203 ATP-dependent Clp protease proteolytic FT subunit. FT /FTId=PRO_0000179698. FT ACT_SITE 107 107 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00444}. FT ACT_SITE 132 132 {ECO:0000255|HAMAP-Rule:MF_00444}. SQ SEQUENCE 203 AA; 22573 MW; 2AFA4E56EC2B04A0 CRC64; MTVKEKKIID QYVPIVVEST GRYERAYDIF SRLLKDRIVF LGSPIDDYVA NLVIAQLLFL EAEDPDKDVY LYINSPGGSV TAGLAIYDTM QYIKCDVSTI CVGQAASMAA VLLAAGAKGK RYALPNARIM IHQPLGGAEG PAKDVEIITR ELLRIKDLLN RILSKHTGQP IEKIEKDTDR DFFMSAEEAK EYGIVDKVVS TRE // ID CHEX_THEMA Reviewed; 155 AA. AC Q9X1V3; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=CheY-P phosphatase CheX; DE EC=3.-.-.-; GN Name=cheX; OrderedLocusNames=TM_1618; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS), AND SUBUNIT. RX PubMed=15546616; DOI=10.1016/j.molcel.2004.10.018; RA Park S.-Y., Chao X., Gonzalez-Bonet G., Beel B.D., Bilwes A.M., RA Crane B.R.; RT "Structure and function of an unusual family of protein phosphatases: RT the bacterial chemotaxis proteins CheC and CheX."; RL Mol. Cell 16:563-574(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RG Midwest center for structural genomics (MCSG); RT "The crystal structure of the protein CheX from Thermotoga maritima."; RL Submitted (JAN-2005) to the PDB data bank. CC -!- FUNCTION: Involved in restoring normal CheY-P levels by CC dephosphorylating CheY-P. It has a greater activity than CheC. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15546616}. CC -!- SIMILARITY: Belongs to the CheC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36685.1; -; Genomic_DNA. DR PIR; D72232; D72232. DR RefSeq; NP_229418.1; NC_000853.1. DR RefSeq; WP_004082082.1; NZ_CP011107.1. DR PDB; 1SQU; X-ray; 2.40 A; A/B=1-155. DR PDB; 1XKO; X-ray; 2.48 A; A/B=1-155. DR PDBsum; 1SQU; -. DR PDBsum; 1XKO; -. DR ProteinModelPortal; Q9X1V3; -. DR SMR; Q9X1V3; 1-155. DR STRING; 243274.TM1618; -. DR EnsemblBacteria; AAD36685; AAD36685; TM_1618. DR GeneID; 897932; -. DR KEGG; tma:TM1618; -. DR PATRIC; 23938210; VBITheMar51294_1637. DR eggNOG; ENOG4108W5Z; Bacteria. DR eggNOG; COG1406; LUCA. DR InParanoid; Q9X1V3; -. DR KO; K03409; -. DR OMA; VSKMMGM; -. DR OrthoDB; EOG683S91; -. DR EvolutionaryTrace; Q9X1V3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR Gene3D; 3.40.1550.10; -; 1. DR InterPro; IPR028976; CheC-like_dom. DR InterPro; IPR028051; CheX-like_dom. DR Pfam; PF13690; CheX; 1. DR SUPFAM; SSF103039; SSF103039; 1. PE 1: Evidence at protein level; KW 3D-structure; Chemotaxis; Complete proteome; Hydrolase; KW Reference proteome. FT CHAIN 1 155 CheY-P phosphatase CheX. FT /FTId=PRO_0000250998. FT HELIX 3 19 {ECO:0000244|PDB:1SQU}. FT STRAND 34 36 {ECO:0000244|PDB:1SQU}. FT STRAND 40 51 {ECO:0000244|PDB:1SQU}. FT STRAND 54 60 {ECO:0000244|PDB:1SQU}. FT HELIX 62 72 {ECO:0000244|PDB:1SQU}. FT TURN 73 75 {ECO:0000244|PDB:1SQU}. FT HELIX 83 105 {ECO:0000244|PDB:1SQU}. FT STRAND 111 113 {ECO:0000244|PDB:1SQU}. FT STRAND 117 120 {ECO:0000244|PDB:1SQU}. FT STRAND 125 127 {ECO:0000244|PDB:1SQU}. FT STRAND 130 141 {ECO:0000244|PDB:1SQU}. FT STRAND 145 151 {ECO:0000244|PDB:1SQU}. SQ SEQUENCE 155 AA; 16449 MW; C5ED437A8400C37C CRC64; MDARIVNALI GSVYETIRDV LGIEPKTGKP STVSHIEIPH SLVTVIGITG GIEGSLIYSF SSETALKVVS AMMGGMEYNQ LDELALSAIG ELGNMTAGKL AMKLEHLGKH VDITPPTVVS GRDLKIKSFG VILKLPISVF SEEDFDLHLS VKSGG // ID CHEY_THEMA Reviewed; 120 AA. AC Q56312; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 123. DE RecName: Full=Chemotaxis protein CheY; GN Name=cheY; OrderedLocusNames=TM_0700; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RX PubMed=8550470; RA Swanson R.V., Sanna M.G., Simon M.I.; RT "Thermostable chemotaxis proteins from the hyperthermophilic bacterium RT Thermotoga maritima."; RL J. Bacteriol. 178:484-489(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND PHOSPHORYLATION AT ASP-54. RX PubMed=9521117; DOI=10.1002/pro.5560070221; RA Usher K.C., de la Cruz A.F.A., Dahlquist F.W., Swanson R.V., RA Simon M.I., Remington S.J.; RT "Crystal structures of CheY from Thermotoga maritima do not support RT conventional explanations for the structural basis of enhanced RT thermostability."; RL Protein Sci. 7:403-412(1998). CC -!- FUNCTION: Involved in the transmission of sensory signals from the CC chemoreceptors to the flagellar motors. CheY seems to regulate the CC clockwise (CW) rotation (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: Phosphorylated by CheA. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 response regulatory domain. CC {ECO:0000255|PROSITE-ProRule:PRU00169}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U30501; AAA96389.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35782.1; -; Genomic_DNA. DR PIR; B72346; B72346. DR RefSeq; NP_228509.1; NC_000853.1. DR RefSeq; WP_004081049.1; NZ_CP011107.1. DR PDB; 1TMY; X-ray; 1.90 A; A=1-120. DR PDB; 1U0S; X-ray; 1.90 A; Y=2-119. DR PDB; 2LLE; NMR; -; A=1-103. DR PDB; 2TMY; X-ray; 2.30 A; A=1-120. DR PDB; 3TMY; X-ray; 2.20 A; A/B=1-120. DR PDB; 4IGA; X-ray; 1.73 A; A=1-120. DR PDB; 4QWV; X-ray; 2.45 A; A=4-104. DR PDB; 4QYW; X-ray; 1.60 A; A=2-120. DR PDB; 4TMY; X-ray; 2.80 A; A/B=1-120. DR PDBsum; 1TMY; -. DR PDBsum; 1U0S; -. DR PDBsum; 2LLE; -. DR PDBsum; 2TMY; -. DR PDBsum; 3TMY; -. DR PDBsum; 4IGA; -. DR PDBsum; 4QWV; -. DR PDBsum; 4QYW; -. DR PDBsum; 4TMY; -. DR ProteinModelPortal; Q56312; -. DR SMR; Q56312; 2-119. DR DIP; DIP-35249N; -. DR IntAct; Q56312; 1. DR STRING; 243274.TM0700; -. DR EnsemblBacteria; AAD35782; AAD35782; TM_0700. DR GeneID; 898367; -. DR KEGG; tma:TM0700; -. DR PATRIC; 23936318; VBITheMar51294_0712. DR eggNOG; ENOG4107YTP; Bacteria. DR eggNOG; COG0784; LUCA. DR InParanoid; Q56312; -. DR KO; K03413; -. DR OMA; VVMCTSV; -. DR OrthoDB; EOG6PKFC7; -. DR EvolutionaryTrace; Q56312; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-KW. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR Pfam; PF00072; Response_reg; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 1: Evidence at protein level; KW 3D-structure; Chemotaxis; Complete proteome; Cytoplasm; KW Flagellar rotation; Magnesium; Metal-binding; Phosphoprotein; KW Reference proteome; Two-component regulatory system. FT CHAIN 1 120 Chemotaxis protein CheY. FT /FTId=PRO_0000081055. FT DOMAIN 4 119 Response regulatory. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. FT METAL 9 9 Magnesium. FT METAL 10 10 Magnesium. FT METAL 54 54 Magnesium. FT METAL 56 56 Magnesium; via carbonyl oxygen. FT MOD_RES 54 54 4-aspartylphosphate. FT {ECO:0000255|PROSITE-ProRule:PRU00169, FT ECO:0000269|PubMed:9521117}. FT STRAND 4 8 {ECO:0000244|PDB:4QYW}. FT HELIX 12 24 {ECO:0000244|PDB:4QYW}. FT STRAND 28 35 {ECO:0000244|PDB:4QYW}. FT HELIX 36 46 {ECO:0000244|PDB:4QYW}. FT STRAND 49 56 {ECO:0000244|PDB:4QYW}. FT STRAND 58 60 {ECO:0000244|PDB:4QYW}. FT HELIX 62 72 {ECO:0000244|PDB:4QYW}. FT STRAND 78 83 {ECO:0000244|PDB:4QYW}. FT HELIX 87 95 {ECO:0000244|PDB:4QYW}. FT STRAND 100 105 {ECO:0000244|PDB:4QYW}. FT HELIX 108 118 {ECO:0000244|PDB:4QYW}. SQ SEQUENCE 120 AA; 13217 MW; 195AC95641264E63 CRC64; MGKRVLIVDD AAFMRMMLKD IITKAGYEVA GEATNGREAV EKYKELKPDI VTMDITMPEM NGIDAIKEIM KIDPNAKIIV CSAMGQQAMV IEAIKAGAKD FIVKPFQPSR VVEALNKVSK // ID CHEC_THEMA Reviewed; 205 AA. AC Q9X006; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=CheY-P phosphatase CheC; DE EC=3.-.-.-; GN Name=cheC; OrderedLocusNames=TM_0904; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND MUTAGENESIS OF GLU-13; RP ASN-16; GLU-112 AND ASN-115. RX PubMed=15546616; DOI=10.1016/j.molcel.2004.10.018; RA Park S.-Y., Chao X., Gonzalez-Bonet G., Beel B.D., Bilwes A.M., RA Crane B.R.; RT "Structure and function of an unusual family of protein phosphatases: RT the bacterial chemotaxis proteins CheC and CheX."; RL Mol. Cell 16:563-574(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CHED. RX PubMed=16469702; DOI=10.1016/j.cell.2005.11.046; RA Chao X., Muff T.J., Park S.-Y., Zhang S., Pollard A.M., Ordal G.W., RA Bilwes A.M., Crane B.R.; RT "A receptor-modifying deamidase in complex with a signaling RT phosphatase reveals reciprocal regulation."; RL Cell 124:561-571(2006). CC -!- FUNCTION: Involved in restoring normal CheY-P levels by CC dephosphorylating CheY-P. Inhibits CheD by incorporating in its CC fold a structural motif that mimics a CheD substrate recognition CC site to bait and inactivate it. CC -!- SUBUNIT: Heterodimer with CheD. The CheC-CheD heterodimer CC interacts with phosphorylated CheY. The CheC-CheD dimer has higher CC phosphatase activity than CheC alone. CC {ECO:0000269|PubMed:16469702}. CC -!- SIMILARITY: Belongs to the CheC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35985.1; -; Genomic_DNA. DR PIR; G72318; G72318. DR RefSeq; NP_228712.1; NC_000853.1. DR RefSeq; WP_004080665.1; NZ_CP011107.1. DR PDB; 1XKR; X-ray; 1.75 A; A=1-205. DR PDB; 2F9Z; X-ray; 2.40 A; A/B=1-205. DR PDBsum; 1XKR; -. DR PDBsum; 2F9Z; -. DR ProteinModelPortal; Q9X006; -. DR SMR; Q9X006; 1-204. DR STRING; 243274.TM0904; -. DR EnsemblBacteria; AAD35985; AAD35985; TM_0904. DR GeneID; 898578; -. DR KEGG; tma:TM0904; -. DR PATRIC; 23936739; VBITheMar51294_0918. DR eggNOG; ENOG4107PHP; Bacteria. DR eggNOG; COG1776; LUCA. DR InParanoid; Q9X006; -. DR KO; K03410; -. DR OMA; ELGNIGT; -. DR OrthoDB; EOG6ZPSZN; -. DR EvolutionaryTrace; Q9X006; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR Gene3D; 3.40.1550.10; -; 1. DR InterPro; IPR007597; CheC. DR InterPro; IPR028976; CheC-like_dom. DR Pfam; PF04509; CheC; 2. DR SUPFAM; SSF103039; SSF103039; 1. PE 1: Evidence at protein level; KW 3D-structure; Chemotaxis; Complete proteome; Hydrolase; KW Reference proteome. FT CHAIN 1 205 CheY-P phosphatase CheC. FT /FTId=PRO_0000250997. FT MUTAGEN 13 13 E->S: Loss of activity, in absence of FT CheD; in presence of CheD, activity FT greater than wild-type CheC alone. Loss FT of activity, in absence of CheD; when FT associated with S-112. In presence of FT CheD, reduced activity but exceeds FT activity of CheC alone; when associated FT with S-112. FT {ECO:0000269|PubMed:15546616}. FT MUTAGEN 16 16 N->S: Loss of activity, in absence of FT CheD; in presence of CheD, activity FT greater than wild-type CheC alone. Loss FT of activity, in absence of CheD; when FT associated with S-115. In presence of FT CheD, almost no activity; when associated FT with S-115. FT {ECO:0000269|PubMed:15546616}. FT MUTAGEN 112 112 E->S: Loss of activity, in absence of FT CheD; in presence of CheD, activity FT greater than wild-type CheC alone. Loss FT of activity, in absence of CheD; when FT associated with S-13. In presence of FT CheD, reduced activity but exceeds FT activity of CheC alone; when associated FT with S-13. {ECO:0000269|PubMed:15546616}. FT MUTAGEN 115 115 N->S: Loss of activity, in absence of FT CheD; in presence of CheD, reduced FT activity. Loss of activity, in absence of FT CheD; when associated with S-16. In FT presence of CheD, almost no activity; FT when associated with S-16. FT {ECO:0000269|PubMed:15546616}. FT HELIX 5 30 {ECO:0000244|PDB:1XKR}. FT STRAND 34 37 {ECO:0000244|PDB:1XKR}. FT STRAND 41 45 {ECO:0000244|PDB:1XKR}. FT HELIX 46 52 {ECO:0000244|PDB:1XKR}. FT STRAND 59 71 {ECO:0000244|PDB:1XKR}. FT STRAND 73 79 {ECO:0000244|PDB:1XKR}. FT HELIX 81 92 {ECO:0000244|PDB:1XKR}. FT HELIX 104 129 {ECO:0000244|PDB:1XKR}. FT STRAND 133 135 {ECO:0000244|PDB:1XKR}. FT STRAND 139 144 {ECO:0000244|PDB:1XKR}. FT HELIX 145 157 {ECO:0000244|PDB:1XKR}. FT STRAND 164 174 {ECO:0000244|PDB:1XKR}. FT STRAND 177 179 {ECO:0000244|PDB:1XKR}. FT STRAND 181 189 {ECO:0000244|PDB:1XKR}. FT HELIX 193 199 {ECO:0000244|PDB:1XKR}. SQ SEQUENCE 205 AA; 22549 MW; 0FF88D0E26A927B7 CRC64; MKISERQKDL LKEIGNIGAG NAATAISYMI NKKVEISVPN VEIVPISKVI FIAKDPEEIV VGVKMPVTGD IEGSVLLIMG TTVVKKILEI LTGRAPDNLL NLDEFSASAL REIGNIMCGT YVSALADFLG FKIDTLPPQL VIDMISAIFA EASIEELEDN SEDQIVFVET LLKVEEEEEP LTSYMMMIPK PGYLVKIFER MGIQE // ID CIMA_THEMA Reviewed; 538 AA. AC Q9WZ22; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=(R)-citramalate synthase {ECO:0000305}; DE EC=2.3.1.182 {ECO:0000250|UniProtKB:Q74C76}; GN Name=cimA {ECO:0000305}; OrderedLocusNames=TM_0552; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl- CC coenzyme A to form (R)-citramalate. CC {ECO:0000250|UniProtKB:Q74C76}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + pyruvate + H(2)O = CoA + (2R)-2- CC hydroxy-2-methylbutanedioate. {ECO:0000250|UniProtKB:Q74C76}. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2- CC oxobutanoate from pyruvate: step 1/3. CC {ECO:0000250|UniProtKB:Q74C76}. CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35637.1; -; Genomic_DNA. DR PIR; F72362; F72362. DR RefSeq; NP_228362.1; NC_000853.1. DR RefSeq; WP_004081335.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ22; -. DR STRING; 243274.TM0552; -. DR EnsemblBacteria; AAD35637; AAD35637; TM_0552. DR GeneID; 897609; -. DR KEGG; tma:TM0552; -. DR PATRIC; 23936011; VBITheMar51294_0560. DR eggNOG; ENOG4105CYQ; Bacteria. DR eggNOG; COG0119; LUCA. DR InParanoid; Q9WZ22; -. DR KO; K01649; -. DR OMA; KSWDFHV; -. DR OrthoDB; EOG6D8B63; -. DR UniPathway; UPA00047; UER00066. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer. DR InterPro; IPR002034; AIPM/Hcit_synth_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005675; Citramal_synthase. DR InterPro; IPR000891; PYR_CT. DR PANTHER; PTHR10277:SF5; PTHR10277:SF5; 1. DR Pfam; PF00682; HMGL-like; 1. DR Pfam; PF08502; LeuA_dimer; 1. DR SMART; SM00917; LeuA_dimer; 1. DR SUPFAM; SSF110921; SSF110921; 1. DR TIGRFAMs; TIGR00977; citramal_synth; 1. DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Isoleucine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 538 (R)-citramalate synthase. FT /FTId=PRO_0000140472. SQ SEQUENCE 538 AA; 60290 MW; 94F3AF0852C59BA1 CRC64; MSIKVYDTTL RDGAQAFGVS FSLEDKIRIA EALDDLGVHY LEGGWPGSNP KDIAFFEAVK GMNFKNLKVA AFSSTRRPDV KIEEDANIQT LIKAETPVYT IFGKSWDLHV EKALRTTLEE NLKMIYDTVS YLKRFADEVI YDAEHFFDGY KANREYALKT LKVAEEAGAD CLVLADTNGG TLPHEIEEII EDVKKHVKAP LGIHAHNDSD VAVANTLAAV RKGAVHVQGT INGLGERCGN ANLCSVIPNL VLKMGLEVIP KENLKKLFDV AHLVAELSGR PHIENMPYVG DYAFAHKGGV HVSAIKRDPR TYEHIDPELV GNRRIISISE LSGKSNVLEK IKEMGFEIDE SSPKVREILK KIKELEAQGY HFEGAEASFE LLVRDMLGKR KKYFEFLGFT VMTIKNRDEE SFSEATVKVR VPDEVAKRLG HDEPFEHTAA EGEGPVEALD RAVRKALEKF YPSLKDTKLT DYKVRILNEQ AGTKATTRVL IESSDGKRRW GTVGVSPNII EASWTALLES LEYKLHKDEE EMRNDEEN // ID CLPX_THEMA Reviewed; 406 AA. AC Q9WXZ3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175}; GN Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175}; GN OrderedLocusNames=TM_0146; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. CC It directs the protease to specific substrates. Can perform CC chaperone functions in the absence of ClpP. {ECO:0000255|HAMAP- CC Rule:MF_00175}. CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric CC ring that, in the presence of ATP, binds to fourteen ClpP subunits CC assembled into a disk-like structure with a central cavity, CC resembling the structure of eukaryotic proteasomes. CC {ECO:0000255|HAMAP-Rule:MF_00175}. CC -!- SIMILARITY: Belongs to the ClpX chaperone family. CC {ECO:0000255|HAMAP-Rule:MF_00175}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35239.1; -; Genomic_DNA. DR PIR; H72411; H72411. DR RefSeq; NP_227961.1; NC_000853.1. DR RefSeq; WP_004082752.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXZ3; -. DR SMR; Q9WXZ3; 5-41. DR STRING; 243274.TM0146; -. DR PRIDE; Q9WXZ3; -. DR EnsemblBacteria; AAD35239; AAD35239; TM_0146. DR GeneID; 896978; -. DR KEGG; tma:TM0146; -. DR PATRIC; 23935136; VBITheMar51294_0145. DR eggNOG; ENOG4105CHN; Bacteria. DR eggNOG; COG1219; LUCA. DR InParanoid; Q9WXZ3; -. DR KO; K03544; -. DR OMA; HYKRVQA; -. DR OrthoDB; EOG625JZK; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00175; ClpX; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010603; Znf_CppX_C4. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF10431; ClpB_D2-small; 1. DR Pfam; PF06689; zf-C4_ClpX; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM01086; ClpB_D2-small; 1. DR SMART; SM00994; zf-C4_ClpX; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00382; clpX; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Metal-binding; KW Nucleotide-binding; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1 406 ATP-dependent Clp protease ATP-binding FT subunit ClpX. FT /FTId=PRO_0000160444. FT ZN_FING 6 32 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00175}. FT NP_BIND 111 118 ATP. {ECO:0000255|HAMAP-Rule:MF_00175}. SQ SEQUENCE 406 AA; 45525 MW; C0AC0562538A9668 CRC64; MAGKFCSFCG RDIQQVERLI AGPNNVYICN ECIDLFHDLL RSDRKVRIKN EIKEIPTPAE IKAELDKYII GQERAKKVLS VAVYNHYKRV FSNLDSNDVE IEKSNVLLIG PTGTGKTYLA RILAKILNVP FAIADATPLT EAGYVGEDVE NVVLRLLEAA NFDVERAQYG IIYIDEIDKI AKKSPNPSIT RDVSGEGVQQ ALLKILEGTI ANVPPQGGRK HPYQEFIKVD TRNILFIAGG AFDGLEEIIK RRIQSTTMGF GAEIKSKKEM RLGEILKHVT PDDLVQYGLI PEFVGRFPVI ATLDDLSEDD LVRILKEPKN AVVRQYQKLF EIDGVKLEVT DEALRIIARK ALKRGTGARA LKNVFEEMMI DMMFELPNLK NVEKVVITEE VALGKEKPIV VMRESA // ID CMR5_THEMA Reviewed; 129 AA. AC P58011; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 1. DT 09-DEC-2015, entry version 55. DE RecName: Full=CRISPR system Cmr subunit Cmr5; DE AltName: Full=CRISPR type III-B/RAMP module-associated protein Cmr5; GN Name=cmr5; OrderedLocusNames=TM_1791.1; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP IDENTIFICATION. RA Medigue C., Bocs S.; RL Unpublished observations (APR-2001). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat), is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC sequences complementary to antecedent mobile elements and target CC invading nucleic acids. CRISPR clusters are transcribed and CC processed into CRISPR RNA (crRNA). Part of the Cmr CC ribonucleoprotein complex (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR system Cmr5 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P58011; -. DR InParanoid; P58011; -. DR OMA; IVQNGLM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW. DR Gene3D; 1.10.520.30; -; 1. DR InterPro; IPR023101; AF1862-like_domain. DR InterPro; IPR010160; CRISPR-assoc_prot_Cmr5. DR Pfam; PF09701; Cas_Cmr5; 1. DR SUPFAM; SSF158568; SSF158568; 1. DR TIGRFAMs; TIGR01881; cas_Cmr5; 1. PE 3: Inferred from homology; KW Antiviral protein; Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 129 CRISPR system Cmr subunit Cmr5. FT /FTId=PRO_0000216221. SQ SEQUENCE 129 AA; 14572 MW; 7829649FF369F831 CRC64; MGTCLEVMKM KTLSLELAKL AMNLVEEVEK DKRDDYLRDV KGLGSMIVQN GLMGTILFLK KKGKNKVVDH LGKMIEHLTL EDGIVERLME NEFLDARTYL KAQIAALECA KWLKRCGEVL LGGEENETT // ID COAD_THEMA Reviewed; 161 AA. AC Q9WZK0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 118. DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151}; DE EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00151}; DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00151}; DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151}; DE Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151}; GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151}; Synonyms=kdtB; GN OrderedLocusNames=TM_0741; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and CC pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate + CC 3'-dephospho-CoA. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SIMILARITY: Belongs to the bacterial CoaD family. CC {ECO:0000255|HAMAP-Rule:MF_00151}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35822.1; -; Genomic_DNA. DR PIR; H72339; H72339. DR RefSeq; NP_228550.1; NC_000853.1. DR RefSeq; WP_004080981.1; NZ_CP011107.1. DR PDB; 1VLH; X-ray; 2.20 A; A/B/C/D/E/F=1-161. DR PDBsum; 1VLH; -. DR ProteinModelPortal; Q9WZK0; -. DR SMR; Q9WZK0; 1-158. DR STRING; 243274.TM0741; -. DR EnsemblBacteria; AAD35822; AAD35822; TM_0741. DR GeneID; 898408; -. DR KEGG; tma:TM0741; -. DR PATRIC; 23936402; VBITheMar51294_0754. DR eggNOG; ENOG4108ZEF; Bacteria. DR eggNOG; COG0669; LUCA. DR InParanoid; Q9WZK0; -. DR KO; K00954; -. DR OMA; YELQIAH; -. DR OrthoDB; EOG6MH5J7; -. DR UniPathway; UPA00241; UER00355. DR EvolutionaryTrace; Q9WZK0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00151; PPAT_bact; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR001980; LPS_biosynth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR PRINTS; PR01020; LPSBIOSNTHSS. DR TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Complete proteome; KW Cytoplasm; Nucleotide-binding; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 161 Phosphopantetheine adenylyltransferase. FT /FTId=PRO_0000156296. FT STRAND 2 7 {ECO:0000244|PDB:1VLH}. FT HELIX 14 24 {ECO:0000244|PDB:1VLH}. FT STRAND 28 35 {ECO:0000244|PDB:1VLH}. FT HELIX 46 56 {ECO:0000244|PDB:1VLH}. FT TURN 57 59 {ECO:0000244|PDB:1VLH}. FT STRAND 63 68 {ECO:0000244|PDB:1VLH}. FT HELIX 72 79 {ECO:0000244|PDB:1VLH}. FT STRAND 83 88 {ECO:0000244|PDB:1VLH}. FT HELIX 94 107 {ECO:0000244|PDB:1VLH}. FT STRAND 112 117 {ECO:0000244|PDB:1VLH}. FT HELIX 120 122 {ECO:0000244|PDB:1VLH}. FT HELIX 127 135 {ECO:0000244|PDB:1VLH}. FT TURN 141 143 {ECO:0000244|PDB:1VLH}. FT HELIX 146 155 {ECO:0000244|PDB:1VLH}. SQ SEQUENCE 161 AA; 18249 MW; 4A0F62B9D368496F CRC64; MKAVYPGSFD PITLGHVDII KRALSIFDEL VVLVTENPRK KCMFTLEERK KLIEEVLSDL DGVKVDVHHG LLVDYLKKHG IKVLVRGLRA VTDYEYELQM ALANKKLYSD LETVFLIASE KFSFISSSLV KEVALYGGDV TEWVPPEVAR ALNEKLKEGK R // ID COAX_THEMA Reviewed; 246 AA. AC Q9WZY5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Type III pantothenate kinase; DE EC=2.7.1.33; DE AltName: Full=PanK-III; DE AltName: Full=Pantothenic acid kinase; GN Name=coaX; OrderedLocusNames=TM_0883; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, SUBUNIT, AND KINETIC RP PARAMETERS. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=16855243; DOI=10.1128/JB.00469-06; RA Yang K., Eyobo Y., Brand L.A., Martynowski D., Tomchick D., RA Strauss E., Zhang H.; RT "Crystal structure of a type III pantothenate kinase: insight into the RT mechanism of an essential coenzyme A biosynthetic enzyme universally RT distributed in bacteria."; RL J. Bacteriol. 188:5532-5540(2006). CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the CC first step in CoA biosynthesis. {ECO:0000269|PubMed:16855243}. CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'- CC phosphopantothenate. CC -!- COFACTOR: CC Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000250}; CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; CC Note=A monovalent cation. Ammonium or potassium. {ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=40 uM for pantothenate (at 50 degrees Celsius) CC {ECO:0000269|PubMed:16855243}; CC KM=6.0 mM for ATP (at 50 degrees Celsius) CC {ECO:0000269|PubMed:16855243}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 1/5. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16855243}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35964.1; -; Genomic_DNA. DR PIR; D72320; D72320. DR RefSeq; NP_228691.1; NC_000853.1. DR RefSeq; WP_004080709.1; NZ_CP011107.1. DR PDB; 2GTD; X-ray; 2.00 A; A/B/C/D/E/F=1-245. DR PDB; 3BEX; X-ray; 1.51 A; A/B/C/D/E/F=1-246. DR PDB; 3BF1; X-ray; 2.30 A; A/B/C/D/E/F=1-246. DR PDB; 3BF3; X-ray; 1.63 A; A/B/C/D/E/F=1-246. DR PDBsum; 2GTD; -. DR PDBsum; 3BEX; -. DR PDBsum; 3BF1; -. DR PDBsum; 3BF3; -. DR ProteinModelPortal; Q9WZY5; -. DR SMR; Q9WZY5; 1-245. DR STRING; 243274.TM0883; -. DR EnsemblBacteria; AAD35964; AAD35964; TM_0883. DR GeneID; 898557; -. DR KEGG; tma:TM0883; -. DR PATRIC; 23936697; VBITheMar51294_0897. DR eggNOG; ENOG4105CGM; Bacteria. DR eggNOG; COG1521; LUCA. DR InParanoid; Q9WZY5; -. DR KO; K03525; -. DR OMA; HEPWLTL; -. DR OrthoDB; EOG6G20K0; -. DR BRENDA; 2.7.1.33; 6331. DR SABIO-RK; Q9WZY5; -. DR UniPathway; UPA00241; UER00352. DR EvolutionaryTrace; Q9WZY5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01274; Pantothen_kinase_3; 1. DR InterPro; IPR004619; Type_III_PanK. DR Pfam; PF03309; Pan_kinase; 1. DR TIGRFAMs; TIGR00671; baf; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Complete proteome; KW Cytoplasm; Kinase; Metal-binding; Nucleotide-binding; Potassium; KW Reference proteome; Transferase. FT CHAIN 1 246 Type III pantothenate kinase. FT /FTId=PRO_0000267598. FT NP_BIND 6 13 ATP. {ECO:0000250}. FT REGION 103 106 Substrate binding. {ECO:0000250}. FT ACT_SITE 105 105 Proton acceptor. {ECO:0000255}. FT METAL 125 125 Monovalent cation. {ECO:0000255}. FT BINDING 128 128 ATP. {ECO:0000255}. FT BINDING 179 179 Substrate. {ECO:0000250}. FT STRAND 1 7 {ECO:0000244|PDB:3BEX}. FT STRAND 9 22 {ECO:0000244|PDB:3BEX}. FT STRAND 24 29 {ECO:0000244|PDB:3BEX}. FT HELIX 36 47 {ECO:0000244|PDB:3BEX}. FT HELIX 48 53 {ECO:0000244|PDB:3BEX}. FT STRAND 54 62 {ECO:0000244|PDB:3BEX}. FT HELIX 64 78 {ECO:0000244|PDB:3BEX}. FT STRAND 89 94 {ECO:0000244|PDB:3BEX}. FT HELIX 99 101 {ECO:0000244|PDB:3BEX}. FT HELIX 104 116 {ECO:0000244|PDB:3BEX}. FT STRAND 121 136 {ECO:0000244|PDB:3BEX}. FT STRAND 139 147 {ECO:0000244|PDB:3BEX}. FT HELIX 149 158 {ECO:0000244|PDB:3BEX}. FT STRAND 173 178 {ECO:0000244|PDB:3BEX}. FT HELIX 179 206 {ECO:0000244|PDB:3BEX}. FT STRAND 211 215 {ECO:0000244|PDB:3BEX}. FT HELIX 219 224 {ECO:0000244|PDB:3BEX}. FT STRAND 228 230 {ECO:0000244|PDB:3BEX}. FT HELIX 234 244 {ECO:0000244|PDB:3BEX}. SQ SEQUENCE 246 AA; 27154 MW; 9E0309AD462CF266 CRC64; MYLLVDVGNT HSVFSITEDG KTFRRWRLST GVFQTEDELF SHLHPLLGDA MREIKGIGVA SVVPTQNTVI ERFSQKYFHI SPIWVKAKNG CVKWNVKNPS EVGADRVANV VAFVKEYGKN GIIIDMGTAT TVDLVVNGSY EGGAILPGFF MMVHSLFRGT AKLPLVEVKP ADFVVGKDTE ENIRLGVVNG SVYALEGIIG RIKEVYGDLP VVLTGGQSKI VKDMIKHEIF DEDLTIKGVY HFCFGD // ID CORA_THEMA Reviewed; 351 AA. AC Q9WZ31; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 110. DE RecName: Full=Cobalt/magnesium transport protein CorA {ECO:0000305}; GN Name=corA; OrderedLocusNames=TM_0561; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP ASP-89; ASP-253; LEU-280; MET-291; LEU-294; PRO-303; GLY-312; MET-313 RP AND ASN-314. RX PubMed=18276588; DOI=10.1074/jbc.M707889200; RA Payandeh J., Li C., Ramjeesingh M., Poduch E., Bear C.E., Pai E.F.; RT "Probing structure-function relationships and gating mechanisms in the RT CorA Mg2+ transport system."; RL J. Biol. Chem. 283:11721-11733(2008). RN [3] RP FUNCTION IN COBALT TRANSPORT, SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=21454699; DOI=10.1074/jbc.M111.222166; RA Xia Y., Lundbaeck A.K., Sahaf N., Nordlund G., Brzezinski P., RA Eshaghi S.; RT "Co2+ selectivity of Thermotoga maritima CorA and its inability to RT regulate Mg2+ homeostasis present a new class of CorA proteins."; RL J. Biol. Chem. 286:16525-16532(2011). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF ILE-310; RP TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND RP TYR-327. RX PubMed=22722933; DOI=10.1074/jbc.M112.371484; RA Palombo I., Daley D.O., Rapp M.; RT "The periplasmic loop provides stability to the open state of the CorA RT magnesium channel."; RL J. Biol. Chem. 287:27547-27555(2012). RN [5] RP FUNCTION, MUTAGENESIS OF ASN-288, AND SUBCELLULAR LOCATION. RX PubMed=23091000; DOI=10.1073/pnas.1210076109; RA Guskov A., Nordin N., Reynaud A., Engman H., Lundback A.K., Jong A.J., RA Cornvik T., Phua T., Eshaghi S.; RT "Structural insights into the mechanisms of Mg2+ uptake, transport, RT and gating by CorA."; RL Proc. Natl. Acad. Sci. U.S.A. 109:18459-18464(2012). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF TYR-311; RP GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327. RX PubMed=23781956; DOI=10.1021/bi4007397; RA Palombo I., Daley D.O., Rapp M.; RT "Why is the GMN motif conserved in the CorA/Mrs2/Alr1 superfamily of RT magnesium transport proteins?"; RL Biochemistry 52:4842-4847(2013). RN [7] {ECO:0000244|PDB:2HN2} RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION, RP TOPOLOGY, MOTIF, DOMAIN, AND MUTAGENESIS OF ASP-253. RX PubMed=16902408; DOI=10.1038/sj.emboj.7601269; RA Payandeh J., Pai E.F.; RT "A structural basis for Mg2+ homeostasis and the CorA translocation RT cycle."; RL EMBO J. 25:3762-3773(2006). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, RP TOPOLOGY, DOMAIN, AND MOTIF. RX PubMed=16598263; DOI=10.1038/nature04642; RA Lunin V.V., Dobrovetsky E., Khutoreskaya G., Zhang R., Joachimiak A., RA Doyle D.A., Bochkarev A., Maguire M.E., Edwards A.M., Koth C.M.; RT "Crystal structure of the CorA Mg2+ transporter."; RL Nature 440:833-837(2006). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, RP TOPOLOGY, DOMAIN, AND MOTIF. RX PubMed=16857941; DOI=10.1126/science.1127121; RA Eshaghi S., Niegowski D., Kohl A., Molina D.M., Lesley S.A., RA Nordlund P.; RT "Crystal structure of a divalent metal ion transporter CorA at 2.9 RT Angstrom resolution."; RL Science 313:354-357(2006). RN [10] {ECO:0000244|PDB:4EEB, ECO:0000244|PDB:4EED} RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN RP COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, RP TOPOLOGY, AND DOMAIN. RX PubMed=23112165; DOI=10.1073/pnas.1209018109; RA Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.; RT "Structural asymmetry in the magnesium channel CorA points to RT sequential allosteric regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012). RN [11] {ECO:0000244|PDB:4I0U} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR RP LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF ASP-89; ASN-288; RP THR-295; THR-299 AND THR-305. RX PubMed=23425532; DOI=10.1042/BJ20121745; RA Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H., RA Eshaghi S.; RT "Exploring the structure and function of Thermotoga maritima CorA RT reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ RT transport."; RL Biochem. J. 451:365-374(2013). RN [12] RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF APOPROTEIN AND IN RP COMPLEX WITH MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND RP DOMAIN. RX PubMed=26871634; DOI=10.1016/j.cell.2015.12.055; RA Matthies D., Dalmas O., Borgnia M.J., Dominik P.K., Merk A., Rao P., RA Reddy B.G., Islam S., Bartesaghi A., Perozo E., Subramaniam S.; RT "Cryo-EM Structures of the magnesium channel CorA reveal symmetry RT break upon gating."; RL Cell 164:747-756(2016). CC -!- FUNCTION: Mediates influx of magnesium ions (PubMed:18276588, CC PubMed:22722933, PubMed:23781956, PubMed:23112165). Mediates CC Co(2+) uptake (PubMed:21454699, PubMed:23091000, PubMed:23425532). CC Has high selectivity for Co(2+) (PubMed:21454699, CC PubMed:23425532). Alternates between open and closed states. CC Activated by low cytoplasmic Mg(2+) levels. Inactive when CC cytoplasmic Mg(2+) levels are high (PubMed:23112165, CC PubMed:23425532, PubMed:26871634). {ECO:0000269|PubMed:18276588, CC ECO:0000269|PubMed:21454699, ECO:0000269|PubMed:22722933, CC ECO:0000269|PubMed:23091000, ECO:0000269|PubMed:23112165, CC ECO:0000269|PubMed:23425532, ECO:0000269|PubMed:23781956, CC ECO:0000305|PubMed:26871634}. CC -!- ENZYME REGULATION: Inhibited by cobalt hexaammine. CC {ECO:0000269|PubMed:18276588}. CC -!- SUBUNIT: Homopentamer (PubMed:22722933, PubMed:23781956, CC PubMed:16902408, PubMed:16598263, PubMed:16857941, CC PubMed:23112165, PubMed:23425532, PubMed:26871634). In the absence CC of Mg(2+), interactions between subunits are weakened, and dimers, CC trimers and tetramers can be observed in vitro (PubMed:22722933, CC PubMed:26871634). {ECO:0000269|PubMed:16598263, CC ECO:0000269|PubMed:16857941, ECO:0000269|PubMed:16902408, CC ECO:0000269|PubMed:22722933, ECO:0000269|PubMed:23112165, CC ECO:0000269|PubMed:23425532, ECO:0000269|PubMed:23781956, CC ECO:0000269|PubMed:26871634}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000269|PubMed:23112165, ECO:0000305|PubMed:16598263, CC ECO:0000305|PubMed:16857941, ECO:0000305|PubMed:16902408, CC ECO:0000305|PubMed:18276588, ECO:0000305|PubMed:21454699, CC ECO:0000305|PubMed:22722933, ECO:0000305|PubMed:23091000, CC ECO:0000305|PubMed:23425532, ECO:0000305|PubMed:23781956, CC ECO:0000305|PubMed:26871634}; Multi-pass membrane protein CC {ECO:0000269|PubMed:16598263, ECO:0000269|PubMed:16857941, CC ECO:0000269|PubMed:16902408, ECO:0000269|PubMed:23112165, CC ECO:0000269|PubMed:23425532, ECO:0000269|PubMed:26871634, CC ECO:0000305|PubMed:23091000}. CC -!- DOMAIN: The central ion permeation pathway is formed by the first CC transmembrane domain from each of the five subunits. Mg(2+) CC binding strengthens interactions between subunits and leads to the CC formation of a symmetrical homopentamer surrounding a closed ion CC permeation pathway (PubMed:23091000, PubMed:16902408, CC PubMed:16598263, PubMed:16857941, PubMed:23112165, CC PubMed:23425532, PubMed:26871634). Co(2+) binding also induces a CC conformation change (PubMed:21454699). Low Mg(2+) concentrations CC trigger both a conformation change within each subunit and a CC loosening of the interactions between subunits. This results in an CC open ion conduction pathway. In addition, this results in a less CC symmetrical shape of the whole complex (PubMed:23112165, CC PubMed:26871634). {ECO:0000269|PubMed:16598263, CC ECO:0000269|PubMed:16857941, ECO:0000269|PubMed:16902408, CC ECO:0000269|PubMed:21454699, ECO:0000269|PubMed:23112165, CC ECO:0000269|PubMed:23425532, ECO:0000269|PubMed:26871634, CC ECO:0000305|PubMed:23091000}. CC -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) CC (TC 1.A.35) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35646.1; -; Genomic_DNA. DR PIR; H72360; H72360. DR RefSeq; NP_228371.1; NC_000853.1. DR RefSeq; WP_004081315.1; NZ_CP011107.1. DR PDB; 2BBH; X-ray; 1.85 A; A=1-266. DR PDB; 2BBJ; X-ray; 3.90 A; A/B/D/E/F=1-351. DR PDB; 2HN2; X-ray; 3.70 A; A/B/C/D/E=1-351. DR PDB; 2IUB; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=1-351. DR PDB; 3JCF; X-ray; 3.80 A; A/B/C/D/E=1-351. DR PDB; 3JCG; X-ray; 7.06 A; A/B/C/D/E=1-351. DR PDB; 3JCH; X-ray; 7.06 A; A/B/C/D/E=1-351. DR PDB; 4EEB; X-ray; 3.80 A; A/B/C/D/E=26-351. DR PDB; 4EED; X-ray; 3.92 A; A/B/C/D/E=26-351. DR PDB; 4I0U; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=1-351. DR PDBsum; 2BBH; -. DR PDBsum; 2BBJ; -. DR PDBsum; 2HN2; -. DR PDBsum; 2IUB; -. DR PDBsum; 3JCF; -. DR PDBsum; 3JCG; -. DR PDBsum; 3JCH; -. DR PDBsum; 4EEB; -. DR PDBsum; 4EED; -. DR PDBsum; 4I0U; -. DR ProteinModelPortal; Q9WZ31; -. DR SMR; Q9WZ31; 5-349. DR DIP; DIP-59006N; -. DR STRING; 243274.TM0561; -. DR TCDB; 1.A.35.3.2; the cora metal ion transporter (mit) family. DR EnsemblBacteria; AAD35646; AAD35646; TM_0561. DR GeneID; 897621; -. DR KEGG; tma:TM0561; -. DR PATRIC; 23936029; VBITheMar51294_0569. DR eggNOG; ENOG4105D7N; Bacteria. DR eggNOG; COG0598; LUCA. DR InParanoid; Q9WZ31; -. DR KO; K03284; -. DR OMA; GENYILY; -. DR OrthoDB; EOG6W9X5H; -. DR BRENDA; 3.6.3.2; 6331. DR EvolutionaryTrace; Q9WZ31; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB. DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB. DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IMP:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IMP:UniProtKB. DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central. DR GO; GO:0006824; P:cobalt ion transport; IMP:UniProtKB. DR GO; GO:1903830; P:magnesium ion transmembrane transport; IMP:UniProtKB. DR GO; GO:0015693; P:magnesium ion transport; IEA:InterPro. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR InterPro; IPR004488; Mg/Co-transport_prot_CorA. DR InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB. DR Pfam; PF01544; CorA; 1. DR TIGRFAMs; TIGR00383; corA; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Cobalt; Coiled coil; KW Complete proteome; Ion transport; Magnesium; Membrane; Metal-binding; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 351 Cobalt/magnesium transport protein CorA. FT /FTId=PRO_0000239049. FT TOPO_DOM 1 292 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 293 313 Helical. {ECO:0000269|PubMed:16598263, FT ECO:0000269|PubMed:16857941, FT ECO:0000269|PubMed:16902408, FT ECO:0000269|PubMed:23112165, FT ECO:0000269|PubMed:23425532, FT ECO:0000269|PubMed:26871634}. FT TOPO_DOM 314 324 Extracellular. {ECO:0000305}. FT TRANSMEM 325 345 Helical. {ECO:0000269|PubMed:16598263, FT ECO:0000269|PubMed:16857941, FT ECO:0000269|PubMed:16902408, FT ECO:0000269|PubMed:23112165, FT ECO:0000269|PubMed:23425532, FT ECO:0000269|PubMed:26871634}. FT TOPO_DOM 346 351 Cytoplasmic. {ECO:0000305}. FT COILED 178 225 {ECO:0000255}. FT MOTIF 312 314 Probable selectivity filter. FT {ECO:0000305|PubMed:16598263, FT ECO:0000305|PubMed:16857941, FT ECO:0000305|PubMed:16902408, FT ECO:0000305|PubMed:23781956}. FT COMPBIAS 346 349 Poly-Lys. FT SITE 288 288 Essential for ion permeation. FT {ECO:0000269|PubMed:23091000}. FT SITE 294 294 Important for closing the ion permeation FT pathway in the closed state. FT {ECO:0000269|PubMed:16598263, FT ECO:0000269|PubMed:16857941, FT ECO:0000269|PubMed:16902408, FT ECO:0000269|PubMed:18276588}. FT SITE 295 295 Threonine that confers selectivity for FT Co(2+) transport. FT {ECO:0000269|PubMed:23425532}. FT MUTAGEN 89 89 D->F,K: Decreases ion transport. FT {ECO:0000269|PubMed:18276588, FT ECO:0000269|PubMed:23425532}. FT MUTAGEN 253 253 D->K: Increases protein stability. FT Decreases ion transport. FT {ECO:0000269|PubMed:16902408, FT ECO:0000269|PubMed:18276588}. FT MUTAGEN 280 280 L->A: Decreases ion transport. FT {ECO:0000269|PubMed:18276588}. FT MUTAGEN 288 288 N->L: Abolishes Co(2+) uptake. FT {ECO:0000269|PubMed:23091000, FT ECO:0000269|PubMed:23425532}. FT MUTAGEN 291 291 M->A: No effect on ion transport. FT {ECO:0000269|PubMed:18276588}. FT MUTAGEN 294 294 L->A,V: Increases ion transport by FT suppression of an obstruction in the FT transmembrane ion permeation pathway. FT {ECO:0000269|PubMed:18276588}. FT MUTAGEN 295 295 T->L: Strongly reduces Co(2+) uptake. FT Abolishes Co(2+) uptake; when associated FT with L-299. FT {ECO:0000269|PubMed:23425532}. FT MUTAGEN 295 295 T->M: Strongly reduces Co(2+) uptake. FT {ECO:0000269|PubMed:23425532}. FT MUTAGEN 295 295 T->S: No significant decrease of Co(2+) FT uptake, but abolishes selectivity for FT Co(2+). {ECO:0000269|PubMed:23425532}. FT MUTAGEN 299 299 T->L: Reduces Co(2+) uptake. Abolishes FT Co(2+) uptake; when associated with L- FT 295. {ECO:0000269|PubMed:23425532}. FT MUTAGEN 299 299 T->M: No effect on Co(2+) uptake. FT {ECO:0000269|PubMed:23425532}. FT MUTAGEN 299 299 T->S: Abolishes Co(2+) uptake. FT {ECO:0000269|PubMed:23425532}. FT MUTAGEN 303 303 P->A,G,I: Increases ion transport by FT suppression of a kink in the FT transmembrane ion permeation pathway. FT {ECO:0000269|PubMed:18276588}. FT MUTAGEN 305 305 T->L: Abolishes Co(2+) uptake. FT {ECO:0000269|PubMed:23425532}. FT MUTAGEN 310 310 I->A: Increases ion transport. FT {ECO:0000269|PubMed:22722933}. FT MUTAGEN 311 311 Y->A: Abolishes pentamerization. FT Abolishes ion transport. FT {ECO:0000269|PubMed:22722933, FT ECO:0000269|PubMed:23781956}. FT MUTAGEN 311 311 Y->F: No effect on pentamerization. No FT effect on ion transport. FT {ECO:0000269|PubMed:23781956}. FT MUTAGEN 312 312 G->A: No effect on pentamerization. FT Abolishes ion transport. FT {ECO:0000269|PubMed:18276588, FT ECO:0000269|PubMed:22722933}. FT MUTAGEN 312 312 G->F: No effect on pentamerization. FT Abolishes ion transport. FT {ECO:0000269|PubMed:23781956}. FT MUTAGEN 313 313 M->A: Abolishes pentamerization. FT Abolishes ion transport. FT {ECO:0000269|PubMed:18276588, FT ECO:0000269|PubMed:22722933}. FT MUTAGEN 313 313 M->C,I,L,V: Abolishes pentamerization. FT Abolishes ion transport. FT {ECO:0000269|PubMed:23781956}. FT MUTAGEN 314 314 N->A: Abolishes pentamerization. FT Abolishes ion transport. FT {ECO:0000269|PubMed:18276588}. FT MUTAGEN 314 314 N->D,E,T: Abolishes pentamerization. FT Abolishes ion transport. FT {ECO:0000269|PubMed:23781956}. FT MUTAGEN 314 314 N->Q: No effect on pentamerization. FT Abolishes ion transport. FT {ECO:0000269|PubMed:23781956}. FT MUTAGEN 315 315 F->A: Abolishes pentamerization. FT Abolishes ion transport. FT {ECO:0000269|PubMed:22722933, FT ECO:0000269|PubMed:23781956}. FT MUTAGEN 315 315 F->W: No effect on pentamerization. FT Increases ion transport. FT {ECO:0000269|PubMed:23781956}. FT MUTAGEN 318 318 M->A: Impairs pentamerization. Decreases FT ion transport. FT {ECO:0000269|PubMed:22722933}. FT MUTAGEN 318 318 M->I,L,V: No effect on pentamerization. FT Decreases ion transport. FT {ECO:0000269|PubMed:23781956}. FT MUTAGEN 321 321 L->A: Impairs pentamerization. Decreases FT ion transport. FT {ECO:0000269|PubMed:22722933}. FT MUTAGEN 321 321 L->I: No effect on pentamerization. FT Decreases ion transport. FT {ECO:0000269|PubMed:23781956}. FT MUTAGEN 321 321 L->V: No effect on pentamerization. No FT effect on ion transport. FT {ECO:0000269|PubMed:23781956}. FT MUTAGEN 327 327 Y->A: Abolishes pentamerization. Strongly FT decreases ion transport. FT {ECO:0000269|PubMed:22722933, FT ECO:0000269|PubMed:23781956}. FT MUTAGEN 327 327 Y->F: No effect on pentamerization. FT Increases ion transport. FT {ECO:0000269|PubMed:23781956}. FT MUTAGEN 327 327 Y->W: Abolishes pentamerization. Mildly FT decreases ion transport. FT {ECO:0000269|PubMed:23781956}. FT STRAND 5 7 {ECO:0000244|PDB:4I0U}. FT STRAND 28 35 {ECO:0000244|PDB:2BBH}. FT STRAND 38 45 {ECO:0000244|PDB:2BBH}. FT HELIX 47 49 {ECO:0000244|PDB:2BBH}. FT HELIX 51 55 {ECO:0000244|PDB:2BBH}. FT STRAND 60 65 {ECO:0000244|PDB:2BBH}. FT HELIX 70 80 {ECO:0000244|PDB:2BBH}. FT HELIX 84 91 {ECO:0000244|PDB:2BBH}. FT STRAND 98 101 {ECO:0000244|PDB:2BBH}. FT STRAND 103 114 {ECO:0000244|PDB:2BBH}. FT TURN 117 120 {ECO:0000244|PDB:4I0U}. FT STRAND 123 132 {ECO:0000244|PDB:2BBH}. FT STRAND 135 143 {ECO:0000244|PDB:2BBH}. FT HELIX 148 155 {ECO:0000244|PDB:2BBH}. FT HELIX 161 163 {ECO:0000244|PDB:2BBH}. FT HELIX 166 197 {ECO:0000244|PDB:2BBH}. FT HELIX 208 242 {ECO:0000244|PDB:2BBH}. FT HELIX 244 272 {ECO:0000244|PDB:4I0U}. FT HELIX 275 310 {ECO:0000244|PDB:4I0U}. FT STRAND 311 313 {ECO:0000244|PDB:4I0U}. FT HELIX 319 322 {ECO:0000244|PDB:4I0U}. FT HELIX 326 344 {ECO:0000244|PDB:4I0U}. FT TURN 345 348 {ECO:0000244|PDB:4I0U}. SQ SEQUENCE 351 AA; 41446 MW; 6A845EC612A4A0BA CRC64; MEEKRLSAKK GLPPGTLVYT GKYREDFEIE VMNYSIEEFR EFKTTDVESV LPFRDSSTPT WINITGIHRT DVVQRVGEFF GIHPLVLEDI LNVHQRPKVE FFENYVFIVL KMFTYDKNLH ELESEQVSLI LTKNCVLMFQ EKIGDVFDPV RERIRYNRGI IRKKRADYLL YSLIDALVDD YFVLLEKIDD EIDVLEEEVL ERPEKETVQR THQLKRNLVE LRKTIWPLRE VLSSLYRDVP PLIEKETVPY FRDVYDHTIQ IADTVETFRD IVSGLLDVYL SSVSNKTNEV MKVLTIIATI FMPLTFIAGI YGMNFEYMPE LRWKWGYPVV LAVMGVIAVI MVVYFKKKKW L // ID COMB_THEMA Reviewed; 227 AA. AC Q9WZQ4; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Probable 2-phosphosulfolactate phosphatase; DE EC=3.1.3.71; GN Name=comB; OrderedLocusNames=TM_0797; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: (2R)-2-phospho-3-sulfolactate + H(2)O = (2R)- CC 3-sulfolactate + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the ComB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35879.1; -; Genomic_DNA. DR PIR; F72334; F72334. DR RefSeq; NP_228606.1; NC_000853.1. DR RefSeq; WP_004080870.1; NZ_CP011107.1. DR PDB; 2YYV; X-ray; 1.65 A; A/B=1-227. DR PDB; 2YZO; X-ray; 1.85 A; A/B=1-227. DR PDBsum; 2YYV; -. DR PDBsum; 2YZO; -. DR ProteinModelPortal; Q9WZQ4; -. DR SMR; Q9WZQ4; 2-225. DR STRING; 243274.TM0797; -. DR EnsemblBacteria; AAD35879; AAD35879; TM_0797. DR GeneID; 898465; -. DR KEGG; tma:TM0797; -. DR PATRIC; 23936514; VBITheMar51294_0809. DR eggNOG; ENOG4108N5B; Bacteria. DR eggNOG; COG2045; LUCA. DR InParanoid; Q9WZQ4; -. DR KO; K05979; -. DR OMA; FRATSCM; -. DR OrthoDB; EOG6SNDT4; -. DR EvolutionaryTrace; Q9WZQ4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0050532; F:2-phosphosulfolactate phosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:InterPro. DR Gene3D; 3.90.1560.10; -; 1. DR HAMAP; MF_00490; ComB; 1. DR InterPro; IPR005238; ComB-like. DR InterPro; IPR022995; ProB_Pase_ComB. DR Pfam; PF04029; 2-ph_phosp; 1. DR SUPFAM; SSF142823; SSF142823; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Magnesium; KW Reference proteome. FT CHAIN 1 227 Probable 2-phosphosulfolactate FT phosphatase. FT /FTId=PRO_0000081477. FT STRAND 3 7 {ECO:0000244|PDB:2YYV}. FT STRAND 15 20 {ECO:0000244|PDB:2YYV}. FT TURN 22 24 {ECO:0000244|PDB:2YYV}. FT HELIX 25 34 {ECO:0000244|PDB:2YYV}. FT STRAND 38 42 {ECO:0000244|PDB:2YYV}. FT HELIX 46 51 {ECO:0000244|PDB:2YYV}. FT STRAND 57 61 {ECO:0000244|PDB:2YYV}. FT HELIX 77 79 {ECO:0000244|PDB:2YYV}. FT HELIX 82 85 {ECO:0000244|PDB:2YYV}. FT STRAND 89 93 {ECO:0000244|PDB:2YYV}. FT HELIX 97 103 {ECO:0000244|PDB:2YYV}. FT STRAND 109 112 {ECO:0000244|PDB:2YYV}. FT HELIX 114 116 {ECO:0000244|PDB:2YYV}. FT HELIX 117 124 {ECO:0000244|PDB:2YYV}. FT STRAND 129 134 {ECO:0000244|PDB:2YYV}. FT HELIX 143 156 {ECO:0000244|PDB:2YYV}. FT HELIX 163 173 {ECO:0000244|PDB:2YYV}. FT HELIX 178 185 {ECO:0000244|PDB:2YYV}. FT HELIX 187 194 {ECO:0000244|PDB:2YYV}. FT HELIX 198 204 {ECO:0000244|PDB:2YYV}. FT STRAND 215 217 {ECO:0000244|PDB:2YYV}. FT STRAND 220 222 {ECO:0000244|PDB:2YYV}. SQ SEQUENCE 227 AA; 24857 MW; ED32447E6140D9F8 CRC64; MVDVVMAPCS PVECRTAVVI DVLRATSTIV TALSNGASGV IPVKTIEEAL EKKKEGVLIC GERNAQKPKG FNLGNSPLEY RKEKISGKTI VLTTTNGTQV IEKIRSEEII AASFLNLSAV VEYLKSKEDI LLVCAGTNGR FSLEDFLLAG AIVKRLKRND LGDGAHAAER YFESVENTRE EIKKHSSHAK RLISLGFEND IEFCTTEDLF KTVPALVNGV FILKEFP // ID COAE_THEMA Reviewed; 180 AA. AC Q9X1A7; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 118. DE RecName: Full=Dephospho-CoA kinase; DE EC=2.7.1.24; DE AltName: Full=Dephosphocoenzyme A kinase; GN Name=coaE; OrderedLocusNames=TM_1387; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group CC of dephosphocoenzyme A to form coenzyme A. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = ADP + CoA. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 5/5. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DPCK (dephospho-CoA kinase) domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36457.1; -; Genomic_DNA. DR PIR; D72262; D72262. DR RefSeq; NP_229188.1; NC_000853.1. DR RefSeq; WP_004081589.1; NZ_CP011107.1. DR PDB; 2GRJ; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-180. DR PDBsum; 2GRJ; -. DR ProteinModelPortal; Q9X1A7; -. DR SMR; Q9X1A7; 1-176. DR STRING; 243274.TM1387; -. DR EnsemblBacteria; AAD36457; AAD36457; TM_1387. DR GeneID; 898091; -. DR KEGG; tma:TM1387; -. DR PATRIC; 23937716; VBITheMar51294_1399. DR eggNOG; ENOG41083IT; Bacteria. DR eggNOG; COG0237; LUCA. DR InParanoid; Q9X1A7; -. DR KO; K00859; -. DR OMA; DVDKEYH; -. DR OrthoDB; EOG6HTP3H; -. DR UniPathway; UPA00241; UER00356. DR EvolutionaryTrace; Q9X1A7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004140; F:dephospho-CoA kinase activity; IBA:GO_Central. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1. DR InterPro; IPR001977; Depp_CoAkinase. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01121; CoaE; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00152; TIGR00152; 1. DR PROSITE; PS51219; DPCK; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Complete proteome; KW Cytoplasm; Kinase; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 180 Dephospho-CoA kinase. FT /FTId=PRO_0000173021. FT DOMAIN 2 180 DPCK. FT NP_BIND 7 14 ATP. {ECO:0000255}. FT STRAND 1 6 {ECO:0000244|PDB:2GRJ}. FT HELIX 13 24 {ECO:0000244|PDB:2GRJ}. FT STRAND 27 30 {ECO:0000244|PDB:2GRJ}. FT HELIX 31 41 {ECO:0000244|PDB:2GRJ}. FT HELIX 43 50 {ECO:0000244|PDB:2GRJ}. FT HELIX 52 54 {ECO:0000244|PDB:2GRJ}. FT STRAND 55 60 {ECO:0000244|PDB:2GRJ}. FT HELIX 62 69 {ECO:0000244|PDB:2GRJ}. FT HELIX 73 96 {ECO:0000244|PDB:2GRJ}. FT STRAND 100 105 {ECO:0000244|PDB:2GRJ}. FT TURN 107 113 {ECO:0000244|PDB:2GRJ}. FT HELIX 114 117 {ECO:0000244|PDB:2GRJ}. FT STRAND 119 125 {ECO:0000244|PDB:2GRJ}. FT HELIX 128 134 {ECO:0000244|PDB:2GRJ}. FT HELIX 138 142 {ECO:0000244|PDB:2GRJ}. FT STRAND 152 156 {ECO:0000244|PDB:2GRJ}. FT HELIX 161 175 {ECO:0000244|PDB:2GRJ}. SQ SEQUENCE 180 AA; 20331 MW; 59321BA1139E5488 CRC64; MVIGVTGKIG TGKSTVCEIL KNKYGAHVVN VDRIGHEVLE EVKEKLVELF GGSVLEDGKV NRKKLAGIVF ESRENLKKLE LLVHPLMKKR VQEIINKTSG LIVIEAALLK RMGLDQLCDH VITVVASRET ILKRNREADR RLKFQEDIVP QGIVVANNST LEDLEKKVEE VMKLVWEKRE // ID CSP_THEMA Reviewed; 66 AA. AC O54310; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 13-APR-2016, entry version 120. DE RecName: Full=Cold shock-like protein; GN Name=csp; OrderedLocusNames=TM_1683; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10048332; DOI=10.1110/ps.8.2.394; RA Welker C., Bohm G., Schurig H., Jaenicke R.; RT "Cloning, overexpression, purification, and physicochemical RT characterization of a cold shock protein homolog from the RT hyperthermophilic bacterium Thermotoga maritima."; RL Protein Sci. 8:394-403(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP MUTAGENESIS. RX PubMed=10431826; DOI=10.1016/S0014-5793(99)00829-7; RA Frankenberg N., Welker C., Jaenicke R.; RT "Does the elimination of ion pairs affect the thermal stability of RT cold shock protein from the hyperthermophilic bacterium Thermotoga RT maritima?"; RL FEBS Lett. 454:299-302(1999). RN [4] RP STRUCTURE BY NMR. RX PubMed=11322871; DOI=10.1046/j.1432-1327.2001.02127.x; RA Kremer W., Schuler B., Harrieder S., Geyer M., Gronwald W., Welker C., RA Jaenicke R., Kalbitzer H.R.; RT "Solution NMR structure of the cold-shock protein from the RT hyperthermophilic bacterium Thermotoga maritima."; RL Eur. J. Biochem. 268:2527-2539(2001). CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 CSD (cold-shock) domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y11219; CAA72105.1; -; mRNA. DR EMBL; AE000512; AAD36750.1; -; Genomic_DNA. DR PIR; E72222; E72222. DR RefSeq; NP_229483.1; NC_000853.1. DR RefSeq; WP_004082199.1; NZ_CP011107.1. DR PDB; 1G6P; NMR; -; A=1-66. DR PDBsum; 1G6P; -. DR ProteinModelPortal; O54310; -. DR SMR; O54310; 1-66. DR STRING; 243274.TM1683; -. DR EnsemblBacteria; AAD36750; AAD36750; TM_1683. DR GeneID; 897898; -. DR KEGG; tma:TM1683; -. DR PATRIC; 23938340; VBITheMar51294_1700. DR eggNOG; ENOG4105VEQ; Bacteria. DR eggNOG; COG1278; LUCA. DR InParanoid; O54310; -. DR KO; K03704; -. DR OMA; PQAENIQ; -. DR OrthoDB; EOG618R0J; -. DR EvolutionaryTrace; O54310; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR019844; Cold-shock_CS. DR InterPro; IPR012156; Cold_shock_CspA. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR002059; CSP_DNA-bd. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF00313; CSD; 1. DR PIRSF; PIRSF002599; Cold_shock_A; 1. DR PRINTS; PR00050; COLDSHOCK. DR SMART; SM00357; CSP; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS00352; COLD_SHOCK; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Complete proteome; Cytoplasm; KW Direct protein sequencing; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 66 Cold shock-like protein. FT /FTId=PRO_0000100339. FT DOMAIN 3 62 CSD. FT MUTAGEN 9 9 D->N: Destabilization at high FT temperature. FT {ECO:0000269|PubMed:10431826}. FT MUTAGEN 61 61 H->N: No effect on thermal stability. FT {ECO:0000269|PubMed:10431826}. FT STRAND 3 9 {ECO:0000244|PDB:1G6P}. FT TURN 10 13 {ECO:0000244|PDB:1G6P}. FT STRAND 14 19 {ECO:0000244|PDB:1G6P}. FT STRAND 29 32 {ECO:0000244|PDB:1G6P}. FT STRAND 42 51 {ECO:0000244|PDB:1G6P}. FT STRAND 53 55 {ECO:0000244|PDB:1G6P}. FT STRAND 58 65 {ECO:0000244|PDB:1G6P}. SQ SEQUENCE 66 AA; 7473 MW; 851E3B79C6114E8E CRC64; MRGKVKWFDS KKGYGFITKD EGGDVFVHWS AIEMEGFKTL KEGQVVEFEI QEGKKGPQAA HVKVVE // ID CSRA_THEMA Reviewed; 83 AA. AC Q9WY93; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Carbon storage regulator homolog; GN Name=csrA; OrderedLocusNames=TM_0251; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Could accelerate the degradation of some genes CC transcripts potentially through selective RNA binding. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CsrA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35354.1; -; Genomic_DNA. DR PIR; D72399; D72399. DR RefSeq; NP_228065.1; NC_000853.1. DR RefSeq; WP_010865081.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY93; -. DR STRING; 243274.TM0251; -. DR DNASU; 897159; -. DR EnsemblBacteria; AAD35354; AAD35354; TM_0251. DR GeneID; 897159; -. DR KEGG; tma:TM0251; -. DR PATRIC; 23935377; VBITheMar51294_0254. DR eggNOG; ENOG4105VM8; Bacteria. DR eggNOG; COG1551; LUCA. DR InParanoid; Q9WY93; -. DR KO; K03563; -. DR OMA; KHVKILR; -. DR OrthoDB; EOG6DC6PM; -. DR BioCyc; TMAR243274:GC6P-264-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00167; CsrA; 1. DR InterPro; IPR003751; CsrA. DR Pfam; PF02599; CsrA; 1. DR ProDom; PD009007; CsrA; 1. DR TIGRFAMs; TIGR00202; csrA; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; RNA-binding. FT CHAIN 1 83 Carbon storage regulator homolog. FT /FTId=PRO_0000177092. SQ SEQUENCE 83 AA; 9176 MW; 46DEAF73B970EFA5 CRC64; MLVLTRRVGE KIVIGEDIVI TVLKIEGNSV KIGIEAPKHV KILREELYEE LKSENIKASE VSKDDLKGVL RNDKGYKGPS ASS // ID CRCB_THEMA Reviewed; 127 AA. AC Q9WXM8; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Putative fluoride ion transporter CrcB {ECO:0000255|HAMAP-Rule:MF_00454}; GN Name=crcB {ECO:0000255|HAMAP-Rule:MF_00454}; GN OrderedLocusNames=TM_0020; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Important for reducing fluoride concentration in the CC cell, thus reducing its toxicity. {ECO:0000255|HAMAP- CC Rule:MF_00454}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00454}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00454}. CC -!- SIMILARITY: Belongs to the CrcB (TC 9.B.71) family. CC {ECO:0000255|HAMAP-Rule:MF_00454}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35114.1; -; Genomic_DNA. DR PIR; F72427; F72427. DR RefSeq; NP_227836.1; NC_000853.1. DR RefSeq; WP_004082466.1; NZ_CP011107.1. DR STRING; 243274.TM0020; -. DR EnsemblBacteria; AAD35114; AAD35114; TM_0020. DR GeneID; 896835; -. DR KEGG; tma:TM0020; -. DR PATRIC; 23934880; VBITheMar51294_0018. DR eggNOG; ENOG4105WMR; Bacteria. DR eggNOG; COG0239; LUCA. DR InParanoid; Q9WXM8; -. DR KO; K06199; -. DR OMA; HMITTGF; -. DR OrthoDB; EOG6091KP; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0015103; F:inorganic anion transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00454; CrcB; 1. DR InterPro; IPR003691; CrcB. DR Pfam; PF02537; CRCB; 1. DR TIGRFAMs; TIGR00494; crcB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 127 Putative fluoride ion transporter CrcB. FT /FTId=PRO_0000110203. FT TRANSMEM 4 24 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 39 59 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 68 88 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 102 122 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. SQ SEQUENCE 127 AA; 13763 MW; 106DC8E00CC2736D CRC64; MIELDYLTIA FGGAIGAVLR YLVSRTINSL LPFSYIPLGT IIVNSVGSFF LSFLMFAAIE KVPLSKEAIL FFGTGLLGAF TTFSTFTYET LSLIEESPAR GVAYALANLL FAFTCAYFGM ILGRGKV // ID CUTA_THEMA Reviewed; 101 AA. AC Q9X0E6; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=Divalent-cation tolerance protein CutA; GN Name=cutA; OrderedLocusNames=TM_1056; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). RX PubMed=14705033; DOI=10.1002/prot.10585; RA Savchenko A., Skarina T., Evdokimova E., Watson J.D., Laskowski R., RA Arrowsmith C.H., Edwards A.M., Joachimiak A., Zhang R.-G.; RT "X-ray crystal structure of CutA from Thermotoga maritima at 1.4 A RT resolution."; RL Proteins 54:162-165(2004). CC -!- FUNCTION: Involved in resistance toward heavy metals. CC {ECO:0000250}. CC -!- SUBUNIT: Homotrimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the CutA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36133.1; -; Genomic_DNA. DR PIR; B72302; B72302. DR RefSeq; NP_228862.1; NC_000853.1. DR RefSeq; WP_004080448.1; NZ_CP011107.1. DR PDB; 1KR4; X-ray; 1.40 A; A=1-101. DR PDB; 1O5J; X-ray; 1.95 A; A=1-101. DR PDB; 1VHF; X-ray; 1.54 A; A=2-101. DR PDBsum; 1KR4; -. DR PDBsum; 1O5J; -. DR PDBsum; 1VHF; -. DR ProteinModelPortal; Q9X0E6; -. DR SMR; Q9X0E6; 1-101. DR STRING; 243274.TM1056; -. DR EnsemblBacteria; AAD36133; AAD36133; TM_1056. DR GeneID; 897513; -. DR KEGG; tma:TM1056; -. DR PATRIC; 23937041; VBITheMar51294_1069. DR eggNOG; ENOG4108531; Bacteria. DR eggNOG; COG1324; LUCA. DR InParanoid; Q9X0E6; -. DR KO; K03926; -. DR OMA; CVNRLST; -. DR OrthoDB; EOG6KWZ1P; -. DR EvolutionaryTrace; Q9X0E6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0010038; P:response to metal ion; IEA:InterPro. DR InterPro; IPR004323; Ion_tolerance_CutA. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR PANTHER; PTHR23419; PTHR23419; 1. DR Pfam; PF03091; CutA1; 1. DR SUPFAM; SSF54913; SSF54913; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 101 Divalent-cation tolerance protein CutA. FT /FTId=PRO_0000157131. FT STRAND 1 10 {ECO:0000244|PDB:1KR4}. FT HELIX 11 23 {ECO:0000244|PDB:1KR4}. FT STRAND 28 41 {ECO:0000244|PDB:1KR4}. FT STRAND 44 58 {ECO:0000244|PDB:1KR4}. FT HELIX 59 61 {ECO:0000244|PDB:1KR4}. FT HELIX 62 72 {ECO:0000244|PDB:1KR4}. FT STRAND 74 77 {ECO:0000244|PDB:1KR4}. FT STRAND 80 83 {ECO:0000244|PDB:1KR4}. FT HELIX 90 99 {ECO:0000244|PDB:1KR4}. SQ SEQUENCE 101 AA; 12177 MW; DB2039392BC83777 CRC64; MILVYSTFPN EEKALEIGRK LLEKRLIACF NAFEIRSGYW WKGEIVQDKE WAAIFKTTEE KEKELYEELR KLHPYETPAI FTLKVENVLT EYMNWLRESV L // ID CSD_THEMA Reviewed; 413 AA. AC Q9X191; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Probable cysteine desulfurase; DE EC=2.8.1.7; GN Name=csd; OrderedLocusNames=TM_1371; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium CC atoms from L-cysteine, L-cystine, L-selenocysteine, and L- CC selenocystine to produce L-alanine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-cysteine + acceptor = L-alanine + S- CC sulfanyl-acceptor. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. Csd subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36460.1; -; Genomic_DNA. DR PIR; D72260; D72260. DR RefSeq; NP_229172.1; NC_000853.1. DR RefSeq; WP_004081567.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X191; -. DR STRING; 243274.TM1371; -. DR EnsemblBacteria; AAD36460; AAD36460; TM_1371. DR GeneID; 898108; -. DR KEGG; tma:TM1371; -. DR PATRIC; 23937682; VBITheMar51294_1383. DR eggNOG; ENOG4105C9B; Bacteria. DR eggNOG; COG0520; LUCA. DR InParanoid; Q9X191; -. DR KO; K04487; -. DR OMA; MIDFVGL; -. DR OrthoDB; EOG68DD0M; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR010970; Cys_dSase_SufS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00266; Aminotran_5; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01979; sufS; 1. PE 3: Inferred from homology; KW Complete proteome; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 413 Probable cysteine desulfurase. FT /FTId=PRO_0000150319. FT ACT_SITE 363 363 Cysteine persulfide intermediate. FT {ECO:0000250}. FT MOD_RES 223 223 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 413 AA; 46749 MW; 092866323FF984F0 CRC64; MLSTGLYEDF PTLKMKINGK RIVYLDSAAT TLKPKQVVKK LEEFYYNSYA NVHRAVHTLA VRATTEFEET REEFAEFLGA SPEEIIFTSG TTMAINLAVV SLLRSGILKE DDLVLVSLLE HHANFVPWLR LSKFHGYRID FIRPSGRFGT LEMDDLLKHR DKNPKVVAIT GLSNVTGQRI PVEELRNVFP NSIILLDGAQ LIPHEPVKPK EIGVDFLAFS LHKMLGPTGV GVLYGKREVL EQMEPFLYGG EMIDRVSLED VTFNELPYKF EAGTPNIADI VASREALRYL KETGFDSVHE KIEQLTQMAL KEMMKIGGVE IYGPLDERQH GIVSFNVKGI HPHDVAHILD QEFGIAVRSG HHCAQPLMSI LKEQSQIDFP NSTCRASFYI YNTEEDVKIL VEGVKKVKEW FSR // ID DAPH_THEMA Reviewed; 236 AA. AC Q9X1K7; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01691}; DE EC=2.3.1.89 {ECO:0000255|HAMAP-Rule:MF_01691}; DE AltName: Full=Tetrahydrodipicolinate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01691}; DE Short=THP acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01691}; DE Short=Tetrahydropicolinate acetylase {ECO:0000255|HAMAP-Rule:MF_01691}; GN Name=dapH {ECO:0000255|HAMAP-Rule:MF_01691}; GN OrderedLocusNames=TM_1519; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the transfer of an acetyl group from acetyl- CC CoA to tetrahydrodipicolinate. {ECO:0000255|HAMAP-Rule:MF_01691}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + (S)-2,3,4,5-tetrahydropyridine- CC 2,6-dicarboxylate + H(2)O = CoA + L-2-acetamido-6- CC oxoheptanedioate. {ECO:0000255|HAMAP-Rule:MF_01691}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate CC (acetylase route): step 1/3. {ECO:0000255|HAMAP-Rule:MF_01691}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC DapH subfamily. {ECO:0000255|HAMAP-Rule:MF_01691}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36586.1; -; Genomic_DNA. DR PIR; H72245; H72245. DR RefSeq; NP_229319.1; NC_000853.1. DR RefSeq; WP_010865352.1; NC_000853.1. DR ProteinModelPortal; Q9X1K7; -. DR SMR; Q9X1K7; 4-219. DR STRING; 243274.TM1519; -. DR EnsemblBacteria; AAD36586; AAD36586; TM_1519. DR GeneID; 897546; -. DR KEGG; tma:TM1519; -. DR PATRIC; 23937996; VBITheMar51294_1536. DR eggNOG; ENOG4105DMJ; Bacteria. DR eggNOG; COG2171; LUCA. DR InParanoid; Q9X1K7; -. DR KO; K00674; -. DR OMA; NNAVIMM; -. DR OrthoDB; EOG68H8BV; -. DR BioCyc; TMAR243274:GC6P-1559-MONOMER; -. DR UniPathway; UPA00034; UER00022. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0047200; F:tetrahydrodipicolinate N-acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01691; DapH; 1. DR InterPro; IPR019873; DapH. DR InterPro; IPR013710; DapH_N. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF08503; DapH_N; 1. DR Pfam; PF00132; Hexapep; 1. DR Pfam; PF14602; Hexapep_2; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR03532; DapD_Ac; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase; Amino-acid biosynthesis; Complete proteome; KW Diaminopimelate biosynthesis; Lysine biosynthesis; Reference proteome; KW Repeat; Transferase. FT CHAIN 1 236 2,3,4,5-tetrahydropyridine-2,6- FT dicarboxylate N-acetyltransferase. FT /FTId=PRO_0000376729. SQ SEQUENCE 236 AA; 25283 MW; 0F6130C1238F317E CRC64; MSELDAREII EMIAKAKKKT PIVAYIKGDL AGIDFSSFKF FGDERFGILF GEYEDFKKLL EEHREKIEDY HLEVKARNSA LPLADLTKYK ARIEPGAIIR DMVEIGEGAV IMMGAVINVG AVIGEGTMID MNAVVGGRAI IGKKCHIGAG AVIAGVIEPP SAKPVVIEDE VLVGANAVIL EGVTVGKGAV VAAGAVVTKD VPPYTVVAGV PARVIKQIDE KTKEKTKIVD ELRNLE // ID DBH_THEMA Reviewed; 90 AA. AC P36206; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 17-FEB-2016, entry version 113. DE RecName: Full=DNA-binding protein HU; GN Name=hup; OrderedLocusNames=TM_0266; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Markiewicz P.G., Ehret S., Miller J.H.; RT "The histone-like protein (HU) of Thermotoga maritima."; RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RX PubMed=9757133; DOI=10.1107/S0907444998000341; RA Christodoulou E., Vorgias C.E.; RT "Cloning, overproduction, purification and crystallization of the DNA RT binding protein HU from the hyperthermophilic eubacterium Thermotoga RT maritima."; RL Acta Crystallogr. D 54:1043-1045(1998). CC -!- FUNCTION: Histone-like DNA-binding protein which is capable of CC wrapping DNA to stabilize it, and thus to prevent its denaturation CC under extreme environmental conditions. CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L23541; AAA27416.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35355.1; -; Genomic_DNA. DR PIR; H72396; H72396. DR RefSeq; NP_228079.1; NC_000853.1. DR RefSeq; WP_010865085.1; NC_000853.1. DR PDB; 1B8Z; X-ray; 1.60 A; A/B=1-90. DR PDB; 1RIY; X-ray; 1.80 A; A=1-90. DR PDBsum; 1B8Z; -. DR PDBsum; 1RIY; -. DR ProteinModelPortal; P36206; -. DR SMR; P36206; 1-90. DR STRING; 243274.TM0266; -. DR EnsemblBacteria; AAD35355; AAD35355; TM_0266. DR GeneID; 897177; -. DR KEGG; tma:TM0266; -. DR PATRIC; 23935409; VBITheMar51294_0270. DR eggNOG; ENOG4105K70; Bacteria. DR eggNOG; COG0776; LUCA. DR InParanoid; P36206; -. DR KO; K03530; -. DR OMA; MNSITYE; -. DR OrthoDB; EOG615VS6; -. DR BioCyc; TMAR243274:GC6P-279-MONOMER; -. DR EvolutionaryTrace; P36206; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW. DR GO; GO:1903506; P:regulation of nucleic acid-templated transcription; IBA:GO_Central. DR Gene3D; 4.10.520.10; -; 1. DR InterPro; IPR000119; Hist_DNA-bd. DR InterPro; IPR020816; Histone-like_DNA-bd_CS. DR InterPro; IPR010992; IHF-like_DNA-bd_dom. DR Pfam; PF00216; Bac_DNA_binding; 1. DR PRINTS; PR01727; DNABINDINGHU. DR SMART; SM00411; BHL; 1. DR SUPFAM; SSF47729; SSF47729; 1. DR PROSITE; PS00045; HISTONE_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA condensation; DNA-binding; KW Reference proteome. FT CHAIN 1 90 DNA-binding protein HU. FT /FTId=PRO_0000104989. FT CONFLICT 2 2 T -> N (in Ref. 1; AAA27416). FT {ECO:0000305}. FT HELIX 3 14 {ECO:0000244|PDB:1B8Z}. FT HELIX 18 37 {ECO:0000244|PDB:1B8Z}. FT STRAND 42 44 {ECO:0000244|PDB:1B8Z}. FT TURN 45 47 {ECO:0000244|PDB:1B8Z}. FT STRAND 48 51 {ECO:0000244|PDB:1B8Z}. FT STRAND 78 81 {ECO:0000244|PDB:1B8Z}. FT HELIX 83 89 {ECO:0000244|PDB:1B8Z}. SQ SEQUENCE 90 AA; 9980 MW; 7C5F31A262DD60D6 CRC64; MTKKELIDRV AKKAGAKKKD VKLILDTILE TITEALAKGE KVQIVGFGSF EVRKAAARKG VNPQTRKPIT IPERKVPKFK PGKALKEKVK // ID DCDA_THEMA Reviewed; 386 AA. AC Q9X1K5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=Diaminopimelate decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120}; DE Short=DAP decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120}; DE Short=DAPDC {ECO:0000255|HAMAP-Rule:MF_02120}; DE EC=4.1.1.20 {ECO:0000255|HAMAP-Rule:MF_02120}; GN Name=lysA {ECO:0000255|HAMAP-Rule:MF_02120}; GN OrderedLocusNames=TM_1517; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH PLP, COFACTOR, RP AND SUBUNIT. RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure analysis of diaminopimelate decarboxylate (LysA)."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Specifically catalyzes the decarboxylation of meso- CC diaminopimelate (meso-DAP) to L-lysine. {ECO:0000255|HAMAP- CC Rule:MF_02120}. CC -!- CATALYTIC ACTIVITY: Meso-2,6-diaminoheptanedioate = L-lysine + CC CO(2). {ECO:0000255|HAMAP-Rule:MF_02120}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02120, ECO:0000269|Ref.2}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_02120}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02120, CC ECO:0000305|Ref.2}. CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II CC family. LysA subfamily. {ECO:0000255|HAMAP-Rule:MF_02120}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36584.1; -; Genomic_DNA. DR PIR; F72245; F72245. DR RefSeq; NP_229317.1; NC_000853.1. DR RefSeq; WP_004081870.1; NZ_CP011107.1. DR PDB; 2YXX; X-ray; 1.70 A; A=1-386. DR PDBsum; 2YXX; -. DR ProteinModelPortal; Q9X1K5; -. DR SMR; Q9X1K5; 2-386. DR STRING; 243274.TM1517; -. DR EnsemblBacteria; AAD36584; AAD36584; TM_1517. DR GeneID; 897217; -. DR KEGG; tma:TM1517; -. DR PATRIC; 23937992; VBITheMar51294_1534. DR eggNOG; ENOG4105CU5; Bacteria. DR eggNOG; COG0019; LUCA. DR InParanoid; Q9X1K5; -. DR KO; K01586; -. DR OMA; LKGNKFG; -. DR OrthoDB; EOG6Z9B18; -. DR UniPathway; UPA00034; UER00027. DR EvolutionaryTrace; Q9X1K5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.37.10; -; 1. DR Gene3D; 3.20.20.10; -; 1. DR HAMAP; MF_02120; LysA; 1. DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C. DR InterPro; IPR002986; DAP_deCOOHase_LysA. DR InterPro; IPR022643; De-COase2_C. DR InterPro; IPR022644; De-COase2_N. DR InterPro; IPR022653; De-COase2_pyr-phos_BS. DR InterPro; IPR000183; Orn/DAP/Arg_de-COase. DR InterPro; IPR029066; PLP-binding_barrel. DR Pfam; PF02784; Orn_Arg_deC_N; 1. DR Pfam; PF00278; Orn_DAP_Arg_deC; 1. DR PRINTS; PR01181; DAPDCRBXLASE. DR PRINTS; PR01179; ODADCRBXLASE. DR SUPFAM; SSF50621; SSF50621; 1. DR SUPFAM; SSF51419; SSF51419; 1. DR TIGRFAMs; TIGR01048; lysA; 1. DR PROSITE; PS00878; ODR_DC_2_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; KW Decarboxylase; Lyase; Lysine biosynthesis; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1 386 Diaminopimelate decarboxylase. FT /FTId=PRO_0000149937. FT REGION 246 249 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_02120, FT ECO:0000269|Ref.2}. FT ACT_SITE 314 314 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 214 214 Pyridoxal phosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02120, FT ECO:0000269|Ref.2}. FT BINDING 249 249 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 285 285 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 289 289 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 315 315 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 343 343 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_02120, ECO:0000269|Ref.2}. FT BINDING 343 343 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT MOD_RES 46 46 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_02120}. FT HELIX 3 11 {ECO:0000244|PDB:2YXX}. FT STRAND 13 19 {ECO:0000244|PDB:2YXX}. FT HELIX 20 33 {ECO:0000244|PDB:2YXX}. FT TURN 34 36 {ECO:0000244|PDB:2YXX}. FT STRAND 39 44 {ECO:0000244|PDB:2YXX}. FT HELIX 45 47 {ECO:0000244|PDB:2YXX}. FT HELIX 51 59 {ECO:0000244|PDB:2YXX}. FT STRAND 63 66 {ECO:0000244|PDB:2YXX}. FT HELIX 69 77 {ECO:0000244|PDB:2YXX}. FT HELIX 82 84 {ECO:0000244|PDB:2YXX}. FT STRAND 85 87 {ECO:0000244|PDB:2YXX}. FT HELIX 94 102 {ECO:0000244|PDB:2YXX}. FT STRAND 107 110 {ECO:0000244|PDB:2YXX}. FT HELIX 113 122 {ECO:0000244|PDB:2YXX}. FT STRAND 128 134 {ECO:0000244|PDB:2YXX}. FT TURN 139 141 {ECO:0000244|PDB:2YXX}. FT HELIX 143 151 {ECO:0000244|PDB:2YXX}. FT STRAND 152 157 {ECO:0000244|PDB:2YXX}. FT HELIX 158 160 {ECO:0000244|PDB:2YXX}. FT HELIX 161 168 {ECO:0000244|PDB:2YXX}. FT STRAND 173 177 {ECO:0000244|PDB:2YXX}. FT STRAND 182 184 {ECO:0000244|PDB:2YXX}. FT HELIX 188 204 {ECO:0000244|PDB:2YXX}. FT STRAND 207 210 {ECO:0000244|PDB:2YXX}. FT STRAND 219 221 {ECO:0000244|PDB:2YXX}. FT HELIX 226 232 {ECO:0000244|PDB:2YXX}. FT HELIX 234 237 {ECO:0000244|PDB:2YXX}. FT STRAND 241 247 {ECO:0000244|PDB:2YXX}. FT HELIX 249 252 {ECO:0000244|PDB:2YXX}. FT HELIX 253 255 {ECO:0000244|PDB:2YXX}. FT STRAND 256 268 {ECO:0000244|PDB:2YXX}. FT STRAND 271 277 {ECO:0000244|PDB:2YXX}. FT TURN 280 282 {ECO:0000244|PDB:2YXX}. FT HELIX 285 288 {ECO:0000244|PDB:2YXX}. FT STRAND 295 297 {ECO:0000244|PDB:2YXX}. FT STRAND 304 310 {ECO:0000244|PDB:2YXX}. FT STRAND 312 315 {ECO:0000244|PDB:2YXX}. FT STRAND 319 327 {ECO:0000244|PDB:2YXX}. FT STRAND 334 339 {ECO:0000244|PDB:2YXX}. FT STRAND 341 344 {ECO:0000244|PDB:2YXX}. FT HELIX 345 347 {ECO:0000244|PDB:2YXX}. FT TURN 351 353 {ECO:0000244|PDB:2YXX}. FT STRAND 358 362 {ECO:0000244|PDB:2YXX}. FT STRAND 368 372 {ECO:0000244|PDB:2YXX}. FT HELIX 377 380 {ECO:0000244|PDB:2YXX}. FT TURN 381 383 {ECO:0000244|PDB:2YXX}. SQ SEQUENCE 386 AA; 43982 MW; BB6FD6E9E7869CDB CRC64; MDILRKVAEI HGTPTYVYFE ETLRKRSRLV KEVFEGVNLL PTFAVKANNN PVLLKILREE GFGMDVVTKG ELLAAKLAGV PSHTVVWNGN GKSRDQMEHF LREDVRIVNV DSFEEMEIWR ELNPEGVEYF IRVNPEVDAK THPHISTGLK KHKFGIPLED LDSFMERFRS MNIRGLHVHI GSQITRVEPF VEAFSKVVRA SERYGFEEIN IGGGWGINYS GEELDLSSYR EKVVPDLKRF KRVIVEIGRY IVAPSGYLLL RVVLVKRRHN KAFVVVDGGM NVLIRPALYS AYHRIFVLGK QGKEMRADVV GPLCESGDVI AYDRELPEVE PGDIIAVENA GAYGYTMSNN YNSTTRPAEV LVRENGRISL IRRRETEMDI FKDVVM // ID DAPA_THEMA Reviewed; 294 AA. AC Q9X1K9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 119. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000255|HAMAP-Rule:MF_00418}; DE Short=HTPA synthase {ECO:0000255|HAMAP-Rule:MF_00418}; DE EC=4.3.3.7 {ECO:0000255|HAMAP-Rule:MF_00418}; GN Name=dapA {ECO:0000255|HAMAP-Rule:MF_00418}; GN OrderedLocusNames=TM_1521; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), FUNCTION, BIOPHYSICOCHEMICAL RP PROPERTIES, ENZYME REGULATION, AND SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=16872276; DOI=10.1042/BJ20060771; RA Pearce F.G., Perugini M.A., McKerchar H.J., Gerrard J.A.; RT "Dihydrodipicolinate synthase from Thermotoga maritima."; RL Biochem. J. 400:359-366(2006). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT RP ALA-166/ALA-167/ALA-168 AND MUTANT ALA-233/ALA-237, MUTAGENESIS OF RP 166-ASP--ASP-168, KINETIC PARAMETERS, AND SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=21803176; DOI=10.1016/j.bbapap.2011.07.016; RA Pearce F.G., Dobson R.C., Jameson G.B., Perugini M.A., Gerrard J.A.; RT "Characterization of monomeric dihydrodipicolinate synthase variant RT reveals the importance of substrate binding in optimizing RT oligomerization."; RL Biochim. Biophys. Acta 1814:1900-1909(2011). CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta- CC semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- CC tetrahydrodipicolinate (HTPA). {ECO:0000305|PubMed:16872276}. CC -!- CATALYTIC ACTIVITY: Pyruvate + L-aspartate-4-semialdehyde = (4S)- CC 4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- ENZYME REGULATION: Is not inhibited by (S)-lysine, in contrast to CC E.coli DapA. {ECO:0000269|PubMed:16872276}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.053 mM for pyruvate (at 30 degrees Celsius, CC PubMed:16872276) {ECO:0000269|PubMed:16872276, CC ECO:0000269|PubMed:21803176}; CC KM=0.08 mM for pyruvate (at 30 degrees Celsius, PubMed:21803176) CC {ECO:0000269|PubMed:16872276, ECO:0000269|PubMed:21803176}; CC KM=0.15 mM for pyruvate (at 45 degrees Celsius, PubMed:21803176) CC {ECO:0000269|PubMed:16872276, ECO:0000269|PubMed:21803176}; CC KM=0.16 mM for L-aspartate-4-semialdehyde (at 30 degrees CC Celsius, PubMed:16872276) {ECO:0000269|PubMed:16872276, CC ECO:0000269|PubMed:21803176}; CC KM=0.23 mM for L-aspartate-4-semialdehyde (at 30 degrees CC Celsius, PubMed:21803176) {ECO:0000269|PubMed:16872276, CC ECO:0000269|PubMed:21803176}; CC KM=0.36 mM for L-aspartate-4-semialdehyde (at 45 degrees CC Celsius, PubMed:21803176) {ECO:0000269|PubMed:16872276, CC ECO:0000269|PubMed:21803176}; CC Vmax=1.01 umol/sec/mg enzyme (at 30 degrees Celsius, CC PubMed:16872276) {ECO:0000269|PubMed:16872276, CC ECO:0000269|PubMed:21803176}; CC Note=kcat is 136 sec(-1) and 465 sec (-1) at 30 and 45 degrees CC Celsius, respectively. {ECO:0000269|PubMed:21803176}; CC Temperature dependence: CC Highly thermostable. Retains over 60% of the activity after 7 CC hours incubation at 90 degrees Celsius. CC {ECO:0000269|PubMed:16872276}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP- CC Rule:MF_00418, ECO:0000269|PubMed:16872276, CC ECO:0000269|PubMed:21803176}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP- CC Rule:MF_00418}. CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate CC synthase (DHDPS), catalyzing the condensation of (S)-aspartate- CC beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate CC (DHDP). However, it was shown in E.coli that the product of the CC enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4- CC hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that CC the consecutive dehydration reaction leading to DHDP is not CC spontaneous but catalyzed by DapB. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36588.1; -; Genomic_DNA. DR PIR; B72246; B72246. DR RefSeq; NP_229321.1; NC_000853.1. DR RefSeq; WP_004081879.1; NZ_CP011107.1. DR PDB; 1O5K; X-ray; 1.80 A; A/B=1-294. DR PDB; 3PB0; X-ray; 2.00 A; A/B/C/D=1-294. DR PDB; 3PB2; X-ray; 1.90 A; A/B/C/D/E/F=1-294. DR PDBsum; 1O5K; -. DR PDBsum; 3PB0; -. DR PDBsum; 3PB2; -. DR ProteinModelPortal; Q9X1K9; -. DR SMR; Q9X1K9; 1-294. DR STRING; 243274.TM1521; -. DR EnsemblBacteria; AAD36588; AAD36588; TM_1521. DR GeneID; 897344; -. DR KEGG; tma:TM1521; -. DR PATRIC; 23938000; VBITheMar51294_1538. DR eggNOG; ENOG4105CDP; Bacteria. DR eggNOG; COG0329; LUCA. DR InParanoid; Q9X1K9; -. DR KO; K01714; -. DR OMA; GMDACVP; -. DR OrthoDB; EOG6W7235; -. DR BRENDA; 4.3.3.7; 6331. DR UniPathway; UPA00034; UER00017. DR EvolutionaryTrace; Q9X1K9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00418; DapA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005263; DapA. DR InterPro; IPR002220; DapA-like. DR InterPro; IPR020625; Schiff_base-form_aldolases_AS. DR InterPro; IPR020624; Schiff_base-form_aldolases_CS. DR PANTHER; PTHR12128; PTHR12128; 1. DR Pfam; PF00701; DHDPS; 1. DR PIRSF; PIRSF001365; DHDPS; 1. DR PRINTS; PR00146; DHPICSNTHASE. DR SMART; SM01130; DHDPS; 1. DR TIGRFAMs; TIGR00674; dapA; 1. DR PROSITE; PS00665; DHDPS_1; 1. DR PROSITE; PS00666; DHDPS_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Diaminopimelate biosynthesis; Lyase; Lysine biosynthesis; KW Reference proteome; Schiff base. FT CHAIN 1 294 4-hydroxy-tetrahydrodipicolinate FT synthase. FT /FTId=PRO_0000103175. FT ACT_SITE 132 132 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT ACT_SITE 161 161 Schiff-base intermediate with substrate. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT BINDING 44 44 Pyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00418}. FT BINDING 206 206 Pyruvate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT SITE 43 43 Part of a proton relay during catalysis. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT SITE 106 106 Part of a proton relay during catalysis. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT MUTAGEN 166 168 DID->AAA: Exists as a monomer in FT solution. Decreased activity and FT substrate affinity. Reduced thermal FT stability. {ECO:0000269|PubMed:21803176}. FT STRAND 3 8 {ECO:0000244|PDB:1O5K}. FT HELIX 20 32 {ECO:0000244|PDB:1O5K}. FT STRAND 37 42 {ECO:0000244|PDB:1O5K}. FT HELIX 43 45 {ECO:0000244|PDB:1O5K}. FT HELIX 47 49 {ECO:0000244|PDB:1O5K}. FT HELIX 52 66 {ECO:0000244|PDB:1O5K}. FT STRAND 72 75 {ECO:0000244|PDB:1O5K}. FT HELIX 81 94 {ECO:0000244|PDB:1O5K}. FT STRAND 97 102 {ECO:0000244|PDB:1O5K}. FT HELIX 111 122 {ECO:0000244|PDB:1O5K}. FT STRAND 129 133 {ECO:0000244|PDB:1O5K}. FT HELIX 135 138 {ECO:0000244|PDB:1O5K}. FT HELIX 144 153 {ECO:0000244|PDB:1O5K}. FT STRAND 157 162 {ECO:0000244|PDB:1O5K}. FT HELIX 167 180 {ECO:0000244|PDB:1O5K}. FT STRAND 185 190 {ECO:0000244|PDB:1O5K}. FT HELIX 191 193 {ECO:0000244|PDB:1O5K}. FT HELIX 194 200 {ECO:0000244|PDB:1O5K}. FT STRAND 204 208 {ECO:0000244|PDB:1O5K}. FT HELIX 209 211 {ECO:0000244|PDB:1O5K}. FT HELIX 214 225 {ECO:0000244|PDB:1O5K}. FT HELIX 229 245 {ECO:0000244|PDB:1O5K}. FT STRAND 248 250 {ECO:0000244|PDB:1O5K}. FT HELIX 253 261 {ECO:0000244|PDB:1O5K}. FT HELIX 278 290 {ECO:0000244|PDB:1O5K}. SQ SEQUENCE 294 AA; 32390 MW; 64C93C64734A351D CRC64; MFRGVGTAIV TPFKNGELDL ESYERLVRYQ LENGVNALIV LGTTGESPTV NEDEREKLVS RTLEIVDGKI PVIVGAGTNS TEKTLKLVKQ AEKLGANGVL VVTPYYNKPT QEGLYQHYKY ISERTDLGIV VYNVPGRTGV NVLPETAARI AADLKNVVGI KEANPDIDQI DRTVSLTKQA RSDFMVWSGN DDRTFYLLCA GGDGVISVVS NVAPKQMVEL CAEYFSGNLE KSREVHRKLR PLMKALFVET NPIPVKAALN LMGFIENELR LPLVPASEKT VELLRNVLKE SGLL // ID DAPB_THEMA Reviewed; 216 AA. AC Q9X1K8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 122. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000255|HAMAP-Rule:MF_00102}; DE Short=HTPA reductase {ECO:0000255|HAMAP-Rule:MF_00102}; DE EC=1.17.1.8 {ECO:0000255|HAMAP-Rule:MF_00102}; GN Name=dapB {ECO:0000255|HAMAP-Rule:MF_00102}; GN OrderedLocusNames=TM_1520; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH NADH, FUNCTION, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME RP REGULATION, AND SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=18250105; DOI=10.1093/jb/mvn012; RA Pearce F.G., Sprissler C., Gerrard J.A.; RT "Characterization of dihydrodipicolinate reductase from Thermotoga RT maritima reveals evolution of substrate binding kinetics."; RL J. Biochem. 143:617-623(2008). CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy- CC tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate CC (Probable). Uses NADPH as a reductant with much more efficiency CC than NADH. {ECO:0000255|HAMAP-Rule:MF_00102, CC ECO:0000269|PubMed:18250105, ECO:0000305}. CC -!- CATALYTIC ACTIVITY: (S)-2,3,4,5-tetrahydropyridine-2,6- CC dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5- CC tetrahydrodipicolinate + NAD(P)H. {ECO:0000255|HAMAP- CC Rule:MF_00102}. CC -!- ENZYME REGULATION: Is inhibited by high concentrations of NADH. CC {ECO:0000269|PubMed:18250105}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.5 uM for NADH (at 30 degrees Celsius) CC {ECO:0000269|PubMed:18250105}; CC KM=0.6 uM for NADPH (at 30 degrees Celsius) CC {ECO:0000269|PubMed:18250105}; CC KM=1.8 uM for NADH (at 45 degrees Celsius) CC {ECO:0000269|PubMed:18250105}; CC KM=2.1 uM for NADPH (at 45 degrees Celsius) CC {ECO:0000269|PubMed:18250105}; CC Temperature dependence: CC Is stable for up to 48 hours at 80 degrees Celsius. Has a CC thermal denaturation midpoint (Tm) of 95.7 degrees Celsius. CC {ECO:0000269|PubMed:18250105}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. CC {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:18250105}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- SIMILARITY: Belongs to the DapB family. {ECO:0000255|HAMAP- CC Rule:MF_00102}. CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate CC reductase (DHDPR), catalyzing the conversion of CC dihydrodipicolinate to tetrahydrodipicolinate. However, it was CC shown in E.coli that the substrate of the enzymatic reaction is CC not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy- CC 2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by CC the DapA-catalyzed reaction. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36587.1; -; Genomic_DNA. DR PIR; A72246; A72246. DR RefSeq; NP_229320.1; NC_000853.1. DR RefSeq; WP_004081877.1; NZ_CP011107.1. DR PDB; 1VM6; X-ray; 2.27 A; A/B/C/D=1-216. DR PDBsum; 1VM6; -. DR ProteinModelPortal; Q9X1K8; -. DR SMR; Q9X1K8; 1-215. DR STRING; 243274.TM1520; -. DR EnsemblBacteria; AAD36587; AAD36587; TM_1520. DR GeneID; 897986; -. DR KEGG; tma:TM1520; -. DR PATRIC; 23937998; VBITheMar51294_1537. DR eggNOG; ENOG4105DUK; Bacteria. DR eggNOG; COG0289; LUCA. DR InParanoid; Q9X1K8; -. DR KO; K00215; -. DR OMA; HNMSIGI; -. DR OrthoDB; EOG6SV5DS; -. DR BRENDA; 1.17.1.8; 6331. DR UniPathway; UPA00034; UER00018. DR EvolutionaryTrace; Q9X1K8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IBA:GO_Central. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00102; DapB; 1. DR InterPro; IPR022663; DapB_C. DR InterPro; IPR000846; DapB_N. DR InterPro; IPR022664; DapB_N_CS. DR InterPro; IPR023940; DHDPR_bac. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR20836; PTHR20836; 1. DR Pfam; PF05173; DapB_C; 1. DR Pfam; PF01113; DapB_N; 1. DR PIRSF; PIRSF000161; DHPR; 1. DR SUPFAM; SSF51735; SSF51735; 2. DR PROSITE; PS01298; DAPB; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 216 4-hydroxy-tetrahydrodipicolinate FT reductase. FT /FTId=PRO_0000141502. FT NP_BIND 7 12 NAD(P). {ECO:0000255|HAMAP-Rule:MF_00102, FT ECO:0000269|PubMed:18250105}. FT NP_BIND 71 73 NAD(P). {ECO:0000255|HAMAP-Rule:MF_00102, FT ECO:0000269|PubMed:18250105}. FT NP_BIND 95 98 NAD(P). {ECO:0000255|HAMAP-Rule:MF_00102, FT ECO:0000269|PubMed:18250105}. FT REGION 137 138 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT ACT_SITE 127 127 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00102}. FT ACT_SITE 131 131 Proton donor. {ECO:0000305}. FT BINDING 128 128 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT STRAND 2 6 {ECO:0000244|PDB:1VM6}. FT TURN 7 9 {ECO:0000244|PDB:1VM6}. FT HELIX 11 22 {ECO:0000244|PDB:1VM6}. FT STRAND 26 32 {ECO:0000244|PDB:1VM6}. FT STRAND 35 38 {ECO:0000244|PDB:1VM6}. FT STRAND 43 47 {ECO:0000244|PDB:1VM6}. FT HELIX 51 53 {ECO:0000244|PDB:1VM6}. FT HELIX 54 64 {ECO:0000244|PDB:1VM6}. FT STRAND 67 70 {ECO:0000244|PDB:1VM6}. FT HELIX 77 86 {ECO:0000244|PDB:1VM6}. FT TURN 87 89 {ECO:0000244|PDB:1VM6}. FT STRAND 90 94 {ECO:0000244|PDB:1VM6}. FT HELIX 100 115 {ECO:0000244|PDB:1VM6}. FT TURN 116 118 {ECO:0000244|PDB:1VM6}. FT STRAND 119 127 {ECO:0000244|PDB:1VM6}. FT HELIX 137 145 {ECO:0000244|PDB:1VM6}. FT STRAND 152 156 {ECO:0000244|PDB:1VM6}. FT STRAND 163 169 {ECO:0000244|PDB:1VM6}. FT STRAND 171 181 {ECO:0000244|PDB:1VM6}. FT HELIX 185 198 {ECO:0000244|PDB:1VM6}. FT STRAND 203 206 {ECO:0000244|PDB:1VM6}. FT HELIX 208 212 {ECO:0000244|PDB:1VM6}. SQ SEQUENCE 216 AA; 23731 MW; 2C5670DF62C85528 CRC64; MKYGIVGYSG RMGQEIQKVF SEKGHELVLK VDVNGVEELD SPDVVIDFSS PEALPKTVDL CKKYRAGLVL GTTALKEEHL QMLRELSKEV PVVQAYNFSI GINVLKRFLS ELVKVLEDWD VEIVETHHRF KKDAPSGTAI LLESALGKSV PIHSLRVGGV PGDHVVVFGN IGETIEIKHR AISRTVFAIG ALKAAEFLVG KDPGMYSFEE VIFGGE // ID DDL_THEMA Reviewed; 303 AA. AC P46805; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 123. DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047}; DE EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047}; DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047}; DE AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047}; GN Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047}; OrderedLocusNames=TM_0259; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-118. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8547314; RA Bouthier de la Tour C., Kaltoum H., Portemer C., Confalonieri F., RA Huber R., Duguet M.; RT "Cloning and sequencing of the gene coding for topoisomerase I from RT the extremely thermophilic eubacterium, Thermotoga maritima."; RL Biochim. Biophys. Acta 1264:279-283(1995). CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D- CC alanyl-D-alanine. {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000250}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_00047}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA68950.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35347.1; -; Genomic_DNA. DR EMBL; U27841; AAA68950.1; ALT_INIT; Genomic_DNA. DR PIR; B72400; B72400. DR RefSeq; NP_228072.1; NC_000853.1. DR RefSeq; WP_010865083.1; NZ_CP011107.1. DR ProteinModelPortal; P46805; -. DR STRING; 243274.TM0259; -. DR EnsemblBacteria; AAD35347; AAD35347; TM_0259. DR GeneID; 897169; -. DR KEGG; tma:TM0259; -. DR PATRIC; 23935395; VBITheMar51294_0263. DR eggNOG; ENOG4105CPF; Bacteria. DR eggNOG; COG1181; LUCA. DR InParanoid; P46805; -. DR KO; K01921; -. DR OMA; IDRAFIV; -. DR OrthoDB; EOG6ND0KB; -. DR BioCyc; TMAR243274:GC6P-272-MONOMER; -. DR BRENDA; 6.3.2.4; 6331. DR UniPathway; UPA00219; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 2. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_00047; Dala_Dala_lig; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR000291; D-Ala_lig_Van_CS. DR InterPro; IPR005905; D_ala_D_ala. DR InterPro; IPR011095; Dala_Dala_lig_C. DR InterPro; IPR011127; Dala_Dala_lig_N. DR InterPro; IPR016185; PreATP-grasp_dom. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR Pfam; PF01820; Dala_Dala_lig_N; 1. DR PIRSF; PIRSF039102; Ddl/VanB; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 1. DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell shape; Cell wall biogenesis/degradation; KW Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 303 D-alanine--D-alanine ligase. FT /FTId=PRO_0000177896. FT DOMAIN 99 293 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_00047}. FT NP_BIND 125 176 ATP. {ECO:0000255|HAMAP-Rule:MF_00047}. FT METAL 248 248 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_00047}. FT METAL 260 260 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_00047}. FT METAL 260 260 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_00047}. FT METAL 262 262 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_00047}. SQ SEQUENCE 303 AA; 34250 MW; A6057C711DA77725 CRC64; MRVALLMGGV SREREISLRS GERVKKALEK LGYEHTVFDV REDFLKKVDQ LKSFDVVFNV LHGTFGEDGT LQAILDFLGI RYTGSDAFSS MICFDKLVTY RFLKGTVEIP DFVEIKEFMK TSPLGYPCVV KPRREGSSIG VFVCESDEEF QHALKEDLPR YGSVIVQKYI PGREMTVSIL ETEKGFEILP VLELRPKRRF YDYVAKYTKG ETEFILPAPL NPSEERLVKE MALKAFVEAG CRGFGRVDGI FSDGRFYFLE INTVPGLTET SDLPASAKAG GIEFEELVEI ILKSAFLKEG VRV // ID DEF_THEMA Reviewed; 164 AA. AC P96113; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 13-APR-2016, entry version 120. DE RecName: Full=Peptide deformylase; DE Short=PDF; DE EC=3.5.1.88; DE AltName: Full=Polypeptide deformylase; GN Name=def; OrderedLocusNames=TM_1661; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9086272; DOI=10.1006/jmbi.1996.0835; RA Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.; RT "A survey of polypeptide deformylase function throughout the RT eubacterial lineage."; RL J. Mol. Biol. 266:939-949(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Removes the formyl group from the N-terminal Met of CC newly synthesized proteins. Requires at least a dipeptide for an CC efficient rate of reaction. N-terminal L-methionine is a CC prerequisite for activity but the enzyme has broad specificity at CC other positions (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H(2)O = formate + CC methionyl peptide. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; CC Note=Binds 1 Fe(2+) ion. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the polypeptide deformylase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y10306; CAA71356.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36728.1; -; Genomic_DNA. DR PIR; C72224; C72224. DR RefSeq; NP_229461.1; NC_000853.1. DR RefSeq; WP_004082176.1; NZ_CP011107.1. DR PDB; 1LME; X-ray; 2.20 A; A/B=1-164. DR PDBsum; 1LME; -. DR ProteinModelPortal; P96113; -. DR SMR; P96113; 1-145. DR STRING; 243274.TM1661; -. DR EnsemblBacteria; AAD36728; AAD36728; TM_1661. DR GeneID; 897909; -. DR KEGG; tma:TM1661; -. DR PATRIC; 23938296; VBITheMar51294_1680. DR eggNOG; ENOG4108Z02; Bacteria. DR eggNOG; COG0242; LUCA. DR InParanoid; P96113; -. DR KO; K01462; -. DR OMA; IQIGVPR; -. DR OrthoDB; EOG664CMF; -. DR BRENDA; 3.5.1.88; 6331. DR EvolutionaryTrace; P96113; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0042586; F:peptide deformylase activity; IBA:GO_Central. DR GO; GO:0043686; P:co-translational protein modification; IBA:GO_Central. DR GO; GO:0031365; P:N-terminal protein amino acid modification; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.45.10; -; 1. DR HAMAP; MF_00163; Pep_deformylase; 1. DR InterPro; IPR000181; Fmet_deformylase. DR InterPro; IPR023635; Peptide_deformylase. DR PANTHER; PTHR10458; PTHR10458; 1. DR Pfam; PF01327; Pep_deformylase; 1. DR PIRSF; PIRSF004749; Pep_def; 1. DR PRINTS; PR01576; PDEFORMYLASE. DR SUPFAM; SSF56420; SSF56420; 1. DR TIGRFAMs; TIGR00079; pept_deformyl; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Iron; Metal-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 164 Peptide deformylase. FT /FTId=PRO_0000082866. FT ACT_SITE 130 130 {ECO:0000250}. FT METAL 87 87 Iron. {ECO:0000250}. FT METAL 129 129 Iron. {ECO:0000250}. FT METAL 133 133 Iron. {ECO:0000250}. FT HELIX 10 12 {ECO:0000244|PDB:1LME}. FT HELIX 24 39 {ECO:0000244|PDB:1LME}. FT STRAND 43 46 {ECO:0000244|PDB:1LME}. FT HELIX 47 50 {ECO:0000244|PDB:1LME}. FT STRAND 54 59 {ECO:0000244|PDB:1LME}. FT STRAND 61 63 {ECO:0000244|PDB:1LME}. FT STRAND 66 76 {ECO:0000244|PDB:1LME}. FT STRAND 80 85 {ECO:0000244|PDB:1LME}. FT STRAND 95 108 {ECO:0000244|PDB:1LME}. FT STRAND 114 120 {ECO:0000244|PDB:1LME}. FT HELIX 121 134 {ECO:0000244|PDB:1LME}. FT HELIX 139 142 {ECO:0000244|PDB:1LME}. SQ SEQUENCE 164 AA; 19024 MW; 9FE94A206DE50842 CRC64; MYRIRVFGDP VLRKRAKPVT KFDENLKKTI ERMIETMYHY DGVGLAAPQV GISQRFFVMD VGNGPVAVIN PEILEIDPET EVAEEGCLSF PEIFVEIERS KRIKVKYQNT RGEYVEEELE GYAARVFQHE FDHLNGVLII DRISPAKRLL LRKKLMDIAR TVKR // ID DISA_THEMA Reviewed; 357 AA. AC Q9WY43; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=DNA integrity scanning protein DisA {ECO:0000255|HAMAP-Rule:MF_01438}; DE AltName: Full=Cyclic di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01438}; DE Short=c-di-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01438}; DE AltName: Full=Diadenylate cyclase {ECO:0000255|HAMAP-Rule:MF_01438}; DE EC=2.7.7.85 {ECO:0000255|HAMAP-Rule:MF_01438}; GN Name=disA {ECO:0000255|HAMAP-Rule:MF_01438}; GN OrderedLocusNames=TM_0200; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF APOPROTEIN AND IN COMPLEXES RP WITH ATP ANALOGS OR PRODUCT C-DI-AMP, FUNCTION, CATALYTIC ACTIVITY, RP SUBSTRATE SPECIFICITY, SUBUNIT, AND DOMAIN. RX PubMed=18439896; DOI=10.1016/j.molcel.2008.02.020; RA Witte G., Hartung S., Buttner K., Hopfner K.P.; RT "Structural biochemistry of a bacterial checkpoint protein reveals RT diadenylate cyclase activity regulated by DNA recombination RT intermediates."; RL Mol. Cell 30:167-178(2008). CC -!- FUNCTION: Participates in a DNA-damage check-point. DisA forms CC globular foci that rapidly scan along the chromosomes searching CC for lesions. {ECO:0000255|HAMAP-Rule:MF_01438}. CC -!- FUNCTION: Has also diadenylate cyclase activity, catalyzing the CC condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c- CC di-AMP likely acts as a signaling molecule that may couple DNA CC integrity with a cellular process. Does not convert GTP to c-di- CC GMP. {ECO:0000255|HAMAP-Rule:MF_01438, CC ECO:0000269|PubMed:18439896}. CC -!- CATALYTIC ACTIVITY: 2 ATP = 2 diphosphate + cyclic di-3',5'- CC adenylate. {ECO:0000255|HAMAP-Rule:MF_01438, CC ECO:0000269|PubMed:18439896}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01438}; CC -!- SUBUNIT: Homooctamer. {ECO:0000255|HAMAP-Rule:MF_01438, CC ECO:0000269|PubMed:18439896}. CC -!- DOMAIN: Consists of three domains: an N-terminal globular domain CC with diadenylate-cyclase (DAC) activity, a central helical domain CC and a C-terminal DNA-binding domain. CC {ECO:0000269|PubMed:18439896}. CC -!- SIMILARITY: Belongs to the DisA family. {ECO:0000255|HAMAP- CC Rule:MF_01438}. CC -!- SIMILARITY: Contains 1 DAC domain. {ECO:0000255|PROSITE- CC ProRule:PRU01130}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35292.1; -; Genomic_DNA. DR PIR; B72405; B72405. DR RefSeq; NP_228015.1; NC_000853.1. DR RefSeq; WP_010865072.1; NC_000853.1. DR PDB; 3C1Y; X-ray; 2.10 A; A/B=1-357. DR PDB; 3C1Z; X-ray; 2.30 A; A/B=1-357. DR PDB; 3C21; X-ray; 2.70 A; A/B=1-357. DR PDB; 3C23; X-ray; 2.50 A; A/B=1-357. DR PDB; 4YVZ; X-ray; 2.50 A; A/B=1-357. DR PDB; 4YXJ; X-ray; 2.55 A; A/B=1-357. DR PDB; 4YXM; X-ray; 2.25 A; A/B=1-357. DR PDBsum; 3C1Y; -. DR PDBsum; 3C1Z; -. DR PDBsum; 3C21; -. DR PDBsum; 3C23; -. DR PDBsum; 4YVZ; -. DR PDBsum; 4YXJ; -. DR PDBsum; 4YXM; -. DR ProteinModelPortal; Q9WY43; -. DR SMR; Q9WY43; 7-355. DR STRING; 243274.TM0200; -. DR EnsemblBacteria; AAD35292; AAD35292; TM_0200. DR GeneID; 897070; -. DR KEGG; tma:TM0200; -. DR PATRIC; 23935272; VBITheMar51294_0202. DR eggNOG; ENOG4105E59; Bacteria. DR eggNOG; COG1623; LUCA. DR InParanoid; Q9WY43; -. DR KO; K07067; -. DR OMA; TEMVMRI; -. DR OrthoDB; EOG6GTZKC; -. DR BioCyc; TMAR243274:GC6P-213-MONOMER; -. DR BRENDA; 2.7.7.85; 6331. DR EvolutionaryTrace; Q9WY43; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0019932; P:second-messenger-mediated signaling; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01438; DisA; 1. DR InterPro; IPR018906; DNA_integrity_scan_DisA_link. DR InterPro; IPR003390; DNA_integrity_scan_DisA_N. DR InterPro; IPR023763; DNA_integrity_scanning_protein. DR InterPro; IPR000445; HhH_motif. DR InterPro; IPR010994; RuvA_2-like. DR Pfam; PF10635; DisA-linker; 1. DR Pfam; PF02457; DisA_N; 1. DR Pfam; PF00633; HHH; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR PROSITE; PS51794; DAC; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; DNA damage; DNA repair; KW DNA-binding; Magnesium; Nucleotide-binding; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 357 DNA integrity scanning protein DisA. FT /FTId=PRO_0000255653. FT DOMAIN 8 148 DAC. {ECO:0000255|PROSITE- FT ProRule:PRU01130}. FT NP_BIND 107 111 ATP. FT BINDING 76 76 ATP; via amide nitrogen. FT BINDING 94 94 ATP; via amide nitrogen and carbonyl FT oxygen. FT HELIX 9 15 {ECO:0000244|PDB:3C1Y}. FT HELIX 16 18 {ECO:0000244|PDB:3C1Y}. FT HELIX 23 33 {ECO:0000244|PDB:3C1Y}. FT STRAND 38 42 {ECO:0000244|PDB:3C1Y}. FT HELIX 46 49 {ECO:0000244|PDB:3C1Y}. FT TURN 50 52 {ECO:0000244|PDB:3C1Y}. FT STRAND 53 62 {ECO:0000244|PDB:3C1Y}. FT HELIX 65 71 {ECO:0000244|PDB:3C1Y}. FT STRAND 74 80 {ECO:0000244|PDB:3C1Y}. FT STRAND 84 94 {ECO:0000244|PDB:3C1Y}. FT HELIX 107 119 {ECO:0000244|PDB:3C1Y}. FT STRAND 120 126 {ECO:0000244|PDB:3C1Y}. FT STRAND 128 131 {ECO:0000244|PDB:3C1Z}. FT STRAND 133 136 {ECO:0000244|PDB:3C1Y}. FT STRAND 141 144 {ECO:0000244|PDB:3C1Y}. FT HELIX 147 180 {ECO:0000244|PDB:3C1Y}. FT HELIX 186 212 {ECO:0000244|PDB:3C1Y}. FT HELIX 214 217 {ECO:0000244|PDB:3C1Y}. FT HELIX 218 228 {ECO:0000244|PDB:3C1Y}. FT HELIX 231 242 {ECO:0000244|PDB:3C1Y}. FT STRAND 243 245 {ECO:0000244|PDB:3C1Y}. FT HELIX 249 260 {ECO:0000244|PDB:3C1Y}. FT STRAND 261 263 {ECO:0000244|PDB:3C23}. FT HELIX 267 273 {ECO:0000244|PDB:3C1Y}. FT HELIX 281 286 {ECO:0000244|PDB:3C1Y}. FT HELIX 294 299 {ECO:0000244|PDB:3C1Y}. FT HELIX 305 315 {ECO:0000244|PDB:3C1Y}. FT HELIX 318 321 {ECO:0000244|PDB:3C1Y}. FT HELIX 326 329 {ECO:0000244|PDB:3C1Y}. FT HELIX 337 354 {ECO:0000244|PDB:3C1Y}. SQ SEQUENCE 357 AA; 40540 MW; 45C1318A21F315A9 CRC64; MGVKSLVPQE LIEKIKLISP GTELRKALDD IINANFGALI FLVDDPKKYE DVIQGGFWLD TDFSAEKLYE LSKMDGAIVL SEDITKIYYA NVHLVPDPTI PTGETGTRHR TAERLAKQTG KVVIAVSRRR NIISLYYKNY KYVVNQVDFL ISKVTQAIST LEKYKDNFNK LLSELEVLEL ENRVTLADVV RTLAKGFELL RIVEEIRPYI VELGEEGRLA RMQLRELTED VDDLLVLLIM DYSSEEVEEE TAQNILQDFI TRREPSPISI SRVLGYDVQQ AAQLDDVLVS ARGYRLLKTV ARIPLSIGYN VVRMFKTLDQ ISKASVEDLK KVEGIGEKRA RAISESISSL KHRKTSE // ID DEOC_THEMA Reviewed; 248 AA. AC Q9X1P5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 124. DE RecName: Full=Deoxyribose-phosphate aldolase; DE Short=DERA; DE EC=4.1.2.4; DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase; DE AltName: Full=Phosphodeoxyriboaldolase; DE Short=Deoxyriboaldolase; GN Name=deoC; OrderedLocusNames=TM_1559; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes a reversible aldol reaction between CC acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy- CC D-ribose 5-phosphate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2-deoxy-D-ribose 5-phosphate = D- CC glyceraldehyde 3-phosphate + acetaldehyde. CC -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate CC degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2- CC deoxy-alpha-D-ribose 1-phosphate: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1 CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36625.1; -; Genomic_DNA. DR PIR; B72240; B72240. DR RefSeq; NP_229359.1; NC_000853.1. DR RefSeq; WP_004081965.1; NZ_CP011107.1. DR PDB; 3R12; X-ray; 1.75 A; A/B=1-248. DR PDB; 3R13; X-ray; 1.83 A; A/B=1-248. DR PDBsum; 3R12; -. DR PDBsum; 3R13; -. DR ProteinModelPortal; Q9X1P5; -. DR SMR; Q9X1P5; 1-247. DR STRING; 243274.TM1559; -. DR EnsemblBacteria; AAD36625; AAD36625; TM_1559. DR GeneID; 897566; -. DR KEGG; tma:TM1559; -. DR PATRIC; 23938080; VBITheMar51294_1577. DR eggNOG; ENOG4105FCI; Bacteria. DR eggNOG; COG0274; LUCA. DR InParanoid; Q9X1P5; -. DR KO; K01619; -. DR OMA; FFSVCVN; -. DR OrthoDB; EOG6QZMW5; -. DR UniPathway; UPA00002; UER00468. DR EvolutionaryTrace; Q9X1P5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IBA:GO_Central. DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central. DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IBA:GO_Central. DR GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00114; DeoC_type1; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011343; DeoC. DR InterPro; IPR002915; DeoC/FbaB/lacD_aldolase. DR InterPro; IPR028581; DeoC_typeI. DR PANTHER; PTHR10889; PTHR10889; 1. DR Pfam; PF01791; DeoC; 1. DR PIRSF; PIRSF001357; DeoC; 1. DR SMART; SM01133; DeoC; 1. DR TIGRFAMs; TIGR00126; deoC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Lyase; Reference proteome; KW Schiff base. FT CHAIN 1 248 Deoxyribose-phosphate aldolase. FT /FTId=PRO_0000057280. FT ACT_SITE 179 179 Schiff-base intermediate with FT acetaldehyde. {ECO:0000250}. FT ACT_SITE 208 208 {ECO:0000250}. FT HELIX 1 16 {ECO:0000244|PDB:3R12}. FT STRAND 22 24 {ECO:0000244|PDB:3R12}. FT HELIX 28 34 {ECO:0000244|PDB:3R12}. FT STRAND 35 39 {ECO:0000244|PDB:3R12}. FT HELIX 46 58 {ECO:0000244|PDB:3R12}. FT STRAND 62 66 {ECO:0000244|PDB:3R12}. FT HELIX 68 70 {ECO:0000244|PDB:3R12}. FT HELIX 71 78 {ECO:0000244|PDB:3R12}. FT STRAND 84 90 {ECO:0000244|PDB:3R12}. FT TURN 91 93 {ECO:0000244|PDB:3R12}. FT HELIX 98 111 {ECO:0000244|PDB:3R12}. FT STRAND 114 119 {ECO:0000244|PDB:3R12}. FT HELIX 122 126 {ECO:0000244|PDB:3R12}. FT HELIX 130 143 {ECO:0000244|PDB:3R12}. FT TURN 144 146 {ECO:0000244|PDB:3R12}. FT STRAND 147 152 {ECO:0000244|PDB:3R12}. FT HELIX 155 157 {ECO:0000244|PDB:3R12}. FT HELIX 160 172 {ECO:0000244|PDB:3R12}. FT STRAND 176 179 {ECO:0000244|PDB:3R12}. FT STRAND 183 186 {ECO:0000244|PDB:3R12}. FT HELIX 191 201 {ECO:0000244|PDB:3R12}. FT STRAND 205 212 {ECO:0000244|PDB:3R12}. FT HELIX 216 224 {ECO:0000244|PDB:3R12}. FT STRAND 228 233 {ECO:0000244|PDB:3R12}. FT HELIX 235 246 {ECO:0000244|PDB:3R12}. SQ SEQUENCE 248 AA; 27285 MW; 7236D2ECA2CA1951 CRC64; MIEYRIEEAV AKYREFYEFK PVRESAGIED VKSAIEHTNL KPFATPDDIK KLCLEARENR FHGVCVNPCY VKLAREELEG TDVKVVTVVG FPLGANETRT KAHEAIFAVE SGADEIDMVI NVGMLKAKEW EYVYEDIRSV VESVKGKVVK VIIETCYLDT EEKIAACVIS KLAGAHFVKT STGFGTGGAT AEDVHLMKWI VGDEMGVKAS GGIRTFEDAV KMIMYGADRI GTSSGVKIVQ GGEERYGG // ID DEOB_THEMA Reviewed; 390 AA. AC Q9WY14; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Phosphopentomutase {ECO:0000255|HAMAP-Rule:MF_00740}; DE EC=5.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00740}; DE AltName: Full=Phosphodeoxyribomutase {ECO:0000255|HAMAP-Rule:MF_00740}; GN Name=deoB {ECO:0000255|HAMAP-Rule:MF_00740}; GN OrderedLocusNames=TM_0167; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of CC pentose. {ECO:0000255|HAMAP-Rule:MF_00740}. CC -!- CATALYTIC ACTIVITY: Alpha-D-ribose 1-phosphate = D-ribose 5- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00740}. CC -!- CATALYTIC ACTIVITY: 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy- CC alpha-D-ribose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00740}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00740}; CC Note=Binds 1 or 2 manganese ions. {ECO:0000255|HAMAP- CC Rule:MF_00740}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D- CC ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1- CC diphosphate from D-ribose 5-phosphate (route II): step 1/3. CC {ECO:0000255|HAMAP-Rule:MF_00740}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00740}. CC -!- SIMILARITY: Belongs to the phosphopentomutase family. CC {ECO:0000255|HAMAP-Rule:MF_00740}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35260.1; -; Genomic_DNA. DR PIR; E72411; E72411. DR RefSeq; NP_227982.1; NC_000853.1. DR RefSeq; WP_004082794.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY14; -. DR STRING; 243274.TM0167; -. DR PRIDE; Q9WY14; -. DR DNASU; 897006; -. DR EnsemblBacteria; AAD35260; AAD35260; TM_0167. DR GeneID; 897006; -. DR KEGG; tma:TM0167; -. DR PATRIC; 23935182; VBITheMar51294_0168. DR eggNOG; ENOG4105CZG; Bacteria. DR eggNOG; COG1015; LUCA. DR InParanoid; Q9WY14; -. DR KO; K01839; -. DR OMA; YLGNCHA; -. DR OrthoDB; EOG6R5C7J; -. DR UniPathway; UPA00087; UER00173. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008973; F:phosphopentomutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro. DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.1250; -; 1. DR Gene3D; 3.40.720.10; -; 2. DR HAMAP; MF_00740; Phosphopentomut; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR010045; DeoB. DR InterPro; IPR006124; Metalloenzyme. DR InterPro; IPR024052; Phosphopentomutase_DeoB_cap. DR Pfam; PF01676; Metalloenzyme; 1. DR PIRSF; PIRSF001491; Ppentomutase; 1. DR SUPFAM; SSF143856; SSF143856; 1. DR SUPFAM; SSF53649; SSF53649; 2. DR TIGRFAMs; TIGR01696; deoB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Isomerase; Manganese; Metal-binding; KW Reference proteome. FT CHAIN 1 390 Phosphopentomutase. FT /FTId=PRO_0000199859. FT METAL 9 9 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_00740}. FT METAL 288 288 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_00740}. FT METAL 324 324 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_00740}. FT METAL 325 325 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_00740}. FT METAL 336 336 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_00740}. SQ SEQUENCE 390 AA; 43253 MW; 032CC0940B5543B0 CRC64; MRVVLIVLDS VGIGEMPDAH LYGDEGSNTI VNTAKAVSGL HLPNMAKLGL GNLDDIPGVE PVKPAEGIYG KMMEKSPGKD TTTGHWEIAG VILKKPFDLF PEGFPKELIE EFERRTGRKV IGNKPASGTE IIKELGPIHE KTGALIVYTS ADSVFQIAAK KEIVPLEELY RYCEIARELL NEMGYKVARV IARPFTGEWP NYVRTPERKD FSLEPEGKTL LDVLTENGIP VYGVGKIADI FAGRGVTENY KTKDNNDGID KTISLMKEKN HDCLIFTNLV DFDTKYGHRN DPVSYAKALE EFDARLPEIM HNLNEDDVLF ITADHGCDPT TPSTDHSREM VPLLGYGGRL KKDVYVGIRE TFADLGQTIA DIFGVPPLEN GTSFKNLIWE // ID DNAJ_THEMA Reviewed; 369 AA. AC Q9WZV3; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 117. DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN OrderedLocusNames=TM_0849; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Participates actively in the response to hyperosmotic CC and heat shock by preventing the aggregation of stress-denatured CC proteins and by disaggregating proteins, also in an autonomous, CC DnaK-independent fashion. Unfolded proteins bind initially to CC DnaJ; upon interaction with the DnaJ-bound protein, DnaK CC hydrolyzes its bound ATP, resulting in the formation of a stable CC complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers CC the release of the substrate protein, thus completing the reaction CC cycle. Several rounds of ATP-dependent interactions between DnaJ, CC DnaK and GrpE are required for fully efficient folding. Also CC involved, together with DnaK and GrpE, in the DNA replication of CC plasmids through activation of initiation proteins. CC {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01152}; CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000255|HAMAP- CC Rule:MF_01152}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- DOMAIN: The J domain is necessary and sufficient to stimulate DnaK CC ATPase activity. Zinc center 1 plays an important role in the CC autonomous, DnaK-independent chaperone activity of DnaJ. Zinc CC center 2 is essential for interaction with DnaK and for DnaJ CC activity. {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000255|HAMAP- CC Rule:MF_01152}. CC -!- SIMILARITY: Contains 1 CR-type zinc finger. {ECO:0000255|HAMAP- CC Rule:MF_01152}. CC -!- SIMILARITY: Contains 1 J domain. {ECO:0000255|HAMAP- CC Rule:MF_01152}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35931.1; -; Genomic_DNA. DR PIR; B72327; B72327. DR RefSeq; NP_228658.1; NC_000853.1. DR RefSeq; WP_004080777.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZV3; -. DR SMR; Q9WZV3; 7-73. DR STRING; 243274.TM0849; -. DR EnsemblBacteria; AAD35931; AAD35931; TM_0849. DR GeneID; 898520; -. DR KEGG; tma:TM0849; -. DR PATRIC; 23936624; VBITheMar51294_0862. DR eggNOG; ENOG4105BZ5; Bacteria. DR eggNOG; COG0484; LUCA. DR InParanoid; Q9WZV3; -. DR KO; K03686; -. DR OMA; RVEYKVQ; -. DR OrthoDB; EOG6BPDKP; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0009408; P:response to heat; IEA:InterPro. DR Gene3D; 1.10.287.110; -; 1. DR Gene3D; 2.10.230.10; -; 1. DR HAMAP; MF_01152; DnaJ; 1. DR InterPro; IPR012724; DnaJ. DR InterPro; IPR002939; DnaJ_C. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR018253; DnaJ_domain_CS. DR InterPro; IPR008971; HSP40/DnaJ_pept-bd. DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF01556; DnaJ_C; 1. DR Pfam; PF00684; DnaJ_CXXCXGXG; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR SUPFAM; SSF49493; SSF49493; 3. DR SUPFAM; SSF57938; SSF57938; 1. DR TIGRFAMs; TIGR02349; DnaJ_bact; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR PROSITE; PS51188; ZF_CR; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; DNA replication; KW Metal-binding; Reference proteome; Repeat; Stress response; Zinc; KW Zinc-finger. FT CHAIN 1 369 Chaperone protein DnaJ. FT /FTId=PRO_0000070917. FT DOMAIN 7 73 J. {ECO:0000255|HAMAP-Rule:MF_01152}. FT REPEAT 156 163 CXXCXGXG motif. FT REPEAT 173 180 CXXCXGXG motif. FT REPEAT 199 206 CXXCXGXG motif. FT REPEAT 213 220 CXXCXGXG motif. FT ZN_FING 143 225 CR-type. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT COMPBIAS 79 126 Gly-rich. FT METAL 156 156 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 159 159 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 173 173 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 176 176 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 199 199 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 202 202 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 213 213 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 216 216 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. SQ SEQUENCE 369 AA; 42358 MW; 595661144ACC017E CRC64; MKKEKKDYYE ILGVPRDATQ EEIKRAYKRL VKEWHPDRHP ENRKEAEQRF KEIQEAYEVL SDPQKRAMYD RFGYVGEQPT YQETESGGFF DDIFRDFENI FNRDIFDVFF GERPHQEERR EYARRGEDIR YEIEVTLSDL INGAEIPVEY ERYETCPRCG GTGVEPNAGY MDCPSCGGTG RIREERRSFF GYFVSERTCE RCGGTGKIPR EYCHECGGSG RVLRKVRRTV KIPPNVEDGT HLRITGGGNA GYYGGPYGDL IIIVRVKPDP RFKKSGSDLV YDVTIDYLQA ILGTTVEVPL PEGGTTMLKI PPGTQPETVF RLKGKGLPNR YGRRGDLIVN VHVEIPKSLS REERKVLEEL AKKRGVTIG // ID DPO3A_THEMA Reviewed; 842 AA. AC Q9ZHG4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 112. DE RecName: Full=DNA polymerase III subunit alpha; DE EC=2.7.7.7; GN Name=dnaE; OrderedLocusNames=TM_0461; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9826752; DOI=10.1093/nar/26.23.5300; RA Huang Y.P., Ito J.; RT "The hyperthermophilic bacterium Thermotoga maritima has two different RT classes of family C DNA polymerases: evolutionary implications."; RL Nucleic Acids Res. 26:5300-5309(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme CC responsible for most of the replicative synthesis in bacteria. CC This DNA polymerase also exhibits 3' to 5' exonuclease activity. CC The alpha chain is the DNA polymerase (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, CC epsilon and theta chains) that associates with a tau subunit. This CC core dimerizes to form the PolIII' complex. PolIII' associates CC with the gamma complex (composed of gamma, delta, delta', psi and CC chi chains) and with the beta chain to form the complete DNA CC polymerase III complex (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF063188; AAC80434.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35546.1; -; Genomic_DNA. DR PIR; E72373; E72373. DR RefSeq; NP_228271.1; NC_000853.1. DR RefSeq; WP_004081505.1; NZ_CP011107.1. DR ProteinModelPortal; Q9ZHG4; -. DR STRING; 243274.TM0461; -. DR PRIDE; Q9ZHG4; -. DR EnsemblBacteria; AAD35546; AAD35546; TM_0461. DR GeneID; 897492; -. DR KEGG; tma:TM0461; -. DR PATRIC; 23935819; VBITheMar51294_0468. DR eggNOG; ENOG4105C0B; Bacteria. DR eggNOG; COG0587; LUCA. DR InParanoid; Q9ZHG4; -. DR KO; K02337; -. DR OMA; AYAHITY; -. DR OrthoDB; EOG6CZQGR; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR InterPro; IPR011708; DNA_pol3_alpha. DR InterPro; IPR029460; DNAPol_HHH. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR Pfam; PF07733; DNA_pol3_alpha; 2. DR Pfam; PF14579; HHH_6; 1. DR SMART; SM00481; POLIIIAc; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA replication; KW DNA-directed DNA polymerase; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 842 DNA polymerase III subunit alpha. FT /FTId=PRO_0000103355. FT CONFLICT 377 377 I -> M (in Ref. 1; AAC80434). FT {ECO:0000305}. SQ SEQUENCE 842 AA; 96500 MW; 19BB813C8085C277 CRC64; MIPWVISPYS FDGSVVRFEK LALLLKRKGL KSVILADRNF HAAVKFNTIM RKHGLIPVHG LWKDGRIFVA RNREEFDSLV RYYNGETHEI EDIPVFQESE LTPVRYLDAS EKKASIFMRK IFGLDEDVQG FPEKCEDVAD ILNAEAYDLR VNHRFPTPPK NWNELLIKKA EPLGEEYISR LKRELEVIKR KGFTPYIYTV EKVVEIAKKM GIKVGPGRGS AVGSLVAYLC GITEVDPIKY DLLFERFLNE ERQEPPDIDV DVEDRRRKDL IKELSKSFQV YQVSTFGNLT EKSLKNLINS VLPDASLEEK NEIYKTVYGL PHHPSVHAAG VVISENPLPL PTRTEEDIPI TDYDMYDLQE IGVVKIDILG LKTLSFIKDF KKEIFDYSDE KTYHLISKGK TLGVFQLEGL QARKLCRRIS PRNMDELSIL LALNRPGPLR SGLDVMFSNS KNVPAFFRKM FPETRGVLIY QEQIMRLAMF AGLSGTEADI LRRAIAKKER EKMEPLLEKM KKGLLEKGME NAEQILEILL NFSSYAFNKS HSVAYAHITY QTAYLKAHHL EEFFKLYFAY NSSDAGKIFL AVQELRNEGY RVHPPDINIS GKDLVFHGKD VYLPLTVVKG VGVTLVEQIE KIRPVSSVRE LQERVTGVPR NVVESLITAG AFDKLYENRK LALEELNKRV EKDILEIRSL FGEKVEQESS NIKIGDITEL EEKSMGFPLT PVHEVPTGLF ARIDDVFTYG RILPVLVKRV SRNIVTDGLS VCRVRTDVPD GVHLVLLSPL QKIIKIWPFN ENTRFVYRVD FTATLEKAGQ NEITEVLKNG AVVRYEGYRP LTDEYRYRVV PR // ID DER_THEMA Reviewed; 439 AA. AC Q9X1F8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 123. DE RecName: Full=GTPase Der; DE Short=TmDer; DE AltName: Full=GTP-binding protein EngA; GN Name=der; Synonyms=engA; OrderedLocusNames=TM_1446; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY. RX PubMed=11387344; DOI=10.1074/jbc.M104455200; RA Hwang J., Inouye M.; RT "An essential GTPase, der, containing double GTP-binding domains from RT Escherichia coli and Thermotoga maritima."; RL J. Biol. Chem. 276:31415-31421(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GDP, GTPASE RP ACTIVITY, GTP-BINDING, DOMAINS, AND MUTAGENESIS OF ASN-118 AND RP ASN-300. RX PubMed=12467572; DOI=10.1016/S0969-2126(02)00905-X; RA Robinson V.L., Hwang J., Fox E., Inouye M., Stock A.M.; RT "Domain arrangement of Der, a switch protein containing two GTPase RT domains."; RL Structure 10:1649-1658(2002). CC -!- FUNCTION: GTPase that plays an essential role in the late steps of CC ribosome biogenesis (By similarity). Has GTPase activity but no CC ATPase activity. GTP, GDP, and dGTP but not GMP, ATP, CTP, and UTP CC compete for GTP binding. {ECO:0000250}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=110 uM for GTP {ECO:0000269|PubMed:11387344}; CC Vmax=0.35 umol/min/ug enzyme {ECO:0000269|PubMed:11387344}; CC Note=At pH 7.5, 70 degrees Celsius, 5 mM MgCl(2) and 400 mM CC KCl.; CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000250}. CC -!- DOMAIN: Each G (guanine nucleotide-binding) domain has activity on CC its own; domain 1 is twice as active as domain 2. The G domains do CC not interact, instead each contacts the C-terminal KH-like domain CC which lies between them. {ECO:0000269|PubMed:12467572}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. EngA (Der) GTPase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 EngA-type G (guanine nucleotide-binding) CC domains. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 KH-like domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36514.1; -; Genomic_DNA. DR PIR; B72253; B72253. DR RefSeq; NP_229245.1; NC_000853.1. DR RefSeq; WP_004081721.1; NZ_CP011107.1. DR PDB; 1MKY; X-ray; 1.90 A; A=2-439. DR PDBsum; 1MKY; -. DR ProteinModelPortal; Q9X1F8; -. DR SMR; Q9X1F8; 2-439. DR STRING; 243274.TM1446; -. DR EnsemblBacteria; AAD36514; AAD36514; TM_1446. DR GeneID; 898030; -. DR KEGG; tma:TM1446; -. DR PATRIC; 23937844; VBITheMar51294_1460. DR eggNOG; ENOG4105DKZ; Bacteria. DR eggNOG; COG1160; LUCA. DR InParanoid; Q9X1F8; -. DR KO; K03977; -. DR OMA; DVMGTPI; -. DR OrthoDB; EOG6DC6K1; -. DR EvolutionaryTrace; Q9X1F8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.30.300.20; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00195; GTPase_Der; 1. DR InterPro; IPR031166; G_ENGA. DR InterPro; IPR016484; GTP-bd_EngA. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR032859; KH_dom-like. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR11649:SF5; PTHR11649:SF5; 1. DR Pfam; PF14714; KH_dom-like; 1. DR Pfam; PF01926; MMR_HSR1; 2. DR PIRSF; PIRSF006485; GTP-binding_EngA; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03594; GTPase_EngA; 1. DR TIGRFAMs; TIGR00231; small_GTP; 2. DR PROSITE; PS51712; G_ENGA; 2. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome; Repeat; Ribosome biogenesis. FT CHAIN 1 439 GTPase Der. FT /FTId=PRO_0000179064. FT DOMAIN 2 168 EngA-type G 1. FT DOMAIN 181 357 EngA-type G 2. FT DOMAIN 358 439 KH-like. FT NP_BIND 8 15 GTP 1. {ECO:0000255}. FT NP_BIND 55 59 GTP 1. {ECO:0000255}. FT NP_BIND 118 121 GTP 1. {ECO:0000255}. FT NP_BIND 190 194 GTP 2. FT NP_BIND 300 303 GTP 2. FT NP_BIND 336 337 GTP 2. FT MUTAGEN 118 118 N->D: 10% of GTPase activity remains. FT {ECO:0000269|PubMed:12467572}. FT MUTAGEN 300 300 N->D: Slight increase of GTPase activity. FT {ECO:0000269|PubMed:12467572}. FT STRAND 3 7 {ECO:0000244|PDB:1MKY}. FT HELIX 14 22 {ECO:0000244|PDB:1MKY}. FT STRAND 40 46 {ECO:0000244|PDB:1MKY}. FT STRAND 49 55 {ECO:0000244|PDB:1MKY}. FT TURN 57 60 {ECO:0000244|PDB:1MKY}. FT HELIX 63 65 {ECO:0000244|PDB:1MKY}. FT HELIX 69 79 {ECO:0000244|PDB:1MKY}. FT STRAND 83 90 {ECO:0000244|PDB:1MKY}. FT TURN 91 93 {ECO:0000244|PDB:1MKY}. FT HELIX 97 109 {ECO:0000244|PDB:1MKY}. FT STRAND 113 119 {ECO:0000244|PDB:1MKY}. FT HELIX 123 129 {ECO:0000244|PDB:1MKY}. FT HELIX 131 134 {ECO:0000244|PDB:1MKY}. FT HELIX 135 137 {ECO:0000244|PDB:1MKY}. FT TURN 147 150 {ECO:0000244|PDB:1MKY}. FT HELIX 153 166 {ECO:0000244|PDB:1MKY}. FT STRAND 171 173 {ECO:0000244|PDB:1MKY}. FT STRAND 181 186 {ECO:0000244|PDB:1MKY}. FT HELIX 193 201 {ECO:0000244|PDB:1MKY}. FT STRAND 206 208 {ECO:0000244|PDB:1MKY}. FT STRAND 221 225 {ECO:0000244|PDB:1MKY}. FT STRAND 228 234 {ECO:0000244|PDB:1MKY}. FT HELIX 255 263 {ECO:0000244|PDB:1MKY}. FT STRAND 265 272 {ECO:0000244|PDB:1MKY}. FT TURN 273 275 {ECO:0000244|PDB:1MKY}. FT HELIX 279 284 {ECO:0000244|PDB:1MKY}. FT HELIX 288 290 {ECO:0000244|PDB:1MKY}. FT STRAND 294 300 {ECO:0000244|PDB:1MKY}. FT HELIX 302 304 {ECO:0000244|PDB:1MKY}. FT HELIX 308 310 {ECO:0000244|PDB:1MKY}. FT HELIX 312 322 {ECO:0000244|PDB:1MKY}. FT HELIX 324 326 {ECO:0000244|PDB:1MKY}. FT STRAND 331 333 {ECO:0000244|PDB:1MKY}. FT TURN 336 339 {ECO:0000244|PDB:1MKY}. FT HELIX 342 345 {ECO:0000244|PDB:1MKY}. FT HELIX 349 356 {ECO:0000244|PDB:1MKY}. FT HELIX 362 373 {ECO:0000244|PDB:1MKY}. FT STRAND 384 391 {ECO:0000244|PDB:1MKY}. FT TURN 392 395 {ECO:0000244|PDB:1MKY}. FT STRAND 396 402 {ECO:0000244|PDB:1MKY}. FT HELIX 409 422 {ECO:0000244|PDB:1MKY}. FT STRAND 432 437 {ECO:0000244|PDB:1MKY}. SQ SEQUENCE 439 AA; 50015 MW; 29CA321453249B58 CRC64; MATVLIVGRP NVGKSTLFNK LVKKKKAIVE DEEGVTRDPV QDTVEWYGKT FKLVDTCGVF DNPQDIISQK MKEVTLNMIR EADLVLFVVD GKRGITKEDE SLADFLRKST VDTILVANKA ENLREFEREV KPELYSLGFG EPIPVSAEHN INLDTLLETI IKKLEEKGLD LESKPEITDA IKVAIVGRPN VGKSTLFNAI LNKERALVSP IPGTTRDPVD DEVFIDGRKY VFVDTAGLRR KSRVEPRTVE KYSNYRVVDS IEKADVVVIV LDATQGITRQ DQRIAGLVER RGRASVVVFN KWDLVEHREK RYDEFTKLFR EKLYFIDYSP LIFTSADKGW NIDRVIDAIN LAYASYTTKV PSSAINSALQ KVLAFTNLPR GLKIFFGLQV DIKPPTFLFF VNSIEKVKNP QKIFLRKLIR DYVFPFEGSP IFLKFKRSR // ID DHE3_THEMA Reviewed; 416 AA. AC P96110; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 13-APR-2016, entry version 119. DE RecName: Full=Glutamate dehydrogenase; DE Short=GDH; DE EC=1.4.1.3; GN Name=gdhA; Synonyms=gdh; OrderedLocusNames=TM_1015; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, AND RP CHARACTERIZATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9680336; DOI=10.1007/s007920050014; RA Kort R., Liebl W., Labedan B., Forterre P., Eggen R.I.L., de Vos W.M.; RT "Glutamate dehydrogenase from the hyperthermophilic bacterium RT Thermotoga maritima: molecular characterization and phylogenetic RT implications."; RL Extremophiles 1:52-60(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=9135121; DOI=10.1006/jmbi.1996.0900; RA Knapp S., de Vos W.M., Rice D., Ladenstein R.; RT "Crystal structure of glutamate dehydrogenase from the RT hyperthermophilic eubacterium Thermotoga maritima at 3.0-A RT resolution."; RL J. Mol. Biol. 267:916-932(1997). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS). RX PubMed=9654452; DOI=10.1006/jmbi.1998.1870; RA Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., RA de Vos W.M.; RT "Engineering activity and stability of Thermotoga maritima glutamate RT dehydrogenase. I. Introduction of a six-residue ion-pair network in RT the hinge region."; RL J. Mol. Biol. 280:287-296(1998). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RX PubMed=10366510; DOI=10.1006/jmbi.1999.2779; RA Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., RA de Vos W.M.; RT "Engineering activity and stability of Thermotoga maritima glutamate RT dehydrogenase. II: construction of a 16-residue ion-pair network at RT the subunit interface."; RL J. Mol. Biol. 289:357-369(1999). CC -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(P)(+) = 2- CC oxoglutarate + NH(3) + NAD(P)H. {ECO:0000255|PROSITE- CC ProRule:PRU10011}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 75 degrees Celsius. Thermostable.; CC -!- SUBUNIT: Homohexamer. CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y09925; CAA71058.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36092.1; -; Genomic_DNA. DR PIR; G72305; G72305. DR PIR; T45284; T45284. DR RefSeq; NP_228821.1; NC_000853.1. DR RefSeq; WP_004080520.1; NZ_CP011107.1. DR PDB; 1B26; X-ray; 3.00 A; A/B/C/D/E/F=1-416. DR PDB; 1B3B; X-ray; 3.10 A; A/B/C/D/E/F=2-416. DR PDB; 2TMG; X-ray; 2.90 A; A/B/C/D/E/F=2-416. DR PDBsum; 1B26; -. DR PDBsum; 1B3B; -. DR PDBsum; 2TMG; -. DR ProteinModelPortal; P96110; -. DR SMR; P96110; 5-413. DR STRING; 243274.TM1015; -. DR EnsemblBacteria; AAD36092; AAD36092; TM_1015. DR GeneID; 896847; -. DR KEGG; tma:TM1015; -. DR PATRIC; 23936959; VBITheMar51294_1028. DR eggNOG; ENOG4105D82; Bacteria. DR eggNOG; COG0334; LUCA. DR InParanoid; P96110; -. DR KO; K00261; -. DR OMA; NMIHASN; -. DR OrthoDB; EOG65XN4D; -. DR BioCyc; RETL1328306-WGS:GSTH-4406-MONOMER; -. DR EvolutionaryTrace; P96110; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH. DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C. DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom. DR InterPro; IPR014362; Glu_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00208; ELFV_dehydrog; 1. DR Pfam; PF02812; ELFV_dehydrog_N; 1. DR PIRSF; PIRSF000185; Glu_DH; 1. DR PRINTS; PR00082; GLFDHDRGNASE. DR SMART; SM00839; ELFV_dehydrog; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; NAD; NADP; KW Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9680336}. FT CHAIN 2 416 Glutamate dehydrogenase. FT /FTId=PRO_0000182764. FT ACT_SITE 105 105 FT CONFLICT 153 153 M -> I (in Ref. 1; CAA71058). FT {ECO:0000305}. FT HELIX 6 20 {ECO:0000244|PDB:2TMG}. FT HELIX 25 32 {ECO:0000244|PDB:2TMG}. FT STRAND 35 45 {ECO:0000244|PDB:2TMG}. FT STRAND 51 62 {ECO:0000244|PDB:2TMG}. FT STRAND 66 69 {ECO:0000244|PDB:2TMG}. FT STRAND 72 77 {ECO:0000244|PDB:2TMG}. FT HELIX 80 97 {ECO:0000244|PDB:2TMG}. FT STRAND 103 109 {ECO:0000244|PDB:2TMG}. FT HELIX 112 114 {ECO:0000244|PDB:2TMG}. FT HELIX 117 130 {ECO:0000244|PDB:2TMG}. FT HELIX 132 134 {ECO:0000244|PDB:2TMG}. FT TURN 137 139 {ECO:0000244|PDB:2TMG}. FT STRAND 140 143 {ECO:0000244|PDB:1B26}. FT HELIX 150 164 {ECO:0000244|PDB:2TMG}. FT STRAND 171 174 {ECO:0000244|PDB:1B3B}. FT HELIX 177 179 {ECO:0000244|PDB:2TMG}. FT TURN 183 187 {ECO:0000244|PDB:2TMG}. FT HELIX 188 203 {ECO:0000244|PDB:2TMG}. FT TURN 208 210 {ECO:0000244|PDB:2TMG}. FT STRAND 212 216 {ECO:0000244|PDB:2TMG}. FT HELIX 220 231 {ECO:0000244|PDB:2TMG}. FT STRAND 236 241 {ECO:0000244|PDB:2TMG}. FT STRAND 246 248 {ECO:0000244|PDB:2TMG}. FT HELIX 255 264 {ECO:0000244|PDB:2TMG}. FT STRAND 265 268 {ECO:0000244|PDB:1B3B}. FT STRAND 272 277 {ECO:0000244|PDB:2TMG}. FT HELIX 279 282 {ECO:0000244|PDB:2TMG}. FT STRAND 288 292 {ECO:0000244|PDB:2TMG}. FT HELIX 301 304 {ECO:0000244|PDB:2TMG}. FT STRAND 310 313 {ECO:0000244|PDB:2TMG}. FT STRAND 316 318 {ECO:0000244|PDB:2TMG}. FT HELIX 322 330 {ECO:0000244|PDB:2TMG}. FT STRAND 334 336 {ECO:0000244|PDB:2TMG}. FT HELIX 338 341 {ECO:0000244|PDB:2TMG}. FT HELIX 344 357 {ECO:0000244|PDB:2TMG}. FT HELIX 364 389 {ECO:0000244|PDB:2TMG}. FT HELIX 393 411 {ECO:0000244|PDB:2TMG}. SQ SEQUENCE 416 AA; 45821 MW; D7294929879CB4F2 CRC64; MPEKSLYEMA VEQFNRAASL MDLESDLAEV LRRPKRVLIV EFPVRMDDGH VEVFTGYRVQ HNVARGPAKG GIRYHPDVTL DEVKALAFWM TWKTAVMNLP FGGGKGGVRV DPKKLSRNEL ERLSRRFFSE IQVIIGPYND IPAPDVNTNA DVMAWYMDTY SMNVGHTVLG IVTGKPVELG GSKGREEATG RGVKVCAGLA MDVLGIDPKK ATVAVQGFGN VGQFAALLIS QELGSKVVAV SDSRGGIYNP EGFDVEELIR YKKEHGTVVT YPKGERITNE ELLELDVDIL VPAALEGAIH AGNAERIKAK AVVEGANGPT TPEADEILSR RGILVVPDIL ANAGGVTVSY FEWVQDLQSF FWDLDQVRNA LEKMMKGAFN DVMKVKEKYN VDMRTAAYIL AIDRVAYATK KRGIYP // ID DNLJ_THEMA Reviewed; 688 AA. AC Q9WXV5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 121. DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588}; DE EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588}; DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588}; GN Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; GN OrderedLocusNames=TM_0100; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: DNA ligase that catalyzes the formation of CC phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl CC groups in double-stranded DNA using NAD as a coenzyme and as the CC energy source for the reaction. It is essential for DNA CC replication and repair of damaged DNA. {ECO:0000255|HAMAP- CC Rule:MF_01588}. CC -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) + CC (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D- CC ribonucleotide + (deoxyribonucleotide)(n+m). {ECO:0000255|HAMAP- CC Rule:MF_01588}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588}; CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}. CC -!- SIMILARITY: Contains 1 BRCT domain. {ECO:0000255|HAMAP- CC Rule:MF_01588}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35194.1; -; Genomic_DNA. DR PIR; D72418; D72418. DR RefSeq; NP_227916.1; NC_000853.1. DR RefSeq; WP_004082648.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXV5; -. DR SMR; Q9WXV5; 9-319. DR STRING; 243274.TM0100; -. DR DNASU; 896927; -. DR EnsemblBacteria; AAD35194; AAD35194; TM_0100. DR GeneID; 896927; -. DR KEGG; tma:TM0100; -. DR PATRIC; 23935040; VBITheMar51294_0098. DR eggNOG; ENOG4105C77; Bacteria. DR eggNOG; COG0272; LUCA. DR InParanoid; Q9WXV5; -. DR KO; K01972; -. DR OMA; FTAKSPR; -. DR OrthoDB; EOG6TTVM9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006288; P:base-excision repair, DNA ligation; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.10190; -; 1. DR HAMAP; MF_01588; DNA_ligase_A; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR018239; DNA_ligase_AS. DR InterPro; IPR033136; DNA_ligase_CS. DR InterPro; IPR001679; DNAligase. DR InterPro; IPR013839; DNAligase_adenylation. DR InterPro; IPR013840; DNAligase_N. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004150; NAD_DNA_ligase_OB. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR004149; Znf_DNAligase_C4. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF01653; DNA_ligase_aden; 1. DR Pfam; PF03120; DNA_ligase_OB; 1. DR Pfam; PF03119; DNA_ligase_ZBD; 1. DR PIRSF; PIRSF001604; LigA; 1. DR SMART; SM00292; BRCT; 1. DR SMART; SM00278; HhH1; 3. DR SMART; SM00532; LIGANc; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52113; SSF52113; 1. DR TIGRFAMs; TIGR00575; dnlj; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS01055; DNA_LIGASE_N1; 1. DR PROSITE; PS01056; DNA_LIGASE_N2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; DNA replication; Ligase; KW Magnesium; Manganese; Metal-binding; NAD; Reference proteome; Zinc. FT CHAIN 1 688 DNA ligase. FT /FTId=PRO_0000161770. FT DOMAIN 590 679 BRCT. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 38 42 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 87 88 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT ACT_SITE 120 120 N6-AMP-lysine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 409 409 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 412 412 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 428 428 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 433 433 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 118 118 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 141 141 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 175 175 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 291 291 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 315 315 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. SQ SEQUENCE 688 AA; 78906 MW; BA991514B52A5126 CRC64; MSERKIPKEV IEEVERLREE IEYHNYRYYV LNDPVITDEE YDRLMRRLIE LERMYPELVT PDSPTQRVGG KVLEGFKTVK HSVPMLSLDN TYNEEEILEF DRRVKKALQE AEVEYVAELK IDGVSIALRY ENGRFVLGAT RGDGIEGEDV SENVKTVRSI PLRLRKPVTI EVRGEIYMPV DEFKRLNDER EEEGLPPFAN PRNAAAGTLR QLNTALVAAR RLDSFIYYVV HPENYGLKTQ WEALQFLKEL GFKVNPHSRL CKNIQEVIDY WKEWKERKRE LDYWVDGVVV KVNRFDFQRI LGETSKAPRW AIAFKFPAEQ ARTRVLDVTI QVGRTGVLTP VAELEPVQLA GTIVKRASLH NFEYIREKDI RIGDYVFVEK AGGIIPQIVK SIPELRTGNE KEIKPPDKCP VCGGKVGKLN PDEVAIRCLN PHCPAKLKRA LRTLVSREAL DIEGLGEKLI DRLVDAGLIK DIADIFYLTP FDLAQLGPGI GQRTIAKILQ EIEEAKKRPL HKLITGLGIP MVGQKTAKIL AEHFKSLEAI ADASYETLKD IPGIGPEIAK SIVEYFRNPK TREIIEKLKK AGVKLEEKVV KLDILRGLTF AVTGTLKNFT REEIIEFLEK LGAKVVNSVS RNTDYLIVGE NPGSKYERAK MLKVKMMSEE EFLEFVRKRA ELKGYNFDEI MRSWKEWS // ID DNAG_THEMA Reviewed; 565 AA. AC Q9X1G3; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 114. DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974}; DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00974}; GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; GN OrderedLocusNames=TM_1452; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA CC molecules used as primers for DNA polymerase during DNA CC replication. {ECO:0000255|HAMAP-Rule:MF_00974}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974}; CC Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP- CC Rule:MF_00974}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00974}; CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000255|HAMAP- CC Rule:MF_00974}. CC -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core CC domain that contains the primase activity, and a C-terminal DnaB- CC binding domain. {ECO:0000255|HAMAP-Rule:MF_00974}. CC -!- SIMILARITY: Belongs to the DnaG primase family. CC {ECO:0000255|HAMAP-Rule:MF_00974}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00974}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36520.1; -; Genomic_DNA. DR PIR; H72253; H72253. DR RefSeq; NP_229251.1; NC_000853.1. DR RefSeq; WP_004081732.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1G3; -. DR STRING; 243274.TM1452; -. DR EnsemblBacteria; AAD36520; AAD36520; TM_1452. DR GeneID; 898024; -. DR KEGG; tma:TM1452; -. DR PATRIC; 23937856; VBITheMar51294_1466. DR eggNOG; ENOG4105C9G; Bacteria. DR eggNOG; COG0358; LUCA. DR InParanoid; Q9X1G3; -. DR KO; K02316; -. DR OMA; SAYSKNV; -. DR OrthoDB; EOG6XDGTR; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.580.10; -; 1. DR Gene3D; 3.90.980.10; -; 1. DR HAMAP; MF_00974; DNA_primase_DnaG; 1. DR InterPro; IPR013264; DNA_primase_core_N. DR InterPro; IPR006295; DNA_primase_DnaG. DR InterPro; IPR030846; DnaG_bac. DR InterPro; IPR006171; Toprim_domain. DR InterPro; IPR002694; Znf_CHC2. DR Pfam; PF08275; Toprim_N; 1. DR Pfam; PF01807; zf-CHC2; 1. DR PIRSF; PIRSF002811; DnaG; 1. DR SMART; SM00493; TOPRIM; 1. DR SMART; SM00400; ZnF_CHCC; 1. DR TIGRFAMs; TIGR01391; dnaG; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-binding; KW DNA-directed RNA polymerase; Magnesium; Metal-binding; KW Nucleotidyltransferase; Primosome; Reference proteome; Transcription; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1 565 DNA primase. FT /FTId=PRO_0000180530. FT DOMAIN 248 329 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT ZN_FING 37 61 CHC2-type. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT METAL 254 254 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00974}. FT METAL 298 298 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00974}. FT METAL 298 298 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT METAL 300 300 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00974}. SQ SEQUENCE 565 AA; 65133 MW; C03A5A050CCB9E71 CRC64; MIPREVIEEI KEKVDIVEVI SEYVNLTRVG SSYRALCPFH SETNPSFYVH PGLKIYHCFG CGASGDVIKF LQEMEGISFQ EALERLAKRA GIDLSLYRTE GTSEYGKYIR LYEETWKRYV KELEKSKEAK DYLKSRGFSE EDIAKFGFGY VPKRSSISIE VAEGMNITLE ELVRYGIALK KGDRFVDRFE GRIVVPIKND SGHIVAFGGR ALGNEEPKYL NSPETRYFSK KKTLFLFDEA KKVAKEVGFF VITEGYFDAL AFRKDGIPTA VAVLGASLSR EAILKLSAYS KNVILCFDND KAGFRATLKS LEDLLDYEFN VLVATPSPYK DPDELFQKEG EGSLKKMLKN SRSFEYFLVT AGEVFFDRNS PAGVRSYLSF LKGWVQKMRR KGYLKHIENL VNEVSSSLQI PENQILNFFE SDRSNTMPVH ETKSSKVYDE GRGLAYLFLN YEDLREKILE LDLEVLEDKN AREFFKRVSL GEDLNKVIEN FPKELKDWIF ETIESIPPPK DPEKFLGDLS EKLKIRRIER RIAEIDDMIK KASNDEERRL LLSMKVDLLR KIKRR // ID DNAA_THEMA Reviewed; 440 AA. AC P46798; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 121. DE RecName: Full=Chromosomal replication initiator protein DnaA; GN Name=dnaA; OrderedLocusNames=TM_0926; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8168477; RA Darimont B., Sterner R.; RT "Sequence, assembly and evolution of a primordial ferredoxin from RT Thermotoga maritima."; RL EMBO J. 13:1772-1781(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Plays an important role in the initiation and regulation CC of chromosomal replication. Binds to the origin of replication; it CC binds specifically double-stranded DNA at a 9 bp consensus (dnaA CC box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic CC phospholipids (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U24145; AAA65438.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36007.1; -; Genomic_DNA. DR PIR; G72317; G72317. DR RefSeq; NP_228734.1; NC_000853.1. DR RefSeq; WP_004080636.1; NZ_CP011107.1. DR PDB; 2Z4R; X-ray; 3.05 A; A/B/C=1-440. DR PDB; 2Z4S; X-ray; 3.00 A; A=1-440. DR PDBsum; 2Z4R; -. DR PDBsum; 2Z4S; -. DR ProteinModelPortal; P46798; -. DR SMR; P46798; 96-335. DR STRING; 243274.TM0926; -. DR EnsemblBacteria; AAD36007; AAD36007; TM_0926. DR GeneID; 898600; -. DR KEGG; tma:TM0926; -. DR PATRIC; 23936783; VBITheMar51294_0940. DR eggNOG; ENOG4105CI4; Bacteria. DR eggNOG; COG0593; LUCA. DR InParanoid; P46798; -. DR KO; K02313; -. DR OMA; QSKTRKR; -. DR OrthoDB; EOG689HR1; -. DR EvolutionaryTrace; P46798; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central. DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1750.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00377; DnaA_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR001957; Chromosome_initiator_DnaA. DR InterPro; IPR020591; Chromosome_initiator_DnaA-like. DR InterPro; IPR018312; Chromosome_initiator_DnaA_CS. DR InterPro; IPR013317; DnaA. DR InterPro; IPR013159; DnaA_C. DR InterPro; IPR024633; DnaA_N_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010921; Trp_repressor/repl_initiator. DR Pfam; PF00308; Bac_DnaA; 1. DR Pfam; PF08299; Bac_DnaA_C; 1. DR Pfam; PF11638; DnaA_N; 1. DR PRINTS; PR00051; DNAA. DR SMART; SM00382; AAA; 1. DR SMART; SM00760; Bac_DnaA_C; 1. DR SUPFAM; SSF48295; SSF48295; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00362; DnaA; 1. DR PROSITE; PS01008; DNAA; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; KW DNA replication; DNA-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 440 Chromosomal replication initiator protein FT DnaA. FT /FTId=PRO_0000114286. FT NP_BIND 137 144 ATP. {ECO:0000255}. FT HELIX 104 106 {ECO:0000244|PDB:2Z4S}. FT TURN 111 113 {ECO:0000244|PDB:2Z4S}. FT HELIX 114 125 {ECO:0000244|PDB:2Z4S}. FT TURN 127 129 {ECO:0000244|PDB:2Z4R}. FT STRAND 133 136 {ECO:0000244|PDB:2Z4S}. FT STRAND 138 142 {ECO:0000244|PDB:2Z4S}. FT HELIX 143 157 {ECO:0000244|PDB:2Z4S}. FT STRAND 158 161 {ECO:0000244|PDB:2Z4R}. FT STRAND 163 167 {ECO:0000244|PDB:2Z4S}. FT HELIX 168 180 {ECO:0000244|PDB:2Z4S}. FT HELIX 184 191 {ECO:0000244|PDB:2Z4S}. FT TURN 192 194 {ECO:0000244|PDB:2Z4S}. FT STRAND 196 201 {ECO:0000244|PDB:2Z4S}. FT HELIX 203 206 {ECO:0000244|PDB:2Z4S}. FT HELIX 210 224 {ECO:0000244|PDB:2Z4S}. FT TURN 225 227 {ECO:0000244|PDB:2Z4S}. FT STRAND 229 236 {ECO:0000244|PDB:2Z4S}. FT HELIX 238 240 {ECO:0000244|PDB:2Z4S}. FT HELIX 246 253 {ECO:0000244|PDB:2Z4S}. FT STRAND 254 256 {ECO:0000244|PDB:2Z4S}. FT HELIX 265 279 {ECO:0000244|PDB:2Z4S}. FT HELIX 287 294 {ECO:0000244|PDB:2Z4S}. FT HELIX 299 315 {ECO:0000244|PDB:2Z4S}. FT STRAND 316 318 {ECO:0000244|PDB:2Z4S}. FT HELIX 322 328 {ECO:0000244|PDB:2Z4S}. FT TURN 331 333 {ECO:0000244|PDB:2Z4S}. SQ SEQUENCE 440 AA; 50304 MW; 2E35ED82650A5C2E CRC64; MKERILQEIK TRVNRKSWEL WFSSFDVKSI EGNKVVFSVG NLFIKEWLEK KYYSVLSKAV KVVLGNDATF EITYEAFEPH SSYSEPLVKK RAVLLTPLNP DYTFENFVVG PGNSFAYHAA LEVAKHPGRY NPLFIYGGVG LGKTHLLQSI GNYVVQNEPD LRVMYITSEK FLNDLVDSMK EGKLNEFREK YRKKVDILLI DDVQFLIGKT GVQTELFHTF NELHDSGKQI VICSDREPQK LSEFQDRLVS RFQMGLVAKL EPPDEETRKS IARKMLEIEH GELPEEVLNF VAENVDDNLR RLRGAIIKLL VYKETTGKEV DLKEAILLLK DFIKPNRVKA MDPIDELIEI VAKVTGVPRE EILSNSRNVK ALTARRIGMY VAKNYLKSSL RTIAEKFNRS HPVVVDSVKK VKDSLLKGNK QLKALIDEVI GEISRRALSG // ID DPO3_THEMA Reviewed; 1367 AA. AC Q9ZHF6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 130. DE RecName: Full=DNA polymerase III PolC-type {ECO:0000255|HAMAP-Rule:MF_00356}; DE Short=PolIII {ECO:0000255|HAMAP-Rule:MF_00356}; DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_00356}; GN Name=polC {ECO:0000255|HAMAP-Rule:MF_00356}; GN OrderedLocusNames=TM_0576; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9826752; DOI=10.1093/nar/26.23.5300; RA Huang Y.P., Ito J.; RT "The hyperthermophilic bacterium Thermotoga maritima has two different RT classes of family C DNA polymerases: evolutionary implications."; RL Nucleic Acids Res. 26:5300-5309(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA CC polymerase also exhibits 3' to 5' exonuclease activity. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). {ECO:0000255|HAMAP-Rule:MF_00356}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00356}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00356}. CC -!- SIMILARITY: Contains 1 exonuclease domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF065313; AAC80438.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35661.1; -; Genomic_DNA. DR PIR; C72360; C72360. DR RefSeq; NP_228386.1; NC_000853.1. DR RefSeq; WP_004081285.1; NZ_CP011107.1. DR PDB; 2P1J; X-ray; 2.50 A; A/B=347-522. DR PDBsum; 2P1J; -. DR ProteinModelPortal; Q9ZHF6; -. DR SMR; Q9ZHF6; 357-520. DR STRING; 243274.TM0576; -. DR EnsemblBacteria; AAD35661; AAD35661; TM_0576. DR GeneID; 897644; -. DR KEGG; tma:TM0576; -. DR PATRIC; 23936061; VBITheMar51294_0585. DR eggNOG; ENOG4105DE5; Bacteria. DR eggNOG; COG2176; LUCA. DR InParanoid; Q9ZHF6; -. DR KO; K03763; -. DR OMA; QGCTGVK; -. DR OrthoDB; EOG6ZWJJS; -. DR EvolutionaryTrace; Q9ZHF6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006259; P:DNA metabolic process; IBA:GO_Central. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.5.140; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00356; DNApol_PolC; 1. DR InterPro; IPR011708; DNA_pol3_alpha. DR InterPro; IPR023223; DNA_polIII_IA3_alpha-helix. DR InterPro; IPR029460; DNAPol_HHH. DR InterPro; IPR006054; DnaQ. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004013; PHP_dom. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR006308; PolC_gram_pos. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF07733; DNA_pol3_alpha; 1. DR Pfam; PF14579; HHH_6; 1. DR Pfam; PF02811; PHP; 1. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR00573; dnaq; 1. DR TIGRFAMs; TIGR01405; polC_Gram_pos; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; DNA replication; KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 1367 DNA polymerase III PolC-type. FT /FTId=PRO_0000204605. FT DOMAIN 358 513 Exonuclease. FT STRAND 358 366 {ECO:0000244|PDB:2P1J}. FT TURN 370 372 {ECO:0000244|PDB:2P1J}. FT STRAND 375 384 {ECO:0000244|PDB:2P1J}. FT STRAND 387 395 {ECO:0000244|PDB:2P1J}. FT HELIX 404 410 {ECO:0000244|PDB:2P1J}. FT HELIX 414 417 {ECO:0000244|PDB:2P1J}. FT HELIX 423 433 {ECO:0000244|PDB:2P1J}. FT STRAND 434 436 {ECO:0000244|PDB:2P1J}. FT STRAND 438 441 {ECO:0000244|PDB:2P1J}. FT HELIX 444 459 {ECO:0000244|PDB:2P1J}. FT STRAND 467 469 {ECO:0000244|PDB:2P1J}. FT HELIX 470 477 {ECO:0000244|PDB:2P1J}. FT HELIX 485 491 {ECO:0000244|PDB:2P1J}. FT HELIX 501 516 {ECO:0000244|PDB:2P1J}. SQ SEQUENCE 1367 AA; 155363 MW; EE5916FA70591F84 CRC64; MKKIENLKWK NVSFKSLEID PDAGVVLVSV EKFSEEIEDL VRLLEKKTRF RVIVNGVQKS NGDLRGKILS LLNGNVPYIK DVVFEGNRLI LKVLGDFARD RIASKLRSTK KQLDELLPPG TEIMLEVVEP PEDLLKKEVP QPEKREEPKG EELKIEDENH IFGQKPRKIV FTPSKIFEYN KKTSVKGKIF KIEKIEGKRT VLLIYLTDGE DSLICKVFND VEKVEGKVSV GDVIVATGDL LLENGEPTLY VKGITKLPEA KRMDKSPVKR VELHAHTKFS DQDAITDVNE YVKRAKEWGF PAIALTDHGN VQAIPYFYDA AKEAGIKPIF GIEAYLVSDV EPVIRNLSDD STFGDATFVV LDFETTGLDP QVDEIIEIGA VKIQGGQIVD EYHTLIKPSR EISRKSSEIT GITQEMLENK RSIEEVLPEF LGFLEDSIIV AHNANFDYRF LRLWIKKVMG LDWERPYIDT LALAKSLLKL RSYSLDSVVE KLGLGPFRHH RALDDARVTA QVFLRFVEMM KKIGITKLSE MEKLKDTIDY TALKPFHCTI LVQNKKGLKN LYKLVSDSYI KYFYGVPRIL KSELIENREG LLVGSACISG ELGRAALEGA SDSELEEIAK FYDYIEVMPL DVIAEDEEDL DRERLKEVYR KLYRIAKKLN KFVVMTGDVH FLDPEDARGR AALLAPQGNR NFENQPALYL RTTEEMLEKA IEIFEDEEIA REVVIENPNR IADMIEEVQP LEKKLHPPII ENADEIVRNL TMKRAYEIYG DPLPEIVQKR VEKELNAIIN HGYAVLYLIA QELVQKSMSD GYVVGSRGSV GSSLVANLLG ITEVNPLPPH YRCPECKYFE VVEDDRYGAG YDLPNKNCPR CGAPLRKDGH GIPFETFMGF EGDKVPDIDL NFSGEYQERA HRFVEELFGK DHVYRAGTIN TIAERSAVGY VRSYEEKTGK KLRKAEMERL VSMITGVKRT TGQHPGGLMI IPKDKEVYDF TPIQYPANDR NAGVFTTHFA YETIHDDLVK IDALGHDDPT FIKMLKDLTG IDPMTIPMDD PDTLAIFSSV KPLGVDPVEL ESDVGTYGIP EFGTEFVRGM LVETRPKSFA ELVRISGLSH GTDVWLNNAR DWINLGYAKL SEVISCRDDI MNFLIHKGME PSLAFKIMEN VRKGKGITEE MESEMRRLKV PEWFIESCKR IKYLFPKAHA VAYVSMAFRI AYFKVHYPLQ FYAAYFTIKG DQFDPVLVLR GKEAIKRRLR ELKAMPAKDA QKKNEVSVLE VALEMILRGF SFLPPDIFKS DAKKFLIEGN SLRIPFNKLP GLGDSVAESI IRAREEKPFT SVEDLMKRTK VNKNHIELMK SLGVLGDLPE TEQFTLF // ID DNAK_THEMA Reviewed; 596 AA. AC Q9WYK6; Q9ZFD2; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 111. DE RecName: Full=Chaperone protein DnaK; DE AltName: Full=HSP70; DE AltName: Full=Heat shock 70 kDa protein; DE AltName: Full=Heat shock protein 70; GN Name=dnaK; Synonyms=hsp70; OrderedLocusNames=TM_0373; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Michelini E.T., Flynn G.C.; RT "The unique chaperone operon of Thermotoga maritima: cloning and RT initial characterization of a functional Hsp70 and sHsp."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}. CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF106330; AAC79725.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35460.1; -; Genomic_DNA. DR PIR; C72385; C72385. DR PIR; T46657; T46657. DR RefSeq; NP_228184.1; NC_000853.1. DR RefSeq; WP_004083187.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYK6; -. DR SMR; Q9WYK6; 8-517. DR STRING; 243274.TM0373; -. DR PRIDE; Q9WYK6; -. DR EnsemblBacteria; AAD35460; AAD35460; TM_0373. DR GeneID; 897332; -. DR KEGG; tma:TM0373; -. DR PATRIC; 23935627; VBITheMar51294_0378. DR eggNOG; ENOG4105CFG; Bacteria. DR eggNOG; COG0443; LUCA. DR InParanoid; Q9WYK6; -. DR KO; K04043; -. DR OMA; EKMAPPQ; -. DR OrthoDB; EOG6JMMSV; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 1.20.1270.10; -; 1. DR Gene3D; 2.60.34.10; -; 1. DR HAMAP; MF_00332; DnaK; 1. DR InterPro; IPR012725; Chaperone_DnaK. DR InterPro; IPR018181; Heat_shock_70_CS. DR InterPro; IPR029048; HSP70_C. DR InterPro; IPR029047; HSP70_peptide-bd. DR InterPro; IPR013126; Hsp_70_fam. DR Pfam; PF00012; HSP70; 2. DR PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF100920; SSF100920; 1. DR TIGRFAMs; TIGR02350; prok_dnaK; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Stress response. FT CHAIN 1 596 Chaperone protein DnaK. FT /FTId=PRO_0000078572. FT MOD_RES 180 180 Phosphothreonine; by autocatalysis. FT {ECO:0000250}. FT CONFLICT 1 9 MAEKKEFVV -> MSKII (in Ref. 1). FT {ECO:0000305}. FT CONFLICT 108 108 A -> P (in Ref. 1; AAC79725). FT {ECO:0000305}. FT CONFLICT 111 111 Y -> F (in Ref. 1; AAC79725). FT {ECO:0000305}. FT CONFLICT 138 140 AGI -> S (in Ref. 1; AAC79725). FT {ECO:0000305}. FT CONFLICT 175 175 D -> PLP (in Ref. 1; AAC79725). FT {ECO:0000305}. FT CONFLICT 188 188 I -> T (in Ref. 1; AAC79725). FT {ECO:0000305}. FT CONFLICT 434 434 I -> M (in Ref. 1; AAC79725). FT {ECO:0000305}. FT CONFLICT 534 534 E -> D (in Ref. 1; AAC79725). FT {ECO:0000305}. SQ SEQUENCE 596 AA; 66052 MW; 7478381447DC420E CRC64; MAEKKEFVVG IDLGTTNSVI AWMKPDGTVE VIPNAEGSRV TPSVVAFTKS GEILVGEPAK RQMILNPERT IKSIKRKMGT DYKVRIDDKE YTPQEISAFI LKKLKNDAEA YLGGEIKKAV ITCPAYFNDA QRQATKEAGI IAGLEVLRII NEPTAAALAY GLDKAGKEEK VLVYDLGGGT FDVSILEIGE GVIEVIATAG NNHLGGDDFD QRLIDWMAEE FKKQHGIDLR EDRQALQRLR DAAEKAKIEL STKMETDVSL PFIAVSPSGQ PLHLEMRITR SLFESLTRDL VEMTRGPIEQ ALNDAKLSPQ DIDEIILVGG MTRVPMVQRF IKEFFGKEPN KSVNPDEAVA IGAAIQAAIL AGTEGAKGRD IVLVDVTPLT LGIEVKGGLF EPIIPRNTKI PVRKSKIFTT VEDGQTEVEI RVYQGERPIA RENIFLGSFK LVGIPPAPRG VPQIEVTFDI DSDGIVHVSA KDLGSGKEQS MVVTGRHKLS EDEIKRMIED AKRYEEQDKR LKEEIELKNR ADDLAYSVEK TLKEHGDKIP ADLKSRLEDM IRELRDAINR NDIPKVKMLF DDLQKESMKI GEYLYKSATG GETSNQ // ID DTD_THEMA Reviewed; 149 AA. AC Q9WZI9; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00518}; DE EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00518}; DE AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase; GN Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518}; OrderedLocusNames=TM_0730; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: D-aminoacyl-tRNA deacylase with broad substrate CC specificity. By recycling D-aminoacyl-tRNA to D-amino acids and CC free tRNA molecules, this enzyme counteracts the toxicity CC associated with the formation of D-aminoacyl-tRNA entities in CC vivo. {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- CATALYTIC ACTIVITY: A D-aminoacyl-tRNA + H(2)O = a D-amino acid + CC tRNA. {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000255|HAMAP- CC Rule:MF_00518}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35812.1; -; Genomic_DNA. DR PIR; E72338; E72338. DR RefSeq; NP_228539.1; NC_000853.1. DR RefSeq; WP_004080996.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZI9; -. DR SMR; Q9WZI9; 1-148. DR STRING; 243274.TM0730; -. DR EnsemblBacteria; AAD35812; AAD35812; TM_0730. DR GeneID; 898397; -. DR KEGG; tma:TM0730; -. DR PATRIC; 23936380; VBITheMar51294_0743. DR eggNOG; ENOG4108YYA; Bacteria. DR eggNOG; COG1490; LUCA. DR InParanoid; Q9WZI9; -. DR KO; K07560; -. DR OMA; VFGADMK; -. DR OrthoDB; EOG6C2WM2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central. DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IBA:GO_Central. DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006450; P:regulation of translational fidelity; IBA:GOC. DR GO; GO:0006399; P:tRNA metabolic process; IBA:GO_Central. DR Gene3D; 3.50.80.10; -; 1. DR HAMAP; MF_00518; Deacylase_Dtd; 1. DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD. DR InterPro; IPR023509; DTD-like_dom. DR PANTHER; PTHR10472; PTHR10472; 1. DR Pfam; PF02580; Tyr_Deacylase; 1. DR SUPFAM; SSF69500; SSF69500; 1. DR TIGRFAMs; TIGR00256; TIGR00256; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Reference proteome. FT CHAIN 1 149 D-aminoacyl-tRNA deacylase. FT /FTId=PRO_0000164611. FT ACT_SITE 80 80 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00518}. SQ SEQUENCE 149 AA; 16519 MW; 902E403DE9219909 CRC64; MRAVVQRVSE AKVVVGEETV GAIKKGLLVF VGVGKNDTEE DCEWLADKVS GLRIFEDEDG KMNLSVKDIN GEVLVVSQFT LYGDCRRGKR PSFTEAAPPD KGKALYEKFV ELLRKKGLKV ETGKFRAHMH VHLVNDGPVT ILLDSSKLF // ID ECFA2_THEMA Reviewed; 266 AA. AC Q9WY65; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 104. DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA2; DE Short=ECF transporter A component EcfA2; DE EC=3.6.3.-; GN Name=ecfA2; Synonyms=ecfA, ecfA'; OrderedLocusNames=TM_0222; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=18540059; DOI=10.1107/S1744309108013778; RA Ethayathulla A.S., Bessho Y., Shinkai A., Padmanabhan B., Singh T.P., RA Kaur P., Yokoyama S.; RT "Purification, crystallization and preliminary X-ray diffraction RT analysis of the putative ABC transporter ATP-binding protein from RT Thermotoga maritima."; RL Acta Crystallogr. F 64:498-500(2008). RN [3] RP FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION, RP EXPRESSION IN E.COLI, ATP-BINDING, AND X-RAY CRYSTALLOGRAPHY (2.7 RP ANGSTROMS) OF 2-266 IN COMPLEX WITH ADP. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23359690; DOI=10.1073/pnas.1217361110; RA Karpowich N.K., Wang D.N.; RT "Assembly and mechanism of a group II ECF transporter."; RL Proc. Natl. Acad. Sci. U.S.A. 110:2534-2539(2013). CC -!- FUNCTION: ATP-binding (A) component of a common energy-coupling CC factor (ECF) ABC-transporter complex. Unlike classic ABC CC transporters this ECF transporter provides the energy necessary to CC transport a number of different substrates (Probable). Expression CC of the complex plus RibU in E.coli allows riboflavin uptake; CC uptake does not occur in the absence of RibU or the EcfA1A2T CC complex. {ECO:0000269|PubMed:23359690, ECO:0000305}. CC -!- SUBUNIT: Forms a heterodimer with EcfA1. Forms a stable energy- CC coupling factor (ECF) transporter complex composed of 2 membrane- CC embedded substrate-binding proteins (S component, RibU, BioY), 2 CC ATP-binding proteins (A component) and 2 transmembrane proteins (T CC component) upon coexpression in E.coli. Stable subcomplexes with CC both A plus T components can also be isolated. This complex CC interacts with at least 2 substrate-specific components, BioY and CC RibU. {ECO:0000269|PubMed:23359690}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000305|PubMed:23359690}; Peripheral membrane protein CC {ECO:0000305|PubMed:23359690}. CC -!- MISCELLANEOUS: Structure 4HLU is probably in the open state. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Energy- CC coupling factor EcfA family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35314.1; -; Genomic_DNA. DR PIR; A72401; A72401. DR RefSeq; NP_228037.1; NC_000853.1. DR RefSeq; WP_004082907.1; NZ_CP011107.1. DR PDB; 2YZ2; X-ray; 2.30 A; A/B=1-266. DR PDB; 4HLU; X-ray; 2.70 A; A/B=2-266. DR PDB; 4ZIR; X-ray; 3.00 A; A=2-266. DR PDBsum; 2YZ2; -. DR PDBsum; 4HLU; -. DR PDBsum; 4ZIR; -. DR ProteinModelPortal; Q9WY65; -. DR SMR; Q9WY65; 1-266. DR DIP; DIP-61612N; -. DR STRING; 243274.TM0222; -. DR TCDB; 3.A.1.25.5; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35314; AAD35314; TM_0222. DR GeneID; 897116; -. DR KEGG; tma:TM0222; -. DR PATRIC; 23935316; VBITheMar51294_0224. DR eggNOG; ENOG4108JJB; Bacteria. DR eggNOG; COG1122; LUCA. DR InParanoid; Q9WY65; -. DR KO; K16787; -. DR OMA; ETIMIKK; -. DR OrthoDB; EOG6T7N3V; -. DR EvolutionaryTrace; Q9WY65; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0032217; F:riboflavin transporter activity; IGI:UniProtKB. DR GO; GO:0032218; P:riboflavin transport; IGI:UniProtKB. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; KW Complete proteome; Hydrolase; Membrane; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 266 Energy-coupling factor transporter ATP- FT binding protein EcfA2. FT /FTId=PRO_0000092115. FT DOMAIN 3 238 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 43 48 ATP. FT REGION 220 266 Required for heterodimer formation. FT ACT_SITE 164 164 Proton acceptor. {ECO:0000250}. FT STRAND 3 13 {ECO:0000244|PDB:2YZ2}. FT STRAND 20 30 {ECO:0000244|PDB:2YZ2}. FT STRAND 35 39 {ECO:0000244|PDB:2YZ2}. FT STRAND 42 44 {ECO:0000244|PDB:4ZIR}. FT HELIX 46 53 {ECO:0000244|PDB:2YZ2}. FT STRAND 60 66 {ECO:0000244|PDB:2YZ2}. FT HELIX 73 76 {ECO:0000244|PDB:2YZ2}. FT HELIX 77 79 {ECO:0000244|PDB:2YZ2}. FT STRAND 80 83 {ECO:0000244|PDB:2YZ2}. FT HELIX 87 90 {ECO:0000244|PDB:2YZ2}. FT HELIX 96 102 {ECO:0000244|PDB:2YZ2}. FT TURN 103 107 {ECO:0000244|PDB:2YZ2}. FT HELIX 114 123 {ECO:0000244|PDB:2YZ2}. FT HELIX 128 131 {ECO:0000244|PDB:2YZ2}. FT HELIX 136 138 {ECO:0000244|PDB:2YZ2}. FT HELIX 141 153 {ECO:0000244|PDB:2YZ2}. FT STRAND 158 164 {ECO:0000244|PDB:2YZ2}. FT TURN 165 168 {ECO:0000244|PDB:2YZ2}. FT HELIX 171 186 {ECO:0000244|PDB:2YZ2}. FT STRAND 190 194 {ECO:0000244|PDB:2YZ2}. FT TURN 199 201 {ECO:0000244|PDB:2YZ2}. FT HELIX 202 204 {ECO:0000244|PDB:2YZ2}. FT STRAND 206 212 {ECO:0000244|PDB:2YZ2}. FT STRAND 215 221 {ECO:0000244|PDB:2YZ2}. FT HELIX 222 228 {ECO:0000244|PDB:2YZ2}. FT HELIX 231 233 {ECO:0000244|PDB:4HLU}. FT HELIX 236 243 {ECO:0000244|PDB:2YZ2}. FT TURN 244 247 {ECO:0000244|PDB:2YZ2}. FT STRAND 252 254 {ECO:0000244|PDB:2YZ2}. FT HELIX 257 260 {ECO:0000244|PDB:2YZ2}. FT TURN 261 263 {ECO:0000244|PDB:2YZ2}. SQ SEQUENCE 266 AA; 30233 MW; EB146157FC21EB4F CRC64; MRIEVVNVSH IFHRGTPLEK KALENVSLVI NEGECLLVAG NTGSGKSTLL QIVAGLIEPT SGDVLYDGER KKGYEIRRNI GIAFQYPEDQ FFAERVFDEV AFAVKNFYPD RDPVPLVKKA MEFVGLDFDS FKDRVPFFLS GGEKRRVAIA SVIVHEPDIL ILDEPLVGLD REGKTDLLRI VEKWKTLGKT VILISHDIET VINHVDRVVV LEKGKKVFDG TRMEFLEKYD PRFFTSKMLV MRRLVLKGED PFSMSDDELL ERVCNS // ID DXR_THEMA Reviewed; 376 AA. AC Q9WZZ1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 111. DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE Short=DXP reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE EC=1.1.1.267 {ECO:0000255|HAMAP-Rule:MF_00183}; DE AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00183}; GN Name=dxr {ECO:0000255|HAMAP-Rule:MF_00183}; OrderedLocusNames=TM_0889; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction CC of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol CC 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00183}. CC -!- CATALYTIC ACTIVITY: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) CC = 1-deoxy-D-xylulose 5-phosphate + NADPH. {ECO:0000255|HAMAP- CC Rule:MF_00183}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00183}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 1/6. {ECO:0000255|HAMAP- CC Rule:MF_00183}. CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP- CC Rule:MF_00183}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35970.1; -; Genomic_DNA. DR PIR; B72321; B72321. DR RefSeq; NP_228697.1; NC_000853.1. DR RefSeq; WP_004080699.1; NZ_CP011107.1. DR PDB; 3A06; X-ray; 2.00 A; A/B=1-376. DR PDB; 3A14; X-ray; 2.00 A; A/B=1-376. DR PDBsum; 3A06; -. DR PDBsum; 3A14; -. DR ProteinModelPortal; Q9WZZ1; -. DR STRING; 243274.TM0889; -. DR EnsemblBacteria; AAD35970; AAD35970; TM_0889. DR GeneID; 898563; -. DR KEGG; tma:TM0889; -. DR PATRIC; 23936709; VBITheMar51294_0903. DR eggNOG; ENOG4105CEA; Bacteria. DR eggNOG; COG0743; LUCA. DR InParanoid; Q9WZZ1; -. DR KO; K00099; -. DR OMA; HKYNVKI; -. DR OrthoDB; EOG6R2H04; -. DR BRENDA; 1.1.1.267; 6331. DR UniPathway; UPA00056; UER00092. DR EvolutionaryTrace; Q9WZZ1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central. DR GO; GO:0070402; F:NADPH binding; IBA:GO_Central. DR GO; GO:0051484; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00183; DXP_reductoisom; 1. DR InterPro; IPR003821; DXP_reductoisomerase. DR InterPro; IPR013644; DXP_reductoisomerase_C. DR InterPro; IPR013512; DXP_reductoisomerase_N. DR InterPro; IPR026877; DXPR_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR30525; PTHR30525; 1. DR Pfam; PF08436; DXP_redisom_C; 1. DR Pfam; PF02670; DXP_reductoisom; 1. DR Pfam; PF13288; DXPR_C; 1. DR PIRSF; PIRSF006205; Dxp_reductismrs; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF69055; SSF69055; 1. DR TIGRFAMs; TIGR00243; Dxr; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isoprene biosynthesis; Metal-binding; KW NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 376 1-deoxy-D-xylulose 5-phosphate FT reductoisomerase. FT /FTId=PRO_0000163723. FT NP_BIND 9 37 NADP. {ECO:0000255|HAMAP-Rule:MF_00183}. FT METAL 142 142 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00183}. FT METAL 144 144 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00183}. FT METAL 209 209 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00183}. FT BINDING 117 117 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 144 144 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 164 164 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 187 187 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 209 209 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT STRAND 4 9 {ECO:0000244|PDB:3A06}. FT TURN 10 12 {ECO:0000244|PDB:3A06}. FT HELIX 14 25 {ECO:0000244|PDB:3A06}. FT STRAND 28 38 {ECO:0000244|PDB:3A06}. FT HELIX 40 50 {ECO:0000244|PDB:3A06}. FT STRAND 54 57 {ECO:0000244|PDB:3A06}. FT STRAND 66 73 {ECO:0000244|PDB:3A06}. FT HELIX 76 84 {ECO:0000244|PDB:3A06}. FT STRAND 87 91 {ECO:0000244|PDB:3A06}. FT HELIX 98 108 {ECO:0000244|PDB:3A06}. FT STRAND 110 114 {ECO:0000244|PDB:3A06}. FT HELIX 118 134 {ECO:0000244|PDB:3A06}. FT STRAND 137 140 {ECO:0000244|PDB:3A06}. FT HELIX 143 151 {ECO:0000244|PDB:3A06}. FT STRAND 157 163 {ECO:0000244|PDB:3A06}. FT STRAND 169 171 {ECO:0000244|PDB:3A06}. FT HELIX 173 176 {ECO:0000244|PDB:3A06}. FT HELIX 181 183 {ECO:0000244|PDB:3A06}. FT HELIX 194 202 {ECO:0000244|PDB:3A06}. FT HELIX 204 217 {ECO:0000244|PDB:3A06}. FT HELIX 221 223 {ECO:0000244|PDB:3A06}. FT STRAND 224 228 {ECO:0000244|PDB:3A06}. FT STRAND 234 239 {ECO:0000244|PDB:3A06}. FT STRAND 245 249 {ECO:0000244|PDB:3A06}. FT HELIX 255 263 {ECO:0000244|PDB:3A06}. FT STRAND 278 280 {ECO:0000244|PDB:3A06}. FT TURN 287 289 {ECO:0000244|PDB:3A06}. FT HELIX 293 295 {ECO:0000244|PDB:3A06}. FT HELIX 296 299 {ECO:0000244|PDB:3A06}. FT HELIX 303 321 {ECO:0000244|PDB:3A06}. FT HELIX 329 339 {ECO:0000244|PDB:3A06}. FT TURN 340 343 {ECO:0000244|PDB:3A06}. FT HELIX 350 371 {ECO:0000244|PDB:3A06}. SQ SEQUENCE 376 AA; 42200 MW; C0D3B68DB0C4BF57 CRC64; MEERTLVILG ATGSIGTQTL DVLKKVKGIR LIGISFHSNL ELAFKIVKEF NVKNVAITGD VEFEDSSINV WKGSHSIEEM LEALKPDITM VAVSGFSGLR AVLASLEHSK RVCLANKESL VCGGFLVKKK LKEKGTELIP VDSEHSAIFQ VMEPEVEKVV LTASGGALRD WKISKIDRAR PEDVLKHPVW NMGARITVDS ATMVNKAFEV LEAMELFELP FEKIEVKIHR EGLVHGAVVL PDGNVKMVVS PPDMRIPISY ALFYPRRVAL EPFFLRTISL SFEDPDPEKY PAFFLLKEIK DSYALRTAFN AADEVAVEAF LKGRIRFGGI HRVIEKTLEE FQGYPQPRTL DDVERIHFEA IKKAERVTEW LSSTSY // ID DXS_THEMA Reviewed; 608 AA. AC Q9X291; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 117. DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315}; DE EC=2.2.1.7 {ECO:0000255|HAMAP-Rule:MF_00315}; DE AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315}; DE Short=DXP synthase {ECO:0000255|HAMAP-Rule:MF_00315}; DE Short=DXPS {ECO:0000255|HAMAP-Rule:MF_00315}; GN Name=dxs {ECO:0000255|HAMAP-Rule:MF_00315}; OrderedLocusNames=TM_1770; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the acyloin condensation reaction between C CC atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield CC 1-deoxy-D-xylulose-5-phosphate (DXP). {ECO:0000255|HAMAP- CC Rule:MF_00315}. CC -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1- CC deoxy-D-xylulose 5-phosphate + CO(2). {ECO:0000255|HAMAP- CC Rule:MF_00315}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00315}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00315}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00315}; CC Note=Binds 1 thiamine pyrophosphate per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00315}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose CC 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D- CC glyceraldehyde 3-phosphate and pyruvate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00315}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00315}. CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00315}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36833.1; -; Genomic_DNA. DR PIR; A72213; A72213. DR RefSeq; NP_229567.1; NC_000853.1. DR RefSeq; WP_004082316.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X291; -. DR STRING; 243274.TM1770; -. DR EnsemblBacteria; AAD36833; AAD36833; TM_1770. DR GeneID; 897852; -. DR KEGG; tma:TM1770; -. DR PATRIC; 23938520; VBITheMar51294_1789. DR eggNOG; ENOG4105C2V; Bacteria. DR eggNOG; COG1154; LUCA. DR InParanoid; Q9X291; -. DR KO; K01662; -. DR OMA; YKGLCGF; -. DR OrthoDB; EOG6BKJ6P; -. DR UniPathway; UPA00064; UER00091. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 3. DR HAMAP; MF_00315; DXP_synth; 1. DR InterPro; IPR005477; Dxylulose-5-P_synthase. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR InterPro; IPR033248; Transketolase_C. DR InterPro; IPR033247; Transketolase_fam. DR InterPro; IPR005474; Transketolase_N. DR PANTHER; PTHR11624; PTHR11624; 2. DR Pfam; PF13292; DXP_synthase_N; 1. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 3. DR SUPFAM; SSF52922; SSF52922; 1. DR TIGRFAMs; TIGR00204; dxs; 1. DR PROSITE; PS00801; TRANSKETOLASE_1; 1. PE 3: Inferred from homology; KW Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding; KW Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate; KW Transferase. FT CHAIN 1 608 1-deoxy-D-xylulose-5-phosphate synthase. FT /FTId=PRO_0000189164. FT REGION 107 109 Thiamine pyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT REGION 139 140 Thiamine pyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT METAL 138 138 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00315}. FT METAL 167 167 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00315}. FT BINDING 66 66 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT BINDING 167 167 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT BINDING 277 277 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT BINDING 350 350 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. SQ SEQUENCE 608 AA; 67397 MW; AA2F16E8FAFF25BC CRC64; MLLDEIKRMS YDELKRLAED IRKRITEVVL KNGGHLASNL GTIELTLALY RVFDPREDAI IWDTGHQAYT HKILTGRDDL FHTIRTFGGL SGFVTRRESP LDWFGTGHAG TSIAAGLGFE KAFELLGEKR HVVVVIGDGA LTSGMALEAL NQLKNLNSKM KIILNDNGMS ISPNVGGLAY HLSKLRTSPI YLKGKKVLKK VLEKTEIGFE VEEEMKYLRD SLKGMIQGTN FFESLGLKYF GPFDGHNIEL LEKVFKRIRD YDYSSVVHVV TKKGKGFTAA EENPTKYHSA SPSGKPKMLS YSELLGHTLS RVAREDKKIV AITAAMADGT GLSIFQKEHP DRFFDLGITE QTCVTFGAAL GLHGMKPVVA IYSTFLQRAY DQIIHDVALQ NAPVLFAIDR SGVVGEDGPT HHGLFDINYL LPVPNMKIIS PSSPEEFVNS LYTVLKHLDG PVAIRYPKES FYGEVESLLE NMKEIDLGWK ILKRGREAAI IATGTILNEV LKIPLDVTVV NALTVKPLDT AVLKEIARDH DLIITVEEAM KIGGFGSFVA QRLQEMGWQG KIVNLGVEDL FVPHGGRKEL LSMLGLDSEG LTKTVLTYIK ARSREGKV // ID EFG_THEMA Reviewed; 692 AA. AC P38525; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 17-FEB-2016, entry version 119. DE RecName: Full=Elongation factor G; DE Short=EF-G; GN Name=fusA; Synonyms=fus; OrderedLocusNames=TM_1503; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1920450; DOI=10.1007/BF02193628; RA Tiboni O., Cantoni R., Creti R., Cammarano P., Sanangelantoni A.M.; RT "Phylogenetic depth of Thermotoga maritima inferred from analysis of RT the fus gene: amino acid sequence of elongation factor G and RT organization of the Thermotoga str operon."; RL J. Mol. Evol. 33:142-151(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step CC during translation elongation. During this step, the ribosome CC changes from the pre-translocational (PRE) to the post- CC translocational (POST) state as the newly formed A-site-bound CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E CC sites, respectively. Catalyzes the coordinated movement of the two CC tRNA molecules, the mRNA and conformational changes in the CC ribosome (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-G/EF-2 CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB19927.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAD36570.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S57688; AAB19927.2; ALT_INIT; Genomic_DNA. DR EMBL; AE000512; AAD36570.1; ALT_INIT; Genomic_DNA. DR PIR; H72243; H72243. DR RefSeq; NP_229303.1; NC_000853.1. DR ProteinModelPortal; P38525; -. DR SMR; P38525; 7-690. DR STRING; 243274.TM1503; -. DR EnsemblBacteria; AAD36570; AAD36570; TM_1503. DR GeneID; 898734; -. DR KEGG; tma:TM1503; -. DR PATRIC; 23937964; VBITheMar51294_1520. DR eggNOG; ENOG4105CEJ; Bacteria. DR eggNOG; COG0480; LUCA. DR InParanoid; P38525; -. DR KO; K02355; -. DR OMA; KLGVAIQ; -. DR OrthoDB; EOG6X6RBF; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR004540; Transl_elong_EFG/EF2. DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF14492; EFG_II; 1. DR Pfam; PF03764; EFG_IV; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SMART; SM00889; EFG_IV; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR00484; EF-G; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; GTP-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 692 Elongation factor G. FT /FTId=PRO_0000091246. FT DOMAIN 9 283 tr-type G. FT NP_BIND 18 25 GTP. {ECO:0000250}. FT NP_BIND 82 86 GTP. {ECO:0000250}. FT NP_BIND 136 139 GTP. {ECO:0000250}. FT CONFLICT 105 105 A -> R (in Ref. 1; AAB19927). FT {ECO:0000305}. FT CONFLICT 234 234 E -> A (in Ref. 1; AAB19927). FT {ECO:0000305}. FT CONFLICT 369 369 V -> F (in Ref. 1; AAB19927). FT {ECO:0000305}. FT CONFLICT 390 391 CD -> WH (in Ref. 1; AAB19927). FT {ECO:0000305}. FT CONFLICT 448 448 T -> N (in Ref. 1; AAB19927). FT {ECO:0000305}. FT CONFLICT 527 539 Missing (in Ref. 1). {ECO:0000305}. SQ SEQUENCE 692 AA; 77846 MW; 02A4DCCD91547580 CRC64; MEARYVDLDK LRNIGIMAHI DAGKTTTTER ILYYTGRKHF IGDVDEGNTT TDWMPQEKER GITIQSAATT CFWKGYRINI IDTPGHVDFT AEVERALRVL DGAIAVFDAT AGVEPQSETV WRQADKYNVP RIAFMNKMDK VGADFYMAVE TLVTKLRANP IPVQMPIGSE KDFQGVIDLI KMKAIYWVSE DGSVYEERDI PEELREEAEM RREEMLEKIA ELDEEILEKY LEGEEISEEE IKRVLRKATI ENKAVPVLCG AAKANKGIQP LLDAVIDYLP SPLDLPPVKG WRVSDGEVVY RKPDENEPFT ALVFKVQVDP YIGKLVYFRV YSGRLEKGSY VYNSTKGQRE RISRIVFMHA DKREEVDYVR PGDIAAGVGL KVSQTGDTLC DEKEPIILEK IDFPEPVISL AVEPVTKADE EKLVKALLAL SEEDPTLQVR VDKETGETII SGMGELHLEI VVDRLKREFG VNVRVGQPQV AYRETIKKSA EAEGKYIRQT GGRGQYGHVI LRIEPIPEEE GKNFEFIDKT VGGVIPKEFM PAIEAGIKEA MMAGPLAGYP VVRVRAIVLD GSYHEVDSSE MAFKIAASMA FKEAMKKAQP VLLEPIMKLE ITTPEEYMGN IISDLNSRRA KVESLETRGH LKVIVAKVPL SETFGYATVL RSLSQGRASY IMQFSHYQEV PEKIAEKIIK VV // ID EFP_THEMA Reviewed; 185 AA. AC Q9X284; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 108. DE RecName: Full=Elongation factor P; DE Short=EF-P; GN Name=efp; OrderedLocusNames=TM_1763; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in peptide bond synthesis. Stimulates efficient CC translation and peptide-bond synthesis on native or reconstituted CC 70S ribosomes in vitro. Probably functions indirectly by altering CC the affinity of the ribosome for aminoacyl-tRNA, thus increasing CC their reactivity as acceptors for peptidyl transferase (By CC similarity). {ECO:0000250}. CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the elongation factor P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36827.1; -; Genomic_DNA. DR PIR; B72212; B72212. DR RefSeq; NP_229560.1; NC_000853.1. DR RefSeq; WP_004082309.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X284; -. DR STRING; 243274.TM1763; -. DR EnsemblBacteria; AAD36827; AAD36827; TM_1763. DR GeneID; 897856; -. DR KEGG; tma:TM1763; -. DR PATRIC; 23938506; VBITheMar51294_1782. DR eggNOG; ENOG4105DRH; Bacteria. DR eggNOG; COG0231; LUCA. DR InParanoid; Q9X284; -. DR KO; K02356; -. DR OMA; MTEDGSY; -. DR OrthoDB; EOG6JQH6Q; -. DR UniPathway; UPA00345; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.140; -; 2. DR HAMAP; MF_00141; EF_P; 1. DR InterPro; IPR015365; Elong-fact-P_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR020599; Transl_elong_fac_P/YeiP. DR InterPro; IPR013185; Transl_elong_KOW-like. DR InterPro; IPR001059; Transl_elong_P/YeiP_cen. DR InterPro; IPR013852; Transl_elong_P/YeiP_CS. DR InterPro; IPR011768; Transl_elongation_fac_P. DR InterPro; IPR008991; Translation_prot_SH3-like. DR Pfam; PF01132; EFP; 1. DR Pfam; PF08207; EFP_N; 1. DR Pfam; PF09285; Elong-fact-P_C; 1. DR PIRSF; PIRSF005901; EF-P; 1. DR SMART; SM01185; EFP; 1. DR SMART; SM00841; Elong-fact-P_C; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR SUPFAM; SSF50249; SSF50249; 2. DR TIGRFAMs; TIGR00038; efp; 1. DR PROSITE; PS01275; EFP; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 185 Elongation factor P. FT /FTId=PRO_0000094355. SQ SEQUENCE 185 AA; 20875 MW; A18A98DF3597A68E CRC64; MIEVGDLKKG MFIIYDGEIY RVLEASKHFM GRGSGLIRTK LKNVKTGFVR EVNFPSGEKV QEAELSFRKA QYLYRDGDHY YFMTLDDYEQ YALSEEEIGD AKYYLVENME VDLVFHEGTP IGIELPTTVE LTVVETEPSF KGDTVSGGGK PAVLETGLKI TVPYFIEVGD KIKVDTRTGE YVGRA // ID DYR_THEMA Reviewed; 169 AA. AC Q60034; P96109; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 124. DE RecName: Full=Dihydrofolate reductase; DE Short=DHFR; DE EC=1.5.1.3; GN Name=folA; Synonyms=dyrA; OrderedLocusNames=TM_1641; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7789791; DOI=10.1016/0378-1119(95)00090-S; RA van de Casteele M., Legrain C., Wilquet V., Glansdorff N.; RT "The dihydrofolate reductase-encoding gene dyrA of the RT hyperthermophilic bacterium Thermotoga maritima."; RL Gene 158:101-105(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9563834; RA Dams T., Schurig H., Jaenicke R.; RT "Homo-dimeric recombinant dihydrofolate reductase from Thermotoga RT maritima shows extreme intrinsic stability."; RL Biol. Chem. 379:367-371(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH METHOTREXATE AND RP NADPH. RX PubMed=10731419; DOI=10.1006/jmbi.2000.3570; RA Dams T., Auerbach G., Bader G., Jacob U., Ploom T., Huber R., RA Jaenicke R.; RT "The crystal structure of dihydrofolate reductase from Thermotoga RT maritima: molecular features of thermostability."; RL J. Mol. Biol. 297:659-672(2000). CC -!- FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential CC reaction for de novo glycine and purine synthesis, and for DNA CC precursor synthesis (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8- CC dihydrofolate + NADPH. {ECO:0000255|PROSITE-ProRule:PRU00660}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Highly thermostable.; CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; CC 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10731419}. CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00660}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD36708.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X81845; CAA57437.1; -; Genomic_DNA. DR EMBL; Y11021; CAA71903.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36708.1; ALT_INIT; Genomic_DNA. DR PIR; A72231; A72231. DR RefSeq; NP_229441.1; NC_000853.1. DR RefSeq; WP_004082129.1; NZ_CP011107.1. DR PDB; 1CZ3; X-ray; 2.10 A; A/B=2-169. DR PDB; 1D1G; X-ray; 2.10 A; A/B=2-169. DR PDBsum; 1CZ3; -. DR PDBsum; 1D1G; -. DR ProteinModelPortal; Q60034; -. DR SMR; Q60034; 2-169. DR STRING; 243274.TM1641; -. DR EnsemblBacteria; AAD36708; AAD36708; TM_1641. DR GeneID; 896828; -. DR KEGG; tma:TM1641; -. DR PATRIC; 23938256; VBITheMar51294_1660. DR eggNOG; ENOG41084X0; Bacteria. DR eggNOG; COG0262; LUCA. DR InParanoid; Q60034; -. DR KO; K00287; -. DR OMA; KGYERVA; -. DR OrthoDB; EOG6KT2V2; -. DR BioCyc; MetaCyc:MONOMER-461; -. DR BioCyc; TMAR243274:GC6P-1687-MONOMER; -. DR UniPathway; UPA00077; UER00158. DR EvolutionaryTrace; Q60034; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.430.10; -; 1. DR InterPro; IPR012259; DHFR. DR InterPro; IPR024072; DHFR-like_dom. DR InterPro; IPR001796; DHFR_dom. DR Pfam; PF00186; DHFR_1; 1. DR PRINTS; PR00070; DHFR. DR SUPFAM; SSF53597; SSF53597; 1. DR PROSITE; PS51330; DHFR_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; NADP; One-carbon metabolism; KW Oxidoreductase; Reference proteome. FT CHAIN 1 169 Dihydrofolate reductase. FT /FTId=PRO_0000186418. FT DOMAIN 3 169 DHFR. {ECO:0000255|PROSITE- FT ProRule:PRU00660}. FT NP_BIND 46 51 NADP. {ECO:0000269|PubMed:10731419}. FT NP_BIND 65 67 NADP. {ECO:0000269|PubMed:10731419}. FT NP_BIND 103 105 NADP. {ECO:0000269|PubMed:10731419}. FT REGION 7 8 Substrate binding. FT {ECO:0000305|PubMed:10731419}. FT REGION 28 30 Substrate binding. FT {ECO:0000305|PubMed:10731419}. FT BINDING 9 9 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000269|PubMed:10731419}. FT BINDING 16 16 NADP; via carbonyl oxygen. FT {ECO:0000269|PubMed:10731419}. FT BINDING 54 54 Substrate. {ECO:0000305|PubMed:10731419}. FT BINDING 59 59 Substrate. {ECO:0000305|PubMed:10731419}. FT BINDING 81 81 NADP; via carbonyl oxygen. FT {ECO:0000269|PubMed:10731419}. FT BINDING 101 101 Substrate; via carbonyl oxygen. FT {ECO:0000305|PubMed:10731419}. FT CONFLICT 68 81 PKTSNNPSLVFFNG -> TQNFQQSFTRFFQR (in Ref. FT 1). {ECO:0000305}. FT CONFLICT 108 108 T -> S (in Ref. 1). {ECO:0000305}. FT CONFLICT 138 139 FE -> LQ (in Ref. 1). {ECO:0000305}. FT STRAND 3 10 {ECO:0000244|PDB:1CZ3}. FT STRAND 15 17 {ECO:0000244|PDB:1CZ3}. FT HELIX 26 39 {ECO:0000244|PDB:1CZ3}. FT STRAND 41 45 {ECO:0000244|PDB:1CZ3}. FT HELIX 46 52 {ECO:0000244|PDB:1CZ3}. FT STRAND 59 64 {ECO:0000244|PDB:1CZ3}. FT STRAND 76 79 {ECO:0000244|PDB:1CZ3}. FT HELIX 83 92 {ECO:0000244|PDB:1CZ3}. FT STRAND 96 102 {ECO:0000244|PDB:1CZ3}. FT HELIX 104 112 {ECO:0000244|PDB:1CZ3}. FT STRAND 117 123 {ECO:0000244|PDB:1CZ3}. FT STRAND 125 130 {ECO:0000244|PDB:1CZ3}. FT STRAND 132 135 {ECO:0000244|PDB:1CZ3}. FT STRAND 141 151 {ECO:0000244|PDB:1CZ3}. FT STRAND 153 155 {ECO:0000244|PDB:1CZ3}. FT STRAND 158 164 {ECO:0000244|PDB:1CZ3}. SQ SEQUENCE 169 AA; 19367 MW; F5DA22C978E2C39D CRC64; MAKVIFVLAM DVSGKIASSV ESWSSFEDRK NFRKITTEIG NVVMGRITFE EIGRPLPERL NVVLTRRPKT SNNPSLVFFN GSPADVVKFL EGKGYERVAV IGGKTVFTEF LREKLVDELF VTVEPYVFGK GIPFFDEFEG YFPLKLLEMR RLNERGTLFL KYSVEKSHR // ID EFGL_THEMA Reviewed; 683 AA. AC Q9X1Y4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 110. DE RecName: Full=Elongation factor G-like protein; GN OrderedLocusNames=TM_1651; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-G/EF-2 CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01059}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36718.1; -; Genomic_DNA. DR PIR; H72227; H72227. DR RefSeq; NP_229451.1; NC_000853.1. DR RefSeq; WP_004082156.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1Y4; -. DR STRING; 243274.TM1651; -. DR EnsemblBacteria; AAD36718; AAD36718; TM_1651. DR GeneID; 897135; -. DR KEGG; tma:TM1651; -. DR PATRIC; 23938276; VBITheMar51294_1670. DR eggNOG; ENOG4105CEJ; Bacteria. DR eggNOG; COG0480; LUCA. DR InParanoid; Q9X1Y4; -. DR KO; K02355; -. DR OMA; HKHKKQT; -. DR OrthoDB; EOG644ZKM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR004540; Transl_elong_EFG/EF2. DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF14492; EFG_II; 1. DR Pfam; PF03764; EFG_IV; 1. DR SMART; SM00838; EFG_C; 1. DR SMART; SM00889; EFG_IV; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR00484; EF-G; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 683 Elongation factor G-like protein. FT /FTId=PRO_0000091278. FT DOMAIN 5 267 tr-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT NP_BIND 14 21 GTP. {ECO:0000250}. FT NP_BIND 73 77 GTP. {ECO:0000250}. FT NP_BIND 127 130 GTP. {ECO:0000250}. SQ SEQUENCE 683 AA; 75903 MW; E9408FF5A2C6A63C CRC64; MGGLQNVRSA ALIGHNGSGK SLLLAQILYK SGLIDKADTK YVDYDPVEEE KGASFSSHVA SLEWKGKKVY LIDTPGFSDF ISEVINGIFV SENIISVVNA VAGVEIQTER TWNMADEMKK PIIVFVNQMD KERANFENVV AELKERFSRK IVPVVVPIGA AENFEGVVDL LKKKAYRYDG DKVQEEDMPE SFNDMRSEIL EDIVEQDEEL MMRYLDGEDI GYDELMRVLK EGYKKGEIVP VLSGSALKGI GLDLLLDYLG DIGVSPEEAP SYKALLEDGT EIEVKFSEEE PFCAYIFKSV VDQFVGRITF AKVIAGVLRP GDTVVNVQKD VTEKVGHVYV PILKQQKEVE SAGPGEIVVL LKLKEGAVGE TLAHRDRRVK IVPPAFPEPM FSRSVHPKSK SDIDKISSGL SRLSDSDPTF VWEYDPETGE TVVSGLGAMH LDVMIERLKK IFGVDVEVGK PKIAYRETIT TTAVAEHKHK KQTGGHGQYG HVKIQLEPLP RGQGYEFVDK IVGGVIPRNF IPSVDKGIRE AMKKGVLAGY PVTDVRVILF DGSYHEVDSS DISFQIAAIQ AFKKGMEAAK PVILEPIMEV EVFVPEENAG DVMGEISSRR GRPLGMEPSG KGMVKVKAEV PLAEMLDFSS KLSSITSGRG YFTMRFQRYE IVPPNIQEKI IEERRREMQE QEK // ID EFTU_THEMA Reviewed; 400 AA. AC P13537; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 133. DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=TM_1502; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=2714630; DOI=10.1016/0378-1097(89)90157-2; RA Bachleitner M., Ludwig W., Stetter K.O., Schleifer K.H.; RT "Nucleotide sequence of the gene coding for the elongation factor Tu RT from the extremely thermophilic eubacterium Thermotoga maritima."; RL FEMS Microbiol. Lett. 48:115-120(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1920450; DOI=10.1007/BF02193628; RA Tiboni O., Cantoni R., Creti R., Cammarano P., Sanangelantoni A.M.; RT "Phylogenetic depth of Thermotoga maritima inferred from analysis of RT the fus gene: amino acid sequence of elongation factor G and RT organization of the Thermotoga str operon."; RL J. Mol. Evol. 33:142-151(1991). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M27479; AAA27415.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36569.1; -; Genomic_DNA. DR EMBL; S57688; AAB19929.1; -; Genomic_DNA. DR PIR; G72243; G72243. DR RefSeq; NP_229302.1; NC_000853.1. DR RefSeq; WP_004081839.1; NZ_CP011107.1. DR ProteinModelPortal; P13537; -. DR SMR; P13537; 2-400. DR STRING; 243274.TM1502; -. DR PRIDE; P13537; -. DR EnsemblBacteria; AAD36569; AAD36569; TM_1502. DR GeneID; 897995; -. DR KEGG; tma:TM1502; -. DR PATRIC; 23937962; VBITheMar51294_1519. DR eggNOG; ENOG4105CGV; Bacteria. DR eggNOG; COG0050; LUCA. DR InParanoid; P13537; -. DR KO; K02358; -. DR OMA; GMVICKP; -. DR OrthoDB; EOG6R5C6X; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central. DR GO; GO:0006414; P:translational elongation; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00118_B; EF_Tu_B; 1. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF50465; SSF50465; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00485; EF-Tu; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; GTP-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 400 Elongation factor Tu. FT /FTId=PRO_0000091421. FT DOMAIN 10 208 tr-type G. FT NP_BIND 19 26 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT NP_BIND 81 85 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT NP_BIND 136 139 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT REGION 19 26 G1. {ECO:0000250}. FT REGION 60 64 G2. {ECO:0000250}. FT REGION 81 84 G3. {ECO:0000250}. FT REGION 136 139 G4. {ECO:0000250}. FT REGION 174 176 G5. {ECO:0000250}. FT CONFLICT 40 40 G -> V (in Ref. 1; AAA27415). FT {ECO:0000305}. SQ SEQUENCE 400 AA; 44467 MW; 73F479FE4F69E9A5 CRC64; MAKEKFVRTK PHVNVGTIGH IDHGKSTLTA AITKYLSLKG LAQYIPYDQI DKAPEEKARG ITINITHVEY ETEKRHYAHI DCPGHADYIK NMITGAAQMD GAILVVAATD GPMPQTREHV LLARQVEVPY MIVFINKTDM VDDPELIDLV EMEVRDLLSQ YGYPGDEVPV IRGSALKAVE APNDPNHEAY KPIQELLDAM DNYIPDPQRD VDKPFLMPIE DVFSITGRGT VVTGRIERGR IRPGDEVEII GLSYEIKKTV VTSVEMFRKE LDEGIAGDNV GCLLRGIDKD EVERGQVLAA PGSIKPHKRF KAQIYVLKKE EGGRHTPFTK GYKPQFYIRT ADVTGEIVGL PEGVEMVMPG DHVEMEIELI YPVAIEKGQR FAVREGGRTV GAGVVTEVIE // ID ECFA1_THEMA Reviewed; 259 AA. AC Q9X1Z1; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA1 {ECO:0000255|HAMAP-Rule:MF_01710}; DE Short=ECF transporter A component EcfA1 {ECO:0000255|HAMAP-Rule:MF_01710}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01710}; GN Name=ecfA1 {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO, ecfA'; GN OrderedLocusNames=TM_1663; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION, RP EXPRESSION IN E.COLI, ATP-BINDING, AND X-RAY CRYSTALLOGRAPHY (2.7 RP ANGSTROMS) OF 5-259 IN COMPLEX WITH ADP. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23359690; DOI=10.1073/pnas.1217361110; RA Karpowich N.K., Wang D.N.; RT "Assembly and mechanism of a group II ECF transporter."; RL Proc. Natl. Acad. Sci. U.S.A. 110:2534-2539(2013). CC -!- FUNCTION: ATP-binding (A) component of a common energy-coupling CC factor (ECF) ABC-transporter complex. Unlike classic ABC CC transporters this ECF transporter provides the energy necessary to CC transport a number of different substrates (Probable). Expression CC of the complex plus RibU in E.coli allows riboflavin uptake; CC uptake does not occur in the absence of RibU or the EcfA1A2T CC complex. {ECO:0000255|HAMAP-Rule:MF_01710, CC ECO:0000269|PubMed:23359690, ECO:0000305}. CC -!- SUBUNIT: Forms a heterodimer with EcfA2. Forms a stable energy- CC coupling factor (ECF) transporter complex composed of 2 membrane- CC embedded substrate-binding proteins (S component, RibU, BioY), 2 CC ATP-binding proteins (A component) and 2 transmembrane proteins (T CC component) upon coexpression in E.coli. Stable subcomplexes with CC both A plus T components can also be isolated. This complex CC interacts with at least 2 substrate-specific components, BioY and CC RibU. {ECO:0000269|PubMed:23359690}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000305|PubMed:23359690}; Peripheral membrane protein CC {ECO:0000305|PubMed:23359690}. CC -!- MISCELLANEOUS: Structure 4HLU is probably in the open state. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Energy- CC coupling factor EcfA family. {ECO:0000255|HAMAP-Rule:MF_01710}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36730.1; -; Genomic_DNA. DR PIR; E72224; E72224. DR RefSeq; NP_229463.1; NC_000853.1. DR RefSeq; WP_004082181.1; NZ_CP011107.1. DR PDB; 4HLU; X-ray; 2.70 A; C/D=2-259. DR PDB; 4ZIR; X-ray; 3.00 A; B=2-259. DR PDBsum; 4HLU; -. DR PDBsum; 4ZIR; -. DR ProteinModelPortal; Q9X1Z1; -. DR DIP; DIP-61611N; -. DR STRING; 243274.TM1663; -. DR TCDB; 3.A.1.25.5; the atp-binding cassette (abc) superfamily. DR DNASU; 897908; -. DR EnsemblBacteria; AAD36730; AAD36730; TM_1663. DR GeneID; 897908; -. DR KEGG; tma:TM1663; -. DR PATRIC; 23938300; VBITheMar51294_1682. DR eggNOG; ENOG4108JJB; Bacteria. DR eggNOG; COG1122; LUCA. DR InParanoid; Q9X1Z1; -. DR KO; K16786; -. DR OMA; QMDHVVA; -. DR OrthoDB; EOG6T7N3V; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0032217; F:riboflavin transporter activity; IGI:UniProtKB. DR GO; GO:0032218; P:riboflavin transport; IGI:UniProtKB. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51246; CBIO; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; KW Complete proteome; Hydrolase; Membrane; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 259 Energy-coupling factor transporter ATP- FT binding protein EcfA1. FT /FTId=PRO_0000092116. FT DOMAIN 3 230 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01710}. FT NP_BIND 38 43 ATP. FT ACT_SITE 157 157 Proton acceptor. {ECO:0000255}. FT STRAND 2 7 {ECO:0000244|PDB:4HLU}. FT STRAND 9 18 {ECO:0000244|PDB:4HLU}. FT STRAND 30 34 {ECO:0000244|PDB:4HLU}. FT HELIX 41 49 {ECO:0000244|PDB:4HLU}. FT STRAND 55 60 {ECO:0000244|PDB:4ZIR}. FT HELIX 67 73 {ECO:0000244|PDB:4HLU}. FT STRAND 74 77 {ECO:0000244|PDB:4HLU}. FT STRAND 79 81 {ECO:0000244|PDB:4HLU}. FT TURN 82 84 {ECO:0000244|PDB:4HLU}. FT STRAND 87 89 {ECO:0000244|PDB:4ZIR}. FT HELIX 90 95 {ECO:0000244|PDB:4HLU}. FT STRAND 98 101 {ECO:0000244|PDB:4HLU}. FT HELIX 108 118 {ECO:0000244|PDB:4HLU}. FT HELIX 129 131 {ECO:0000244|PDB:4HLU}. FT HELIX 134 146 {ECO:0000244|PDB:4HLU}. FT STRAND 151 157 {ECO:0000244|PDB:4HLU}. FT TURN 158 161 {ECO:0000244|PDB:4HLU}. FT HELIX 164 178 {ECO:0000244|PDB:4HLU}. FT TURN 179 181 {ECO:0000244|PDB:4HLU}. FT STRAND 183 187 {ECO:0000244|PDB:4HLU}. FT HELIX 191 193 {ECO:0000244|PDB:4HLU}. FT STRAND 199 204 {ECO:0000244|PDB:4HLU}. FT STRAND 207 212 {ECO:0000244|PDB:4HLU}. FT HELIX 214 220 {ECO:0000244|PDB:4HLU}. FT STRAND 223 225 {ECO:0000244|PDB:4HLU}. FT HELIX 229 237 {ECO:0000244|PDB:4HLU}. FT HELIX 242 246 {ECO:0000244|PDB:4ZIR}. SQ SEQUENCE 259 AA; 29376 MW; 80B492FFF04A2C6A CRC64; MKITLNSVSF RYNGDYVLKD VNAEFETGKI YVVVGKNGSG KTTLLKILAG LLEAEGEIFL DGSPADPFLL RKNVGYVFQN PSSQIIGATV EEDVAFSLEI MGLDESEMRK RIKKVLELVG LSGLEKEDPL NLSGGQKQRL AIASMLARDT RFLALDEPVS MLDPPSQREI FQVLESLKNE GKGIILVTHE LEYLDDMDFI LHISNGTIDF CGSWEEFVER EFDDVEIPFK WKLWKKCGKI NLWEDRYENS GNQRRRDTV // ID ECFT_THEMA Reviewed; 271 AA. AC Q9X2I1; G4FGR0; DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=Energy-coupling factor transporter transmembrane protein EcfT; DE Short=ECF transporter T component EcfT; GN Name=ecfT; OrderedLocusNames=TM_1868; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION, AND RP EXPRESSION IN E.COLI. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23359690; DOI=10.1073/pnas.1217361110; RA Karpowich N.K., Wang D.N.; RT "Assembly and mechanism of a group II ECF transporter."; RL Proc. Natl. Acad. Sci. U.S.A. 110:2534-2539(2013). CC -!- FUNCTION: Transmembrane (T) component of an energy-coupling factor CC (ECF) ABC-transporter complex. Unlike classic ABC transporters CC this ECF transporter provides the energy necessary to transport a CC number of different substrates (Probable). Expression of the CC complex plus RibU in E.coli allows riboflavin uptake; uptake does CC not occur in the absence of RibU or the EcfA1A2T complex. CC {ECO:0000269|PubMed:23359690, ECO:0000305}. CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter CC complex composed of 2 membrane-embedded substrate-binding proteins CC (S component, RibU, BioY), 2 ATP-binding proteins (A component) CC and 2 transmembrane proteins (T component) upon coexpression in CC E.coli. A stable subcomplex with both A and T components are also CC isolated. This complex interacts with at least 2 substrate- CC specific components, BioY and RibU. {ECO:0000269|PubMed:23359690}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000305|PubMed:23359690}; Multi-pass membrane protein CC {ECO:0000305|PubMed:23359690}. CC -!- SIMILARITY: Belongs to the energy-coupling factor EcfT family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36930.1; -; Genomic_DNA. DR PIR; E72202; E72202. DR RefSeq; NP_229664.1; NC_000853.1. DR RefSeq; WP_004082419.1; NZ_CP011107.1. DR STRING; 243274.TM1868; -. DR TCDB; 3.A.1.25.5; the atp-binding cassette (abc) superfamily. DR DNASU; 897358; -. DR EnsemblBacteria; AAD36930; AAD36930; TM_1868. DR GeneID; 897358; -. DR KEGG; tma:TM1868; -. DR PATRIC; 23938725; VBITheMar51294_1889. DR eggNOG; ENOG4105EK6; Bacteria. DR eggNOG; COG0619; LUCA. DR InParanoid; Q9X2I1; -. DR KO; K16785; -. DR OMA; GLKPIIW; -. DR OrthoDB; EOG6ZSP8P; -. DR BioCyc; TMAR243274:GC6P-1919-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032217; F:riboflavin transporter activity; IGI:UniProtKB. DR GO; GO:0032218; P:riboflavin transport; IGI:UniProtKB. DR InterPro; IPR003339; ABC/ECF_trnsptr_transmembrane. DR Pfam; PF02361; CbiQ; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 271 Energy-coupling factor transporter FT transmembrane protein EcfT. FT /FTId=PRO_0000422260. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 104 124 Helical. {ECO:0000255}. FT TRANSMEM 149 169 Helical. {ECO:0000255}. FT TRANSMEM 197 217 Helical. {ECO:0000255}. FT TRANSMEM 243 263 Helical. {ECO:0000255}. SQ SEQUENCE 271 AA; 30641 MW; 9C782BE2FD0BF2AB CRC64; MRLPTVLIGR YIPVDSIVHR LDPRAKLLGM IFLISAVLIV PNLLFYLVPG LAIFLLMFLS RTGFKIYLAG LRSLWFFLVF AVLVQFFSSS EGEKIFWMIT DRAIWSAVYI MLRLVLIILL AENFSATTPP LLSARAIESI FSTFGARKIG HEIGMVMTIA MRFVPVLALE ADRILKAQIA RGANFERGKF FDRIRALVVI IVPLLISALR KAEELAVAME ARLYTGEPPK TRFKDIKWKP MDTLYVLLTA GVLVLVLFGR YFVDGVFQYG S // ID END4_THEMA Reviewed; 287 AA. AC Q9WYJ7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=Probable endonuclease 4 {ECO:0000255|HAMAP-Rule:MF_00152}; DE EC=3.1.21.2 {ECO:0000255|HAMAP-Rule:MF_00152}; DE AltName: Full=Endodeoxyribonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152}; DE AltName: Full=Endonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152}; GN Name=nfo {ECO:0000255|HAMAP-Rule:MF_00152}; OrderedLocusNames=TM_0362; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves CC phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) CC to produce new 5'-ends that are base-free deoxyribose 5-phosphate CC residues. It preferentially attacks modified AP sites created by CC bleomycin and neocarzinostatin. {ECO:0000255|HAMAP-Rule:MF_00152}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphooligonucleotide end-products. {ECO:0000255|HAMAP- CC Rule:MF_00152}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00152}; CC Note=Binds 3 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_00152}; CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family. CC {ECO:0000255|HAMAP-Rule:MF_00152}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35449.1; -; Genomic_DNA. DR PIR; B72387; B72387. DR RefSeq; NP_228173.1; NC_000853.1. DR RefSeq; WP_010865102.1; NZ_CP011107.1. DR PDB; 2X7V; X-ray; 2.30 A; A=1-287. DR PDB; 2X7W; X-ray; 2.36 A; A=1-287. DR PDB; 4HNO; X-ray; 0.92 A; A=2-285. DR PDBsum; 2X7V; -. DR PDBsum; 2X7W; -. DR PDBsum; 4HNO; -. DR ProteinModelPortal; Q9WYJ7; -. DR STRING; 243274.TM0362; -. DR EnsemblBacteria; AAD35449; AAD35449; TM_0362. DR GeneID; 897321; -. DR KEGG; tma:TM0362; -. DR PATRIC; 23935605; VBITheMar51294_0367. DR eggNOG; ENOG4105EFU; Bacteria. DR eggNOG; COG0648; LUCA. DR InParanoid; Q9WYJ7; -. DR KO; K01151; -. DR OMA; MKYVGAH; -. DR OrthoDB; EOG6Z0QCM; -. DR BioCyc; TMAR243274:GC6P-376-MONOMER; -. DR BRENDA; 3.1.21.2; 6331. DR EvolutionaryTrace; Q9WYJ7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IBA:GO_Central. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central. DR Gene3D; 3.20.20.150; -; 1. DR HAMAP; MF_00152; Nfo; 1. DR InterPro; IPR001719; AP_endonuc_2. DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR PANTHER; PTHR21445; PTHR21445; 1. DR Pfam; PF01261; AP_endonuc_2; 1. DR SMART; SM00518; AP2Ec; 1. DR SUPFAM; SSF51658; SSF51658; 1. DR TIGRFAMs; TIGR00587; nfo; 1. DR PROSITE; PS00729; AP_NUCLEASE_F2_1; 1. DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 1. DR PROSITE; PS00731; AP_NUCLEASE_F2_3; 1. DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA damage; DNA repair; Endonuclease; KW Hydrolase; Metal-binding; Nuclease; Reference proteome; Zinc. FT CHAIN 1 287 Probable endonuclease 4. FT /FTId=PRO_0000190880. FT METAL 69 69 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 109 109 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 144 144 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 144 144 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 178 178 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 181 181 Zinc 3. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 215 215 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 228 228 Zinc 3. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 230 230 Zinc 3. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT METAL 260 260 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00152}. FT STRAND 4 7 {ECO:0000244|PDB:4HNO}. FT HELIX 14 16 {ECO:0000244|PDB:4HNO}. FT HELIX 17 23 {ECO:0000244|PDB:4HNO}. FT STRAND 27 31 {ECO:0000244|PDB:4HNO}. FT STRAND 37 39 {ECO:0000244|PDB:4HNO}. FT HELIX 46 58 {ECO:0000244|PDB:4HNO}. FT HELIX 63 65 {ECO:0000244|PDB:4HNO}. FT STRAND 66 69 {ECO:0000244|PDB:4HNO}. FT HELIX 81 101 {ECO:0000244|PDB:4HNO}. FT STRAND 105 108 {ECO:0000244|PDB:4HNO}. FT HELIX 118 133 {ECO:0000244|PDB:4HNO}. FT STRAND 140 144 {ECO:0000244|PDB:4HNO}. FT HELIX 157 166 {ECO:0000244|PDB:4HNO}. FT HELIX 170 172 {ECO:0000244|PDB:4HNO}. FT STRAND 173 178 {ECO:0000244|PDB:4HNO}. FT HELIX 179 184 {ECO:0000244|PDB:4HNO}. FT HELIX 192 205 {ECO:0000244|PDB:4HNO}. FT HELIX 208 210 {ECO:0000244|PDB:4HNO}. FT STRAND 211 216 {ECO:0000244|PDB:4HNO}. FT STRAND 218 221 {ECO:0000244|PDB:4HNO}. FT STRAND 235 238 {ECO:0000244|PDB:4HNO}. FT HELIX 239 247 {ECO:0000244|PDB:4HNO}. FT HELIX 250 253 {ECO:0000244|PDB:4HNO}. FT STRAND 257 259 {ECO:0000244|PDB:4HNO}. FT HELIX 265 281 {ECO:0000244|PDB:4HNO}. SQ SEQUENCE 287 AA; 32435 MW; A2BEE00CE7AE4A5A CRC64; MIKIGAHMPI SKGFDRVPQD TVNIGGNSFQ IFPHNARSWS AKLPSDEAAT KFKREMKKHG IDWENAFCHS GYLINLASPK DDIWQKSVEL LKKEVEICRK LGIRYLNIHP GSHLGTGEEE GIDRIVRGLN EVLNNTEGVV ILLENVSQKG GNIGYKLEQL KKIRDLVDQR DRVAITYDTC HGFDSGYDIT KKEGVEALLN EIESLFGLER LKMIHLNDSK YPLGAAKDRH ERIGSGFIGE EGFAVFFSFK EIQEVPWILE TPGGNEEHAE DIKKVFEIIE KFGIEVD // ID ENGB_THEMA Reviewed; 195 AA. AC Q9X1H7; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 104. DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321}; GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; GN OrderedLocusNames=TM_1466; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Necessary for normal cell division and for the CC maintenance of normal septation. {ECO:0000255|HAMAP- CC Rule:MF_00321}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00321}; CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. EngB GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00321}. CC -!- SIMILARITY: Contains 1 EngB-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|HAMAP-Rule:MF_00321}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36534.1; -; Genomic_DNA. DR PIR; C72252; C72252. DR RefSeq; NP_229266.1; NC_000853.1. DR RefSeq; WP_004081764.1; NZ_CP011107.1. DR PDB; 3PQC; X-ray; 1.90 A; A/B=1-195. DR PDB; 3PR1; X-ray; 2.30 A; A=1-195. DR PDBsum; 3PQC; -. DR PDBsum; 3PR1; -. DR ProteinModelPortal; Q9X1H7; -. DR STRING; 243274.TM1466; -. DR EnsemblBacteria; AAD36534; AAD36534; TM_1466. DR GeneID; 897720; -. DR KEGG; tma:TM1466; -. DR PATRIC; 23937886; VBITheMar51294_1481. DR eggNOG; ENOG4105WHM; Bacteria. DR eggNOG; COG0218; LUCA. DR InParanoid; Q9X1H7; -. DR KO; K03978; -. DR OMA; SQLFQCP; -. DR OrthoDB; EOG6ND0NG; -. DR EvolutionaryTrace; Q9X1H7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00321; GTPase_EngB; 1. DR InterPro; IPR030393; G_ENGB_dom. DR InterPro; IPR019987; GTP-bd_ribosome_bio_YsxC. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03598; GTPase_YsxC; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51706; G_ENGB; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Complete proteome; KW GTP-binding; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome; Septation. FT CHAIN 1 195 Probable GTP-binding protein EngB. FT /FTId=PRO_0000157794. FT DOMAIN 22 194 EngB-type G. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT NP_BIND 30 37 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 56 60 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 74 77 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 141 144 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 173 175 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT METAL 37 37 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT METAL 58 58 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT STRAND 6 12 {ECO:0000244|PDB:3PQC}. FT HELIX 15 17 {ECO:0000244|PDB:3PR1}. FT STRAND 25 31 {ECO:0000244|PDB:3PQC}. FT HELIX 36 44 {ECO:0000244|PDB:3PQC}. FT STRAND 61 66 {ECO:0000244|PDB:3PQC}. FT TURN 67 69 {ECO:0000244|PDB:3PQC}. FT STRAND 70 74 {ECO:0000244|PDB:3PQC}. FT STRAND 78 81 {ECO:0000244|PDB:3PQC}. FT HELIX 85 101 {ECO:0000244|PDB:3PQC}. FT STRAND 105 113 {ECO:0000244|PDB:3PQC}. FT HELIX 120 131 {ECO:0000244|PDB:3PQC}. FT STRAND 136 141 {ECO:0000244|PDB:3PQC}. FT HELIX 143 145 {ECO:0000244|PDB:3PQC}. FT HELIX 148 150 {ECO:0000244|PDB:3PQC}. FT HELIX 151 163 {ECO:0000244|PDB:3PQC}. FT STRAND 170 172 {ECO:0000244|PDB:3PQC}. FT TURN 175 177 {ECO:0000244|PDB:3PQC}. FT HELIX 181 192 {ECO:0000244|PDB:3PQC}. SQ SEQUENCE 195 AA; 22454 MW; D37A2E1262902FE4 CRC64; MIIRDVELVK VARTPGDYPP PLKGEVAFVG RSNVGKSSLL NALFNRKIAF VSKTPGKTRS INFYLVNSKY YFVDLPGYGY AKVSKKERML WKRLVEDYFK NRWSLQMVFL LVDGRIPPQD SDLMMVEWMK SLNIPFTIVL TKMDKVKMSE RAKKLEEHRK VFSKYGEYTI IPTSSVTGEG ISELLDLIST LLKEN // ID ENO_THEMA Reviewed; 429 AA. AC P42848; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 122. DE RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318}; DE EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318}; GN Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=TM_0877; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF 1-24, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP ENZYME REGULATION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=7757011; DOI=10.1002/pro.5560040209; RA Schurig H., Rutkat K., Rachel R., Jaenicke R.; RT "Octameric enolase from the hyperthermophilic bacterium Thermotoga RT maritima: purification, characterization, and image processing."; RL Protein Sci. 4:228-236(1995). CC -!- FUNCTION: Catalyzes the reversible conversion of 2- CC phosphoglycerate into phosphoenolpyruvate. It is essential for the CC degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP- CC Rule:MF_00318, ECO:0000269|PubMed:7757011}. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + CC H(2)O. {ECO:0000255|HAMAP-Rule:MF_00318, CC ECO:0000269|PubMed:7757011}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00318, CC ECO:0000269|PubMed:7757011}; CC -!- ENZYME REGULATION: The covalent binding to the substrate causes CC inactivation of the enzyme, and possibly serves as a signal for CC the export of the protein (By similarity). Inhibited by fluoride CC and phosphate. {ECO:0000255|HAMAP-Rule:MF_00318, CC ECO:0000269|PubMed:7757011}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.07 mM for 2-phospho-D-glycerate (at 75 degrees Celsius) CC {ECO:0000269|PubMed:7757011}; CC KM=0.03 mM for magnesium (at 75 degrees Celsius) CC {ECO:0000269|PubMed:7757011}; CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:7757011}; CC Temperature dependence: CC Optimum temperature is 90 degrees Celsius. CC {ECO:0000269|PubMed:7757011}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC -!- SUBUNIT: Homooctamer. Forms a ring-shaped particle. CC {ECO:0000269|PubMed:7757011}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. CC Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface CC {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are CC present in both the cytoplasm and on the cell surface. The export CC of enolase possibly depends on the covalent binding to the CC substrate; once secreted, it remains attached to the cell surface. CC {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35958.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35958.1; ALT_INIT; Genomic_DNA. DR PIR; G72323; G72323. DR RefSeq; NP_228685.1; NC_000853.1. DR RefSeq; WP_004080719.1; NZ_CP011107.1. DR RefSeq; WP_010865214.1; NC_000853.1. DR ProteinModelPortal; P42848; -. DR SMR; P42848; 5-428. DR STRING; 243274.TM0877; -. DR PRIDE; P42848; -. DR EnsemblBacteria; AAD35958; AAD35958; TM_0877. DR GeneID; 898551; -. DR KEGG; tma:TM0877; -. DR KEGG; tmi:THEMA_00250; -. DR KEGG; tmw:THMA_0899; -. DR PATRIC; 23936685; VBITheMar51294_0891. DR eggNOG; ENOG4105C70; Bacteria. DR eggNOG; COG0148; LUCA. DR InParanoid; P42848; -. DR KO; K01689; -. DR OMA; EFMIIPV; -. DR OrthoDB; EOG65J589; -. DR BioCyc; TMAR243274:GC6P-907-MONOMER; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.120; -; 1. DR Gene3D; 3.30.390.10; -; 1. DR HAMAP; MF_00318; Enolase; 1. DR InterPro; IPR000941; Enolase. DR InterPro; IPR020810; Enolase_C. DR InterPro; IPR029065; Enolase_C-like. DR InterPro; IPR020809; Enolase_CS. DR InterPro; IPR020811; Enolase_N. DR InterPro; IPR029017; Enolase_N-like. DR PANTHER; PTHR11902; PTHR11902; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; SSF51604; 1. DR SUPFAM; SSF54826; SSF54826; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; KW Lyase; Magnesium; Metal-binding; Reference proteome; Secreted. FT CHAIN 1 429 Enolase. FT /FTId=PRO_0000133994. FT REGION 365 368 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 206 206 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 338 338 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 243 243 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 286 286 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 313 313 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 156 156 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 165 165 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 286 286 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 313 313 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 338 338 Substrate (covalent); in inhibited form. FT {ECO:0000255|HAMAP-Rule:MF_00318}. FT BINDING 389 389 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. SQ SEQUENCE 429 AA; 46870 MW; 35D65899D3AE56CB CRC64; MYVEIVDVRA REVLDSRGNP TVEAEVVLED GTMGRAIVPS GASTGKFEAL EIRDKDKKRY LGKGVLKAVE NVNETIAPAL IGMNAFDQPL VDKTLIELDG TENKSKLGAN AILAVSMAVA RAAANYLGLP LYKYLGGVNA KVLPVPLMNV INGGQHADNN LDLQEFMIVP AGFDSFREAL RAGAEIFHTL KKILHEAGHV TAVGDEGGFA PNLSSNEEAI KVLIEAIEKA GYKPGEEVFI ALDCAASSFY DEEKGVYYVD GEEKSSEVLM GYYEELVAKY PIISIEDPFA EEDWDAFVEF TKRVGNKVQI VGDDLYVTNV KRLSKGIELK ATNSILIKLN QIGTVTETLD AVEMAQKNNM TAIISHRSGE SEDTFIADLA VATNAGFIKT GSLSRSERIA KYNQLLRIEE ELGKVAEFRG LKSFYSIKR // ID END3_THEMA Reviewed; 213 AA. AC Q9WYK0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 115. DE RecName: Full=Endonuclease III {ECO:0000255|HAMAP-Rule:MF_00942}; DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00942}; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_00942}; GN Name=nth {ECO:0000255|HAMAP-Rule:MF_00942}; OrderedLocusNames=TM_0366; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase CC activity and AP-lyase activity. The DNA N-glycosylase activity CC releases various damaged pyrimidines from DNA by cleaving the N- CC glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The CC AP-lyase activity cleaves the phosphodiester bond 3' to the AP CC site by a beta-elimination, leaving a 3'-terminal unsaturated CC sugar and a product with a terminal 5'-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00942}. CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. {ECO:0000255|HAMAP-Rule:MF_00942}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00942}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00942}; CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000255|HAMAP- CC Rule:MF_00942}. CC -!- SIMILARITY: Contains 1 HhH domain. {ECO:0000255|HAMAP- CC Rule:MF_00942}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35453.1; -; Genomic_DNA. DR PIR; F72387; F72387. DR RefSeq; NP_228177.1; NC_000853.1. DR RefSeq; WP_004083173.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYK0; -. DR STRING; 243274.TM0366; -. DR EnsemblBacteria; AAD35453; AAD35453; TM_0366. DR GeneID; 897325; -. DR KEGG; tma:TM0366; -. DR PATRIC; 23935613; VBITheMar51294_0371. DR eggNOG; ENOG4105CSM; Bacteria. DR eggNOG; COG0177; LUCA. DR InParanoid; Q9WYK0; -. DR KO; K10773; -. DR OMA; VSPRCST; -. DR OrthoDB; EOG6H4KC5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR Gene3D; 1.10.1670.10; -; 1. DR Gene3D; 1.10.340.30; -; 1. DR HAMAP; MF_00942; Nth; 1. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR004036; Endonuclease-III-like_CS2. DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS. DR InterPro; IPR003651; Endouclease3_FeS-loop_motif. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR000445; HhH_motif. DR InterPro; IPR023170; HTH_base_excis_C. DR InterPro; IPR005759; Nth. DR Pfam; PF10576; EndIII_4Fe-2S; 1. DR Pfam; PF00633; HHH; 1. DR Pfam; PF00730; HhH-GPD; 1. DR PIRSF; PIRSF001435; Nth; 1. DR SMART; SM00478; ENDO3c; 1. DR SMART; SM00525; FES; 1. DR SUPFAM; SSF48150; SSF48150; 1. DR TIGRFAMs; TIGR01083; nth; 1. DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1. DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; DNA damage; DNA repair; DNA-binding; KW Glycosidase; Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding; KW Reference proteome. FT CHAIN 1 213 Endonuclease III. FT /FTId=PRO_0000102224. FT DOMAIN 101 120 HhH. {ECO:0000255|HAMAP-Rule:MF_00942}. FT METAL 180 180 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. FT METAL 187 187 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. FT METAL 190 190 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. FT METAL 196 196 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. SQ SEQUENCE 213 AA; 24928 MW; D9716CD6FEFA85D4 CRC64; MIEELAREIV KRFPRNHKET DPFRVLISTV LSQRTRDENT EKASKKLFEV YRTPQELAKA KPEDLYDLIK ESGMYRQKAE RIVEISRILV EKYGGRVPDS LEELLKLPGV GRKTANIVLW VGFKKPALAV DTHVHRISNR LGWVKTRTPE ETEEALKKLL PEDLWGPING SMVEFGRRIC KPQNPLCEEC FLKNHCEFYR RRGKGEVRNR TER // ID EFTS_THEMA Reviewed; 199 AA. AC Q9X1U1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 111. DE RecName: Full=Elongation factor Ts; DE Short=EF-Ts; GN Name=tsf; OrderedLocusNames=TM_1605; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the CC exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- CC Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36672.1; -; Genomic_DNA. DR PIR; A72235; A72235. DR RefSeq; NP_229405.1; NC_000853.1. DR RefSeq; WP_004082052.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1U1; -. DR SMR; Q9X1U1; 4-195. DR STRING; 243274.TM1605; -. DR EnsemblBacteria; AAD36672; AAD36672; TM_1605. DR GeneID; 897465; -. DR KEGG; tma:TM1605; -. DR PATRIC; 23938184; VBITheMar51294_1624. DR eggNOG; ENOG4105CU7; Bacteria. DR eggNOG; COG0264; LUCA. DR InParanoid; Q9X1U1; -. DR KO; K02357; -. DR OMA; IAACPNV; -. DR OrthoDB; EOG66B42N; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central. DR Gene3D; 3.30.479.20; -; 2. DR HAMAP; MF_00050; EF_Ts; 1. DR InterPro; IPR001816; Transl_elong_EFTs/EF1B. DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer. DR InterPro; IPR018101; Transl_elong_Ts_CS. DR InterPro; IPR009060; UBA-like. DR PANTHER; PTHR11741; PTHR11741; 1. DR Pfam; PF00889; EF_TS; 1. DR SUPFAM; SSF46934; SSF46934; 1. DR SUPFAM; SSF54713; SSF54713; 1. DR TIGRFAMs; TIGR00116; tsf; 1. DR PROSITE; PS01126; EF_TS_1; 1. DR PROSITE; PS01127; EF_TS_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 199 Elongation factor Ts. FT /FTId=PRO_0000161220. FT REGION 81 84 Involved in Mg(2+) ion dislocation from FT EF-Tu. {ECO:0000250}. SQ SEQUENCE 199 AA; 22811 MW; 87A80DA2C4E98B12 CRC64; MEISMDLIKK LREMTGAGIL DCKKALEEAN GDMEKAVEIL RKKGAATAEK KAGRTTKEGI IVAYVHFNGR IGVLLEMNCE TDFVARTDEF KELAYNLAKQ VAAMKPLYVR REDVPAEVIE KEKEIYRAQI KDKPENIVEK IVEGKLEKFF EQACLYEQTY IFDDTKKVKD LINELIAKTG ENIRVSRFTR YEIGEGYED // ID ERA_THEMA Reviewed; 300 AA. AC Q9WZV1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367}; GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=TM_0847; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: An essential GTPase that binds both GDP and GTP, with CC rapid nucleotide exchange. Plays a role in 16S rRNA processing and CC 30S ribosomal subunit biogenesis and possibly also in cell cycle CC regulation and energy metabolism. {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00367}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane CC {ECO:0000255|HAMAP-Rule:MF_00367}; Peripheral membrane protein CC {ECO:0000255|HAMAP-Rule:MF_00367}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. Era GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC -!- SIMILARITY: Contains 1 Era-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 KH type-2 domain. {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35929.1; -; Genomic_DNA. DR PIR; H72326; H72326. DR RefSeq; NP_228656.1; NC_000853.1. DR RefSeq; WP_008193047.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZV1; -. DR STRING; 243274.TM0847; -. DR EnsemblBacteria; AAD35929; AAD35929; TM_0847. DR GeneID; 898518; -. DR KEGG; tma:TM0847; -. DR PATRIC; 23936620; VBITheMar51294_0860. DR eggNOG; ENOG4105CWT; Bacteria. DR eggNOG; COG1159; LUCA. DR InParanoid; Q9WZV1; -. DR KO; K03595; -. DR OMA; FDDITHN; -. DR OrthoDB; EOG68DD1Q; -. DR BioCyc; TMAR243274:GC6P-876-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.300.20; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00367; GTPase_Era; 1. DR InterPro; IPR030388; G_ERA_dom. DR InterPro; IPR005662; GTP-bd_Era. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR004044; KH_dom_type_2. DR InterPro; IPR009019; KH_prok-type. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR Pfam; PF07650; KH_2; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54814; SSF54814; 1. DR TIGRFAMs; TIGR00436; era; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51713; G_ERA; 1. DR PROSITE; PS50823; KH_TYPE_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; KW GTP-binding; Membrane; Nucleotide-binding; Reference proteome; KW Ribosome biogenesis; RNA-binding; rRNA-binding. FT CHAIN 1 300 GTPase Era. FT /FTId=PRO_0000180066. FT DOMAIN 4 172 Era-type G. FT DOMAIN 195 280 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_00367}. FT NP_BIND 12 19 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. FT NP_BIND 59 63 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. FT NP_BIND 121 124 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. SQ SEQUENCE 300 AA; 33521 MW; CCDE61A7BA45F25D CRC64; MSIKSGFVAL AGKPNVGKST FINAVMGRKV VIVSDKPQTT RNRINCIYTD KDSQIIFVDT PGIHKPLHRL GEYMVKAAVQ ALKGVDLVLF MLDAADGFTK TDEHVAKIVN DSGTKTIIAV NKIDVAGEEK AKAVGELAKS MVENVVSVHY ISALKGEGVF EVLEKIKEEL PEGPQYYPED MVTDRPLSFM AAEIIREKIF HLTRQEVPHS TAVVIEEIKD RPNGVLYIRA NIYVERDSQK GILIGKNGSM IKKIGTLARE ELEFLVGRKV YLDLNVKVKE KWREKDFIIL QEIGLKDDIK // ID ESTD_THEMA Reviewed; 412 AA. AC Q9WYH1; G4FHP9; DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Esterase EstD {ECO:0000312|EMBL:AHD17901.1}; DE EC=3.1.1.1 {ECO:0000269|PubMed:17466017}; DE Flags: Precursor; GN Name=estD {ECO:0000303|PubMed:17466017}; GN OrderedLocusNames=TM_0336 {ECO:0000312|EMBL:AAD35423.1}; GN ORFNames=THEMA_03040 {ECO:0000312|EMBL:AHD17901.1}, GN Tmari_0334 {ECO:0000312|EMBL:AGL49259.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RG DOE Joint Genome Institute; RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, RP 3D-STRUCTURE MODELING, MUTAGENESIS OF SER-243; ASP-347 AND HIS-378, RP ACTIVE SITE, AND BIOTECHNOLOGY. RX PubMed=17466017; DOI=10.1111/j.1742-4658.2007.05817.x; RA Levisson M., van der Oost J., Kengen S.W.; RT "Characterization and structural modeling of a new type of RT thermostable esterase from Thermotoga maritima."; RL FEBS J. 274:2832-2842(2007). CC -!- FUNCTION: Exhibits significant esterase activity with a preference CC for short acyl chain esters (C4-C8) in vitro. Its physiological CC function is not known. Displays neither proteolytic activity using CC casein as substrate, nor peptidase activity when assayed with L- CC leucine p-nitroanilide and L-proline p-nitroanilide. CC {ECO:0000269|PubMed:17466017}. CC -!- CATALYTIC ACTIVITY: A carboxylic ester + H(2)O = an alcohol + a CC carboxylate. {ECO:0000269|PubMed:17466017}. CC -!- ENZYME REGULATION: Is strongly inhibited by phenylmethylsulfonyl CC fluoride, a serine protease inhibitor, and by mercury chloride. CC Diethyl pyrocarbonate, a histidine modifier, also inhibits the CC reaction, albeit less pronounced than phenylmethylsulfonyl CC fluoride. EDTA and dithiothreitol have no effect on enzyme CC activity. {ECO:0000269|PubMed:17466017}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=148 uM for pNP-acetate (at pH 7 and 70 degrees Celsius) CC {ECO:0000269|PubMed:17466017}; CC KM=227 uM for pNP-butyrate (at pH 7 and 70 degrees Celsius) CC {ECO:0000269|PubMed:17466017}; CC KM=66 uM for pNP-valerate (at pH 7 and 70 degrees Celsius) CC {ECO:0000269|PubMed:17466017}; CC KM=11 uM for pNP-octanoate (at pH 7 and 70 degrees Celsius) CC {ECO:0000269|PubMed:17466017}; CC KM=72 uM for pNP-decanoate (at pH 7 and 70 degrees Celsius) CC {ECO:0000269|PubMed:17466017}; CC Note=kcat is 1.0 sec(-1) with pNP-acetate as substrate. kcat is CC 14.9 sec(-1) with pNP-butyrate as substrate. kcat is 10.2 sec(- CC 1) with pNP-valerate as substrate. kcat is 1.6 sec(-1) with pNP- CC octanoate as substrate. kcat is 1.3 sec(-1) with pNP-decanoate CC as substrate (at pH 7 and 70 degrees Celsius). CC {ECO:0000269|PubMed:17466017}; CC pH dependence: CC Optimum pH is 7. {ECO:0000269|PubMed:17466017}; CC Temperature dependence: CC Optimum temperature is around 95 degrees Celsius. Shows >70% of CC its maximal activity in the pH range of 5-9. Displays a CC relatively high thermostability with a half-life of 1 hour at CC 100 degrees Celsius. {ECO:0000269|PubMed:17466017}; CC -!- SUBUNIT: Exists mainly as a monomer and, to some extent as a CC dimer. {ECO:0000269|PubMed:17466017}. CC -!- BIOTECHNOLOGY: The high thermal stability and activity in the CC presence of organic solvents makes EstD an attractive catalyst for CC future applications in industry. {ECO:0000305|PubMed:17466017}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Esterase 10 CC family. {ECO:0000305|PubMed:17466017}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35423.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49259.1; -; Genomic_DNA. DR EMBL; CP007013; AHD17901.1; -; Genomic_DNA. DR PIR; B72391; B72391. DR RefSeq; NP_228147.1; NC_000853.1. DR RefSeq; WP_004083104.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYH1; -. DR STRING; 243274.TM0336; -. DR ESTHER; thema-TM0336; Bacterial_EstLip_FamX. DR EnsemblBacteria; AAD35423; AAD35423; TM_0336. DR EnsemblBacteria; AGL49259; AGL49259; Tmari_0334. DR EnsemblBacteria; AHD17901; AHD17901; THEMA_03040. DR GeneID; 897291; -. DR KEGG; tma:TM0336; -. DR KEGG; tmi:THEMA_03040; -. DR KEGG; tmm:Tmari_0334; -. DR KEGG; tmw:THMA_0344; -. DR PATRIC; 23935553; VBITheMar51294_0341. DR eggNOG; ENOG4105F6J; Bacteria. DR eggNOG; COG1073; LUCA. DR InParanoid; Q9WYH1; -. DR KO; K06889; -. DR OMA; APRIATY; -. DR OrthoDB; EOG6N0HKG; -. DR BioCyc; TMAR243274:GC6P-350-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB. DR GO; GO:0008152; P:metabolic process; IDA:UniProtKB. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR024981; DUF3887. DR InterPro; IPR022742; Hydrolase_4. DR Pfam; PF13026; DUF3887; 1. DR Pfam; PF12146; Hydrolase_4; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR PROSITE; PS00120; LIPASE_SER; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Reference proteome; Serine esterase; KW Signal. FT SIGNAL 1 20 {ECO:0000255}. FT CHAIN 21 412 Esterase EstD. FT /FTId=PRO_0000432501. FT ACT_SITE 243 243 Nucleophile. FT {ECO:0000305|PubMed:17466017}. FT ACT_SITE 347 347 Charge relay system. FT {ECO:0000305|PubMed:17466017}. FT ACT_SITE 378 378 Charge relay system. FT {ECO:0000305|PubMed:17466017}. FT MUTAGEN 243 243 S->A: Loss of enzymatic activity. FT {ECO:0000269|PubMed:17466017}. FT MUTAGEN 347 347 D->N: Loss of enzymatic activity. FT {ECO:0000269|PubMed:17466017}. FT MUTAGEN 378 378 H->N: Loss of enzymatic activity. FT {ECO:0000269|PubMed:17466017}. SQ SEQUENCE 412 AA; 46550 MW; 70BC812D936425A5 CRC64; MRLTVFLSLF LGVMVFGAFD QEAFLFVQHL TSENFESALN MCSNQVKAQL SVQSLSNIWN SLKAQLSDFR EIAGYEKIIQ AEYEIYNFTL KFDRGEISAL VTMDREGKVA GLFFKQATKT EYELPDYVDP ESFEEKDITV NGLPGKITIP KGSGPFPAVV LVHGSGPNDM DETIGPNKIF KDIAYGLSSK GIIVLRYHKR TFVEKVDPTT LTVEKEVIED ALEAVKILKE RKDVSRVYVL GHSLGAMLTP EIAERSKADG VVMIAPPARP LEEVMEDQLK YLQSLGLASN VEETLNILEK LKRKEIPPDE FVLGAPAKYF YDLRERDPAS IAKRLTIPML LIFGGRDYQV TEKDQEIWLK ELSGRENVKI LVFDDLNHLM ISGEGKSTPV EYMKKGHVDK RVIDEIARWM VK // ID EX7L_THEMA Reviewed; 394 AA. AC Q9X289; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378}; DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378}; DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378}; DE Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378}; GN Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378}; GN OrderedLocusNames=TM_1768; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large CC acid-insoluble oligonucleotides, which are then degraded further CC into small acid-soluble oligonucleotides. {ECO:0000255|HAMAP- CC Rule:MF_00378}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to 3'- CC or 3'- to 5'-direction to yield nucleoside 5'-phosphates. CC {ECO:0000255|HAMAP-Rule:MF_00378}. CC -!- SUBUNIT: Heterooligomer composed of large and small subunits. CC {ECO:0000255|HAMAP-Rule:MF_00378}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}. CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP- CC Rule:MF_00378}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36832.1; -; Genomic_DNA. DR PIR; G72212; G72212. DR RefSeq; NP_229565.1; NC_000853.1. DR RefSeq; WP_004082314.1; NZ_CP011107.1. DR STRING; 243274.TM1768; -. DR EnsemblBacteria; AAD36832; AAD36832; TM_1768. DR GeneID; 897853; -. DR KEGG; tma:TM1768; -. DR PATRIC; 23938516; VBITheMar51294_1787. DR eggNOG; ENOG4105DVS; Bacteria. DR eggNOG; COG1570; LUCA. DR InParanoid; Q9X289; -. DR KO; K03601; -. DR OMA; PRKGHIF; -. DR OrthoDB; EOG64R65J; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro. DR GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00378; Exonuc_7_L; 1. DR InterPro; IPR003753; Exonuc_VII_L. DR InterPro; IPR020579; Exonuc_VII_lsu_C. DR InterPro; IPR025824; OB-fold_nuc-bd_dom. DR Pfam; PF02601; Exonuc_VII_L; 2. DR Pfam; PF13742; tRNA_anti_2; 1. DR TIGRFAMs; TIGR00237; xseA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 394 Exodeoxyribonuclease 7 large subunit. FT /FTId=PRO_0000197897. SQ SEQUENCE 394 AA; 45353 MW; 072E5D28D0E19A10 CRC64; MKDYTYSVTE INEYIKDLIE GDPYLTNVSV YGEISGVRPR KGHIFFSLVE ENARLECVIF GGDNMGIRLQ EGRMALVEGS VSVYIPHGTY RFICSNVRYL DQAGMYQIKF ETTLKKLLEE GLLSRPKKTV PRFPRKIGII TSRDSAALQD VIRTARERKA PIEIYVFHTS VQGDSAREEL IKALRKANEY DLDLVMIVRG GGSKEDLWVF NEEDVIREIL RLRHPVVTGI GHEIDRVIAD FVADVSMHTP TGAAEYVIPD ASEIHEDLDS FFEKLITSLS NRFDMEERRL ETLYFRLRMI GRRKLELNEF KIERVKELAA KLRKKLMDYF EHNQKKLDSL GRMLESLNPL RPLERGFVLV KKDEKIVKES TDLKRGDVVS LVFKDGTKKA QVIG // ID EX7S_THEMA Reviewed; 75 AA. AC Q9X290; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 13-APR-2016, entry version 102. DE RecName: Full=Exodeoxyribonuclease 7 small subunit; DE EC=3.1.11.6; DE AltName: Full=Exodeoxyribonuclease VII small subunit; DE Short=Exonuclease VII small subunit; GN Name=xseB; OrderedLocusNames=TM_1769; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large CC acid-insoluble oligonucleotides, which are then degraded further CC into small acid-soluble oligonucleotides. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to 3'- CC or 3'- to 5'-direction to yield nucleoside 5'-phosphates. CC -!- SUBUNIT: Heterooligomer composed of large and small subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the XseB family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD36843.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36843.1; ALT_INIT; Genomic_DNA. DR PIR; H72212; H72212. DR RefSeq; NP_229566.1; NC_000853.1. DR ProteinModelPortal; Q9X290; -. DR STRING; 243274.TM1769; -. DR EnsemblBacteria; AAD36843; AAD36843; TM_1769. DR GeneID; 897773; -. DR KEGG; tma:TM1769; -. DR PATRIC; 23938518; VBITheMar51294_1788. DR eggNOG; COG1722; LUCA. DR InParanoid; Q9X290; -. DR KO; K03602; -. DR OMA; VEMEDDL; -. DR OrthoDB; EOG69KV31; -. DR BioCyc; TMAR243274:GC6P-1818-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro. DR GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.1040; -; 1. DR HAMAP; MF_00337; Exonuc_7_S; 1. DR InterPro; IPR003761; Exonuc_VII_S. DR Pfam; PF02609; Exonuc_VII_S; 1. DR PIRSF; PIRSF006488; Exonuc_VII_S; 1. DR ProDom; PD028235; Exonuc_VII_S; 1. DR TIGRFAMs; TIGR01280; xseB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 75 Exodeoxyribonuclease 7 small subunit. FT /FTId=PRO_0000207026. SQ SEQUENCE 75 AA; 9041 MW; D46FE7222161ACB0 CRC64; MNFEEMMKEL EEIVNRLENE DLPLEESIKL FERGVELYRK CKEILQQNRL KIIDVMKELE GEIDASGRDQ ENELR // ID FLGH_THEMA Reviewed; 199 AA. AC Q9X1M6; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Flagellar L-ring protein; DE AltName: Full=Basal body L-ring protein; DE Flags: Precursor; GN Name=flgH; OrderedLocusNames=TM_1540; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Assembles around the rod to form the L-ring and probably CC protects the motor/basal body from shearing forces during CC rotation. {ECO:0000250}. CC -!- SUBUNIT: The basal body constitutes a major portion of the CC flagellar organelle and consists of four rings (L,P,S, and M) CC mounted on a central rod. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}. Bacterial CC flagellum basal body {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36607.1; -; Genomic_DNA. DR PIR; H72242; H72242. DR RefSeq; NP_229340.1; NC_000853.1. DR RefSeq; WP_004081924.1; NZ_CP011107.1. DR STRING; 243274.TM1540; -. DR EnsemblBacteria; AAD36607; AAD36607; TM_1540. DR GeneID; 897976; -. DR KEGG; tma:TM1540; -. DR PATRIC; 23938040; VBITheMar51294_1558. DR eggNOG; ENOG4105TZT; Bacteria. DR eggNOG; COG2063; LUCA. DR InParanoid; Q9X1M6; -. DR KO; K02393; -. DR OMA; ATKEHTA; -. DR OrthoDB; EOG6GTZJM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009427; C:bacterial-type flagellum basal body, distal rod, L ring; IEA:InterPro. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003774; F:motor activity; IEA:InterPro. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR HAMAP; MF_00415; FlgH; 1. DR InterPro; IPR000527; Flag_Lring. DR Pfam; PF02107; FlgH; 1. DR PRINTS; PR01008; FLGLRINGFLGH. PE 3: Inferred from homology; KW Bacterial flagellum; Cell outer membrane; Complete proteome; Membrane; KW Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 199 Flagellar L-ring protein. FT /FTId=PRO_0000009475. SQ SEQUENCE 199 AA; 21896 MW; D2A487647F95E22C CRC64; MRRISIVLLI VFATSIFPFS IWNSAGESEY KNLLSIKKAS KVGDILTIVI RESNNVSSER ESLEIQKTLL NILGNVVNAA AGVNLNNFIP INNNSPERQR GGKVQSSVVA KISAVVVDID PYGNLVVEGR KTIKVDKDYQ EIIVKGKVRP DDIEIGNEVD SSKLADSEIW VNGKLVFSEE PGKESFFDKI LAFLAGLFT // ID FABG_THEMA Reviewed; 246 AA. AC Q9X248; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 110. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase FabG; DE EC=1.1.1.100; DE AltName: Full=3-ketoacyl-acyl carrier protein reductase; DE AltName: Full=Beta-Ketoacyl-acyl carrier protein reductase; DE AltName: Full=Beta-ketoacyl-ACP reductase; GN Name=fabG; OrderedLocusNames=TM_1724; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of beta- CC ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the CC first reductive step in the elongation cycle of fatty acid CC biosynthesis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + CC NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36790.1; -; Genomic_DNA. DR PIR; H72219; H72219. DR RefSeq; NP_229523.1; NC_000853.1. DR RefSeq; WP_004082240.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X248; -. DR STRING; 243274.TM1724; -. DR EnsemblBacteria; AAD36790; AAD36790; TM_1724. DR GeneID; 897230; -. DR KEGG; tma:TM1724; -. DR PATRIC; 23938424; VBITheMar51294_1742. DR eggNOG; ENOG4105CHR; Bacteria. DR eggNOG; ENOG410XNW1; LUCA. DR InParanoid; Q9X248; -. DR KO; K00059; -. DR OMA; VVCDKLA; -. DR OrthoDB; EOG6N3CR8; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR011284; 3oxo_ACP_reduc. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01830; 3oxo_ACP_reduc; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 246 3-oxoacyl-[acyl-carrier-protein] FT reductase FabG. FT /FTId=PRO_0000054693. FT NP_BIND 62 63 NADP. {ECO:0000250}. FT NP_BIND 154 158 NADP. {ECO:0000250}. FT ACT_SITE 154 154 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10001}. FT BINDING 89 89 NADP; via carbonyl oxygen. {ECO:0000250}. FT BINDING 141 141 Substrate. {ECO:0000250}. FT BINDING 187 187 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. SQ SEQUENCE 246 AA; 26402 MW; 8C08904D28099142 CRC64; MRLEGKVCLI TGAASGIGKA TTLLFAQEGA TVIAGDISKE NLDSLVKEAE GLPGKVDPYV LNVTDRDQIK EVVEKVVQKY GRIDVLVNNA GITRDALLVR MKEEDWDAVI NVNLKGVFNV TQMVVPYMIK QRNGSIVNVS SVVGIYGNPG QTNYAASKAG VIGMTKTWAK ELAGRNIRVN AVAPGFIETP MTEKLPEKAR ETALSRIPLG RFGKPEEVAQ VILFLASDES SYVTGQVIGI DGGLVI // ID FABZ_THEMA Reviewed; 137 AA. AC Q9WZQ8; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ {ECO:0000255|HAMAP-Rule:MF_00406}; DE EC=4.2.1.59 {ECO:0000255|HAMAP-Rule:MF_00406}; DE AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase {ECO:0000255|HAMAP-Rule:MF_00406}; DE Short=(3R)-hydroxymyristoyl-ACP dehydrase {ECO:0000255|HAMAP-Rule:MF_00406}; DE AltName: Full=Beta-hydroxyacyl-ACP dehydratase {ECO:0000255|HAMAP-Rule:MF_00406}; GN Name=fabZ {ECO:0000255|HAMAP-Rule:MF_00406}; GN OrderedLocusNames=TM_0801; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in unsaturated fatty acids biosynthesis. CC Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and CC long chain saturated and unsaturated beta-hydroxyacyl-ACPs. CC {ECO:0000255|HAMAP-Rule:MF_00406}. CC -!- CATALYTIC ACTIVITY: A (3R)-3-hydroxyacyl-[acyl-carrier protein] = CC a trans-2-enoyl-[acyl-carrier protein] + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00406}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00406}. CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00406}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35883.1; -; Genomic_DNA. DR PIR; B72335; B72335. DR RefSeq; NP_228610.1; NC_000853.1. DR RefSeq; WP_004080862.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZQ8; -. DR STRING; 243274.TM0801; -. DR EnsemblBacteria; AAD35883; AAD35883; TM_0801. DR GeneID; 898469; -. DR KEGG; tma:TM0801; -. DR PATRIC; 23936522; VBITheMar51294_0813. DR eggNOG; ENOG4108YXN; Bacteria. DR eggNOG; COG0764; LUCA. DR InParanoid; Q9WZQ8; -. DR KO; K02372; -. DR OMA; PTENELY; -. DR OrthoDB; EOG6JTCGM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.129.10; -; 1. DR HAMAP; MF_00406; FabZ; 1. DR InterPro; IPR013114; FabA_FabZ. DR InterPro; IPR010084; FabZ. DR InterPro; IPR029069; HotDog_dom. DR Pfam; PF07977; FabA; 1. DR SUPFAM; SSF54637; SSF54637; 1. DR TIGRFAMs; TIGR01750; fabZ; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Lyase; Reference proteome. FT CHAIN 1 137 3-hydroxyacyl-[acyl-carrier-protein] FT dehydratase FabZ. FT /FTId=PRO_0000091754. FT ACT_SITE 46 46 {ECO:0000255|HAMAP-Rule:MF_00406}. SQ SEQUENCE 137 AA; 15300 MW; ED2FB248F02299D0 CRC64; MNIDYVKSIL PHRYPFLLVD GVIEESEDRI VAFKNISISD PVFQGHFPEY PIYPGVLIVE GLAQTAGILL LKSVEGIPLF LGIDEARFKK EVRPGDRLIY EVRKLGEKLG TVQVEGVAKV DDKIVAKARL LLGVKKK // ID FLGI_THEMA Reviewed; 331 AA. AC Q9X1M5; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 2. DT 13-APR-2016, entry version 92. DE RecName: Full=Flagellar P-ring protein; DE AltName: Full=Basal body P-ring protein; DE Flags: Precursor; GN Name=flgI; OrderedLocusNames=TM_1539; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Assembles around the rod to form the L-ring and probably CC protects the motor/basal body from shearing forces during CC rotation. {ECO:0000250}. CC -!- SUBUNIT: The basal body constitutes a major portion of the CC flagellar organelle and consists of four rings (L,P,S, and M) CC mounted on a central rod. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Bacterial flagellum CC basal body {ECO:0000250}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD36606.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36606.1; ALT_INIT; Genomic_DNA. DR PIR; G72242; G72242. DR RefSeq; NP_229339.1; NC_000853.1. DR RefSeq; WP_004081923.1; NZ_CP011107.1. DR STRING; 243274.TM1539; -. DR EnsemblBacteria; AAD36606; AAD36606; TM_1539. DR GeneID; 897386; -. DR KEGG; tma:TM1539; -. DR PATRIC; 23938038; VBITheMar51294_1557. DR eggNOG; ENOG4105D92; Bacteria. DR eggNOG; COG1706; LUCA. DR InParanoid; Q9X1M5; -. DR KO; K02394; -. DR OMA; IIIDERS; -. DR OrthoDB; EOG64JFMG; -. DR BioCyc; TMAR243274:GC6P-1579-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009428; C:bacterial-type flagellum basal body, distal rod, P ring; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR HAMAP; MF_00416; FlgI; 1. DR InterPro; IPR001782; Flag_FlgI. DR Pfam; PF02119; FlgI; 2. DR PRINTS; PR01010; FLGPRINGFLGI. PE 3: Inferred from homology; KW Bacterial flagellum; Complete proteome; Periplasm; Reference proteome; KW Signal. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 331 Flagellar P-ring protein. FT /FTId=PRO_0000009525. SQ SEQUENCE 331 AA; 35421 MW; 97E6CABB1F1B47F9 CRC64; MKKRLAVLLV IVLTITFSFS VTTRIKDIAF FRGARDNQLF GIGLVVGLNG TGDSGNVNSP LLLEMMKKFG VQVSENDLKS KNTALVMVLA DIPPFAKEGM RIDCVVASIA DAKSLAGGYL LQTPLYGADG KVYAVAQGSV IIGGEDVKLS SNLQKRYRVV GYLLEGAIVE RDIPSDMLDG DSVTILLRQP DITTAARVAR AINEKFEMDL AKAIDPSAIK LTVPSAFQDD LITFLSLVEE IEVQPDVPAR IVVNERTGTV LFGGDVKLSD FVISYGNFTI SVTGGKIGDK DATISNLVSA LKAAGATPQD IIAILQVIYE SGYITGELII M // ID FLIE_THEMA Reviewed; 94 AA. AC Q9X186; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Flagellar hook-basal body complex protein FliE {ECO:0000255|HAMAP-Rule:MF_00724}; GN Name=fliE {ECO:0000255|HAMAP-Rule:MF_00724}; GN OrderedLocusNames=TM_1366; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body CC {ECO:0000255|HAMAP-Rule:MF_00724}. CC -!- SIMILARITY: Belongs to the FliE family. {ECO:0000255|HAMAP- CC Rule:MF_00724}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36436.1; -; Genomic_DNA. DR PIR; G72263; G72263. DR RefSeq; NP_229167.1; NC_000853.1. DR RefSeq; WP_004081562.1; NZ_CP011107.1. DR STRING; 243274.TM1366; -. DR EnsemblBacteria; AAD36436; AAD36436; TM_1366. DR GeneID; 898114; -. DR KEGG; tma:TM1366; -. DR PATRIC; 23937670; VBITheMar51294_1378. DR eggNOG; ENOG4105VQ0; Bacteria. DR eggNOG; COG1677; LUCA. DR InParanoid; Q9X186; -. DR KO; K02408; -. DR OMA; HQVTIAM; -. DR OrthoDB; EOG60GRZ6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell. DR GO; GO:0003774; F:motor activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR HAMAP; MF_00724; FliE; 1. DR InterPro; IPR001624; FliE. DR Pfam; PF02049; FliE; 1. DR PRINTS; PR01006; FLGHOOKFLIE. DR TIGRFAMs; TIGR00205; fliE; 1. PE 3: Inferred from homology; KW Bacterial flagellum; Complete proteome; Reference proteome. FT CHAIN 1 94 Flagellar hook-basal body complex protein FT FliE. FT /FTId=PRO_0000105567. SQ SEQUENCE 94 AA; 10626 MW; E37A4987F091BBE1 CRC64; MVDRIEGLGP LSQSGKTQKK SENNFSEALK EALEKVNDIQ KKAEKAADDF AQGRISNIHE VIIEAEKASI ALRLTVEVRN RIVEAYRDIM RMQI // ID FER_THEMA Reviewed; 60 AA. AC P46797; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=Ferredoxin; GN Name=fdx; OrderedLocusNames=TM_0927; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8168477; RA Darimont B., Sterner R.; RT "Sequence, assembly and evolution of a primordial ferredoxin from RT Thermotoga maritima."; RL EMBO J. 13:1772-1781(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). RX PubMed=8939753; DOI=10.1016/S0969-2126(96)00137-2; RA Macedo-Ribeiro S., Darimont B., Sterner R., Huber R.; RT "Small structural changes account for the high thermostability of RT 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga RT maritima."; RL Structure 4:1291-1301(1996). RN [4] RP STRUCTURE BY NMR. RX PubMed=8647119; DOI=10.1111/j.1432-1033.1996.0726p.x; RA Sticht H., Wildegger G., Bentrop D., Darimont B., Sterner R., RA Roesch P.; RT "An NMR-derived model for the solution structure of oxidized RT Thermotoga maritima 1[Fe4-S4] ferredoxin."; RL Eur. J. Biochem. 237:726-735(1996). CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer CC electrons in a wide variety of metabolic reactions. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 1 [4Fe-4S] cluster.; CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X82178; CAA57669.1; -; Genomic_DNA. DR EMBL; U24145; AAA65437.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36008.1; -; Genomic_DNA. DR PIR; S44350; S44350. DR RefSeq; NP_228735.1; NC_000853.1. DR RefSeq; WP_004080635.1; NZ_CP011107.1. DR PDB; 1ROF; NMR; -; A=1-60. DR PDB; 1VJW; X-ray; 1.75 A; A=1-60. DR PDBsum; 1ROF; -. DR PDBsum; 1VJW; -. DR ProteinModelPortal; P46797; -. DR SMR; P46797; 1-60. DR STRING; 243274.TM0927; -. DR EnsemblBacteria; AAD36008; AAD36008; TM_0927. DR GeneID; 898601; -. DR KEGG; tma:TM0927; -. DR PATRIC; 23936785; VBITheMar51294_0941. DR eggNOG; ENOG41084T3; Bacteria. DR eggNOG; COG1141; LUCA. DR InParanoid; P46797; -. DR KO; K05337; -. DR OMA; LDCAKDA; -. DR OrthoDB; EOG60SCM3; -. DR EvolutionaryTrace; P46797; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR001080; 3Fe4S_ferredoxin. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR PRINTS; PR00352; 3FE4SFRDOXIN. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing; KW Disulfide bond; Electron transport; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; Repeat; Transport. FT CHAIN 1 60 Ferredoxin. FT /FTId=PRO_0000159203. FT DOMAIN 2 29 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 30 60 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 10 10 Iron-sulfur (4Fe-4S). FT {ECO:0000269|PubMed:8939753}. FT METAL 13 13 Iron-sulfur (4Fe-4S). FT {ECO:0000269|PubMed:8939753}. FT METAL 16 16 Iron-sulfur (4Fe-4S). FT {ECO:0000269|PubMed:8939753}. FT METAL 51 51 Iron-sulfur (4Fe-4S). FT {ECO:0000269|PubMed:8939753}. FT DISULFID 20 43 {ECO:0000269|PubMed:8939753}. FT STRAND 3 5 {ECO:0000244|PDB:1ROF}. FT TURN 7 9 {ECO:0000244|PDB:1VJW}. FT HELIX 15 19 {ECO:0000244|PDB:1VJW}. FT TURN 21 23 {ECO:0000244|PDB:1VJW}. FT STRAND 24 26 {ECO:0000244|PDB:1VJW}. FT STRAND 30 35 {ECO:0000244|PDB:1VJW}. FT HELIX 43 50 {ECO:0000244|PDB:1VJW}. SQ SEQUENCE 60 AA; 6213 MW; A00A03A13FDF1690 CRC64; MKVRVDADAC IGCGVCENLC PDVFQLGDDG KAKVLQPETD LPCAKDAADS CPTGAISVEE // ID FLIW_THEMA Reviewed; 149 AA. AC Q9WXT6; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=Flagellar assembly factor FliW {ECO:0000255|HAMAP-Rule:MF_01185}; GN Name=fliW {ECO:0000255|HAMAP-Rule:MF_01185}; GN OrderedLocusNames=TM_0081; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds to the C-terminal region of flagellin, which is CC implicated in polymerization, and participates in the assembly of CC the flagellum. {ECO:0000255|HAMAP-Rule:MF_01185}. CC -!- SUBUNIT: Interacts with flagellin. {ECO:0000255|HAMAP- CC Rule:MF_01185}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01185}. CC -!- SIMILARITY: Belongs to the FliW family. {ECO:0000255|HAMAP- CC Rule:MF_01185}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35175.1; -; Genomic_DNA. DR PIR; C72419; C72419. DR RefSeq; NP_227897.1; NC_000853.1. DR RefSeq; WP_004082606.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXT6; -. DR STRING; 243274.TM0081; -. DR EnsemblBacteria; AAD35175; AAD35175; TM_0081. DR GeneID; 896908; -. DR KEGG; tma:TM0081; -. DR PATRIC; 23935002; VBITheMar51294_0079. DR eggNOG; ENOG4105W5T; Bacteria. DR eggNOG; COG1699; LUCA. DR InParanoid; Q9WXT6; -. DR KO; K13626; -. DR OMA; VAVFCIV; -. DR OrthoDB; EOG64V2JN; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.290.10; -; 1. DR HAMAP; MF_01185; FliW; 1. DR InterPro; IPR003775; Flagellar_assembly_factor_FliW. DR InterPro; IPR024046; Flagellar_assmbl_FliW_dom. DR Pfam; PF02623; FliW; 1. DR SUPFAM; SSF141457; SSF141457; 1. PE 3: Inferred from homology; KW Bacterial flagellum biogenesis; Complete proteome; Cytoplasm; KW Reference proteome. FT CHAIN 1 149 Flagellar assembly factor FliW. FT /FTId=PRO_0000273010. SQ SEQUENCE 149 AA; 16996 MW; 8D9A9A3959D6E8DF CRC64; MVYKTKLGEI EISDESIFTF EKGIPGFEHL RKFALVFPQE TFPIGWLLSL EDSEVGLPVV DPKLVRADYD PAVPSEDLEE IEAENQEALL FFCVLTIPPG KPEKTTINLR APIILNQKKK KGIQTILENE DYQLRHLLSE EIERSKTVV // ID FLIM_THEMA Reviewed; 328 AA. AC Q9WZE6; G4FDE5; DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Flagellar motor switch protein FliM {ECO:0000312|EMBL:AAD35762.1}; GN Name=fliM {ECO:0000250|UniProtKB:P06974}; OrderedLocusNames=TM_0679; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] {ECO:0000312|EMBL:AAD35762.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000305, ECO:0000312|PDB:2HP7} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 44-226, INTERACTION WITH RP CHEY, AND MUTAGENESIS OF GLU-60. RX PubMed=16882724; DOI=10.1073/pnas.0602811103; RA Park S.Y., Lowder B., Bilwes A.M., Blair D.F., Crane B.R.; RT "Structure of FliM provides insight into assembly of the switch RT complex in the bacterial flagella motor."; RL Proc. Natl. Acad. Sci. U.S.A. 103:11886-11891(2006). RN [3] {ECO:0000305, ECO:0000312|PDB:3SOH} RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 46-233 IN COMPLEX WITH FLIG, RP AND INTERACTION WITH FLIG. RX PubMed=21673656; DOI=10.1038/emboj.2011.188; RA Paul K., Gonzalez-Bonet G., Bilwes A.M., Crane B.R., Blair D.; RT "Architecture of the flagellar rotor."; RL EMBO J. 30:2962-2971(2011). RN [4] {ECO:0000305, ECO:0000312|PDB:4FHR} RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 46-230 IN COMPLEX WITH FLIG, RP AND INTERACTION WITH FLIG. RX PubMed=22896702; DOI=10.1074/jbc.C112.378380; RA Vartanian A.S., Paz A., Fortgang E.A., Abramson J., Dahlquist F.W.; RT "Structure of flagellar motor proteins in complex allows for insights RT into motor structure and switching."; RL J. Biol. Chem. 287:35779-35783(2012). CC -!- FUNCTION: FliM is one of three proteins (FliG, FliN, FliM) that CC forms the rotor-mounted switch complex (C ring), located at the CC base of the basal body. This complex interacts with the CheY and CC CheX chemotaxis proteins, in addition to contacting components of CC the motor that determine the direction of flagellar rotation (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts (via N-terminus) with unphosphorylated CheY. CC Interacts (via central domain) with FliG (via central domain or CC via central domain and C-terminus). {ECO:0000269|PubMed:16882724, CC ECO:0000269|PubMed:21673656, ECO:0000269|PubMed:22896702}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. Bacterial flagellum CC basal body {ECO:0000250|UniProtKB:P06974}. CC -!- SIMILARITY: Belongs to the FliM family. {ECO:0000255}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35762.1; -; Genomic_DNA. DR PIR; E72347; E72347. DR RefSeq; NP_228487.1; NC_000853.1. DR RefSeq; WP_004081085.1; NZ_CP011107.1. DR PDB; 2HP7; X-ray; 2.00 A; A=44-226. DR PDB; 3SOH; X-ray; 3.50 A; A/C=46-233. DR PDB; 4FHR; X-ray; 1.93 A; A=46-230. DR PDB; 4IGA; X-ray; 1.73 A; B=1-20. DR PDB; 4QRM; X-ray; 4.32 A; A/C/E/G/I/K/M/O/Q/S/U=46-228. DR PDBsum; 2HP7; -. DR PDBsum; 3SOH; -. DR PDBsum; 4FHR; -. DR PDBsum; 4IGA; -. DR PDBsum; 4QRM; -. DR ProteinModelPortal; Q9WZE6; -. DR SMR; Q9WZE6; 44-226. DR DIP; DIP-61248N; -. DR IntAct; Q9WZE6; 1. DR MINT; MINT-8212457; -. DR STRING; 243274.TM0679; -. DR EnsemblBacteria; AAD35762; AAD35762; TM_0679. DR GeneID; 898347; -. DR KEGG; tma:TM0679; -. DR PATRIC; 23936274; VBITheMar51294_0690. DR eggNOG; ENOG4105D24; Bacteria. DR eggNOG; COG1868; LUCA. DR InParanoid; Q9WZE6; -. DR KO; K02416; -. DR OMA; NPQFTQI; -. DR OrthoDB; EOG68M4DH; -. DR BioCyc; TMAR243274:GC6P-704-MONOMER; -. DR EvolutionaryTrace; Q9WZE6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003774; F:motor activity; IEA:InterPro. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR GO; GO:0050918; P:positive chemotaxis; IBA:GO_Central. DR InterPro; IPR028976; CheC-like_dom. DR InterPro; IPR001689; Flag_FliM. DR InterPro; IPR001543; SpoA. DR Pfam; PF02154; FliM; 1. DR Pfam; PF01052; FliMN_C; 1. DR PIRSF; PIRSF002888; FliM; 1. DR PRINTS; PR00955; FLGMOTORFLIM. DR SUPFAM; SSF101801; SSF101801; 1. DR SUPFAM; SSF103039; SSF103039; 1. DR TIGRFAMs; TIGR01397; fliM_switch; 1. PE 1: Evidence at protein level; KW 3D-structure; Bacterial flagellum; Cell inner membrane; Cell membrane; KW Chemotaxis; Complete proteome; Flagellar rotation; Membrane; KW Reference proteome. FT CHAIN 1 328 Flagellar motor switch protein FliM. FT /FTId=PRO_0000421240. FT REGION 1 45 Interaction with unphosphorylated CheY. FT {ECO:0000269|PubMed:16882724}. FT MUTAGEN 60 60 E->C: No appreciable effect on the FT binding affinity for CheY. FT {ECO:0000269|PubMed:16882724}. FT HELIX 7 16 {ECO:0000244|PDB:4IGA}. FT HELIX 49 73 {ECO:0000244|PDB:4FHR}. FT STRAND 79 88 {ECO:0000244|PDB:4FHR}. FT HELIX 89 95 {ECO:0000244|PDB:4FHR}. FT STRAND 101 107 {ECO:0000244|PDB:4FHR}. FT STRAND 114 118 {ECO:0000244|PDB:4FHR}. FT HELIX 120 130 {ECO:0000244|PDB:4FHR}. FT HELIX 145 165 {ECO:0000244|PDB:4FHR}. FT TURN 166 169 {ECO:0000244|PDB:4FHR}. FT STRAND 174 181 {ECO:0000244|PDB:4FHR}. FT HELIX 183 185 {ECO:0000244|PDB:4FHR}. FT STRAND 193 204 {ECO:0000244|PDB:4FHR}. FT STRAND 207 216 {ECO:0000244|PDB:4FHR}. FT HELIX 217 220 {ECO:0000244|PDB:4FHR}. FT HELIX 221 223 {ECO:0000244|PDB:4FHR}. FT TURN 228 232 {ECO:0000244|PDB:3SOH}. SQ SEQUENCE 328 AA; 37888 MW; 3E122C1FFAEBB093 CRC64; MSDVLSQEEI NQLIEALMKG ELKEEDLLKE EEEKKVKPYD FKRPSKFSKE QLRTFQMIHE NFGRALSTYL SGRLRTFVDV EISIDQLTYE EFIRSVMIPS FIVIFTGDVF EGSAIFEMRL DLFYTMLDII MGGPGENPPN RPPTEIETSI MRKEVTNMLT LLAQAWSDFQ YFIPSIENVE TNPQFVQIVP PNEIVLLVTA SVSWGEFTSF INVCWPFSLL EPLLEKLSDR FWMMGRKPEK VEERMEELRK ASQKIPVTVQ AVIGETELRL KEILDLEVGD VIRLGTHYKD EIRIDVEGRP KFRGIPGVFK GKYAVKVTGE FTNGGEYE // ID FLID_THEMA Reviewed; 608 AA. AC Q9X0K7; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 92. DE RecName: Full=Flagellar hook-associated protein 2; DE Short=HAP2; DE AltName: Full=Filament cap protein; DE AltName: Full=Flagellar cap protein; GN Name=fliD; OrderedLocusNames=TM_1123; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Required for the morphogenesis and for the elongation of CC the flagellar filament by facilitating polymerization of the CC flagellin monomers at the tip of growing filament. Forms a capping CC structure, which prevents flagellin subunits (transported through CC the central channel of the flagellum) from leaking out without CC polymerization at the distal end (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homopentamer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. CC -!- SIMILARITY: Belongs to the FliD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36199.1; -; Genomic_DNA. DR PIR; H72292; H72292. DR RefSeq; NP_228929.1; NC_000853.1. DR RefSeq; WP_004080294.1; NZ_CP011107.1. DR STRING; 243274.TM1123; -. DR DNASU; 898641; -. DR EnsemblBacteria; AAD36199; AAD36199; TM_1123. DR GeneID; 898641; -. DR KEGG; tma:TM1123; -. DR PATRIC; 23937181; VBITheMar51294_1139. DR eggNOG; ENOG4107V1F; Bacteria. DR eggNOG; COG1345; LUCA. DR InParanoid; Q9X0K7; -. DR KO; K02407; -. DR OMA; QEAYTEV; -. DR OrthoDB; EOG6H1PW8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009421; C:bacterial-type flagellum filament cap; IBA:GO_Central. DR GO; GO:0009424; C:bacterial-type flagellum hook; IEA:InterPro. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:InterPro. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IBA:GO_Central. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR InterPro; IPR010810; Flagellin_hook_IN_motif. DR InterPro; IPR010809; FliD_C. DR InterPro; IPR003481; FliD_N. DR Pfam; PF07196; Flagellin_IN; 2. DR Pfam; PF07195; FliD_C; 1. DR Pfam; PF02465; FliD_N; 1. PE 3: Inferred from homology; KW Bacterial flagellum; Coiled coil; Complete proteome; KW Reference proteome; Secreted. FT CHAIN 1 608 Flagellar hook-associated protein 2. FT /FTId=PRO_0000177025. FT COILED 47 75 {ECO:0000255}. SQ SEQUENCE 608 AA; 67511 MW; D680BF088C13A87D CRC64; MDLSKIASTI NMRYYSQLGG FQVGGAVSGL DTQSIINAIL EAESQPLQNL TEKYEKYELM QEAYTEVKTK LREFRDLVYS FKLQSTVVQK TAVSSSSLLS AEASSVAVTG VYHVKIVQTA TYTTLAGASE VVPPPDSTKT FGELDYMYTP QEGTVRLYNN ETGNYVEVQV LSTDTIDDIV SKLNSALSSA GITGSVSYDT STGKISITSD KNFSLVDITG NFTKVFHLDE ASLNYSGGNY SFTSTASVSG LSTAKTLQQI ATYTSKTIIS GKVKINGVEI DVDQNDTLSS LIEKINDSEA GVTASYDYHA NRVVIISKTS GPEAITLEDT YGTGLFSLLG IENHSLYVGQ KAHLQISMDG TNWADVYSDT NDVEYNGVTF HISGMTSETI TVDVRVDTDA IVEKIKEFVD KWNETMDYLN EKLTEESITD KDEEEMTEEE KMKGVLKGDD LLEEIFSRLR GFITYKAEGD INYLWELGIS TGDIGTGYEN MMKGHLEVDE EKLKQIVEED PNKVWEFFGG ENGFATQLDD YLWELVKFNG RIDQVAGISG RIEREQRFLA TQIASWIERL SKREQELWRK FSVMEEVISQ LQSQGSWISQ ALQGSSNK // ID FLIG_THEMA Reviewed; 335 AA. AC Q9WY63; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 124. DE RecName: Full=Flagellar motor switch protein FliG; GN Name=fliG; OrderedLocusNames=TM_0220; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF 209-214, AND X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) RP OF 235-335. RX PubMed=10440379; DOI=10.1038/22794; RA Lloyd S.A., Whitby F.G., Blair D.F., Hill C.P.; RT "Structure of the C-terminal domain of FliG, a component of the rotor RT in the bacterial flagellar motor."; RL Nature 400:472-475(1999). RN [3] RP SUBUNIT, INTERACTION WITH FLIF, AND NMR AND FLUORESCENCE SPECTROSCOPY RP OF N-TERMINUS. RX PubMed=22670715; DOI=10.1021/bi3004582; RA Levenson R., Zhou H., Dahlquist F.W.; RT "Structural insights into the interaction between the bacterial RT flagellar motor proteins FliF and FliG."; RL Biochemistry 51:5052-5060(2012). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 104-335. RX PubMed=12093724; DOI=10.1093/emboj/cdf332; RA Brown P.N., Hill C.P., Blair D.F.; RT "Crystal structure of the middle and C-terminal domains of the RT flagellar rotor protein FliG."; RL EMBO J. 21:3225-3234(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 117-193 IN COMPLEX WITH RP FLIM, INTERACTION WITH FLIM, AND MOTIF. RX PubMed=21673656; DOI=10.1038/emboj.2011.188; RA Paul K., Gonzalez-Bonet G., Bilwes A.M., Crane B.R., Blair D.; RT "Architecture of the flagellar rotor."; RL EMBO J. 30:2962-2971(2011). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 104-335 OF MUTANT DEL RP 170-172. RX PubMed=21572987; DOI=10.1371/journal.pbio.1000616; RA Minamino T., Imada K., Kinoshita M., Nakamura S., Morimoto Y.V., RA Namba K.; RT "Structural insight into the rotational switching mechanism of the RT bacterial flagellar motor."; RL PLoS Biol. 9:E1000616-E1000616(2011). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 115-327 IN COMPLEX WITH RP FLIM, AND INTERACTION WITH FLIM. RX PubMed=22896702; DOI=10.1074/jbc.C112.378380; RA Vartanian A.S., Paz A., Fortgang E.A., Abramson J., Dahlquist F.W.; RT "Structure of flagellar motor proteins in complex allows for insights RT into motor structure and switching."; RL J. Biol. Chem. 287:35779-35783(2012). CC -!- FUNCTION: One of the proteins that forms a switch complex that is CC proposed to be located at the base of the basal body. This complex CC interacts with chemotaxis proteins (such as CheY) in addition to CC contacting components of the motor that determine the direction of CC flagellar rotation (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer in the absence of FliF. Interacts (via N- CC terminus) with FliF (via C-terminus) forming a heterodimer. CC Interacts (via central domain or via central domain and C- CC terminus) with FliM (via central domain). CC {ECO:0000269|PubMed:21673656, ECO:0000269|PubMed:22670715, CC ECO:0000269|PubMed:22896702}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side CC {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FliG family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35312.1; -; Genomic_DNA. DR PIR; F72404; F72404. DR RefSeq; NP_228035.1; NC_000853.1. DR RefSeq; WP_004082903.1; NZ_CP011107.1. DR PDB; 1LKV; X-ray; 2.80 A; X=104-335. DR PDB; 1QC7; X-ray; 2.20 A; A/B=235-335. DR PDB; 3AJC; X-ray; 2.30 A; A=104-335. DR PDB; 3SOH; X-ray; 3.50 A; B/D=117-193. DR PDB; 4FHR; X-ray; 1.93 A; B=115-327. DR PDB; 4QRM; X-ray; 4.32 A; B/D/F/H/J/L/N/P/R/T/V=117-187. DR PDBsum; 1LKV; -. DR PDBsum; 1QC7; -. DR PDBsum; 3AJC; -. DR PDBsum; 3SOH; -. DR PDBsum; 4FHR; -. DR PDBsum; 4QRM; -. DR ProteinModelPortal; Q9WY63; -. DR SMR; Q9WY63; 115-327. DR IntAct; Q9WY63; 1. DR MINT; MINT-8212472; -. DR STRING; 243274.TM0220; -. DR EnsemblBacteria; AAD35312; AAD35312; TM_0220. DR GeneID; 897112; -. DR KEGG; tma:TM0220; -. DR PATRIC; 23935312; VBITheMar51294_0222. DR eggNOG; ENOG4105CS3; Bacteria. DR eggNOG; COG1536; LUCA. DR InParanoid; Q9WY63; -. DR KO; K02410; -. DR OMA; TLQVRPF; -. DR OrthoDB; EOG683S79; -. DR EvolutionaryTrace; Q9WY63; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003774; F:motor activity; IEA:InterPro. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR Gene3D; 1.10.220.30; -; 3. DR InterPro; IPR000090; Flg_Motor_Flig. DR InterPro; IPR023087; Flg_Motor_Flig_C. DR InterPro; IPR011002; FliG_a-hlx. DR InterPro; IPR032779; FliG_M. DR InterPro; IPR028263; FliG_N. DR PANTHER; PTHR30534; PTHR30534; 1. DR Pfam; PF01706; FliG_C; 1. DR Pfam; PF14841; FliG_M; 1. DR Pfam; PF14842; FliG_N; 1. DR PIRSF; PIRSF003161; FliG; 1. DR PRINTS; PR00954; FLGMOTORFLIG. DR SUPFAM; SSF48029; SSF48029; 2. DR TIGRFAMs; TIGR00207; fliG; 1. PE 1: Evidence at protein level; KW 3D-structure; Bacterial flagellum; Cell inner membrane; Cell membrane; KW Chemotaxis; Complete proteome; Direct protein sequencing; KW Flagellar rotation; Membrane; Reference proteome. FT CHAIN 1 335 Flagellar motor switch protein FliG. FT /FTId=PRO_0000184097. FT MOTIF 126 129 Part of the EHPQR-motif; important for FT interaction with FliM. FT SITE 161 161 Part of the EHPQR-motif; important for FT interaction with FliM. FT HELIX 109 111 {ECO:0000244|PDB:3AJC}. FT HELIX 116 123 {ECO:0000244|PDB:4FHR}. FT HELIX 128 136 {ECO:0000244|PDB:4FHR}. FT HELIX 140 148 {ECO:0000244|PDB:4FHR}. FT HELIX 152 154 {ECO:0000244|PDB:4FHR}. FT HELIX 155 164 {ECO:0000244|PDB:4FHR}. FT HELIX 170 183 {ECO:0000244|PDB:4FHR}. FT HELIX 190 192 {ECO:0000244|PDB:3SOH}. FT HELIX 198 207 {ECO:0000244|PDB:4FHR}. FT HELIX 210 223 {ECO:0000244|PDB:4FHR}. FT HELIX 225 235 {ECO:0000244|PDB:4FHR}. FT HELIX 238 243 {ECO:0000244|PDB:4FHR}. FT HELIX 246 253 {ECO:0000244|PDB:4FHR}. FT HELIX 258 265 {ECO:0000244|PDB:4FHR}. FT HELIX 270 277 {ECO:0000244|PDB:4FHR}. FT HELIX 282 294 {ECO:0000244|PDB:4FHR}. FT HELIX 300 319 {ECO:0000244|PDB:4FHR}. SQ SEQUENCE 335 AA; 37816 MW; 64C41D122622ABDA CRC64; MPEKKIDGRR KAAVLLVALG PEKAAQVMKH LDEETVEQLV VEIANIGRVT PEEKKQVLEE FLSLAKAKEM ISEGGIEYAK KVLEKAFGPE RARKIIERLT SSLQVKPFSF VRDTDPVQLV NFLQSEHPQT IAVVLSYLDP PVAAQILGAL PEELQTEVLK RIALLERTSP EVVKEIERNL EKKISGFVSR TFSKVGGIDT AAEIMNNLDR TTEKKIMDKL VQENPELADE IRRRMFVFED ILKLDDRSIQ LVLREVDTRD LALALKGASD ELKEKIFKNM SKRAAALLKD ELEYMGPVRL KDVEEAQQKI INIIRRLEEA GEIVIARGGG EELIM // ID G3P_THEMA Reviewed; 333 AA. AC P17721; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 13-APR-2016, entry version 141. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:7877172}; DE Short=GAPDH {ECO:0000303|PubMed:7877172}; DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P09124}; DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:7877172}; GN Name=gap; OrderedLocusNames=TM_0688; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8508805; DOI=10.1111/j.1432-1033.1993.tb17894.x; RA Tomschy A., Glockhuber R., Jaenicke R.; RT "Functional expression of D-glyceraldehyde-3-phosphate dehydrogenase RT from the hyperthermophilic eubacterium Thermotoga maritima in RT Escherichia coli. Authenticity and kinetic properties of the RT recombinant enzyme."; RL Eur. J. Biochem. 214:43-50(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP PROTEIN SEQUENCE OF 2-333. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=2401296; DOI=10.1111/j.1432-1033.1990.tb19190.x; RA Schultes V., Deutzmann R., Jaenicke R.; RT "Complete amino-acid sequence of glyceraldehyde-3-phosphate RT dehydrogenase from the hyperthermophilic eubacterium Thermotoga RT maritima."; RL Eur. J. Biochem. 192:25-31(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND RP SUBSTRATE ANALOG, AND SUBUNIT. RX PubMed=7877172; DOI=10.1006/jmbi.1994.0103; RA Korndoerfer I., Steipe B., Huber R., Tomschy A., Jaenicke R.; RT "The crystal structure of holo-glyceraldehyde-3-phosphate RT dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima RT at 2.5-A resolution."; RL J. Mol. Biol. 246:511-521(1995). CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of CC glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) CC using the cofactor NAD. The first reaction step involves the CC formation of a hemiacetal intermediate between G3P and a cysteine CC residue, and this hemiacetal intermediate is then oxidized to a CC thioester, with concomitant reduction of NAD to NADH. The reduced CC NADH is then exchanged with the second NAD, and the thioester is CC attacked by a nucleophilic inorganic phosphate to produce BPG. CC {ECO:0000250|UniProtKB:P00362}. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC {ECO:0000250|UniProtKB:P09124}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7877172}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X72629; CAA51205.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35770.1; -; Genomic_DNA. DR PIR; S33325; DEHGGT. DR RefSeq; NP_228497.1; NC_000853.1. DR RefSeq; WP_004081074.1; NZ_CP011107.1. DR PDB; 1HDG; X-ray; 2.50 A; O/Q=2-333. DR PDBsum; 1HDG; -. DR ProteinModelPortal; P17721; -. DR SMR; P17721; 2-333. DR STRING; 243274.TM0688; -. DR EnsemblBacteria; AAD35770; AAD35770; TM_0688. DR GeneID; 898355; -. DR KEGG; tma:TM0688; -. DR PATRIC; 23936294; VBITheMar51294_0700. DR eggNOG; ENOG4105C17; Bacteria. DR eggNOG; COG0057; LUCA. DR InParanoid; P17721; -. DR KO; K00134; -. DR OMA; FVRVLSW; -. DR OrthoDB; EOG66TG3S; -. DR BioCyc; MetaCyc:MONOMER-401; -. DR UniPathway; UPA00109; UER00184. DR EvolutionaryTrace; P17721; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10836; PTHR10836; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR SMART; SM00846; Gp_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; KW Glycolysis; NAD; Nucleotide-binding; Oxidoreductase; KW Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2401296}. FT CHAIN 2 333 Glyceraldehyde-3-phosphate dehydrogenase. FT /FTId=PRO_0000145711. FT NP_BIND 11 12 NAD. {ECO:0000269|PubMed:7877172}. FT REGION 151 153 Glyceraldehyde 3-phosphate binding. FT {ECO:0000269|PubMed:7877172}. FT REGION 210 211 Glyceraldehyde 3-phosphate binding. FT {ECO:0000269|PubMed:7877172}. FT ACT_SITE 152 152 Nucleophile. FT {ECO:0000250|UniProtKB:P00362}. FT BINDING 35 35 NAD. {ECO:0000269|PubMed:7877172}. FT BINDING 121 121 NAD. {ECO:0000269|PubMed:7877172}. FT BINDING 182 182 Glyceraldehyde 3-phosphate. FT {ECO:0000269|PubMed:7877172}. FT BINDING 183 183 NAD. {ECO:0000269|PubMed:7877172}. FT BINDING 197 197 Glyceraldehyde 3-phosphate. FT {ECO:0000269|PubMed:7877172}. FT BINDING 233 233 Glyceraldehyde 3-phosphate. FT {ECO:0000269|PubMed:7877172}. FT BINDING 315 315 NAD. {ECO:0000269|PubMed:7877172}. FT SITE 179 179 Activates thiol group during catalysis. FT {ECO:0000250|UniProtKB:Q6GIL8}. FT STRAND 3 7 {ECO:0000244|PDB:1HDG}. FT HELIX 11 23 {ECO:0000244|PDB:1HDG}. FT STRAND 29 34 {ECO:0000244|PDB:1HDG}. FT HELIX 39 47 {ECO:0000244|PDB:1HDG}. FT TURN 50 52 {ECO:0000244|PDB:1HDG}. FT STRAND 59 61 {ECO:0000244|PDB:1HDG}. FT STRAND 63 68 {ECO:0000244|PDB:1HDG}. FT STRAND 71 76 {ECO:0000244|PDB:1HDG}. FT HELIX 81 83 {ECO:0000244|PDB:1HDG}. FT HELIX 86 89 {ECO:0000244|PDB:1HDG}. FT STRAND 93 96 {ECO:0000244|PDB:1HDG}. FT STRAND 98 100 {ECO:0000244|PDB:1HDG}. FT HELIX 104 107 {ECO:0000244|PDB:1HDG}. FT HELIX 109 112 {ECO:0000244|PDB:1HDG}. FT STRAND 116 122 {ECO:0000244|PDB:1HDG}. FT STRAND 128 130 {ECO:0000244|PDB:1HDG}. FT TURN 133 135 {ECO:0000244|PDB:1HDG}. FT HELIX 137 139 {ECO:0000244|PDB:1HDG}. FT STRAND 146 148 {ECO:0000244|PDB:1HDG}. FT HELIX 152 168 {ECO:0000244|PDB:1HDG}. FT STRAND 170 180 {ECO:0000244|PDB:1HDG}. FT STRAND 185 189 {ECO:0000244|PDB:1HDG}. FT TURN 195 198 {ECO:0000244|PDB:1HDG}. FT HELIX 201 203 {ECO:0000244|PDB:1HDG}. FT STRAND 206 208 {ECO:0000244|PDB:1HDG}. FT HELIX 212 219 {ECO:0000244|PDB:1HDG}. FT HELIX 221 223 {ECO:0000244|PDB:1HDG}. FT TURN 224 226 {ECO:0000244|PDB:1HDG}. FT STRAND 227 235 {ECO:0000244|PDB:1HDG}. FT STRAND 240 250 {ECO:0000244|PDB:1HDG}. FT HELIX 254 265 {ECO:0000244|PDB:1HDG}. FT TURN 266 272 {ECO:0000244|PDB:1HDG}. FT STRAND 273 276 {ECO:0000244|PDB:1HDG}. FT HELIX 282 285 {ECO:0000244|PDB:1HDG}. FT STRAND 291 295 {ECO:0000244|PDB:1HDG}. FT TURN 296 298 {ECO:0000244|PDB:1HDG}. FT STRAND 300 302 {ECO:0000244|PDB:1HDG}. FT TURN 303 305 {ECO:0000244|PDB:1HDG}. FT STRAND 306 313 {ECO:0000244|PDB:1HDG}. FT HELIX 317 329 {ECO:0000244|PDB:1HDG}. FT HELIX 330 332 {ECO:0000244|PDB:1HDG}. SQ SEQUENCE 333 AA; 36425 MW; 12B77104AB5E1CD0 CRC64; MARVAINGFG RIGRLVYRII YERKNPDIEV VAINDLTDTK TLAHLLKYDS VHKKFPGKVE YTENSLIVDG KEIKVFAEPD PSKLPWKDLG VDFVIESTGV FRNREKAELH LQAGAKKVII TAPAKGEDIT VVIGCNEDQL KPEHTIISCA SCTTNSIAPI VKVLHEKFGI VSGMLTTVHS YTNDQRVLDL PHKDLRRARA AAVNIIPTTT GAAKAVALVV PEVKGKLDGM AIRVPTPDGS ITDLTVLVEK ETTVEEVNAV MKEATEGRLK GIIGYNDEPI VSSDIIGTTF SGIFDATITN VIGGKLVKVA SWYDNEYGYS NRVVDTLELL LKM // ID FOLD_THEMA Reviewed; 271 AA. AC Q9X288; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Bifunctional protein FolD {ECO:0000255|HAMAP-Rule:MF_01576}; DE Includes: DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01576}; DE EC=1.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01576}; DE Includes: DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01576}; DE EC=3.5.4.9 {ECO:0000255|HAMAP-Rule:MF_01576}; GN Name=folD {ECO:0000255|HAMAP-Rule:MF_01576}; GN OrderedLocusNames=TM_1767; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the oxidation of 5,10- CC methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and CC then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- CC formyltetrahydrofolate. {ECO:0000255|HAMAP-Rule:MF_01576}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP(+) = CC 5,10-methenyltetrahydrofolate + NADPH. {ECO:0000255|HAMAP- CC Rule:MF_01576}. CC -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10- CC formyltetrahydrofolate. {ECO:0000255|HAMAP-Rule:MF_01576}. CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000255|HAMAP-Rule:MF_01576}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01576}. CC -!- SIMILARITY: Belongs to the tetrahydrofolate CC dehydrogenase/cyclohydrolase family. {ECO:0000255|HAMAP- CC Rule:MF_01576}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36831.1; -; Genomic_DNA. DR PIR; F72212; F72212. DR RefSeq; NP_229564.1; NC_000853.1. DR RefSeq; WP_004082313.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X288; -. DR STRING; 243274.TM1767; -. DR EnsemblBacteria; AAD36831; AAD36831; TM_1767. DR GeneID; 897086; -. DR KEGG; tma:TM1767; -. DR PATRIC; 23938514; VBITheMar51294_1786. DR eggNOG; ENOG4105CN0; Bacteria. DR eggNOG; COG0190; LUCA. DR InParanoid; Q9X288; -. DR KO; K01491; -. DR OMA; LMFNTIK; -. DR OrthoDB; EOG6K6VBB; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IBA:GO_Central. DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IBA:GO_Central. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01576; THF_DHG_CYH; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000672; THF_DH/CycHdrlase. DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom. DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom. DR Pfam; PF00763; THF_DHG_CYH; 1. DR Pfam; PF02882; THF_DHG_CYH_C; 1. DR PRINTS; PR00085; THFDHDRGNASE. DR SUPFAM; SSF51735; SSF51735; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Hydrolase; Methionine biosynthesis; Multifunctional enzyme; NADP; KW One-carbon metabolism; Oxidoreductase; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 271 Bifunctional protein FolD. FT /FTId=PRO_0000268544. FT NP_BIND 154 156 NADP. {ECO:0000255|HAMAP-Rule:MF_01576}. FT BINDING 181 181 NADP. {ECO:0000255|HAMAP-Rule:MF_01576}. FT BINDING 222 222 NADP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01576}. SQ SEQUENCE 271 AA; 29557 MW; 32F46E4AAC99F09C CRC64; MWIDCKTIAR SIEERTKERV EKLGFTPKLV SVACTDDPSA LSYLKSQRKK AEKLGIAFEI MNVSPEEIVS TLKKLGSDES VNGVFVARPF PLGLDEKEIL SSVPVEKDVE GVNPANLGLL LYDEEIFPPC TAEAAVRILE RETNLSGKRV TVVGRSVTVG KPLALMLLKK GRDATVTVCH SRTVNLEEIT KNSDIVVVAV GRAHFLKKNM VKEGAIVIDV GINYVDGKLQ GDVDPSVEEI ARVTPVPGGV GQVTTALLFE HVVRAAERQR K // ID G6PD_THEMA Reviewed; 496 AA. AC Q9X0N9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966}; DE Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966}; DE EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966}; GN Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966}; OrderedLocusNames=TM_1155; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6- CC phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966}. CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = 6-phospho-D- CC glucono-1,5-lactone + NADPH. {ECO:0000255|HAMAP-Rule:MF_00966}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 1/3. {ECO:0000255|HAMAP-Rule:MF_00966}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase CC family. {ECO:0000255|HAMAP-Rule:MF_00966}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36231.1; -; Genomic_DNA. DR PIR; G72289; G72289. DR RefSeq; NP_228961.1; NC_000853.1. DR RefSeq; WP_004080226.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0N9; -. DR STRING; 243274.TM1155; -. DR PRIDE; Q9X0N9; -. DR EnsemblBacteria; AAD36231; AAD36231; TM_1155. DR GeneID; 898331; -. DR KEGG; tma:TM1155; -. DR PATRIC; 23937247; VBITheMar51294_1172. DR eggNOG; ENOG4105D8W; Bacteria. DR eggNOG; COG0364; LUCA. DR InParanoid; Q9X0N9; -. DR KO; K00036; -. DR OMA; TIFEPIW; -. DR OrthoDB; EOG61308Z; -. DR SABIO-RK; Q9X0N9; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00966; G6PD; 1. DR InterPro; IPR001282; G6P_DH. DR InterPro; IPR019796; G6P_DH_AS. DR InterPro; IPR022675; G6P_DH_C. DR InterPro; IPR022674; G6P_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR23429; PTHR23429; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00871; zwf; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 496 Glucose-6-phosphate 1-dehydrogenase. FT /FTId=PRO_0000068136. FT NP_BIND 31 38 NADP. {ECO:0000255|HAMAP-Rule:MF_00966}. FT ACT_SITE 245 245 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00966}. FT BINDING 65 65 NADP. {ECO:0000255|HAMAP-Rule:MF_00966}. FT BINDING 153 153 NADP. {ECO:0000255|HAMAP-Rule:MF_00966}. FT BINDING 183 183 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00966}. FT BINDING 187 187 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00966}. FT BINDING 221 221 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00966}. FT BINDING 240 240 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00966}. FT BINDING 345 345 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00966}. FT BINDING 350 350 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00966}. SQ SEQUENCE 496 AA; 57536 MW; 572106FCE08F20E8 CRC64; MKCSLGLEKC PDDTLRCFPK IEQPFGIVIF GASGDLTKRK LIPALNRLFE AGILPERFFV LGAARTKMDD KKFRSRFDAN PDFLEHCSYI SVDYQDPESF KQLKNTIETL IKRIDSSNLV FYLAVPPDLY IPILENLSKT GLNEKPARVV IEKPFGKDLE SARRLEDTLQ KYFQEDQIFR IDHYLGKETV QNILVFRFAN FIFEEIWNNK FVDHVQITMA EDIGVEHRAG YFENVGLLRD IFQNHMLQIL ALIAMEPPSS FNGENFRNER VKLLRSIRPF PVEELESWIV RGQYGRGVVN GKEVPAYREE PGVAKDSNVE TFVAMKLFID NWRWSGVPFY LRSGKRLPKK ITEVAVVFKK IPHSIFAGVP SDELEPNTIV FTLQPNEGIS LEFQVKRPCP GMFPQLLSMD FRYEDYFGVK LPDAYERLLL DVILGDPTLF MRRDDLEVSW ELLDPVLKAW ENDPVRFSPY VYPAGTWGPR EADLLIERDG RKWRKL // ID FMT_THEMA Reviewed; 313 AA. AC Q9WYZ8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=Methionyl-tRNA formyltransferase; DE EC=2.1.2.9; GN Name=fmt; OrderedLocusNames=TM_0528; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Modifies the free amino group of the aminoacyl moiety of CC methionyl-tRNA(fMet). The formyl group appears to play a dual role CC in the initiator identity of N-formylmethionyl-tRNA by: (I) CC promoting its recognition by IF2 and (II) impairing its binding to CC EFTu-GTP (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl- CC tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35613.1; -; Genomic_DNA. DR PIR; F72366; F72366. DR RefSeq; NP_228338.1; NC_000853.1. DR RefSeq; WP_004081384.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYZ8; -. DR STRING; 243274.TM0528; -. DR EnsemblBacteria; AAD35613; AAD35613; TM_0528. DR GeneID; 897580; -. DR KEGG; tma:TM0528; -. DR PATRIC; 23935963; VBITheMar51294_0536. DR eggNOG; ENOG4105CAE; Bacteria. DR eggNOG; COG0223; LUCA. DR InParanoid; Q9WYZ8; -. DR KO; K00604; -. DR OMA; GCINSHA; -. DR OrthoDB; EOG6B09WV; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IBA:GO_Central. DR GO; GO:0006413; P:translational initiation; IBA:GOC. DR Gene3D; 3.10.25.10; -; 1. DR Gene3D; 3.40.50.170; -; 1. DR HAMAP; MF_00182; Formyl_trans; 1. DR InterPro; IPR005794; Fmt. DR InterPro; IPR005793; Formyl_trans_C. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR011034; Formyl_transferase_C-like. DR InterPro; IPR001555; GART_AS. DR Pfam; PF02911; Formyl_trans_C; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR SUPFAM; SSF50486; SSF50486; 1. DR SUPFAM; SSF53328; SSF53328; 1. DR TIGRFAMs; TIGR00460; fmt; 1. DR PROSITE; PS00373; GART; 1. PE 3: Inferred from homology; KW Complete proteome; Protein biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 313 Methionyl-tRNA formyltransferase. FT /FTId=PRO_0000083071. FT REGION 109 112 Tetrahydrofolate (THF) binding. FT {ECO:0000250}. SQ SEQUENCE 313 AA; 35328 MW; 5CB94FEA0CF06202 CRC64; MRIVFVGTPE FAAEILEHLI KNGFNVVGVV TQPDKPRGRG RKVAPTPVKA VAEKHEVPFI QPESINKKEA LEFLRSVRPD VIIVASYGKI LGEKVLSLPR LGCYNIHPSL LPKYRGASPI QRVLENGEER TGVTIYKMVK ELDAGPIALQ KEISVDPFET FDQLEKRLIE LSKEMLIEFL EKLKTGNIEL KEQDHSRATY APMIKKEDLI VDFSKDAESV KNKIRAYDSR PGARAFLGNV EVKLFGVTAI DSSGDEPGLI NYIDREGAWI GTGDGKVKVR YIQFPGKKKM TFWEAKNGRL IIEGMRFERR YES // ID FTHS_THEMA Reviewed; 542 AA. AC Q9X287; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543}; DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543}; DE AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543}; DE Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543}; DE Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543}; GN Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=TM_1766; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + formate + tetrahydrofolate = ADP + CC phosphate + 10-formyltetrahydrofolate. {ECO:0000255|HAMAP- CC Rule:MF_01543}. CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000255|HAMAP-Rule:MF_01543}. CC -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase CC family. {ECO:0000255|HAMAP-Rule:MF_01543}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36830.1; -; Genomic_DNA. DR PIR; E72212; E72212. DR RefSeq; NP_229563.1; NC_000853.1. DR RefSeq; WP_010865397.1; NZ_CP011107.1. DR PDB; 3DO6; X-ray; 1.85 A; A/B=1-542. DR PDBsum; 3DO6; -. DR ProteinModelPortal; Q9X287; -. DR SMR; Q9X287; 1-540. DR STRING; 243274.TM1766; -. DR EnsemblBacteria; AAD36830; AAD36830; TM_1766. DR GeneID; 897854; -. DR KEGG; tma:TM1766; -. DR PATRIC; 23938512; VBITheMar51294_1785. DR eggNOG; ENOG4105CKU; Bacteria. DR eggNOG; COG2759; LUCA. DR InParanoid; Q9X287; -. DR KO; K01938; -. DR OMA; CGEIMTM; -. DR OrthoDB; EOG6PCPSP; -. DR BioCyc; TMAR243274:GC6P-1815-MONOMER; -. DR UniPathway; UPA00193; -. DR EvolutionaryTrace; Q9X287; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_01543; FTHFS; 1. DR InterPro; IPR000559; Formate_THF_ligase. DR InterPro; IPR020628; Formate_THF_ligase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01268; FTHFS; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00721; FTHFS_1; 1. DR PROSITE; PS00722; FTHFS_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Ligase; KW Nucleotide-binding; One-carbon metabolism; Reference proteome. FT CHAIN 1 542 Formate--tetrahydrofolate ligase. FT /FTId=PRO_0000199403. FT NP_BIND 53 60 ATP. {ECO:0000255|HAMAP-Rule:MF_01543}. FT HELIX 4 10 {ECO:0000244|PDB:3DO6}. FT HELIX 15 17 {ECO:0000244|PDB:3DO6}. FT STRAND 18 21 {ECO:0000244|PDB:3DO6}. FT TURN 22 24 {ECO:0000244|PDB:3DO6}. FT STRAND 25 28 {ECO:0000244|PDB:3DO6}. FT HELIX 32 35 {ECO:0000244|PDB:3DO6}. FT TURN 36 38 {ECO:0000244|PDB:3DO6}. FT STRAND 43 51 {ECO:0000244|PDB:3DO6}. FT HELIX 59 72 {ECO:0000244|PDB:3DO6}. FT STRAND 77 81 {ECO:0000244|PDB:3DO6}. FT HELIX 86 91 {ECO:0000244|PDB:3DO6}. FT STRAND 102 106 {ECO:0000244|PDB:3DO6}. FT HELIX 107 111 {ECO:0000244|PDB:3DO6}. FT TURN 112 115 {ECO:0000244|PDB:3DO6}. FT HELIX 117 137 {ECO:0000244|PDB:3DO6}. FT STRAND 144 149 {ECO:0000244|PDB:3DO6}. FT STRAND 153 157 {ECO:0000244|PDB:3DO6}. FT HELIX 160 162 {ECO:0000244|PDB:3DO6}. FT STRAND 163 168 {ECO:0000244|PDB:3DO6}. FT HELIX 172 174 {ECO:0000244|PDB:3DO6}. FT STRAND 178 180 {ECO:0000244|PDB:3DO6}. FT STRAND 182 184 {ECO:0000244|PDB:3DO6}. FT HELIX 185 187 {ECO:0000244|PDB:3DO6}. FT HELIX 189 196 {ECO:0000244|PDB:3DO6}. FT HELIX 200 208 {ECO:0000244|PDB:3DO6}. FT STRAND 211 215 {ECO:0000244|PDB:3DO6}. FT STRAND 220 222 {ECO:0000244|PDB:3DO6}. FT HELIX 223 226 {ECO:0000244|PDB:3DO6}. FT HELIX 229 235 {ECO:0000244|PDB:3DO6}. FT TURN 236 240 {ECO:0000244|PDB:3DO6}. FT STRAND 243 247 {ECO:0000244|PDB:3DO6}. FT STRAND 252 255 {ECO:0000244|PDB:3DO6}. FT STRAND 261 264 {ECO:0000244|PDB:3DO6}. FT HELIX 270 279 {ECO:0000244|PDB:3DO6}. FT STRAND 281 290 {ECO:0000244|PDB:3DO6}. FT TURN 291 293 {ECO:0000244|PDB:3DO6}. FT HELIX 294 300 {ECO:0000244|PDB:3DO6}. FT HELIX 302 306 {ECO:0000244|PDB:3DO6}. FT STRAND 311 317 {ECO:0000244|PDB:3DO6}. FT HELIX 319 325 {ECO:0000244|PDB:3DO6}. FT HELIX 330 332 {ECO:0000244|PDB:3DO6}. FT HELIX 338 357 {ECO:0000244|PDB:3DO6}. FT STRAND 362 367 {ECO:0000244|PDB:3DO6}. FT HELIX 374 385 {ECO:0000244|PDB:3DO6}. FT TURN 386 388 {ECO:0000244|PDB:3DO6}. FT STRAND 390 394 {ECO:0000244|PDB:3DO6}. FT HELIX 396 399 {ECO:0000244|PDB:3DO6}. FT HELIX 400 403 {ECO:0000244|PDB:3DO6}. FT HELIX 405 414 {ECO:0000244|PDB:3DO6}. FT HELIX 430 440 {ECO:0000244|PDB:3DO6}. FT STRAND 445 449 {ECO:0000244|PDB:3DO6}. FT HELIX 451 462 {ECO:0000244|PDB:3DO6}. FT STRAND 470 473 {ECO:0000244|PDB:3DO6}. FT STRAND 476 481 {ECO:0000244|PDB:3DO6}. FT STRAND 493 496 {ECO:0000244|PDB:3DO6}. FT STRAND 498 502 {ECO:0000244|PDB:3DO6}. FT TURN 503 506 {ECO:0000244|PDB:3DO6}. FT STRAND 507 511 {ECO:0000244|PDB:3DO6}. FT HELIX 526 529 {ECO:0000244|PDB:3DO6}. FT STRAND 538 540 {ECO:0000244|PDB:3DO6}. SQ SEQUENCE 542 AA; 58538 MW; BC3AE16461AF326E CRC64; MKPIKEIADQ LELKDDILYP YGHYIAKIDH RFLKSLENHE DGKLILVTAV TPTPAGEGKT TTSIGLSMSL NRIGKKSIVT LREPSLGPTL GLKGGATGGG RSRVLPSDEI NLHFTGDMHA VASAHNLLAA VLDSHIKHGN ELKIDITRVF WKRTMDMNDR ALRSIVIGLG GSANGFPRED SFIITAASEV MAILALSENM KDLKERLGKI IVALDADRKI VRISDLGIQG AMAVLLKDAI NPNLVQTTEG TPALIHCGPF ANIAHGTNSI IATKMAMKLS EYTVTEAGFG ADLGAEKFID FVSRVGGFYP NAAVLVATVR ALKYHGGANL KNIHEENLEA LKEGFKNLRV HVENLRKFNL PVVVALNRFS TDTEKEIAYV VKECEKLGVR VAVSEVFKKG SEGGVELAKA VAEAAKDVEP AYLYEMNDPV EKKIEILAKE IYRAGRVEFS DTAKNALKFI KKHGFDELPV IVAKTPKSIS HDPSLRGAPE GYTFVVSDLF VSAGAGFVVA LSGDINLMPG LPKKPNALNM DVDDSGNIVG VS // ID FTSH_THEMA Reviewed; 610 AA. AC Q9WZ49; DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 119. DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458}; DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458}; GN Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; GN OrderedLocusNames=TM_0580; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 147-610 WITH BOUND ADP, RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF ASP-500. RX PubMed=16484367; DOI=10.1073/pnas.0600031103; RA Bieniossek C., Schalch T., Bumann M., Meister M., Meier R., RA Baumann U.; RT "The molecular architecture of the metalloprotease FtsH."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3066-3071(2006). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 147-610 OF MUTANT ALA-207 RP WITHOUT NUCLEOTIDE, SUBUNIT, AND MUTAGENESIS OF GLY-404. RX PubMed=19955424; DOI=10.1073/pnas.0910708106; RA Bieniossek C., Niederhauser B., Baumann U.M.; RT "The crystal structure of apo-FtsH reveals domain movements necessary RT for substrate unfolding and translocation."; RL Proc. Natl. Acad. Sci. U.S.A. 106:21579-21584(2009). CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc CC metallopeptidase for both cytoplasmic and membrane proteins. Plays CC a role in the quality control of integral membrane proteins. CC {ECO:0000255|HAMAP-Rule:MF_01458}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01458}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01458}; CC -!- SUBUNIT: The isolated ADP-bound cytosolic domain forms a 6-fold CC symmetric protease disk and a 2-fold symmetric AAA ATPase ring. In CC the absence of nucleotide the AAA ATPase ring also forms symmetric CC hexamers. {ECO:0000269|PubMed:16484367, CC ECO:0000269|PubMed:19955424}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_01458}. CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase CC family. {ECO:0000255|HAMAP-Rule:MF_01458}. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase CC M41 family. {ECO:0000255|HAMAP-Rule:MF_01458}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35665.1; -; Genomic_DNA. DR PIR; E72358; E72358. DR RefSeq; NP_228390.1; NC_000853.1. DR RefSeq; WP_004081278.1; NZ_CP011107.1. DR PDB; 2CE7; X-ray; 2.44 A; A/B/C/D/E/F=147-610. DR PDB; 2CEA; X-ray; 2.75 A; A/B/C/D/E/F=147-610. DR PDB; 3KDS; X-ray; 2.60 A; E/F/G=147-610. DR PDB; 4M8A; X-ray; 1.50 A; A/B/C=34-101. DR PDB; 4Q0F; X-ray; 1.95 A; A/B/C=34-101. DR PDBsum; 2CE7; -. DR PDBsum; 2CEA; -. DR PDBsum; 3KDS; -. DR PDBsum; 4M8A; -. DR PDBsum; 4Q0F; -. DR ProteinModelPortal; Q9WZ49; -. DR SMR; Q9WZ49; 150-606. DR DIP; DIP-49026N; -. DR STRING; 243274.TM0580; -. DR MEROPS; M41.021; -. DR DNASU; 897649; -. DR EnsemblBacteria; AAD35665; AAD35665; TM_0580. DR GeneID; 897649; -. DR KEGG; tma:TM0580; -. DR PATRIC; 23936071; VBITheMar51294_0589. DR eggNOG; ENOG4105C3H; Bacteria. DR eggNOG; COG0465; LUCA. DR InParanoid; Q9WZ49; -. DR KO; K03798; -. DR OMA; HTEAWTI; -. DR OrthoDB; EOG6PKFBJ; -. DR BRENDA; 3.4.24.B17; 6331. DR BRENDA; 3.4.24.B20; 6331. DR EvolutionaryTrace; Q9WZ49; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030163; P:protein catabolic process; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01458; FtsH; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR005936; FtsH. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011546; Pept_M41_FtsH_extracell. DR InterPro; IPR000642; Peptidase_M41. DR Pfam; PF00004; AAA; 1. DR Pfam; PF06480; FtsH_ext; 1. DR Pfam; PF01434; Peptidase_M41; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01241; FtsH_fam; 1. DR PROSITE; PS00674; AAA; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; KW Complete proteome; Hydrolase; Membrane; Metal-binding; KW Metalloprotease; Nucleotide-binding; Protease; Reference proteome; KW Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1 610 ATP-dependent zinc metalloprotease FtsH. FT /FTId=PRO_0000400412. FT TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TRANSMEM 6 26 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TOPO_DOM 27 107 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TRANSMEM 108 128 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TOPO_DOM 129 610 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT NP_BIND 204 208 ATP. FT ACT_SITE 424 424 {ECO:0000255|HAMAP-Rule:MF_01458}. FT METAL 423 423 Zinc; catalytic. FT METAL 427 427 Zinc; catalytic. FT METAL 500 500 Zinc; catalytic. FT BINDING 164 164 ATP; via amide nitrogen and carbonyl FT oxygen. FT BINDING 209 209 ATP; via amide nitrogen. FT BINDING 343 343 ATP. FT BINDING 371 371 ATP. FT MUTAGEN 404 404 G->L: Complete loss of protease activity FT and of oligomerization. FT {ECO:0000269|PubMed:19955424}. FT MUTAGEN 500 500 D->A: Complete loss of protease activity. FT {ECO:0000269|PubMed:16484367}. FT HELIX 38 46 {ECO:0000244|PDB:4M8A}. FT STRAND 52 57 {ECO:0000244|PDB:4M8A}. FT STRAND 61 67 {ECO:0000244|PDB:4M8A}. FT STRAND 72 76 {ECO:0000244|PDB:4M8A}. FT HELIX 78 80 {ECO:0000244|PDB:4M8A}. FT HELIX 84 92 {ECO:0000244|PDB:4M8A}. FT STRAND 96 99 {ECO:0000244|PDB:4M8A}. FT HELIX 160 162 {ECO:0000244|PDB:2CE7}. FT HELIX 167 181 {ECO:0000244|PDB:2CE7}. FT HELIX 184 187 {ECO:0000244|PDB:2CE7}. FT TURN 188 190 {ECO:0000244|PDB:2CE7}. FT STRAND 195 200 {ECO:0000244|PDB:2CE7}. FT HELIX 207 218 {ECO:0000244|PDB:2CE7}. FT STRAND 222 226 {ECO:0000244|PDB:2CE7}. FT HELIX 227 229 {ECO:0000244|PDB:2CE7}. FT TURN 230 232 {ECO:0000244|PDB:2CE7}. FT HELIX 237 251 {ECO:0000244|PDB:2CE7}. FT STRAND 254 260 {ECO:0000244|PDB:2CE7}. FT HELIX 262 264 {ECO:0000244|PDB:2CE7}. FT HELIX 279 293 {ECO:0000244|PDB:2CE7}. FT HELIX 296 298 {ECO:0000244|PDB:2CE7}. FT STRAND 300 307 {ECO:0000244|PDB:2CE7}. FT HELIX 309 311 {ECO:0000244|PDB:2CE7}. FT HELIX 314 317 {ECO:0000244|PDB:2CE7}. FT STRAND 324 327 {ECO:0000244|PDB:2CE7}. FT HELIX 333 344 {ECO:0000244|PDB:2CE7}. FT HELIX 355 360 {ECO:0000244|PDB:2CE7}. FT HELIX 367 383 {ECO:0000244|PDB:2CE7}. FT STRAND 387 389 {ECO:0000244|PDB:2CE7}. FT HELIX 391 401 {ECO:0000244|PDB:2CE7}. FT HELIX 414 433 {ECO:0000244|PDB:2CE7}. FT STRAND 442 444 {ECO:0000244|PDB:2CE7}. FT HELIX 453 456 {ECO:0000244|PDB:2CE7}. FT HELIX 469 479 {ECO:0000244|PDB:2CE7}. FT HELIX 481 490 {ECO:0000244|PDB:2CE7}. FT HELIX 495 497 {ECO:0000244|PDB:2CE7}. FT HELIX 498 513 {ECO:0000244|PDB:2CE7}. FT TURN 519 521 {ECO:0000244|PDB:2CE7}. FT HELIX 547 574 {ECO:0000244|PDB:2CE7}. FT HELIX 576 589 {ECO:0000244|PDB:2CE7}. FT STRAND 590 593 {ECO:0000244|PDB:2CE7}. FT HELIX 594 600 {ECO:0000244|PDB:2CE7}. SQ SEQUENCE 610 AA; 68099 MW; 83F76468C8495DDF CRC64; MNRSNIWNLL FTILIIVTLF WLARFFYVEN SPVSKLSYTS FVQMVEDERS VVSEVVIRDD GVLRVYTKDG RVYEVDAPWA VNDSQLIEKL VSKGIKVSGE RSGSSSFWIN VLGTLIPTIL FIVVWLFIMR SLSGRNNQAF TFTKSRATMY KPSGNKRVTF KDVGGAEEAI EELKEVVEFL KDPSKFNRIG ARMPKGILLV GPPGTGKTLL ARAVAGEANV PFFHISGSDF VELFVGVGAA RVRDLFAQAK AHAPCIVFID EIDAVGRHRG AGLGGGHDER EQTLNQLLVE MDGFDSKEGI IVMAATNRPD ILDPALLRPG RFDKKIVVDP PDMLGRKKIL EIHTRNKPLA EDVNLEIIAK RTPGFVGADL ENLVNEAALL AAREGRDKIT MKDFEEAIDR VIAGPARKSK LISPKEKRII AYHEAGHAVV STVVPNGEPV HRISIIPRGY KALGYTLHLP EEDKYLVSRN ELLDKLTALL GGRAAEEVVF GDVTSGAAND IERATEIARN MVCQLGMSEE LGPLAWGKEE QEVFLGKEIT RLRNYSEEVA SKIDEEVKKI VTNCYERAKE IIRKYRKQLD NIVEILLEKE TIEGDELRRI LSEEFEKVVE // ID FTSZ_THEMA Reviewed; 351 AA. AC O08398; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 125. DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909}; GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; GN OrderedLocusNames=TM_0836; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CHARACTERIZATION. RX PubMed=9605973; RX DOI=10.1002/(SICI)1097-0169(1998)40:1<71::AID-CM7>3.0.CO;2-I; RA Lu C., Stricker J., Erickson H.P.; RT "FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga RT maritima -- quantitation, GTP hydrolysis, and assembly."; RL Cell Motil. Cytoskeleton 40:71-86(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=15558053; DOI=10.1038/nsmb855; RA Oliva M.A., Cordell S.C., Lowe J.; RT "Structural insights into FtsZ protofilament formation."; RL Nat. Struct. Mol. Biol. 11:1243-1250(2004). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 336-351 IN COMPLEX WITH RP FTSA. RX PubMed=22473211; DOI=10.1038/emboj.2012.76; RA Szwedziak P., Wang Q., Freund S.M., Lowe J.; RT "FtsA forms actin-like protofilaments."; RL EMBO J. 31:2249-2260(2012). CC -!- FUNCTION: Essential cell division protein that forms a contractile CC ring structure (Z ring) at the future cell division site. The CC regulation of the ring assembly controls the timing and the CC location of cell division. One of the functions of the FtsZ ring CC is to recruit other cell division proteins to the septum to CC produce a new cell wall between the dividing cells. Binds GTP and CC shows GTPase activity. {ECO:0000255|HAMAP-Rule:MF_00909, CC ECO:0000269|PubMed:9605973}. CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure CC in a strictly GTP-dependent manner. Interacts directly with CC several other division proteins (By similarity). Interacts with CC FtsA (PubMed:22473211). {ECO:0000255|HAMAP-Rule:MF_00909, CC ECO:0000269|PubMed:22473211}. CC -!- INTERACTION: CC Q9WZU0:ftsA; NbExp=4; IntAct=EBI-7808310, EBI-7808292; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}. CC Note=Assembles at midcell at the inner surface of the cytoplasmic CC membrane. {ECO:0000255|HAMAP-Rule:MF_00909}. CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP- CC Rule:MF_00909}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U65944; AAC24604.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35918.1; -; Genomic_DNA. DR PIR; H72328; H72328. DR RefSeq; NP_228645.1; NC_000853.1. DR RefSeq; WP_004080800.1; NZ_CP011107.1. DR PDB; 1W5F; X-ray; 2.00 A; A/B=1-351. DR PDB; 4A2A; X-ray; 1.80 A; C/D=336-351. DR PDBsum; 1W5F; -. DR PDBsum; 4A2A; -. DR ProteinModelPortal; O08398; -. DR SMR; O08398; 22-334. DR IntAct; O08398; 1. DR MINT; MINT-8382767; -. DR STRING; 243274.TM0836; -. DR EnsemblBacteria; AAD35918; AAD35918; TM_0836. DR GeneID; 898507; -. DR KEGG; tma:TM0836; -. DR PATRIC; 23936598; VBITheMar51294_0849. DR eggNOG; ENOG4105CDK; Bacteria. DR eggNOG; COG0206; LUCA. DR InParanoid; O08398; -. DR KO; K03531; -. DR OMA; GMAMMGI; -. DR OrthoDB; EOG6S7XZG; -. DR EvolutionaryTrace; O08398; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-KW. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.20; -; 1. DR Gene3D; 3.40.50.1440; -; 1. DR HAMAP; MF_00909; FtsZ; 1. DR InterPro; IPR000158; Cell_div_FtsZ. DR InterPro; IPR020805; Cell_div_FtsZ_CS. DR InterPro; IPR024757; FtsZ_C. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR Pfam; PF12327; FtsZ_C; 1. DR Pfam; PF00091; Tubulin; 1. DR PRINTS; PR00423; CELLDVISFTSZ. DR SMART; SM00864; Tubulin; 1. DR SMART; SM00865; Tubulin_C; 1. DR SUPFAM; SSF52490; SSF52490; 1. DR SUPFAM; SSF55307; SSF55307; 1. DR TIGRFAMs; TIGR00065; ftsZ; 1. DR PROSITE; PS01134; FTSZ_1; 1. DR PROSITE; PS01135; FTSZ_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Complete proteome; Cytoplasm; KW GTP-binding; Nucleotide-binding; Reference proteome; Septation. FT CHAIN 1 351 Cell division protein FtsZ. FT /FTId=PRO_0000114391. FT NP_BIND 31 35 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT NP_BIND 118 120 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 149 149 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 153 153 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 197 197 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT CONFLICT 102 102 V -> A (in Ref. 1; AAC24604). FT {ECO:0000305}. FT STRAND 24 29 {ECO:0000244|PDB:1W5F}. FT HELIX 30 43 {ECO:0000244|PDB:1W5F}. FT STRAND 48 55 {ECO:0000244|PDB:1W5F}. FT HELIX 57 61 {ECO:0000244|PDB:1W5F}. FT STRAND 66 70 {ECO:0000244|PDB:1W5F}. FT TURN 73 78 {ECO:0000244|PDB:1W5F}. FT HELIX 85 94 {ECO:0000244|PDB:1W5F}. FT HELIX 96 102 {ECO:0000244|PDB:1W5F}. FT TURN 103 105 {ECO:0000244|PDB:1W5F}. FT STRAND 107 114 {ECO:0000244|PDB:1W5F}. FT HELIX 119 133 {ECO:0000244|PDB:1W5F}. FT STRAND 137 144 {ECO:0000244|PDB:1W5F}. FT HELIX 147 149 {ECO:0000244|PDB:1W5F}. FT HELIX 151 166 {ECO:0000244|PDB:1W5F}. FT STRAND 169 175 {ECO:0000244|PDB:1W5F}. FT HELIX 176 180 {ECO:0000244|PDB:1W5F}. FT HELIX 189 212 {ECO:0000244|PDB:1W5F}. FT HELIX 219 228 {ECO:0000244|PDB:1W5F}. FT STRAND 232 243 {ECO:0000244|PDB:1W5F}. FT HELIX 246 255 {ECO:0000244|PDB:1W5F}. FT HELIX 264 266 {ECO:0000244|PDB:1W5F}. FT STRAND 268 276 {ECO:0000244|PDB:1W5F}. FT HELIX 282 293 {ECO:0000244|PDB:1W5F}. FT STRAND 300 308 {ECO:0000244|PDB:1W5F}. FT STRAND 316 324 {ECO:0000244|PDB:1W5F}. FT HELIX 330 333 {ECO:0000244|PDB:1W5F}. FT HELIX 341 344 {ECO:0000244|PDB:4A2A}. FT HELIX 348 350 {ECO:0000244|PDB:4A2A}. SQ SEQUENCE 351 AA; 38307 MW; 5F2E11FDAA92AFE7 CRC64; MGFDLDVEKK KENRNIPQAN NLKIKVIGVG GAGNNAINRM IEIGIHGVEF VAVNTDLQVL EASNADVKIQ IGENITRGLG AGGRPEIGEQ AALESEEKIR EVLQDTHMVF ITAGFGGGTG TGASPVIAKI AKEMGILTVA IVTTPFYFEG PERLKKAIEG LKKLRKHVDT LIKISNNKLM EELPRDVKIK DAFLKADETL HQGVKGISEL ITKRGYINLD FADIESVMKD AGAAILGIGV GKGEHRAREA AKKAMESKLI EHPVENASSI VFNITAPSNI RMEEVHEAAM IIRQNSSEDA DVKFGLIFDD EVPDDEIRVI FIATRFPDED KILFPEGDIP AIYRYGLEGL L // ID GATB_THEMA Reviewed; 482 AA. AC Q9X100; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; DE Short=Asp/Glu-ADT subunit B; DE EC=6.3.5.-; GN Name=gatB; OrderedLocusNames=TM_1273; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) CC or Gln-tRNA(Gln) through the transamidation of misacylated Asp- CC tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both CC of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction CC takes place in the presence of glutamine and ATP through an CC activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36348.1; -; Genomic_DNA. DR PIR; H72274; H72274. DR RefSeq; NP_229078.1; NC_000853.1. DR RefSeq; WP_004079967.1; NZ_CP011107.1. DR PDB; 3AL0; X-ray; 3.37 A; B=1-482. DR PDBsum; 3AL0; -. DR ProteinModelPortal; Q9X100; -. DR DIP; DIP-59229N; -. DR STRING; 243274.TM1273; -. DR EnsemblBacteria; AAD36348; AAD36348; TM_1273. DR GeneID; 898210; -. DR KEGG; tma:TM1273; -. DR PATRIC; 23937484; VBITheMar51294_1288. DR eggNOG; ENOG4105CHT; Bacteria. DR eggNOG; COG0064; LUCA. DR InParanoid; Q9X100; -. DR KO; K02434; -. DR OMA; ESADYRY; -. DR OrthoDB; EOG6RJV5B; -. DR EvolutionaryTrace; Q9X100; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00121; GatB; 1. DR InterPro; IPR004413; Apn/Gln-ADT_bsu. DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E. DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat. DR InterPro; IPR018027; Asn/Gln_amidotransferase. DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrfrase-rel. DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS. DR PANTHER; PTHR11659; PTHR11659; 1. DR Pfam; PF02934; GatB_N; 1. DR Pfam; PF02637; GatB_Yqey; 1. DR SMART; SM00845; GatB_Yqey; 1. DR SUPFAM; SSF89095; SSF89095; 1. DR TIGRFAMs; TIGR00133; gatB; 1. DR PROSITE; PS01234; GATB; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 482 Aspartyl/glutamyl-tRNA(Asn/Gln) FT amidotransferase subunit B. FT /FTId=PRO_0000148857. FT STRAND 8 14 {ECO:0000244|PDB:3AL0}. FT STRAND 21 27 {ECO:0000244|PDB:3AL0}. FT TURN 40 44 {ECO:0000244|PDB:3AL0}. FT HELIX 54 66 {ECO:0000244|PDB:3AL0}. FT STRAND 73 75 {ECO:0000244|PDB:3AL0}. FT STRAND 78 81 {ECO:0000244|PDB:3AL0}. FT STRAND 90 94 {ECO:0000244|PDB:3AL0}. FT STRAND 96 98 {ECO:0000244|PDB:3AL0}. FT STRAND 104 108 {ECO:0000244|PDB:3AL0}. FT STRAND 111 125 {ECO:0000244|PDB:3AL0}. FT STRAND 130 133 {ECO:0000244|PDB:3AL0}. FT STRAND 136 139 {ECO:0000244|PDB:3AL0}. FT STRAND 142 147 {ECO:0000244|PDB:3AL0}. FT HELIX 148 150 {ECO:0000244|PDB:3AL0}. FT STRAND 155 160 {ECO:0000244|PDB:3AL0}. FT HELIX 167 184 {ECO:0000244|PDB:3AL0}. FT HELIX 191 193 {ECO:0000244|PDB:3AL0}. FT STRAND 195 201 {ECO:0000244|PDB:3AL0}. FT STRAND 206 208 {ECO:0000244|PDB:3AL0}. FT HELIX 225 236 {ECO:0000244|PDB:3AL0}. FT STRAND 239 245 {ECO:0000244|PDB:3AL0}. FT STRAND 254 256 {ECO:0000244|PDB:3AL0}. FT TURN 257 260 {ECO:0000244|PDB:3AL0}. FT STRAND 261 263 {ECO:0000244|PDB:3AL0}. FT HELIX 289 292 {ECO:0000244|PDB:3AL0}. FT STRAND 295 299 {ECO:0000244|PDB:3AL0}. FT HELIX 305 314 {ECO:0000244|PDB:3AL0}. FT HELIX 318 324 {ECO:0000244|PDB:3AL0}. FT HELIX 328 340 {ECO:0000244|PDB:3AL0}. FT HELIX 344 352 {ECO:0000244|PDB:3AL0}. FT HELIX 354 358 {ECO:0000244|PDB:3AL0}. FT TURN 359 363 {ECO:0000244|PDB:3AL0}. FT STRAND 368 370 {ECO:0000244|PDB:3AL0}. FT HELIX 373 383 {ECO:0000244|PDB:3AL0}. FT TURN 384 386 {ECO:0000244|PDB:3AL0}. FT HELIX 392 395 {ECO:0000244|PDB:3AL0}. FT HELIX 397 403 {ECO:0000244|PDB:3AL0}. FT HELIX 407 414 {ECO:0000244|PDB:3AL0}. FT HELIX 425 434 {ECO:0000244|PDB:3AL0}. FT HELIX 437 443 {ECO:0000244|PDB:3AL0}. FT HELIX 452 460 {ECO:0000244|PDB:3AL0}. FT HELIX 468 478 {ECO:0000244|PDB:3AL0}. SQ SEQUENCE 482 AA; 55436 MW; 34988170E32F312F CRC64; MRYRPVIGLE IHVQLSTKTK AFCSCPADVF ELPPNTAICP VCTGQPGALP VPNEEMIRFA VKTALALNCK IHKYSRFDRK NYFYPDLPKG YQISQYFYPI ATEGFLEIDG DEGRKKVRIR RLHLEEDAGK LVHEGDSITR ASYSLVDMNR CGVPLIEIVT EPDISSPREA RVFMEKLRSI VRYLGVSTGD MEKGALRCDA NISVVDTETG RQSNRVEVKN MNSFRFVERA LEYEFERIVK AMERGEDVER ETRGWDMATK ITVSMRGKEE ESDYRYFPEP DIPPVVLSDE YLEEVKKELP ELPDEKAERF MREYGLPEYD AKVLTSSKEL AEFFEECVKV VNRPKDLSNW IMTEVLRELN ERNIEITESK LTPQHFADLF KLMDEGKISI KIAKEIFPEV FETGKMPSQI VEEKGLTQIN DEKLIEELVK KAMEQNPKAV QDYKSGKKKA AGFFVGYVMR ETKGKANPEL TNRIIQKLLE GE // ID GCK_THEMA Reviewed; 417 AA. AC Q9X1S1; G4FFX3; DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=D-glycerate 2-kinase; DE Short=GCK; DE EC=2.7.1.165; GN OrderedLocusNames=TM_1585; ORFNames=THEMA_06355, Tmari_1593; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RG DOE Joint Genome Institute; RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF LYS-47 AND RP ARG-325, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=18156253; DOI=10.1128/JB.01469-07; RA Yang C., Rodionov D.A., Rodionova I.A., Li X., Osterman A.L.; RT "Glycerate 2-kinase of Thermotoga maritima and genomic reconstruction RT of related metabolic pathways."; RL J. Bacteriol. 190:1773-1782(2008). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS), AND SUBUNIT. RX PubMed=16865707; DOI=10.1002/prot.21058; RA Schwarzenbacher R., McMullan D., Krishna S.S., Xu Q., Miller M.D., RA Canaves J.M., Elsliger M.A., Floyd R., Grzechnik S.K., Jaroszewski L., RA Klock H.E., Koesema E., Kovarik J.S., Kreusch A., Kuhn P., RA McPhillips T.M., Morse A.T., Quijano K., Spraggon G., Stevens R.C., RA van den Bedem H., Wolf G., Hodgson K.O., Wooley J., Deacon A.M., RA Godzik A., Lesley S.A., Wilson I.A.; RT "Crystal structure of a glycerate kinase (TM1585) from Thermotoga RT maritima at 2.70 A resolution reveals a new fold."; RL Proteins 65:243-248(2006). CC -!- FUNCTION: Involved in the degradation of serine via 3- CC hydroxypyruvate. Catalyzes the ATP-dependent phosphorylation of D- CC glycerate to 2-phosphoglycerate. {ECO:0000269|PubMed:18156253}. CC -!- CATALYTIC ACTIVITY: ATP + D-glycerate = ADP + 2-phospho-D- CC glycerate. {ECO:0000269|PubMed:18156253}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:18156253}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.095 mM for ATP {ECO:0000269|PubMed:18156253}; CC KM=0.15 mM for D-glycerate {ECO:0000269|PubMed:18156253}; CC Note=Kcat is 14.4 sec(-1) for phosphorylation of D-glycerate.; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16865707, CC ECO:0000269|PubMed:18156253}. CC -!- SIMILARITY: Belongs to the glycerate kinase type-1 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36652.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50517.1; -; Genomic_DNA. DR EMBL; CP007013; AHD18518.1; -; Genomic_DNA. DR PIR; A72236; A72236. DR RefSeq; NP_229385.1; NC_000853.1. DR RefSeq; WP_004082016.1; NZ_CP011107.1. DR PDB; 2B8N; X-ray; 2.53 A; A/B=1-417. DR PDBsum; 2B8N; -. DR ProteinModelPortal; Q9X1S1; -. DR SMR; Q9X1S1; 4-417. DR STRING; 243274.TM1585; -. DR EnsemblBacteria; AAD36652; AAD36652; TM_1585. DR EnsemblBacteria; AGL50517; AGL50517; Tmari_1593. DR EnsemblBacteria; AHD18518; AHD18518; THEMA_06355. DR GeneID; 897953; -. DR KEGG; tma:TM1585; -. DR KEGG; tmi:THEMA_06355; -. DR KEGG; tmm:Tmari_1593; -. DR KEGG; tmw:THMA_1620; -. DR PATRIC; 23938134; VBITheMar51294_1604. DR eggNOG; ENOG4105D1Z; Bacteria. DR eggNOG; COG2379; LUCA. DR InParanoid; Q9X1S1; -. DR KO; K00050; -. DR OMA; IYEAGHP; -. DR OrthoDB; EOG6TTVJX; -. DR BioCyc; TMAR243274:GC6P-1626-MONOMER; -. DR SABIO-RK; Q9X1S1; -. DR EvolutionaryTrace; Q9X1S1; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008887; F:glycerate kinase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central. DR Gene3D; 3.40.1480.10; -; 1. DR InterPro; IPR007835; MOFRL. DR InterPro; IPR025286; MOFRL_assoc_dom. DR Pfam; PF13660; DUF4147; 1. DR Pfam; PF05161; MOFRL; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 417 D-glycerate 2-kinase. FT /FTId=PRO_0000428994. FT MUTAGEN 47 47 K->A: Very low residual kinase activity. FT {ECO:0000269|PubMed:18156253}. FT MUTAGEN 47 47 K->R: Significant decrease of the kinase FT activity with a 180-fold decrease of FT catalytic efficiency. FT {ECO:0000269|PubMed:18156253}. FT MUTAGEN 325 325 R->A,K: Significant decrease of the FT kinase activity with a 17-fold decrease FT of catalytic efficiency. FT {ECO:0000269|PubMed:18156253}. FT HELIX 5 20 {ECO:0000244|PDB:2B8N}. FT HELIX 24 29 {ECO:0000244|PDB:2B8N}. FT HELIX 32 35 {ECO:0000244|PDB:2B8N}. FT STRAND 39 46 {ECO:0000244|PDB:2B8N}. FT HELIX 49 60 {ECO:0000244|PDB:2B8N}. FT HELIX 61 63 {ECO:0000244|PDB:2B8N}. FT STRAND 64 72 {ECO:0000244|PDB:2B8N}. FT STRAND 84 88 {ECO:0000244|PDB:2B8N}. FT STRAND 90 92 {ECO:0000244|PDB:2B8N}. FT HELIX 95 108 {ECO:0000244|PDB:2B8N}. FT STRAND 116 121 {ECO:0000244|PDB:2B8N}. FT HELIX 125 128 {ECO:0000244|PDB:2B8N}. FT HELIX 138 150 {ECO:0000244|PDB:2B8N}. FT HELIX 155 163 {ECO:0000244|PDB:2B8N}. FT STRAND 166 168 {ECO:0000244|PDB:2B8N}. FT TURN 169 171 {ECO:0000244|PDB:2B8N}. FT HELIX 172 177 {ECO:0000244|PDB:2B8N}. FT STRAND 180 187 {ECO:0000244|PDB:2B8N}. FT TURN 195 197 {ECO:0000244|PDB:2B8N}. FT HELIX 198 200 {ECO:0000244|PDB:2B8N}. FT HELIX 210 219 {ECO:0000244|PDB:2B8N}. FT HELIX 226 232 {ECO:0000244|PDB:2B8N}. FT STRAND 241 249 {ECO:0000244|PDB:2B8N}. FT HELIX 251 264 {ECO:0000244|PDB:2B8N}. FT STRAND 268 276 {ECO:0000244|PDB:2B8N}. FT HELIX 280 297 {ECO:0000244|PDB:2B8N}. FT STRAND 303 311 {ECO:0000244|PDB:2B8N}. FT HELIX 325 336 {ECO:0000244|PDB:2B8N}. FT TURN 337 339 {ECO:0000244|PDB:2B8N}. FT STRAND 343 349 {ECO:0000244|PDB:2B8N}. FT STRAND 355 358 {ECO:0000244|PDB:2B8N}. FT STRAND 361 365 {ECO:0000244|PDB:2B8N}. FT HELIX 368 374 {ECO:0000244|PDB:2B8N}. FT HELIX 379 384 {ECO:0000244|PDB:2B8N}. FT HELIX 388 394 {ECO:0000244|PDB:2B8N}. FT STRAND 410 416 {ECO:0000244|PDB:2B8N}. SQ SEQUENCE 417 AA; 44722 MW; FEE01EC89CC8E445 CRC64; MFDPESLKKL AIEIVKKSIE AVFPDRAVKE TLPKLNLDRV ILVAVGKAAW RMAKAAYEVL GKKIRKGVVV TKYGHSEGPI DDFEIYEAGH PVPDENTIKT TRRVLELVDQ LNENDTVLFL LSGGGSSLFE LPLEGVSLEE IQKLTSALLK SGASIEEINT VRKHLSQVKG GRFAERVFPA KVVALVLSDV LGDRLDVIAS GPAWPDSSTS EDALKVLEKY GIETSESVKR AILQETPKHL SNVEIHLIGN VQKVCDEAKS LAKEKGFNAE IITTSLDCEA REAGRFIASI MKEVKFKDRP LKKPAALIFG GETVVHVKGN GIGGRNQELA LSAAIALEGI EGVILCSAGT DGTDGPTDAA GGIVDGSTAK TLKAMGEDPY QYLKNNDSYN ALKKSGALLI TGPTGTNVND LIIGLIV // ID GCSH_THEMA Reviewed; 124 AA. AC Q9WY55; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 111. DE RecName: Full=Glycine cleavage system H protein {ECO:0000255|HAMAP-Rule:MF_00272}; GN Name=gcvH {ECO:0000255|HAMAP-Rule:MF_00272}; GN OrderedLocusNames=TM_0212; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. The H protein shuttles the methylamine group of glycine CC from the P protein to the T protein. {ECO:0000255|HAMAP- CC Rule:MF_00272}. CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00272}; CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000255|HAMAP- CC Rule:MF_00272}; CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H. {ECO:0000255|HAMAP-Rule:MF_00272}. CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000255|HAMAP- CC Rule:MF_00272}. CC -!- SIMILARITY: Contains 1 lipoyl-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_00272}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35304.1; -; Genomic_DNA. DR PIR; F72403; F72403. DR RefSeq; NP_228027.1; NC_000853.1. DR RefSeq; WP_010865076.1; NC_000853.1. DR PDB; 1ZKO; X-ray; 1.65 A; A/B=1-124. DR PDB; 2KA7; NMR; -; A=1-124. DR PDBsum; 1ZKO; -. DR PDBsum; 2KA7; -. DR ProteinModelPortal; Q9WY55; -. DR SMR; Q9WY55; 1-123. DR STRING; 243274.TM0212; -. DR EnsemblBacteria; AAD35304; AAD35304; TM_0212. DR GeneID; 897090; -. DR KEGG; tma:TM0212; -. DR PATRIC; 23935296; VBITheMar51294_0214. DR eggNOG; ENOG4105KE9; Bacteria. DR eggNOG; COG0509; LUCA. DR InParanoid; Q9WY55; -. DR KO; K02437; -. DR OMA; NTDPYGE; -. DR OrthoDB; EOG60CWTC; -. DR BioCyc; TMAR243274:GC6P-225-MONOMER; -. DR EvolutionaryTrace; Q9WY55; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00272; GcvH; 1. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR002930; GCV_H. DR InterPro; IPR017453; GCV_H_sub. DR InterPro; IPR011053; Single_hybrid_motif. DR PANTHER; PTHR11715; PTHR11715; 1. DR Pfam; PF01597; GCV_H; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR TIGRFAMs; TIGR00527; gcvH; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00189; LIPOYL; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Lipoyl; Reference proteome. FT CHAIN 1 124 Glycine cleavage system H protein. FT /FTId=PRO_0000166258. FT DOMAIN 19 101 Lipoyl-binding. {ECO:0000255|PROSITE- FT ProRule:PRU01066}. FT MOD_RES 60 60 N6-lipoyllysine. {ECO:0000255|HAMAP- FT Rule:MF_00272}. FT STRAND 2 6 {ECO:0000244|PDB:1ZKO}. FT STRAND 10 16 {ECO:0000244|PDB:1ZKO}. FT STRAND 19 24 {ECO:0000244|PDB:1ZKO}. FT HELIX 26 32 {ECO:0000244|PDB:1ZKO}. FT STRAND 34 39 {ECO:0000244|PDB:1ZKO}. FT STRAND 52 60 {ECO:0000244|PDB:1ZKO}. FT STRAND 62 66 {ECO:0000244|PDB:1ZKO}. FT STRAND 71 76 {ECO:0000244|PDB:1ZKO}. FT HELIX 78 81 {ECO:0000244|PDB:1ZKO}. FT HELIX 86 89 {ECO:0000244|PDB:1ZKO}. FT TURN 91 95 {ECO:0000244|PDB:1ZKO}. FT STRAND 98 103 {ECO:0000244|PDB:1ZKO}. FT HELIX 105 110 {ECO:0000244|PDB:1ZKO}. FT HELIX 114 122 {ECO:0000244|PDB:1ZKO}. SQ SEQUENCE 124 AA; 13915 MW; 90B7CDE430A16C9F CRC64; MKMKKYTKTH EWVSIEDKVA TVGITNHAQE QLGDVVYVDL PEVGREVKKG EVVASIESVK AAADVYAPLS GKIVEVNEKL DTEPELINKD PEGEGWLFKM EISDEGELED LLDEQAYQEF CAQE // ID GAL1_THEMA Reviewed; 350 AA. AC P56838; O33837; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 1. DT 13-APR-2016, entry version 113. DE RecName: Full=Galactokinase {ECO:0000255|HAMAP-Rule:MF_00246}; DE EC=2.7.1.6 {ECO:0000255|HAMAP-Rule:MF_00246}; DE AltName: Full=Galactose kinase {ECO:0000255|HAMAP-Rule:MF_00246}; GN Name=galK {ECO:0000255|HAMAP-Rule:MF_00246}; GN OrderedLocusNames=TM_1190; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9741105; RA Liebl W., Wagner B., Schellhase J.; RT "Properties of an alpha-galactosidase, and structure of its gene galA, RT within an alpha- and beta-galactoside utilization gene cluster of the RT hyperthermophilic bacterium Thermotoga maritima."; RL Syst. Appl. Microbiol. 21:1-11(1998). CC -!- FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to CC D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). CC {ECO:0000255|HAMAP-Rule:MF_00246}. CC -!- CATALYTIC ACTIVITY: ATP + alpha-D-galactose = ADP + alpha-D- CC galactose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_00246}. CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism. CC {ECO:0000255|HAMAP-Rule:MF_00246}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00246}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00246}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36265.1; -; Genomic_DNA. DR EMBL; AJ001072; CAA04516.1; -; Genomic_DNA. DR PIR; C72283; C72283. DR RefSeq; NP_228995.1; NC_000853.1. DR RefSeq; WP_004080140.1; NZ_CP011107.1. DR ProteinModelPortal; P56838; -. DR STRING; 243274.TM1190; -. DR EnsemblBacteria; AAD36265; AAD36265; TM_1190. DR GeneID; 898294; -. DR KEGG; tma:TM1190; -. DR PATRIC; 23937322; VBITheMar51294_1208. DR eggNOG; ENOG4105CRD; Bacteria. DR eggNOG; COG0153; LUCA. DR InParanoid; P56838; -. DR KO; K00849; -. DR OMA; QYVGCAC; -. DR OrthoDB; EOG6DG2SH; -. DR BioCyc; MetaCyc:MONOMER-505; -. DR UniPathway; UPA00214; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004335; F:galactokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; -; 1. DR HAMAP; MF_00246; Galactokinase; 1. DR InterPro; IPR000705; Galactokinase. DR InterPro; IPR022963; Galactokinase_bac. DR InterPro; IPR019741; Galactokinase_CS. DR InterPro; IPR019539; GalKase_gal-bd. DR InterPro; IPR013750; GHMP_kinase_C_dom. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS. DR InterPro; IPR006206; Mevalonate/galactokinase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10457; PTHR10457; 1. DR PANTHER; PTHR10457:SF6; PTHR10457:SF6; 1. DR Pfam; PF10509; GalKase_gal_bdg; 1. DR Pfam; PF08544; GHMP_kinases_C; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF000530; Galactokinase; 1. DR PRINTS; PR00473; GALCTOKINASE. DR PRINTS; PR00959; MEVGALKINASE. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55060; SSF55060; 1. DR TIGRFAMs; TIGR00131; gal_kin; 1. DR PROSITE; PS00106; GALACTOKINASE; 1. DR PROSITE; PS00627; GHMP_KINASES_ATP; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Cytoplasm; KW Galactose metabolism; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 350 Galactokinase. FT /FTId=PRO_0000184631. FT NP_BIND 96 102 ATP. {ECO:0000255|HAMAP-Rule:MF_00246}. FT REGION 14 17 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00246}. FT ACT_SITE 146 146 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00246}. FT METAL 102 102 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00246}. FT METAL 134 134 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00246}. FT BINDING 46 46 ATP. {ECO:0000255|HAMAP-Rule:MF_00246}. FT BINDING 196 196 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00246}. FT SITE 8 8 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00246}. SQ SEQUENCE 350 AA; 39589 MW; 4ADA4705151B7695 CRC64; MKVKAPGRIN IIGEHTDYND GYVLPFAVNR YVFLSIEGSE RFIFHSENVN ETVEMEKIEK LNKWTDYISG VIASFEKRGY RVSPVKISVS SNLPIGAGLS SSAALEVATA YAISEYFGFN VPKLELVKIA REAEVEFVGV RCGIMDQFTA VFGKKDHAIF LDTMTLEYEY VPLKLEGYEI NLVDSNVKHE LSSSEYNRRR QECEEVLKTL EKKSFREVTK EDLERLSGTL RKRAQHVLEE NERVLKSVQA LKEGDFETLG KLLFSSHESL RDLYEVSCEE TDFIVDYLRG KEGILGARMV GGGFGGGVIV LSKKGAFGKI KEELVESYRK RFGIDLIFHE IESSDGVQKI // ID G6PI_THEMA Reviewed; 448 AA. AC Q9X1A5; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Glucose-6-phosphate isomerase; DE Short=GPI; DE EC=5.3.1.9; DE AltName: Full=Phosphoglucose isomerase; DE Short=PGI; DE AltName: Full=Phosphohexose isomerase; DE Short=PHI; GN Name=pgi; OrderedLocusNames=TM_1385; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6- CC phosphate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36455.1; -; Genomic_DNA. DR PIR; B72262; B72262. DR RefSeq; NP_229186.1; NC_000853.1. DR RefSeq; WP_004081585.1; NZ_CP011107.1. DR PDB; 2Q8N; X-ray; 1.82 A; A/B/C=1-448. DR PDBsum; 2Q8N; -. DR ProteinModelPortal; Q9X1A5; -. DR SMR; Q9X1A5; 1-448. DR STRING; 243274.TM1385; -. DR EnsemblBacteria; AAD36455; AAD36455; TM_1385. DR GeneID; 898093; -. DR KEGG; tma:TM1385; -. DR PATRIC; 23937712; VBITheMar51294_1397. DR eggNOG; ENOG4105C89; Bacteria. DR eggNOG; COG0166; LUCA. DR InParanoid; Q9X1A5; -. DR KO; K01810; -. DR OMA; ISVMMAY; -. DR OrthoDB; EOG64R61J; -. DR BioCyc; MetaCyc:MONOMER-381; -. DR UniPathway; UPA00109; UER00181. DR EvolutionaryTrace; Q9X1A5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1390.10; -; 1. DR HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. DR InterPro; IPR023096; G6P_Isomerase_C. DR InterPro; IPR018189; Phosphoglucose_isomerase_CS. DR PANTHER; PTHR11469; PTHR11469; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Gluconeogenesis; KW Glycolysis; Isomerase; Reference proteome. FT CHAIN 1 448 Glucose-6-phosphate isomerase. FT /FTId=PRO_0000180757. FT ACT_SITE 281 281 Proton donor. {ECO:0000250}. FT ACT_SITE 310 310 {ECO:0000250}. FT ACT_SITE 422 422 {ECO:0000250}. FT STRAND 4 6 {ECO:0000244|PDB:2Q8N}. FT HELIX 8 10 {ECO:0000244|PDB:2Q8N}. FT TURN 12 14 {ECO:0000244|PDB:2Q8N}. FT HELIX 21 40 {ECO:0000244|PDB:2Q8N}. FT HELIX 44 47 {ECO:0000244|PDB:2Q8N}. FT HELIX 50 57 {ECO:0000244|PDB:2Q8N}. FT HELIX 60 63 {ECO:0000244|PDB:2Q8N}. FT STRAND 67 72 {ECO:0000244|PDB:2Q8N}. FT HELIX 75 77 {ECO:0000244|PDB:2Q8N}. FT HELIX 79 88 {ECO:0000244|PDB:2Q8N}. FT HELIX 93 95 {ECO:0000244|PDB:2Q8N}. FT TURN 98 103 {ECO:0000244|PDB:2Q8N}. FT STRAND 106 110 {ECO:0000244|PDB:2Q8N}. FT HELIX 115 122 {ECO:0000244|PDB:2Q8N}. FT HELIX 127 129 {ECO:0000244|PDB:2Q8N}. FT STRAND 130 135 {ECO:0000244|PDB:2Q8N}. FT STRAND 137 139 {ECO:0000244|PDB:2Q8N}. FT HELIX 142 157 {ECO:0000244|PDB:2Q8N}. FT HELIX 162 164 {ECO:0000244|PDB:2Q8N}. FT STRAND 166 170 {ECO:0000244|PDB:2Q8N}. FT STRAND 172 175 {ECO:0000244|PDB:2Q8N}. FT HELIX 176 184 {ECO:0000244|PDB:2Q8N}. FT STRAND 187 190 {ECO:0000244|PDB:2Q8N}. FT HELIX 197 199 {ECO:0000244|PDB:2Q8N}. FT HELIX 204 212 {ECO:0000244|PDB:2Q8N}. FT HELIX 217 230 {ECO:0000244|PDB:2Q8N}. FT HELIX 236 238 {ECO:0000244|PDB:2Q8N}. FT HELIX 240 253 {ECO:0000244|PDB:2Q8N}. FT STRAND 258 265 {ECO:0000244|PDB:2Q8N}. FT HELIX 266 268 {ECO:0000244|PDB:2Q8N}. FT HELIX 269 283 {ECO:0000244|PDB:2Q8N}. FT STRAND 299 304 {ECO:0000244|PDB:2Q8N}. FT HELIX 307 309 {ECO:0000244|PDB:2Q8N}. FT TURN 310 312 {ECO:0000244|PDB:2Q8N}. FT HELIX 313 318 {ECO:0000244|PDB:2Q8N}. FT STRAND 323 330 {ECO:0000244|PDB:2Q8N}. FT HELIX 345 347 {ECO:0000244|PDB:2Q8N}. FT TURN 348 352 {ECO:0000244|PDB:2Q8N}. FT HELIX 355 372 {ECO:0000244|PDB:2Q8N}. FT STRAND 377 385 {ECO:0000244|PDB:2Q8N}. FT HELIX 387 407 {ECO:0000244|PDB:2Q8N}. FT HELIX 416 418 {ECO:0000244|PDB:2Q8N}. FT HELIX 419 428 {ECO:0000244|PDB:2Q8N}. SQ SEQUENCE 448 AA; 50493 MW; 7FDE91F297851F71 CRC64; MSLKFDFSNL FEPNISGGLT DEDVKSVEEK VTSAVRNFVE NTPDFAKLDR SWIDSVKSLE DWIINFDTVV VLGIGGSGLG NLALHYSLRP LNWNEMTREE RNGYARVFVV DNVDPDLMSS VLDRIDPKTT LFNVISKSGS TAEVMATYSI ARGILEAYGL DPREHMLITT DPEKGFLRKL VKEEGFRSLE VPPGVGGRFS VLTPVGLLSA MAEGIDIDEL HEGAKDAFEK SMKENILENP AAMIALTHYL YLNKGKSISV MMAYSNRMIY LVDWYRQLWA ESLGKRYNLK GEEVFTGQTP VKALGATDQH SQIQLYNEGP NDKVITFLRV ENFDREIVIP ETGRAELSYL ARKKLSELLL AEQTGTEEAL RENNRPNMRV TFDGLTPYNV GQFFAYYEAA TAFMGYLLEI NPFDQPGVEL GKKITFALMG REGYTYEIKE RSKKVIIE // ID GATA_THEMA Reviewed; 475 AA. AC Q9X0Z9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A; DE Short=Glu-ADT subunit A; DE EC=6.3.5.7; GN Name=gatA; OrderedLocusNames=TM_1272; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) CC through the transamidation of misacylated Glu-tRNA(Gln) in CC organisms which lack glutaminyl-tRNA synthetase. The reaction CC takes place in the presence of glutamine and ATP through an CC activated gamma-phospho-Glu-tRNA(Gln) (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36347.1; -; Genomic_DNA. DR PIR; G72274; G72274. DR RefSeq; NP_229077.1; NC_000853.1. DR RefSeq; WP_010865293.1; NC_000853.1. DR PDB; 2GI3; X-ray; 1.80 A; A=1-475. DR PDB; 3AL0; X-ray; 3.37 A; A=1-475. DR PDBsum; 2GI3; -. DR PDBsum; 3AL0; -. DR ProteinModelPortal; Q9X0Z9; -. DR SMR; Q9X0Z9; 1-475. DR DIP; DIP-59228N; -. DR STRING; 243274.TM1272; -. DR EnsemblBacteria; AAD36347; AAD36347; TM_1272. DR GeneID; 898211; -. DR KEGG; tma:TM1272; -. DR KEGG; tmi:THEMA_07975; -. DR PATRIC; 23937482; VBITheMar51294_1287. DR eggNOG; ENOG4105C3P; Bacteria. DR eggNOG; COG0154; LUCA. DR InParanoid; Q9X0Z9; -. DR KO; K02433; -. DR OMA; SKQYRER; -. DR OrthoDB; EOG61P6R9; -. DR BioCyc; TMAR243274:GC6P-1303-MONOMER; -. DR BRENDA; 6.3.5.7; 6331. DR EvolutionaryTrace; Q9X0Z9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.1300.10; -; 1. DR HAMAP; MF_00120; GatA; 1. DR InterPro; IPR000120; Amidase. DR InterPro; IPR020556; Amidase_CS. DR InterPro; IPR023631; Amidase_dom. DR InterPro; IPR004412; GatA. DR PANTHER; PTHR11895; PTHR11895; 1. DR Pfam; PF01425; Amidase; 1. DR SUPFAM; SSF75304; SSF75304; 1. DR TIGRFAMs; TIGR00132; gatA; 1. DR PROSITE; PS00571; AMIDASES; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 475 Glutamyl-tRNA(Gln) amidotransferase FT subunit A. FT /FTId=PRO_0000105221. FT ACT_SITE 66 66 Charge relay system. {ECO:0000250}. FT ACT_SITE 141 141 Charge relay system. {ECO:0000250}. FT ACT_SITE 165 165 Acyl-ester intermediate. {ECO:0000250}. FT HELIX 6 8 {ECO:0000244|PDB:2GI3}. FT HELIX 11 14 {ECO:0000244|PDB:2GI3}. FT HELIX 19 22 {ECO:0000244|PDB:2GI3}. FT HELIX 25 40 {ECO:0000244|PDB:2GI3}. FT STRAND 43 46 {ECO:0000244|PDB:2GI3}. FT TURN 57 60 {ECO:0000244|PDB:2GI3}. FT STRAND 62 66 {ECO:0000244|PDB:2GI3}. FT STRAND 72 74 {ECO:0000244|PDB:2GI3}. FT HELIX 81 83 {ECO:0000244|PDB:2GI3}. FT HELIX 93 101 {ECO:0000244|PDB:2GI3}. FT STRAND 104 109 {ECO:0000244|PDB:2GI3}. FT HELIX 113 115 {ECO:0000244|PDB:2GI3}. FT STRAND 118 120 {ECO:0000244|PDB:2GI3}. FT STRAND 140 142 {ECO:0000244|PDB:2GI3}. FT HELIX 143 150 {ECO:0000244|PDB:2GI3}. FT STRAND 153 164 {ECO:0000244|PDB:2GI3}. FT HELIX 167 173 {ECO:0000244|PDB:2GI3}. FT STRAND 175 179 {ECO:0000244|PDB:2GI3}. FT TURN 195 197 {ECO:0000244|PDB:2GI3}. FT STRAND 199 206 {ECO:0000244|PDB:2GI3}. FT HELIX 207 217 {ECO:0000244|PDB:2GI3}. FT TURN 236 239 {ECO:0000244|PDB:2GI3}. FT STRAND 246 250 {ECO:0000244|PDB:2GI3}. FT HELIX 251 255 {ECO:0000244|PDB:2GI3}. FT HELIX 260 275 {ECO:0000244|PDB:2GI3}. FT STRAND 279 283 {ECO:0000244|PDB:2GI3}. FT HELIX 288 290 {ECO:0000244|PDB:2GI3}. FT HELIX 291 304 {ECO:0000244|PDB:2GI3}. FT STRAND 311 316 {ECO:0000244|PDB:3AL0}. FT HELIX 324 335 {ECO:0000244|PDB:3AL0}. FT HELIX 336 380 {ECO:0000244|PDB:2GI3}. FT STRAND 381 388 {ECO:0000244|PDB:2GI3}. FT STRAND 390 392 {ECO:0000244|PDB:3AL0}. FT TURN 396 398 {ECO:0000244|PDB:2GI3}. FT HELIX 402 406 {ECO:0000244|PDB:2GI3}. FT TURN 407 412 {ECO:0000244|PDB:2GI3}. FT HELIX 413 418 {ECO:0000244|PDB:2GI3}. FT STRAND 422 430 {ECO:0000244|PDB:2GI3}. FT STRAND 433 440 {ECO:0000244|PDB:2GI3}. FT HELIX 446 459 {ECO:0000244|PDB:2GI3}. SQ SEQUENCE 475 AA; 52529 MW; 4F01EA3A2DCBD9A0 CRC64; MIDLDFRKLT IEECLKLSEE EREKLPQLSL ETIKRLDPHV KAFISVRENV SVEKKGKFWG IPVAIKDNIL TLGMRTTCAS RILENYESVF DATVVKKMKE AGFVVVGKAN LDEFAMGSST ERSAFFPTRN PWDLERVPGG SSGGSAAAVS AGMVVAALGS DTGGSVRQPA SLCGVVGYKP TYGLVSRYGL VAFASSLDQI GPITKTVRDA AILMEIISGR DENDATTVNR KVDFLSEIEE GVSGMKFAVP EEIYEHDIEE GVSERFEEAL KLLERLGAKV ERVKIPHIKY SVATYYVIAP AEASSNLARF DGVKYGLRIK EKGLREMYMK TRNVGFGEEV RRRIMIGTFT LSAAYYEAYF NKAMKVRRKI SDELNEVLSQ YDAILTPTSP VTAFKIGEIK DPLTYYLMDI FTIPANLAGL PAISVPFGFS NNLPVGVQVI GRRFADGKVF RIARAIEKNS PYNENGMFPL PEVKA // ID GCSPA_THEMA Reviewed; 437 AA. AC Q9WY56; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712}; DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00712}; DE AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712}; DE AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712}; DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712}; GN Name=gcvPA {ECO:0000255|HAMAP-Rule:MF_00712}; GN OrderedLocusNames=TM_0213; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. The P protein binds the alpha-amino group of glycine CC through its pyridoxal phosphate cofactor; CO(2) is released and CC the remaining methylamine moiety is then transferred to the CC lipoamide cofactor of the H protein. {ECO:0000255|HAMAP- CC Rule:MF_00712}. CC -!- CATALYTIC ACTIVITY: Glycine + [glycine-cleavage complex H CC protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H CC protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_00712}. CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H. In this organism, the P 'protein' is a heterodimer CC of two subunits. {ECO:0000255|HAMAP-Rule:MF_00712}. CC -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00712}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35305.1; -; Genomic_DNA. DR PIR; G72403; G72403. DR RefSeq; NP_228028.1; NC_000853.1. DR RefSeq; WP_004082888.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY56; -. DR STRING; 243274.TM0213; -. DR EnsemblBacteria; AAD35305; AAD35305; TM_0213. DR GeneID; 897091; -. DR KEGG; tma:TM0213; -. DR PATRIC; 23935298; VBITheMar51294_0215. DR eggNOG; ENOG4107QK8; Bacteria. DR eggNOG; COG0403; LUCA. DR InParanoid; Q9WY56; -. DR KO; K00282; -. DR OMA; SMYDGST; -. DR OrthoDB; EOG6XWV3B; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central. DR GO; GO:0016594; F:glycine binding; IBA:GO_Central. DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR HAMAP; MF_00712; GcvPA; 1. DR InterPro; IPR023010; GcvPA. DR InterPro; IPR020580; GDC-P_N. DR InterPro; IPR020581; GDC_P. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR PANTHER; PTHR11773; PTHR11773; 1. DR Pfam; PF02347; GDC-P; 1. DR PIRSF; PIRSF006815; GcvPA; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 437 Probable glycine dehydrogenase FT (decarboxylating) subunit 1. FT /FTId=PRO_0000166980. SQ SEQUENCE 437 AA; 48942 MW; DDF0EDE9BB29BB1A CRC64; MNYPYIPHTD EDVRAMLDFI GVSSIEELFS SIPVSARSSL NIPESRDEFS VFKQLKEISE MNNSLEDYAV FLGAGVYKRY VPTVVYDLAM KPDFLTAYTP YQAEVSQGTL QALFEYQTMV CELTGMEVAN ASMYDGATAL AEAALMSFRL TGKEKVVVAR SVHPEYRAVL RTYLEKRGFT VVEAGYDETG RVLLEEVDEE TAAIAVQYPN FFGIIEDLDY VRSRSGNALL IVVVEPVSLA LLEPPGSYGA DIVVGEGQSL GLPMWFGGYS LGIFATREEY VRQMPGRLIG QTVDQAGNTA YTMILQTREQ HIRRARATSN ICSNHAHAAL IAAVYMSVMG PDGLKEVARR SYNAAHYLQE RLEEIGFKLC FSGEFFNEFV FNVPEDYPDR WRKMMEKKIL GPLPLEEFYP ELGDTALACA TEVISKEDIE KLLEAMK // ID GLDA_THEMA Reviewed; 364 AA. AC Q9WYQ4; DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Glycerol dehydrogenase; DE Short=GDH; DE Short=GLDH; DE EC=1.1.1.6; GN Name=gldA; OrderedLocusNames=TM_0423; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH ZINC AND RP SUBSTRATE ANALOG. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=12193646; DOI=10.1073/pnas.142413399; RA Lesley S.A., Kuhn P., Godzik A., Deacon A.M., Mathews I., Kreusch A., RA Spraggon G., Klock H.E., McMullan D., Shin T., Vincent J., Robb A., RA Brinen L.S., Miller M.D., McPhillips T.M., Miller M.A., Scheibe D., RA Canaves J.M., Guda C., Jaroszewski L., Selby T.L., Elsliger M.-A., RA Wooley J., Taylor S.S., Hodgson K.O., Wilson I.A., Schultz P.G., RA Stevens R.C.; RT "Structural genomics of the Thermotoga maritima proteome implemented RT in a high-throughput structure determination pipeline."; RL Proc. Natl. Acad. Sci. U.S.A. 99:11664-11669(2002). CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of glycerol to CC dihydroxyacetone (glycerone). Allows microorganisms to utilize CC glycerol as a source of carbon under anaerobic conditions (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Glycerol + NAD(+) = glycerone + NADH. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone CC phosphate from glycerol (oxidative route): step 1/2. CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35508.1; -; Genomic_DNA. DR PIR; G72378; G72378. DR RefSeq; NP_228233.1; NC_000853.1. DR RefSeq; WP_004083283.1; NZ_CP011107.1. DR PDB; 1KQ3; X-ray; 1.50 A; A=1-364. DR PDBsum; 1KQ3; -. DR ProteinModelPortal; Q9WYQ4; -. DR SMR; Q9WYQ4; 1-363. DR STRING; 243274.TM0423; -. DR EnsemblBacteria; AAD35508; AAD35508; TM_0423. DR GeneID; 897429; -. DR KEGG; tma:TM0423; -. DR PATRIC; 23935729; VBITheMar51294_0428. DR eggNOG; ENOG4105DCT; Bacteria. DR eggNOG; COG0371; LUCA. DR InParanoid; Q9WYQ4; -. DR KO; K00005; -. DR OMA; TVLAFCR; -. DR OrthoDB; EOG67432X; -. DR UniPathway; UPA00617; UER00668. DR EvolutionaryTrace; Q9WYQ4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019588; P:anaerobic glycerol catabolic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR001670; ADH_Fe. DR InterPro; IPR018211; ADH_Fe_CS. DR Pfam; PF00465; Fe-ADH; 1. DR PROSITE; PS00913; ADH_IRON_1; 1. DR PROSITE; PS00060; ADH_IRON_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Glycerol metabolism; Metal-binding; KW NAD; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 364 Glycerol dehydrogenase. FT /FTId=PRO_0000350665. FT NP_BIND 92 96 NAD. {ECO:0000250}. FT NP_BIND 114 117 NAD. {ECO:0000250}. FT METAL 169 169 Zinc; catalytic. FT {ECO:0000269|PubMed:12193646}. FT METAL 252 252 Zinc; catalytic. FT {ECO:0000269|PubMed:12193646}. FT METAL 269 269 Zinc; catalytic. FT {ECO:0000269|PubMed:12193646}. FT BINDING 37 37 NAD. {ECO:0000250}. FT BINDING 119 119 Substrate. {ECO:0000305}. FT BINDING 123 123 NAD. {ECO:0000250}. FT BINDING 125 125 NAD; via carbonyl oxygen. {ECO:0000250}. FT BINDING 129 129 NAD. {ECO:0000250}. FT BINDING 169 169 Substrate. {ECO:0000305}. FT BINDING 252 252 Substrate. {ECO:0000305}. FT BINDING 269 269 Substrate. {ECO:0000305}. FT STRAND 9 14 {ECO:0000244|PDB:1KQ3}. FT HELIX 17 20 {ECO:0000244|PDB:1KQ3}. FT HELIX 21 26 {ECO:0000244|PDB:1KQ3}. FT STRAND 30 36 {ECO:0000244|PDB:1KQ3}. FT HELIX 38 43 {ECO:0000244|PDB:1KQ3}. FT HELIX 49 52 {ECO:0000244|PDB:1KQ3}. FT STRAND 54 62 {ECO:0000244|PDB:1KQ3}. FT HELIX 69 76 {ECO:0000244|PDB:1KQ3}. FT STRAND 85 91 {ECO:0000244|PDB:1KQ3}. FT HELIX 92 104 {ECO:0000244|PDB:1KQ3}. FT STRAND 109 115 {ECO:0000244|PDB:1KQ3}. FT STRAND 123 129 {ECO:0000244|PDB:1KQ3}. FT STRAND 135 140 {ECO:0000244|PDB:1KQ3}. FT STRAND 146 151 {ECO:0000244|PDB:1KQ3}. FT HELIX 152 157 {ECO:0000244|PDB:1KQ3}. FT HELIX 160 183 {ECO:0000244|PDB:1KQ3}. FT STRAND 190 192 {ECO:0000244|PDB:1KQ3}. FT HELIX 195 220 {ECO:0000244|PDB:1KQ3}. FT HELIX 226 246 {ECO:0000244|PDB:1KQ3}. FT HELIX 250 258 {ECO:0000244|PDB:1KQ3}. FT HELIX 262 264 {ECO:0000244|PDB:1KQ3}. FT HELIX 269 283 {ECO:0000244|PDB:1KQ3}. FT HELIX 288 301 {ECO:0000244|PDB:1KQ3}. FT HELIX 307 310 {ECO:0000244|PDB:1KQ3}. FT HELIX 317 327 {ECO:0000244|PDB:1KQ3}. FT HELIX 333 336 {ECO:0000244|PDB:1KQ3}. FT STRAND 337 339 {ECO:0000244|PDB:1KQ3}. FT HELIX 343 360 {ECO:0000244|PDB:1KQ3}. SQ SEQUENCE 364 AA; 39692 MW; B44E20CACC6F1582 CRC64; MITTTIFPGR YVQGAGAINI LEEELSRFGE RAFVVIDDFV DKNVLGENFF SSFTKVRVNK QIFGGECSDE EIERLSGLVE EETDVVVGIG GGKTLDTAKA VAYKLKKPVV IVPTIASTDA PCSALSVIYT PNGEFKRYLF LPRNPDVVLV DTEIVAKAPA RFLVAGMGDA LATWFEAESC KQKYAPNMTG RLGSMTAYAL ARLCYETLLE YGVLAKRSVE EKSVTPALEK IVEANTLLSG LGFESGGLAA AHAIHNGLTV LENTHKYLHG EKVAIGVLAS LFLTDKPRKM IEEVYSFCEE VGLPTTLAEI GLDGVSDEDL MKVAEKACDK NETIHNEPQP VTSKDVFFAL KAADRYGRMR KNLT // ID GAL7_THEMA Reviewed; 318 AA. AC O33836; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 13-APR-2016, entry version 119. DE RecName: Full=Galactose-1-phosphate uridylyltransferase; DE Short=Gal-1-P uridylyltransferase; DE EC=2.7.7.12; DE AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase; GN Name=galT; OrderedLocusNames=TM_1191; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9741105; RA Liebl W., Wagner B., Schellhase J.; RT "Properties of an alpha-galactosidase, and structure of its gene galA, RT within an alpha- and beta-galactoside utilization gene cluster of the RT hyperthermophilic bacterium Thermotoga maritima."; RL Syst. Appl. Microbiol. 21:1-11(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + alpha-D-galactose 1- CC phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000305}; CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism. CC -!- SIMILARITY: Belongs to the galactose-1-phosphate CC uridylyltransferase type 1 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ001072; CAA04515.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36266.1; -; Genomic_DNA. DR PIR; D72283; D72283. DR RefSeq; NP_228996.1; NC_000853.1. DR RefSeq; WP_004080138.1; NZ_CP011107.1. DR ProteinModelPortal; O33836; -. DR STRING; 243274.TM1191; -. DR EnsemblBacteria; AAD36266; AAD36266; TM_1191. DR GeneID; 898293; -. DR KEGG; tma:TM1191; -. DR PATRIC; 23937324; VBITheMar51294_1209. DR eggNOG; ENOG4105F0Z; Bacteria. DR eggNOG; COG1085; LUCA. DR InParanoid; O33836; -. DR KO; K00965; -. DR OMA; WHYAPFF; -. DR OrthoDB; EOG6CCH5M; -. DR BioCyc; MetaCyc:MONOMER-506; -. DR UniPathway; UPA00214; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.428.10; -; 2. DR InterPro; IPR001937; GalP_UDPtransf1. DR InterPro; IPR019779; GalP_UDPtransf1_His-AS. DR InterPro; IPR005850; GalP_Utransf_C. DR InterPro; IPR005849; GalP_Utransf_N. DR InterPro; IPR011146; HIT-like. DR PANTHER; PTHR11943; PTHR11943; 1. DR Pfam; PF02744; GalP_UDP_tr_C; 1. DR Pfam; PF01087; GalP_UDP_transf; 1. DR PIRSF; PIRSF000808; GalT; 1. DR SUPFAM; SSF54197; SSF54197; 2. DR TIGRFAMs; TIGR00209; galT_1; 1. DR PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Galactose metabolism; KW Iron; Metal-binding; Nucleotidyltransferase; Reference proteome; KW Transferase; Zinc. FT CHAIN 1 318 Galactose-1-phosphate FT uridylyltransferase. FT /FTId=PRO_0000169898. FT ACT_SITE 143 143 Tele-UMP-histidine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU10033}. FT METAL 32 32 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU10033}. FT METAL 35 35 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU10033}. FT METAL 90 90 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU10033}. FT METAL 141 141 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU10033}. SQ SEQUENCE 318 AA; 37633 MW; E913778A6D770C6E CRC64; MMELRYNPLT DEWVIVSAAT QKRPVQPSKT ECPICVGGLE LPEEYDLVTF ENRYPSLKKD PPPVNWKEKG PFRKEESRGV CEVVVYTSDH NTALPGMPLK QIEKLVEMWV DRTRDLSQHD FVKYIFIFEN RGKEVGASLP HPHGQIYAFP FLPKRIEVKI GAMRKWYEEK RKCPICEVLE SEGEERKVYE TEHFLALVPF YARFPYEVHI YPKRHVSTLL EFSKEEKKEF AKVLKVVTAK YDKLFDQEFP YMMMFFQAPF NEEDVSHFFH FHVEFNPPKR DRDKLKWMAS VETGTWAFIN PVVPEEAARQ LRETEVEI // ID GATC_THEMA Reviewed; 96 AA. AC Q9WY94; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C; DE Short=Glu-ADT subunit C; DE EC=6.3.5.-; GN Name=gatC; OrderedLocusNames=TM_0252; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) CC or Gln-tRNA(Gln) through the transamidation of misacylated Asp- CC tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both CC of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction CC takes place in the presence of glutamine and ATP through an CC activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35342.1; -; Genomic_DNA. DR PIR; E72399; E72399. DR RefSeq; NP_228066.1; NC_000853.1. DR RefSeq; WP_004082956.1; NZ_CP011107.1. DR PDB; 3AL0; X-ray; 3.37 A; C=2-96. DR PDBsum; 3AL0; -. DR ProteinModelPortal; Q9WY94; -. DR DIP; DIP-59230N; -. DR STRING; 243274.TM0252; -. DR EnsemblBacteria; AAD35342; AAD35342; TM_0252. DR GeneID; 897161; -. DR KEGG; tma:TM0252; -. DR PATRIC; 23935379; VBITheMar51294_0255. DR eggNOG; ENOG41084A9; Bacteria. DR eggNOG; COG0721; LUCA. DR InParanoid; Q9WY94; -. DR KO; K02435; -. DR OMA; EGVEPMF; -. DR OrthoDB; EOG625K3N; -. DR EvolutionaryTrace; Q9WY94; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00122; GatC; 1. DR InterPro; IPR003837; Asp/Glu-ADT_csu. DR Pfam; PF02686; Glu-tRNAGln; 1. DR SUPFAM; SSF141000; SSF141000; 1. DR TIGRFAMs; TIGR00135; gatC; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 96 Glutamyl-tRNA(Gln) amidotransferase FT subunit C. FT /FTId=PRO_0000105352. FT HELIX 8 13 {ECO:0000244|PDB:3AL0}. FT TURN 14 17 {ECO:0000244|PDB:3AL0}. FT STRAND 22 24 {ECO:0000244|PDB:3AL0}. FT HELIX 25 39 {ECO:0000244|PDB:3AL0}. FT TURN 40 42 {ECO:0000244|PDB:3AL0}. FT HELIX 74 78 {ECO:0000244|PDB:3AL0}. FT STRAND 88 92 {ECO:0000244|PDB:3AL0}. SQ SEQUENCE 96 AA; 11309 MW; C3CAE53D43EA4404 CRC64; MIKVTKDLVL HLENLARLEL SEDQRESLMK DFQEILDYVE LLNEVDVEGV EPMYTPVEDS AKLRKGDPRF FEMRDLIKKN FPEEKDGHIK VPGIHR // ID GCH4_THEMA Reviewed; 259 AA. AC Q9WXP6; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 84. DE RecName: Full=GTP cyclohydrolase FolE2; DE EC=3.5.4.16; DE AltName: Full=GTP cyclohydrolase 1B; GN Name=folE2; OrderedLocusNames=TM_0039; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=17032654; DOI=10.1074/jbc.M607114200; RA El Yacoubi B., Bonnett S., Anderson J.N., Swairjo M.A., RA Iwata-Reuyl D., de Crecy-Lagard V.; RT "Discovery of a new prokaryotic type I GTP cyclohydrolase family."; RL J. Biol. Chem. 281:37586-37593(2006). CC -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate. CC {ECO:0000269|PubMed:17032654}. CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = formate + 2-amino-4-hydroxy-6- CC (erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. CC {ECO:0000269|PubMed:17032654}. CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step CC 1/1. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35133.1; -; Genomic_DNA. DR PIR; D72425; D72425. DR RefSeq; NP_227855.1; NC_000853.1. DR RefSeq; WP_004082504.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXP6; -. DR STRING; 243274.TM0039; -. DR EnsemblBacteria; AAD35133; AAD35133; TM_0039. DR GeneID; 896863; -. DR KEGG; tma:TM0039; -. DR PATRIC; 23934918; VBITheMar51294_0037. DR eggNOG; ENOG4105DZA; Bacteria. DR eggNOG; COG1469; LUCA. DR InParanoid; Q9WXP6; -. DR KO; K09007; -. DR OMA; INMYVDL; -. DR OrthoDB; EOG6X6RBH; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-HAMAP. DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1. DR InterPro; IPR022838; GTP_cyclohydrolase_FolE2. DR InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA. DR Pfam; PF02649; GCHY-1; 1. DR TIGRFAMs; TIGR00294; TIGR00294; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 259 GTP cyclohydrolase FolE2. FT /FTId=PRO_0000147732. FT SITE 143 143 May be catalytically important. FT {ECO:0000250}. SQ SEQUENCE 259 AA; 30309 MW; 89A5C0EA52EEF34D CRC64; MKDVQNEKDP RMVPLKKVGI KDLHWPLKVI LKEDGYQSTV AQISCSVDLH REKRGIHMSR FIEVLNKLEV ITPQIFEEIL DDLIEIMEAK RAHLEIHFPY FIWKESPVSR KKSPLKVDCF VEAEKEKNFS FKIGVRTPVH TLCPCSKEIS DYGAHNQRAF VEITVKTRKF IWFEDLVEIA EKNASSPLYT LLKRPDEKFV TEKAYENPRF VEDVARDVAL ELEKDPRITW YRVYVESMES IHNHNAFACV EKGDFVLEG // ID GCSPB_THEMA Reviewed; 474 AA. AC Q9WY57; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713}; DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00713}; DE AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713}; DE AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713}; DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713}; GN Name=gcvPB {ECO:0000255|HAMAP-Rule:MF_00713}; GN OrderedLocusNames=TM_0214; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. The P protein binds the alpha-amino group of glycine CC through its pyridoxal phosphate cofactor; CO(2) is released and CC the remaining methylamine moiety is then transferred to the CC lipoamide cofactor of the H protein. {ECO:0000255|HAMAP- CC Rule:MF_00713}. CC -!- CATALYTIC ACTIVITY: Glycine + [glycine-cleavage complex H CC protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H CC protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_00713}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00713}; CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H. In this organism, the P 'protein' is a heterodimer CC of two subunits. {ECO:0000255|HAMAP-Rule:MF_00713}. CC -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00713}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35306.1; -; Genomic_DNA. DR PIR; H72403; H72403. DR RefSeq; NP_228029.1; NC_000853.1. DR RefSeq; WP_004082890.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY57; -. DR SMR; Q9WY57; 2-473. DR STRING; 243274.TM0214; -. DR EnsemblBacteria; AAD35306; AAD35306; TM_0214. DR GeneID; 897096; -. DR KEGG; tma:TM0214; -. DR PATRIC; 23935300; VBITheMar51294_0216. DR eggNOG; ENOG4105CBI; Bacteria. DR eggNOG; COG1003; LUCA. DR InParanoid; Q9WY57; -. DR KO; K00283; -. DR OMA; MHINLHK; -. DR OrthoDB; EOG6HMXDX; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central. DR GO; GO:0016594; F:glycine binding; IBA:GO_Central. DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central. DR Gene3D; 3.40.640.10; -; 1. DR HAMAP; MF_00713; GcvPB; 1. DR InterPro; IPR023012; GcvPB. DR InterPro; IPR020580; GDC-P_N. DR InterPro; IPR020581; GDC_P. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR PANTHER; PTHR11773; PTHR11773; 1. DR Pfam; PF02347; GDC-P; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1 474 Probable glycine dehydrogenase FT (decarboxylating) subunit 2. FT /FTId=PRO_0000167021. FT MOD_RES 262 262 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00713}. SQ SEQUENCE 474 AA; 53468 MW; 992607C3A1B61EF8 CRC64; MTIFERSKKG RKAFRLPESD IPEYSLPDRF LRRTPPELPE VSEPDLVRHY TNLARKNYSV DLGIYPLGSC TMKYNPKLNE KAANLEGFRE IHPYQPVETV QGSLRLMYEL KKMLCEITGM DDMTLQPAAG AHGELTGMLI VREYFKNRGD TGRKKVLVPD SAHGTNPASA SMVGFEVVEI KSKNGMVDVE DLKKLLDEEV AAVMLTNPNT LGLFEKDILK IAEMTHECGA LLYYDGANLN AIMGKVRPGD MGFDIVHLNL HKTFSTPHGM GGPGSGPVGV KKHLVDFLPF PQVKKNGELY ELFVPEKTIG RVRSFFGNFP VLVKAYTYIL TMGRDGLERV SEMAVLNANY LKKKIEKFLE IPYNGFCMHE FVASAEKVFR ETGVRTLDIA KRILDFGVHP PTVYFPLIVP EALMIEPTET ENKETLDKYA EILERVVKEA YENPDALKNA PHNTPVRRVN EVLASKKPVF RWRG // ID GLMS_THEMA Reviewed; 606 AA. AC Q9WXZ5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 13-APR-2016, entry version 111. DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164}; DE EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164}; GN Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164}; GN OrderedLocusNames=TM_0148; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, CC converting fructose-6P into glucosamine-6P using glutamine as a CC nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L- CC glutamate + D-glucosamine 6-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00164}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- SIMILARITY: Contains 2 SIS domains. {ECO:0000255|HAMAP- CC Rule:MF_00164}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35241.1; -; Genomic_DNA. DR PIR; B72412; B72412. DR RefSeq; NP_227963.1; NC_000853.1. DR RefSeq; WP_004082756.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXZ5; -. DR STRING; 243274.TM0148; -. DR MEROPS; C44.971; -. DR EnsemblBacteria; AAD35241; AAD35241; TM_0148. DR GeneID; 896981; -. DR KEGG; tma:TM0148; -. DR PATRIC; 23935140; VBITheMar51294_0147. DR eggNOG; ENOG4105C46; Bacteria. DR eggNOG; COG0449; LUCA. DR InParanoid; Q9WXZ5; -. DR KO; K00820; -. DR OMA; GEFFCAS; -. DR OrthoDB; EOG6KT2Q1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_00164; GlmS; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR005855; GlmS_trans. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR001347; SIS. DR PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1. DR Pfam; PF01380; SIS; 2. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR01135; glmS; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. DR PROSITE; PS51464; SIS; 2. PE 3: Inferred from homology; KW Aminotransferase; Complete proteome; Cytoplasm; KW Glutamine amidotransferase; Reference proteome; Repeat; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000255|HAMAP- FT Rule:MF_00164}. FT CHAIN 2 606 Glutamine--fructose-6-phosphate FT aminotransferase [isomerizing]. FT /FTId=PRO_0000135400. FT DOMAIN 2 217 Glutamine amidotransferase type-2. FT {ECO:0000255|HAMAP-Rule:MF_00164}. FT DOMAIN 284 423 SIS 1. {ECO:0000255|HAMAP-Rule:MF_00164}. FT DOMAIN 455 596 SIS 2. {ECO:0000255|HAMAP-Rule:MF_00164}. FT ACT_SITE 2 2 Nucleophile; for GATase activity. FT {ECO:0000255|HAMAP-Rule:MF_00164}. FT ACT_SITE 601 601 For Fru-6P isomerization activity. FT {ECO:0000255|HAMAP-Rule:MF_00164}. SQ SEQUENCE 606 AA; 68082 MW; FDB0BE7AE1B14174 CRC64; MCGIVGMVGE NLKLEDLVTS LQKLEYRGYD SAGIAYLGDS FGVYKKKGRI DVLKNGLKQK LNDRFFVGIA HTRWATHGEP NDMNAHPHMD CKEEIAVVHN GIIENYREIR EFLEQRGHVF SSETDTEVIA HLVEEEFEGD LLDAVLKAVK KLKGAYAIAV VHKNVPDTIV AARKGSPLVA GIGSGVGILA SDVTPLLRFT KDVVFLEDGD VMVLRKDGFE IYNTDGVKQQ RRVYHVNWDE KAAEKGGYKH FMYKEIMEDP QALVNALVGR VKNDRPFFEE LEYYEELLKN ADRIRVVSCG TSYYAGLVFK YFLENHTDID VEIEVSSEFR YKRPHIKEGD VLIAISQSGE TADTLESVRL AKKHGAKIVS IVNVVGSTLD RESDVTLFMN AGPEIGVAAT KTYVAELAVL YLLGLKIMEI NGYWDREAEE ILDKLVRMPE LLENVLRKDP QIRELSEKYK DYRNFMYIGR GYGYPTALEG ALKLKEITYI HATAYQAGEL KHGPIALLDV DFPVFAVMPD DSLFFKTKSN VIESKSRNAP VIVLGTEGNR SLEEITGDII HVPPTHESLY PLMMAPVIQL FAYHIADLKG LDPDKPRNLA KSVTVE // ID GCST_THEMA Reviewed; 364 AA. AC Q9WY54; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=Aminomethyltransferase {ECO:0000255|HAMAP-Rule:MF_00259}; DE EC=2.1.2.10 {ECO:0000255|HAMAP-Rule:MF_00259}; DE AltName: Full=Glycine cleavage system T protein {ECO:0000255|HAMAP-Rule:MF_00259}; GN Name=gcvT {ECO:0000255|HAMAP-Rule:MF_00259}; GN OrderedLocusNames=TM_0211; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. {ECO:0000255|HAMAP-Rule:MF_00259}. CC -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine CC + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10- CC methylenetetrahydrofolate + NH(3). {ECO:0000255|HAMAP- CC Rule:MF_00259}. CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H. {ECO:0000255|HAMAP-Rule:MF_00259}. CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP- CC Rule:MF_00259}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35303.1; -; Genomic_DNA. DR PIR; E72403; E72403. DR RefSeq; NP_228026.1; NC_000853.1. DR RefSeq; WP_004082884.1; NZ_CP011107.1. DR PDB; 1WOO; X-ray; 2.40 A; A=1-364. DR PDB; 1WOP; X-ray; 2.00 A; A=1-364. DR PDB; 1WOR; X-ray; 1.95 A; A=1-364. DR PDB; 1WOS; X-ray; 1.84 A; A=1-364. DR PDBsum; 1WOO; -. DR PDBsum; 1WOP; -. DR PDBsum; 1WOR; -. DR PDBsum; 1WOS; -. DR ProteinModelPortal; Q9WY54; -. DR SMR; Q9WY54; 1-362. DR STRING; 243274.TM0211; -. DR EnsemblBacteria; AAD35303; AAD35303; TM_0211. DR GeneID; 897085; -. DR KEGG; tma:TM0211; -. DR PATRIC; 23935294; VBITheMar51294_0213. DR eggNOG; ENOG4105D43; Bacteria. DR eggNOG; COG0404; LUCA. DR InParanoid; Q9WY54; -. DR KO; K00605; -. DR OMA; LGWLVHL; -. DR OrthoDB; EOG6T1WS5; -. DR EvolutionaryTrace; Q9WY54; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.30.110; -; 1. DR Gene3D; 3.30.1360.120; -; 2. DR HAMAP; MF_00259; GcvT; 1. DR InterPro; IPR006223; GCS_T. DR InterPro; IPR022903; GCS_T_bac. DR InterPro; IPR028896; GCST/DmdA. DR InterPro; IPR013977; GCV_T_C. DR InterPro; IPR006222; GCV_T_N. DR InterPro; IPR029043; GcvT/YgfZ_C. DR InterPro; IPR027266; TrmE/GcvT_dom1. DR PANTHER; PTHR13847:SF5; PTHR13847:SF5; 1. DR Pfam; PF01571; GCV_T; 1. DR Pfam; PF08669; GCV_T_C; 1. DR PIRSF; PIRSF006487; GcvT; 1. DR SUPFAM; SSF101790; SSF101790; 1. DR TIGRFAMs; TIGR00528; gcvT; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminotransferase; Complete proteome; Reference proteome; KW Transferase. FT CHAIN 1 364 Aminomethyltransferase. FT /FTId=PRO_0000122610. FT HELIX 7 12 {ECO:0000244|PDB:1WOS}. FT STRAND 16 20 {ECO:0000244|PDB:1WOS}. FT STRAND 23 30 {ECO:0000244|PDB:1WOS}. FT HELIX 32 41 {ECO:0000244|PDB:1WOS}. FT STRAND 44 47 {ECO:0000244|PDB:1WOS}. FT STRAND 51 58 {ECO:0000244|PDB:1WOS}. FT HELIX 61 68 {ECO:0000244|PDB:1WOS}. FT STRAND 69 71 {ECO:0000244|PDB:1WOS}. FT STRAND 80 87 {ECO:0000244|PDB:1WOS}. FT STRAND 93 103 {ECO:0000244|PDB:1WOS}. FT STRAND 106 111 {ECO:0000244|PDB:1WOS}. FT HELIX 113 115 {ECO:0000244|PDB:1WOS}. FT HELIX 116 124 {ECO:0000244|PDB:1WOS}. FT STRAND 133 136 {ECO:0000244|PDB:1WOS}. FT HELIX 138 140 {ECO:0000244|PDB:1WOS}. FT STRAND 141 148 {ECO:0000244|PDB:1WOS}. FT HELIX 151 155 {ECO:0000244|PDB:1WOS}. FT HELIX 156 158 {ECO:0000244|PDB:1WOS}. FT STRAND 159 161 {ECO:0000244|PDB:1WOS}. FT HELIX 163 165 {ECO:0000244|PDB:1WOP}. FT STRAND 170 176 {ECO:0000244|PDB:1WOS}. FT STRAND 179 185 {ECO:0000244|PDB:1WOS}. FT STRAND 188 199 {ECO:0000244|PDB:1WOS}. FT HELIX 200 202 {ECO:0000244|PDB:1WOS}. FT HELIX 203 217 {ECO:0000244|PDB:1WOS}. FT STRAND 220 222 {ECO:0000244|PDB:1WOO}. FT HELIX 224 233 {ECO:0000244|PDB:1WOS}. FT TURN 239 241 {ECO:0000244|PDB:1WOS}. FT HELIX 249 252 {ECO:0000244|PDB:1WOS}. FT HELIX 255 257 {ECO:0000244|PDB:1WOS}. FT HELIX 267 275 {ECO:0000244|PDB:1WOS}. FT STRAND 279 289 {ECO:0000244|PDB:1WOS}. FT STRAND 297 300 {ECO:0000244|PDB:1WOS}. FT STRAND 303 314 {ECO:0000244|PDB:1WOS}. FT TURN 315 318 {ECO:0000244|PDB:1WOS}. FT STRAND 319 327 {ECO:0000244|PDB:1WOS}. FT STRAND 335 340 {ECO:0000244|PDB:1WOS}. FT TURN 341 343 {ECO:0000244|PDB:1WOS}. FT STRAND 344 351 {ECO:0000244|PDB:1WOS}. SQ SEQUENCE 364 AA; 40333 MW; 66F33CCC151CC6F1 CRC64; MKRTPLFEKH VELGAKMVDF AGWEMPLYYT SIFEEVMAVR KSVGMFDVSH MGEFLVKGPE AVSFIDFLIT NDFSSLPDGK AIYSVMCNEN GGIIDDLVVY KVSPDEALMV VNAANIEKDF NWIKSHSKNF DVEVSNISDT TALIAFQGPK AQETLQELVE DGLEEIAYYS FRKSIVAGVE TLVSRTGYTG EDGFELMLEA KNAPKVWDAL MNLLRKIDGR PAGLGARDVC RLEATYLLYG QDMDENTNPF EVGLSWVVKL NKDFVGKEAL LKAKEKVERK LVALELSGKR IARKGYEVLK NGERVGEITS GNFSPTLGKS IALALVSKSV KIGDQLGVVF PGGKLVEALV VKKPFYRGSV RREV // ID GLPK2_THEMA Reviewed; 496 AA. AC Q9X1E4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 107. DE RecName: Full=Glycerol kinase 2 {ECO:0000255|HAMAP-Rule:MF_00186}; DE EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186}; DE AltName: Full=ATP:glycerol 3-phosphotransferase 2 {ECO:0000255|HAMAP-Rule:MF_00186}; DE AltName: Full=Glycerokinase 2 {ECO:0000255|HAMAP-Rule:MF_00186}; DE Short=GK 2 {ECO:0000255|HAMAP-Rule:MF_00186}; GN Name=glpK2 {ECO:0000255|HAMAP-Rule:MF_00186}; GN OrderedLocusNames=TM_1430; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and CC metabolism. Catalyzes the phosphorylation of glycerol to yield sn- CC glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- ENZYME REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP). CC {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol CC kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00186}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD36500.1; Type=Erroneous termination; Positions=483; Note=Translated as Trp.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36500.1; ALT_SEQ; Genomic_DNA. DR PIR; C72254; C72254. DR RefSeq; NP_229230.1; NC_000853.1. DR RefSeq; WP_010865340.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1E4; -. DR SMR; Q9X1E4; 2-495. DR STRING; 243274.TM1430; -. DR EnsemblBacteria; AAD36500; AAD36500; TM_1430. DR GeneID; 898045; -. DR KEGG; tma:TM1430; -. DR PATRIC; 23937808; VBITheMar51294_1442. DR eggNOG; ENOG4108JQ0; Bacteria. DR eggNOG; COG0554; LUCA. DR InParanoid; Q9X1E4; -. DR KO; K00864; -. DR OMA; GWVEHEP; -. DR OrthoDB; EOG6RZB46; -. DR BioCyc; TMAR243274:GC6P-1468-MONOMER; -. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central. DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR HAMAP; MF_00186; Glycerol_kin; 1. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR InterPro; IPR005999; Glycerol_kin. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR TIGRFAMs; TIGR01311; glycerol_kin; 1. DR PROSITE; PS00933; FGGY_KINASES_1; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glycerol metabolism; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 496 Glycerol kinase 2. FT /FTId=PRO_0000059514. FT NP_BIND 11 13 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT NP_BIND 408 412 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT REGION 81 82 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT REGION 242 243 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 11 11 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 15 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 133 133 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 264 264 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 307 307 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 311 311 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 326 326 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. SQ SEQUENCE 496 AA; 55576 MW; 7FA72A4CBD29E701 CRC64; MKYVLSLDQG TTSSRAIVFD EKGNVVSKVN KEFRQIYPRP GWVEHDPVEI WESQIEVAKK AIEEAGIKPE DIAAIGITNQ RETTIVWDKN TGKPVYNAIV WQCRRTAPIC DELKEKGYSE FIRERTGLVI DAYFSGTKIK WILDNVEGVR EKAEKGEVLF GTVDTWLIWN LTGGRVHVTD YSNASRTMIF NIHKLDWDDE ILELLNIPRA MLPQVMPSSH VYGYTAKDIF GVEIPIAGDA GDQQAALFGQ ACFQPGMLKN TYGTGCFLLM NTGEKAFESK SGLLTTIAWG INGKVYYALE GSIFITGAAV QWLRDGLKII SNAAETEELA TKVPDNGGVF FVPAFVGLGA PYWDMYARGL IIGITRGTTR EHIVRAVLES IAYQTRDVVE VMEKDSDIKV ETLRVDGGAV VNNFLMQFQA DILGVPVERP VVNETTALGA AYLAGLAVGY WKDQEEIASL WQLDRRFEPS MNSEERERLY SKWKEAVSRS LGWEKR // ID GLGC_THEMA Reviewed; 423 AA. AC Q9WY82; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00624}; DE EC=2.7.7.27 {ECO:0000255|HAMAP-Rule:MF_00624}; DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00624}; DE Short=ADPGlc PPase {ECO:0000255|HAMAP-Rule:MF_00624}; DE AltName: Full=ADP-glucose synthase {ECO:0000255|HAMAP-Rule:MF_00624}; GN Name=glgC {ECO:0000255|HAMAP-Rule:MF_00624}; GN OrderedLocusNames=TM_0240; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the synthesis of ADP-glucose, a sugar donor CC used in elongation reactions on alpha-glucans. {ECO:0000255|HAMAP- CC Rule:MF_00624}. CC -!- CATALYTIC ACTIVITY: ATP + alpha-D-glucose 1-phosphate = CC diphosphate + ADP-glucose. {ECO:0000255|HAMAP-Rule:MF_00624}. CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00624}. CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate CC adenylyltransferase family. {ECO:0000255|HAMAP-Rule:MF_00624}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35331.1; -; Genomic_DNA. DR PIR; B72403; B72403. DR RefSeq; NP_228054.1; NC_000853.1. DR RefSeq; WP_004082942.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY82; -. DR STRING; 243274.TM0240; -. DR EnsemblBacteria; AAD35331; AAD35331; TM_0240. DR GeneID; 897141; -. DR KEGG; tma:TM0240; -. DR PATRIC; 23935355; VBITheMar51294_0243. DR eggNOG; ENOG4105CNB; Bacteria. DR eggNOG; COG0448; LUCA. DR InParanoid; Q9WY82; -. DR KO; K00975; -. DR OMA; KAVAHHF; -. DR OrthoDB; EOG6W9X86; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.550.10; -; 2. DR HAMAP; MF_00624; GlgC; 1. DR InterPro; IPR005836; ADP_Glu_pyroP_CS. DR InterPro; IPR011831; GlgC. DR InterPro; IPR023049; GlgC_bac. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 1. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 2. DR TIGRFAMs; TIGR02091; glgC; 1. DR PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1. DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; KW Glycogen biosynthesis; Glycogen metabolism; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 423 Glucose-1-phosphate adenylyltransferase. FT /FTId=PRO_0000195340. SQ SEQUENCE 423 AA; 47139 MW; 013DE78538FCC62E CRC64; MGNTVAMILA GGQGTRLGVL TERIAKPAVP FGGKYRLIDF TLSNCVNSGI YRVGVLTQYR PHVLSKHIGI GRPWDLDRKD GGVEILPPYV GRHESDWYKG TANAVYQNLE FLEENDAELV LILSGDHVYA MNYNDLIDYH LLKEADGTIA CMEVPIEEAS RFGIMITDVD GRIVDFEEKP AKPRSNLASL GIYVFNYEFL KKVLIEDEND PNSSHDFGKD VIPRILRENL GSLYAFRFDG YWRDVGTLRS YWEANLELVL PVPPFNLYDP NWRFFTHTEE MPPAYVAPGS KVSTSLVSEG AEVYGNVFNS VIFQGVKIGR GTVVKNSVIM TRTEIGENCY LENVIIAENV KIGSNVRMGV GEDAESKLDP KVYSGLLTVV GMNSVIPDDM VIGKNCVIGI GVRPEDFKSK TLESGDYVIV REE // ID GLMM_THEMA Reviewed; 429 AA. AC Q9WY28; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=Phosphoglucosamine mutase {ECO:0000255|HAMAP-Rule:MF_01554}; DE EC=5.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01554}; GN Name=glmM {ECO:0000255|HAMAP-Rule:MF_01554}; GN OrderedLocusNames=TM_0184; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to CC glucosamine-1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01554}. CC -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 1-phosphate = D- CC glucosamine 6-phosphate. {ECO:0000255|HAMAP-Rule:MF_01554}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01554}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01554}; CC -!- PTM: Activated by phosphorylation. {ECO:0000255|HAMAP- CC Rule:MF_01554}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000255|HAMAP-Rule:MF_01554}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35277.1; -; Genomic_DNA. DR PIR; C72408; C72408. DR RefSeq; NP_227999.1; NC_000853.1. DR RefSeq; WP_004082821.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY28; -. DR STRING; 243274.TM0184; -. DR DNASU; 897032; -. DR EnsemblBacteria; AAD35277; AAD35277; TM_0184. DR GeneID; 897032; -. DR KEGG; tma:TM0184; -. DR PATRIC; 23935224; VBITheMar51294_0185. DR eggNOG; ENOG4107QJF; Bacteria. DR eggNOG; COG1109; LUCA. DR InParanoid; Q9WY28; -. DR KO; K03431; -. DR OMA; MIKNSAI; -. DR OrthoDB; EOG6TN467; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.310.50; -; 1. DR Gene3D; 3.40.120.10; -; 3. DR HAMAP; MF_01554_B; GlmM_B; 1. DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I. DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III. DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II. DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III. DR InterPro; IPR005843; A-D-PHexomutase_C. DR InterPro; IPR016066; A-D-PHexomutase_CS. DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF. DR InterPro; IPR006352; GlmM_bact. DR Pfam; PF02878; PGM_PMM_I; 1. DR Pfam; PF02879; PGM_PMM_II; 1. DR Pfam; PF02880; PGM_PMM_III; 1. DR Pfam; PF00408; PGM_PMM_IV; 1. DR PRINTS; PR00509; PGMPMM. DR SUPFAM; SSF53738; SSF53738; 3. DR SUPFAM; SSF55957; SSF55957; 1. DR TIGRFAMs; TIGR01455; glmM; 1. DR PROSITE; PS00710; PGM_PMM; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Magnesium; Metal-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1 429 Phosphoglucosamine mutase. FT /FTId=PRO_0000147991. FT ACT_SITE 96 96 Phosphoserine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01554}. FT METAL 96 96 Magnesium; via phosphate group. FT {ECO:0000255|HAMAP-Rule:MF_01554}. FT METAL 230 230 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT METAL 232 232 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT METAL 234 234 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT MOD_RES 96 96 Phosphoserine. {ECO:0000255|HAMAP- FT Rule:MF_01554}. SQ SEQUENCE 429 AA; 46949 MW; 909E25177B441E6E CRC64; MRVKYFGTDG IRGIFGETLT DELAFKVGKA LGEIVGEGKV IVGKDTRVSG DSLEAAISAG LTSMGVDVLL CGILPTPAVA LLTRITRSFG VVISASHNPP EYNGIKVLKG GYKIPDEMEA EIEKRLENGS FLTRSVVGRT KSFREGRDMY IGAVLEMFRD LDLTGEMVSL DLANGATTTT AREVFEFLGA KVEVFNDSQD GLLINQGCGA THPRFLAEEM KNGKVGFTFD GDGDRVIAVD EERNVVNGDR IIGILAVGLK EEGRLNSDTV VGTVMTNGGL EDFLKEKGIR LLRTKVGDKY VLEKMLESGA NLGGERSGHI IILDRSTTGD GLITALELMR VLKRSGRKLS DFAKEIPDYP QITKNVRRTE RMSLENENLR KIVEESTSRG YRVVIRPSGT EPVIRITVEG KDREEIEKIV EEISRVLES // ID GLGA_THEMA Reviewed; 486 AA. AC Q9WZZ7; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Glycogen synthase {ECO:0000255|HAMAP-Rule:MF_00484}; DE EC=2.4.1.21 {ECO:0000255|HAMAP-Rule:MF_00484}; DE AltName: Full=Starch [bacterial glycogen] synthase {ECO:0000255|HAMAP-Rule:MF_00484}; GN Name=glgA {ECO:0000255|HAMAP-Rule:MF_00484}; GN OrderedLocusNames=TM_0895; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose. CC {ECO:0000255|HAMAP-Rule:MF_00484}. CC -!- CATALYTIC ACTIVITY: ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP CC + (1,4-alpha-D-glucosyl)(n+1). {ECO:0000255|HAMAP-Rule:MF_00484}. CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00484}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. CC Bacterial/plant glycogen synthase subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00484}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35976.1; -; Genomic_DNA. DR PIR; H72321; H72321. DR RefSeq; NP_228703.1; NC_000853.1. DR RefSeq; WP_004080686.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZZ7; -. DR STRING; 243274.TM0895; -. DR CAZy; GT5; Glycosyltransferase Family 5. DR EnsemblBacteria; AAD35976; AAD35976; TM_0895. DR GeneID; 898569; -. DR KEGG; tma:TM0895; -. DR PATRIC; 23936721; VBITheMar51294_0909. DR eggNOG; ENOG4105CXW; Bacteria. DR eggNOG; COG0297; LUCA. DR InParanoid; Q9WZZ7; -. DR KO; K00703; -. DR OMA; NLQINGM; -. DR OrthoDB; EOG6JTC6Z; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro. DR GO; GO:0009011; F:starch synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00484; Glycogen_synth; 1. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR011835; GS/SS. DR InterPro; IPR013534; Starch_synth_cat_dom. DR Pfam; PF08323; Glyco_transf_5; 1. DR Pfam; PF00534; Glycos_transf_1; 1. DR TIGRFAMs; TIGR02095; glgA; 1. PE 3: Inferred from homology; KW Complete proteome; Glycogen biosynthesis; Glycosyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 486 Glycogen synthase. FT /FTId=PRO_0000188658. FT BINDING 15 15 ADP-glucose. {ECO:0000255|HAMAP- FT Rule:MF_00484}. SQ SEQUENCE 486 AA; 55456 MW; 99241A36AE2CF435 CRC64; MKVVFVSYEV FPFAKVGGLA DVAGTLPKYL KKHGVDVTIV MPKHRIVEKN AEKFGYEIKK VAESLSVSHV KTDQKFDIYE SVLPGSDVKT YFVANDYYFS AEDVYAGPDL GEQAIFFCAA TLDLVKHLDL KPDIVHVNDW QTALIPVYLK TVYRDDPYFS RTATVLTIHN LGYQGVFDPK YLSFAGLPDY VYTIDGLEFY GQLNFLKGGI VFSDVINTVS PTYAEEIQTE EYGEKLDGVL RMRSKDLYGI LNGIDYELYN PATDRYIYVN YDVNRLELKW ENKVKLQEEL GLPVNKETAV AGLISRLVPQ KGLDLLVDVM DYLTLFDLQI VVLGTGDEQY ENAFRKFQER YPDKVSANIK FDVELAQKIY AGADIFLMPS RYEPCGLGQM FSMRYGTIPV VRYTGGLADT VKEYDPQSME GTGFGFKKYD SAHLLKAVSK ALHFYYREKD HWRRIMTNAM NTDLSWDRSA KEYVDLYKKA LAKVGR // ID GLMU_THEMA Reviewed; 445 AA. AC Q9X1W4; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631}; DE Includes: DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631}; DE EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631}; DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631}; DE Includes: DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631}; DE EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631}; GN Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631}; GN OrderedLocusNames=TM_1629; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de CC novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP- CC GlcNAc). The C-terminal domain catalyzes the transfer of acetyl CC group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) CC to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is CC converted into UDP-GlcNAc by the transfer of uridine 5- CC monophosphate (from uridine 5-triphosphate), a reaction catalyzed CC by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CC CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate CC = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01631}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate CC from alpha-D-glucosamine 6-phosphate (route II): step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N- CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36696.1; -; Genomic_DNA. DR PIR; E72229; E72229. DR RefSeq; NP_229429.1; NC_000853.1. DR RefSeq; WP_004082105.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1W4; -. DR STRING; 243274.TM1629; -. DR EnsemblBacteria; AAD36696; AAD36696; TM_1629. DR GeneID; 896999; -. DR KEGG; tma:TM1629; -. DR PATRIC; 23938232; VBITheMar51294_1648. DR eggNOG; ENOG4105CAJ; Bacteria. DR eggNOG; COG1207; LUCA. DR InParanoid; Q9X1W4; -. DR KO; K04042; -. DR OMA; SITANYD; -. DR OrthoDB; EOG6Z6FQZ; -. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00113; UER00533. DR UniPathway; UPA00973; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_01631; GlmU; 1. DR InterPro; IPR005882; Bifunctional_GlmU. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 3. DR Pfam; PF12804; NTP_transf_3; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR01173; glmU; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase; Cell shape; Cell wall biogenesis/degradation; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotidyltransferase; KW Peptidoglycan synthesis; Reference proteome; Repeat; Transferase. FT CHAIN 1 445 Bifunctional protein GlmU. FT /FTId=PRO_0000233868. FT REGION 1 218 Pyrophosphorylase. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 6 9 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 74 75 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 96 98 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 219 239 Linker. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 240 445 N-acetyltransferase. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 374 375 Acetyl-CoA binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT ACT_SITE 351 351 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT METAL 98 98 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT METAL 216 216 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 20 20 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 69 69 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 134 134 UDP-GlcNAc; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 147 147 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 162 162 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 216 216 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 321 321 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 339 339 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 354 354 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 365 365 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 368 368 Acetyl-CoA; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 393 393 Acetyl-CoA. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 411 411 Acetyl-CoA; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 428 428 Acetyl-CoA. {ECO:0000255|HAMAP- FT Rule:MF_01631}. SQ SEQUENCE 445 AA; 49011 MW; FCB39AE6D8FC94EB CRC64; MRALVLAAGK GTRMKSKIPK VLHPLSGRPM IEWVIETAGK VAQKVGVVLG FEAELVRKAL PEWVDVFVQG EQLGTAHAVM CAKDFIEPGD DVLILYGDVP LISENTLKRM IEEHRKGADV TILVADLEDP SGYGRVIQDG DKYRIIEDTD LPEELKSVTT INTGFYVFSG DFLLRALPEI KNENAKGEYY LTDAVNFAEK VRVVRTDDLL EITGVNTRKT LVWLEEQLRM RKIEELLENG VTILDPATTY IHYSVEIGMD TVIYPMTFIE GKSRVGENCE IGPMTRIVDC EIGNNVKITR SECFKSVIED DVSVGPFARL REGTILKKSS KIGNFVEIKK STIGEGTKAQ HLSYIGDAFV GKNVNVGAGT ITCNYDGKKK NPTFIEDGAF IGSNSSLVAP VRIGKGALIG AGSVITEDVP PYSLGLGRAR QVVKEGWVLK KRKEE // ID GLPF_THEMA Reviewed; 234 AA. AC Q9X1E3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 110. DE RecName: Full=Probable glycerol uptake facilitator protein; GN Name=glpF; OrderedLocusNames=TM_1429; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Glycerol enters the cell via the glycerol diffusion CC facilitator protein. This membrane protein facilitates the CC movement of glycerol across the cytoplasmic membrane (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing CC three membrane-spanning domains and a pore-forming loop with the CC signature motif Asn-Pro-Ala (NPA). CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36499.1; -; Genomic_DNA. DR PIR; B72254; B72254. DR RefSeq; NP_229229.1; NC_000853.1. DR RefSeq; WP_004081684.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1E3; -. DR STRING; 243274.TM1429; -. DR EnsemblBacteria; AAD36499; AAD36499; TM_1429. DR GeneID; 898046; -. DR KEGG; tma:TM1429; -. DR PATRIC; 23937806; VBITheMar51294_1441. DR eggNOG; ENOG4105D8C; Bacteria. DR eggNOG; COG0580; LUCA. DR InParanoid; Q9X1E3; -. DR KO; K02440; -. DR OMA; KIFTWLA; -. DR OrthoDB; EOG6P8TRZ; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015254; F:glycerol channel activity; IBA:GO_Central. DR GO; GO:0015250; F:water channel activity; IBA:GO_Central. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0015793; P:glycerol transport; IBA:GOC. DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central. DR GO; GO:0006833; P:water transport; IBA:GOC. DR Gene3D; 1.20.1080.10; -; 1. DR InterPro; IPR023271; Aquaporin-like. DR InterPro; IPR000425; MIP. DR InterPro; IPR022357; MIP_CS. DR PANTHER; PTHR19139; PTHR19139; 1. DR Pfam; PF00230; MIP; 1. DR PRINTS; PR00783; MINTRINSICP. DR SUPFAM; SSF81338; SSF81338; 1. DR TIGRFAMs; TIGR00861; MIP; 1. DR PROSITE; PS00221; MIP; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Glycerol metabolism; Membrane; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 234 Probable glycerol uptake facilitator FT protein. FT /FTId=PRO_0000064092. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 36 56 Helical. {ECO:0000255}. FT TRANSMEM 82 102 Helical. {ECO:0000255}. FT TRANSMEM 134 154 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 214 234 Helical. {ECO:0000255}. FT MOTIF 64 66 NPA 1. FT MOTIF 185 187 NPA 2. SQ SEQUENCE 234 AA; 24863 MW; 3A42AE91066D1C8E CRC64; MSVYLAEFLG TMLLIILGDG VVANVVLKKS KGHNSGWIVI TTGWGLAVAM SVYLVGRISG AHINPAVTIG LAFIGQFPWS KVPGYIFSQI LGAFVGAILV YLTYLPHWKE TDDPDAKLAV FCTGPAVRKY GANLLTEIIG TMVLLMGVLG IGANKLADGL NPLLVGFLVW SIGLSLGGPT GYAINPARDF GPRLAHAILP IPGKRDSDWS YSWVPIIGPI IGGILGASLY NWLF // ID GLYA_THEMA Reviewed; 427 AA. AC Q9WZH9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051}; DE Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051}; DE Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051}; DE EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051}; GN Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051}; GN OrderedLocusNames=TM_0720; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and CC glycine with tetrahydrofolate (THF) serving as the one-carbon CC carrier. This reaction serves as the major source of one-carbon CC groups required for the biosynthesis of purines, thymidylate, CC methionine, and other important biomolecules. Also exhibits THF- CC independent aldolase activity toward beta-hydroxyamino acids, CC producing glycine and aldehydes, via a retro-aldol mechanism. CC {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine + CC H(2)O = tetrahydrofolate + L-serine. {ECO:0000255|HAMAP- CC Rule:MF_00051}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine CC from L-serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP- CC Rule:MF_00051}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35802.1; -; Genomic_DNA. DR PIR; F72341; F72341. DR RefSeq; NP_228529.1; NC_000853.1. DR RefSeq; WP_004081014.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZH9; -. DR SMR; Q9WZH9; 9-386. DR STRING; 243274.TM0720; -. DR EnsemblBacteria; AAD35802; AAD35802; TM_0720. DR GeneID; 898387; -. DR KEGG; tma:TM0720; -. DR PATRIC; 23936360; VBITheMar51294_0733. DR eggNOG; ENOG4105C65; Bacteria. DR eggNOG; COG0112; LUCA. DR InParanoid; Q9WZH9; -. DR KO; K00600; -. DR OMA; KTYAQNV; -. DR OrthoDB; EOG6Z0QB2; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-HAMAP. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00051; SHMT; 1. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR InterPro; IPR001085; Ser_HO-MeTrfase. DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS. DR PANTHER; PTHR11680; PTHR11680; 1. DR Pfam; PF00464; SHMT; 1. DR PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00096; SHMT; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW One-carbon metabolism; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 427 Serine hydroxymethyltransferase. FT /FTId=PRO_0000113684. FT REGION 122 124 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT REGION 351 353 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 32 32 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 52 52 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 54 54 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 61 61 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 62 62 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 96 96 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 118 118 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00051}. FT BINDING 173 173 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 201 201 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 226 226 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 233 233 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 259 259 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 359 359 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT MOD_RES 227 227 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00051}. SQ SEQUENCE 427 AA; 47458 MW; 63F63D7723148751 CRC64; MWKHVKQVDP EIYEVLVNEL KRQEYGLELI ASENFASLAV IETMGSMLTN KYAEGYPKKR YYGGCEWVDR AEERAIERAK RLFGAKFANV QPHSGSQANM AVYLALAQPG DTIMGMSLSH GGHLTHGAPV NFSGKIFKVV PYGVNLETET IDYDEVRRLA LEHKPKIIVA GGSAYARIID FKRFREIADE VGAYLMVDMA HFAGLVAAGI HPNPLEYAHV VTSTTHKTLR GPRGGLILTN DPEIAKAVDK TIFPGIQGGP LMHVIAAKAV CFKEAMTEEF KEYQKQVVKN AKKMAEEFQK RGYRIVSGGT DTHLFLVDLT PKDITGKAAE KALESCGITV NKNTIPNEKR SPFVASGIRI GTPAVTTRGM KEEEMEEIAE MIDLVLSNVI DENGTVKPEV REEVSKKVRE LCERFPLYRD KIEGVEI // ID GLNA_THEMA Reviewed; 439 AA. AC P36205; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 112. DE RecName: Full=Glutamine synthetase; DE Short=GS; DE EC=6.3.1.2; DE AltName: Full=Glutamate--ammonia ligase; GN Name=glnA; OrderedLocusNames=TM_0943; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1348781; RA Sanangelantoni A.M., Forlani G., Ambroselli F., Cammarano P., RA Tiboni O.; RT "The glnA gene of the extremely thermophilic eubacterium Thermotoga RT maritima: cloning, primary structure, and expression in Escherichia RT coli."; RL J. Gen. Microbiol. 138:383-393(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate + CC L-glutamine. CC -!- ENZYME REGULATION: The activity of this enzyme is controlled by CC adenylation under conditions of abundant glutamine. The fully CC adenylated enzyme complex is inactive (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two CC hexagons. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X60160; CAA42729.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36024.1; -; Genomic_DNA. DR PIR; B72313; B72313. DR RefSeq; NP_228751.1; NC_000853.1. DR RefSeq; WP_004080619.1; NZ_CP011107.1. DR ProteinModelPortal; P36205; -. DR STRING; 243274.TM0943; -. DR EnsemblBacteria; AAD36024; AAD36024; TM_0943. DR GeneID; 898680; -. DR KEGG; tma:TM0943; -. DR PATRIC; 23936817; VBITheMar51294_0957. DR eggNOG; ENOG4105C5F; Bacteria. DR eggNOG; COG0174; LUCA. DR InParanoid; P36205; -. DR KO; K01915; -. DR OMA; ERSHHEM; -. DR OrthoDB; EOG6B360N; -. DR BioCyc; MetaCyc:MONOMER-502; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro. DR GO; GO:0009399; P:nitrogen fixation; IEA:InterPro. DR Gene3D; 3.10.20.70; -; 1. DR Gene3D; 3.30.590.10; -; 1. DR InterPro; IPR008147; Gln_synt_b-grasp. DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom. DR InterPro; IPR008146; Gln_synth_cat_dom. DR InterPro; IPR027303; Gln_synth_gly_rich_site. DR InterPro; IPR004809; Gln_synth_I. DR InterPro; IPR027302; Gln_synth_N_conserv_site. DR Pfam; PF00120; Gln-synt_C; 1. DR Pfam; PF03951; Gln-synt_N; 1. DR SMART; SM01230; Gln-synt_C; 1. DR SUPFAM; SSF54368; SSF54368; 1. DR TIGRFAMs; TIGR00653; GlnA; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00181; GLNA_ATP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1 439 Glutamine synthetase. FT /FTId=PRO_0000153273. FT MOD_RES 369 369 O-AMP-tyrosine. {ECO:0000250}. FT CONFLICT 204 204 A -> G (in Ref. 1; CAA42729). FT {ECO:0000305}. FT CONFLICT 280 280 A -> R (in Ref. 1; CAA42729). FT {ECO:0000305}. FT CONFLICT 336 336 S -> T (in Ref. 1; CAA42729). FT {ECO:0000305}. SQ SEQUENCE 439 AA; 50035 MW; ABE3E674BD2F2359 CRC64; MTIETIKRII EEENVRFIRL QFTDINGTLK NLEITPDVFL ESWEDGIMFD GSSIEGFVRI EESDMYLKPV LDTFAVLPWT VDGAKSARVI CDVYTPDGKP FEGDPRYRLR RMMEKAEQLG YTPYAGPEME FFILPINEKG EPVPEFLDHG GYFDLLPLSK VEEIRRDIAI ALEKMGITVE ATHHEVAPSQ HEVDFRYDTF LRTADNAQTV KLVIKTMAIF HGYHATFMPK PFYGVNGSGM HVHMSLFRGD KNAFYDPDDP LGLSKELRYF VGGILKHAKA LAAVTNPTIN SYKRLVPGYE APVYISWSVG NRSALIRIPK ARGKATRLEY RSPDPSCNIY LAFAAILAAG LDGIINKIEP PAPVEENIYH MTSERREELN IESLPGSLKE AVEELKKDDV IIDALGEHIF EKFVEAAEKD WKEFSTYVTN WELQRYLYL // ID GLPK1_THEMA Reviewed; 492 AA. AC Q9X049; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Glycerol kinase 1 {ECO:0000255|HAMAP-Rule:MF_00186}; DE EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186}; DE AltName: Full=ATP:glycerol 3-phosphotransferase 1 {ECO:0000255|HAMAP-Rule:MF_00186}; DE AltName: Full=Glycerokinase 1 {ECO:0000255|HAMAP-Rule:MF_00186}; DE Short=GK 1 {ECO:0000255|HAMAP-Rule:MF_00186}; GN Name=glpK1 {ECO:0000255|HAMAP-Rule:MF_00186}; GN OrderedLocusNames=TM_0952; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and CC metabolism. Catalyzes the phosphorylation of glycerol to yield sn- CC glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- ENZYME REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP). CC {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol CC kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00186}. CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00186}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36033.1; -; Genomic_DNA. DR PIR; C72314; C72314. DR RefSeq; NP_228760.1; NC_000853.1. DR RefSeq; WP_004080610.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X049; -. DR STRING; 243274.TM0952; -. DR EnsemblBacteria; AAD36033; AAD36033; TM_0952. DR GeneID; 898689; -. DR KEGG; tma:TM0952; -. DR PATRIC; 23936835; VBITheMar51294_0966. DR eggNOG; ENOG4108JQ0; Bacteria. DR eggNOG; COG0554; LUCA. DR InParanoid; Q9X049; -. DR KO; K00864; -. DR OMA; ATLMQFQ; -. DR OrthoDB; EOG6RZB46; -. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central. DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR HAMAP; MF_00186; Glycerol_kin; 1. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR InterPro; IPR005999; Glycerol_kin. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR TIGRFAMs; TIGR01311; glycerol_kin; 1. DR PROSITE; PS00933; FGGY_KINASES_1; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glycerol metabolism; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 492 Glycerol kinase 1. FT /FTId=PRO_0000059513. FT NP_BIND 10 12 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT NP_BIND 407 411 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT REGION 80 81 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 10 10 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 14 14 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 132 132 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 263 263 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 306 306 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 325 325 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. SQ SEQUENCE 492 AA; 55091 MW; 7D09C7849FB0221E CRC64; MYVLAIDQST SGTKAIIFDE KGGIVHRVTV YHKQYYPKPG WVEHDPEEIF RNTLDACRKV IEESGIKPLE IEALAITNQR ETTILWEKKS GKPVYNAVVW QCQRGASLCE EIKKRGLEGK IKEKTGLVVD PYFSASKIRW ILDNVEGVKN KAKQGEIAFG TVDSWLIWKL TKGEVHATDF SNASRTLLLN IHELRWDEEV LEIFEIPPEI LPELKSSDSV FGYTDLGFLP KKIPIVGVMG DSSAALFGQG GFYSGDIKVT YGTGSSTMLN IGEKPNVSDS PIVCSVGWVV KETSSYVLEG NIHSAGDTIV WLKEKLGIIS DPSETEKIAL SLENNGGVYL VPAFVGLGAP YWRSDVKAAI LGLQRNHGKE HVVRAALESI AYQVRDIFEE MVRISSKEPT EVRADGGITR NRFLMQFQAD ILNIPVLVSN IEEVSARGVA FVALLHLGAF SDLEEIRQKI TYREKYEPRM GDELREMYYE GWKTAIRKLL TE // ID GRPE_THEMA Reviewed; 172 AA. AC Q9WZV4; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 92. DE RecName: Full=Protein GrpE {ECO:0000255|HAMAP-Rule:MF_01151}; DE AltName: Full=HSP-70 cofactor {ECO:0000255|HAMAP-Rule:MF_01151}; GN Name=grpE {ECO:0000255|HAMAP-Rule:MF_01151}; GN OrderedLocusNames=TM_0850; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Participates actively in the response to hyperosmotic CC and heat shock by preventing the aggregation of stress-denatured CC proteins, in association with DnaK and GrpE. It is the nucleotide CC exchange factor for DnaK and may function as a thermosensor. CC Unfolded proteins bind initially to DnaJ; upon interaction with CC the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting CC in the formation of a stable complex. GrpE releases ADP from DnaK; CC ATP binding to DnaK triggers the release of the substrate protein, CC thus completing the reaction cycle. Several rounds of ATP- CC dependent interactions between DnaJ, DnaK and GrpE are required CC for fully efficient folding. {ECO:0000255|HAMAP-Rule:MF_01151}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01151}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}. CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000255|HAMAP- CC Rule:MF_01151}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35932.1; -; Genomic_DNA. DR PIR; C72327; C72327. DR RefSeq; NP_228659.1; NC_000853.1. DR RefSeq; WP_004080776.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZV4; -. DR STRING; 243274.TM0850; -. DR EnsemblBacteria; AAD35932; AAD35932; TM_0850. DR GeneID; 898521; -. DR KEGG; tma:TM0850; -. DR PATRIC; 23936626; VBITheMar51294_0863. DR eggNOG; ENOG41085Z1; Bacteria. DR eggNOG; COG0576; LUCA. DR InParanoid; Q9WZV4; -. DR KO; K03687; -. DR OMA; ESGYKFH; -. DR OrthoDB; EOG6FJNJ9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 2.30.22.10; -; 1. DR Gene3D; 3.90.20.20; -; 1. DR HAMAP; MF_01151; GrpE; 1. DR InterPro; IPR000740; GrpE. DR InterPro; IPR013805; GrpE_coiled_coil. DR InterPro; IPR009012; GrpE_head. DR PANTHER; PTHR21237; PTHR21237; 1. DR Pfam; PF01025; GrpE; 1. DR PRINTS; PR00773; GRPEPROTEIN. DR SUPFAM; SSF51064; SSF51064; 1. DR PROSITE; PS01071; GRPE; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome; KW Stress response. FT CHAIN 1 172 Protein GrpE. FT /FTId=PRO_0000113882. SQ SEQUENCE 172 AA; 20401 MW; 1FA5A08BF5F2D2E3 CRC64; MSEKEKKELT QECEELKEKY KELEEYAKRL KAEYENYREE VAREKRELIK NANEYLISKL IPVLDDFERA LNQGEKGDAF YEGVKMIYKK LLNVLEKEGL TKIHVGEKFD PFEHEAVERV ETEDVEEYTI LEVVESGYKF HGKVLKPAKV KVAVKPRKKE ERKVEEPSDK KE // ID GREA_THEMA Reviewed; 156 AA. AC Q9X232; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Transcription elongation factor GreA {ECO:0000255|HAMAP-Rule:MF_00105}; DE AltName: Full=Transcript cleavage factor GreA {ECO:0000255|HAMAP-Rule:MF_00105}; GN Name=greA {ECO:0000255|HAMAP-Rule:MF_00105}; GN OrderedLocusNames=TM_1706; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Necessary for efficient RNA polymerase transcription CC elongation past template-encoded arresting sites. The arresting CC sites in DNA have the property of trapping a certain fraction of CC elongating RNA polymerases that pass through, resulting in locked CC ternary complexes. Cleavage of the nascent transcript by cleavage CC factors such as GreA or GreB allows the resumption of elongation CC from the new 3'terminus. GreA releases sequences of 2 to 3 CC nucleotides. {ECO:0000255|HAMAP-Rule:MF_00105}. CC -!- SIMILARITY: Belongs to the GreA/GreB family. {ECO:0000255|HAMAP- CC Rule:MF_00105}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36773.1; -; Genomic_DNA. DR PIR; D72221; D72221. DR RefSeq; NP_229506.1; NC_000853.1. DR RefSeq; WP_004082222.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X232; -. DR STRING; 243274.TM1706; -. DR EnsemblBacteria; AAD36773; AAD36773; TM_1706. DR GeneID; 897160; -. DR KEGG; tma:TM1706; -. DR PATRIC; 23938386; VBITheMar51294_1723. DR eggNOG; ENOG4108UKH; Bacteria. DR eggNOG; COG0782; LUCA. DR InParanoid; Q9X232; -. DR KO; K03624; -. DR OMA; HNEGRIA; -. DR OrthoDB; EOG686NQ9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.180; -; 1. DR Gene3D; 3.10.50.30; -; 1. DR HAMAP; MF_00105; GreA_GreB; 1. DR InterPro; IPR018151; TF_GreA/GreB_CS. DR InterPro; IPR006359; Tscrpt_elong_fac_GreA. DR InterPro; IPR028624; Tscrpt_elong_fac_GreA/B. DR InterPro; IPR001437; Tscrpt_elong_fac_GreA/B_C. DR InterPro; IPR023459; Tscrpt_elong_fac_GreA/B_fam. DR InterPro; IPR022691; Tscrpt_elong_fac_GreA/B_N. DR Pfam; PF01272; GreA_GreB; 1. DR Pfam; PF03449; GreA_GreB_N; 1. DR PIRSF; PIRSF006092; GreA_GreB; 1. DR SUPFAM; SSF46557; SSF46557; 1. DR TIGRFAMs; TIGR01462; greA; 1. DR PROSITE; PS00829; GREAB_1; 1. DR PROSITE; PS00830; GREAB_2; 1. PE 3: Inferred from homology; KW Coiled coil; Complete proteome; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 156 Transcription elongation factor GreA. FT /FTId=PRO_0000176985. FT COILED 1 32 {ECO:0000255|HAMAP-Rule:MF_00105}. SQ SEQUENCE 156 AA; 17848 MW; 6939A227908E9FF9 CRC64; MKKVRLTREG YEKLKKELED LKRKFMYEIS ERIKEARELG DLSENSEYEA AKNEQGRVGS RIMEIEQILS NAEIIEDSEE SDEVTLGKWV VIKNLDTGEE HKFRIVTPQE ADFFAQKLSS DSPLGKSLLG RKVGDVVKVK APSGVQRYQV IAVMNK // ID GYRB_THEMA Reviewed; 636 AA. AC P77993; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 128. DE RecName: Full=DNA gyrase subunit B {ECO:0000255|HAMAP-Rule:MF_01898}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_01898}; GN Name=gyrB {ECO:0000255|HAMAP-Rule:MF_01898}; Synonyms=top2B; GN OrderedLocusNames=TM_0833; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8863738; DOI=10.1016/0378-1119(96)00508-2; RA Guipaud O., Labedan B., Forterre P.; RT "A gyrB-like gene from the hyperthermophilic bacterion Thermotoga RT maritima."; RL Gene 174:121-128(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: A type II topoisomerase that negatively supercoils CC closed circular double-stranded (ds) DNA in an ATP-dependent CC manner to modulate DNA topology and maintain chromosomes in an CC underwound state. Negative supercoiling favors strand separation, CC and DNA replication, transcription, recombination and repair, all CC of which involve strand separation. Also able to catalyze the CC interconversion of other topological isomers of dsDNA rings, CC including catenanes and knotted rings. Type II topoisomerases CC break and join 2 DNA strands simultaneously in an ATP-dependent CC manner. {ECO:0000255|HAMAP-Rule:MF_01898}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_01898}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898}; CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt CC bridges with both the protein and the DNA. Can also accept other CC divalent metal cations, such as Mn(2+) or Ca(2+). CC {ECO:0000255|HAMAP-Rule:MF_01898}; CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. CC In the heterotetramer, GyrA contains the active site tyrosine that CC forms a transient covalent intermediate with DNA, while GyrB binds CC cofactors and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP- CC Rule:MF_01898}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}. CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming CC negative supercoils. Not all organisms have 2 type II CC topoisomerases; in organisms with a single type II topoisomerase CC this enzyme also has to decatenate newly replicated chromosomes. CC {ECO:0000255|HAMAP-Rule:MF_01898}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family. CC {ECO:0000255|HAMAP-Rule:MF_01898}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_01898}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U49692; AAC44498.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35915.1; -; Genomic_DNA. DR PIR; JC4960; JC4960. DR RefSeq; NP_228642.1; NC_000853.1. DR RefSeq; WP_004080806.1; NZ_CP011107.1. DR ProteinModelPortal; P77993; -. DR SMR; P77993; 8-395. DR STRING; 243274.TM0833; -. DR DNASU; 898504; -. DR EnsemblBacteria; AAD35915; AAD35915; TM_0833. DR GeneID; 898504; -. DR KEGG; tma:TM0833; -. DR PATRIC; 23936592; VBITheMar51294_0846. DR eggNOG; ENOG4105C7D; Bacteria. DR eggNOG; COG0187; LUCA. DR InParanoid; P77993; -. DR KO; K02470; -. DR OMA; IKNMITA; -. DR OrthoDB; EOG6P334W; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009295; C:nucleoid; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR Gene3D; 3.40.50.670; -; 1. DR HAMAP; MF_01898; GyrB; 1. DR InterPro; IPR002288; DNA_gyrase_B_C. DR InterPro; IPR011557; GyrB. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR001241; Topo_IIA. DR InterPro; IPR013760; Topo_IIA-like_dom. DR InterPro; IPR013506; Topo_IIA_bsu_dom2. DR InterPro; IPR013759; Topo_IIA_cen_dom. DR InterPro; IPR018522; TopoIIA_CS. DR InterPro; IPR006171; Toprim_domain. DR Pfam; PF00204; DNA_gyraseB; 1. DR Pfam; PF00986; DNA_gyraseB_C; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR00418; TPI2FAMILY. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR TIGRFAMs; TIGR01059; gyrB; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase; KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; KW Topoisomerase. FT CHAIN 1 636 DNA gyrase subunit B. FT /FTId=PRO_0000145355. FT DOMAIN 421 535 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT METAL 427 427 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01898}. FT METAL 500 500 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01898}. FT METAL 500 500 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT METAL 502 502 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT SITE 452 452 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT SITE 455 455 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT CONFLICT 152 152 V -> M (in Ref. 1; AAC44498). FT {ECO:0000305}. SQ SEQUENCE 636 AA; 72428 MW; B21E0E0CBEC6F89E CRC64; MEKYSAESIK VLKGLEPVRM RPGMYIGSTG KRGLHHLVYE VVDNSVDEAL AGYCDWIRVT LHEDGSVEVE DNGRGIPVDI HPEEGRSALE VVFTVLHAGG KFSKDSYKIS GGLHGVGVSV VNALSEWLEV RVHRDGKIYR QRYERGKPVT PVEVIGETDK HGTIVRFKPD PLIFSETEFD PDILEHRLRE IAFLVPGLKI EFEDRINGEK KTFKFDGGIV EYVKYLNRGK KALHDVIHIK RTEKVKTKNG EDEVIVEIAF QYTDSYSEDI VSFANTIKTV DGGTHVTAFK STLTRLMNEY GKKHNFLKKD DSFQGEDVRE GLTAVISVYV KNPEFEGQTK SKLGNEEVKE AVTKAMREEL KKIFDANPEL VKTILSKIMS TKQAREAAKR AREMVRRKNV LQNTTLPGKL ADCSSTHREK TELFIVEGDS AGGSAKQARD REFQAVLPIR GKILNVEKSS LDRLLKNEQI SDIIVAVGTG IGDDFDESKL RYGRIIIMTD ADIDGAHIRT LLLTLFYRYM RPLIEQGRVY IALPPLYRIK AGREEFYVYS DQELAEYKEK LQGKRIEIQR YKGLGEMNPE QLWETTMNPE TRKIIRVTIE DAEEADRLFE ILMGNDPSSR REFIERHALK VKELDI // ID GNGF_THEMA Reviewed; 314 AA. AC Q9X235; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Putative gluconeogenesis factor {ECO:0000255|HAMAP-Rule:MF_00973}; GN OrderedLocusNames=TM_1709; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Required for morphogenesis under gluconeogenic growth CC conditions. {ECO:0000255|HAMAP-Rule:MF_00973}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00973}. CC -!- SIMILARITY: Belongs to the gluconeogenesis factor family. CC {ECO:0000255|HAMAP-Rule:MF_00973}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36776.1; -; Genomic_DNA. DR PIR; G72221; G72221. DR RefSeq; NP_229509.1; NC_000853.1. DR RefSeq; WP_004082225.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X235; -. DR STRING; 243274.TM1709; -. DR EnsemblBacteria; AAD36776; AAD36776; TM_1709. DR GeneID; 897884; -. DR KEGG; tma:TM1709; -. DR PATRIC; 23938392; VBITheMar51294_1726. DR eggNOG; ENOG4105CHW; Bacteria. DR eggNOG; COG0391; LUCA. DR InParanoid; Q9X235; -. DR OMA; LKMARSG; -. DR OrthoDB; EOG63VBZF; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00973; Gluconeogen_factor; 1. DR InterPro; IPR002882; CofD/UPF0052. DR InterPro; IPR010119; Gluconeogen_factor. DR Pfam; PF01933; UPF0052; 1. DR TIGRFAMs; TIGR01826; CofD_related; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 314 Putative gluconeogenesis factor. FT /FTId=PRO_0000107819. SQ SEQUENCE 314 AA; 34633 MW; 886FBE17F3E06F44 CRC64; MKVVAVGGGT GLSTLLKGLK NIDSFEITAV VSVTDEGGSS GKLRKELNVP PPGDVRNNIV ALAKDEDLLA KLMSYRFSEG SFKGHSLGNL IIAALTKIEG SFSEAIRILE RVLAIKGRVL PVSEDHARLV ARFEDGEEVI GETNIVRKGG KIVEVRLDRP IDALPEVLEA IERADIIIFG PGSLYTSIIT NVLVNGVKDA IKKSKAKKIY VCNLMTQPGE TTGYRVSDHV KELERYLEQS VDFVLVNTRK PSEEVLERYR KEGSDFVEID AENIQNTILA EPFLVEIVDP SDGQRKIRHD SVKLADVIER ISRW // ID GUAA_THEMA Reviewed; 501 AA. AC Q9X2E0; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 124. DE RecName: Full=GMP synthase [glutamine-hydrolyzing]; DE EC=6.3.5.2; DE AltName: Full=GMP synthetase; DE AltName: Full=Glutamine amidotransferase; GN Name=guaA; OrderedLocusNames=TM_1820; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP + CC diphosphate + GMP + L-glutamate. CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln CC route): step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36883.1; -; Genomic_DNA. DR PIR; G72206; G72206. DR RefSeq; NP_229617.1; NC_000853.1. DR RefSeq; WP_004082366.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2E0; -. DR SMR; Q9X2E0; 185-501. DR STRING; 243274.TM1820; -. DR MEROPS; C26.A21; -. DR EnsemblBacteria; AAD36883; AAD36883; TM_1820. DR GeneID; 897443; -. DR KEGG; tma:TM1820; -. DR PATRIC; 23938627; VBITheMar51294_1840. DR eggNOG; ENOG4105CM0; Bacteria. DR eggNOG; COG0518; LUCA. DR eggNOG; COG0519; LUCA. DR InParanoid; Q9X2E0; -. DR KO; K01951; -. DR OMA; MSHGDSV; -. DR OrthoDB; EOG6JHRJV; -. DR UniPathway; UPA00189; UER00296. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00344; GMP_synthase; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR001674; GMP_synth_C. DR InterPro; IPR004739; GMP_synth_N. DR InterPro; IPR022955; GMP_synthase. DR InterPro; IPR025777; GMPS_ATP_PPase_dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR020536; ThiI_AANH. DR Pfam; PF00117; GATase; 1. DR Pfam; PF00958; GMP_synt_C; 1. DR Pfam; PF02568; ThiI; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR00884; guaA_Cterm; 1. DR TIGRFAMs; TIGR00888; guaA_Nterm; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS51553; GMPS_ATP_PPASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutamine amidotransferase; KW GMP biosynthesis; Ligase; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 501 GMP synthase [glutamine-hydrolyzing]. FT /FTId=PRO_0000140197. FT DOMAIN 1 185 Glutamine amidotransferase type-1. FT DOMAIN 186 376 GMPS ATP-PPase. FT NP_BIND 213 219 ATP. {ECO:0000250}. FT ACT_SITE 75 75 Nucleophile. {ECO:0000250}. FT ACT_SITE 159 159 {ECO:0000250}. FT ACT_SITE 161 161 {ECO:0000250}. SQ SEQUENCE 501 AA; 57040 MW; 56E7EEB3FC587090 CRC64; MVLVVDYGSQ YSRLITRRIR ENEVYSEVVF PDDKVDLSKV DAVILSGGPR SVYEEDAPKL PEWFQEYKGP VLAICYGMQL IVKELGGEVR RGRGEYGRTL VELSRDPIFE GIPEKVHVWM SHGDEVVRLP EGFHPIAVSE TGVIAAATDG KRFWLLQFHP EVHHTEYGDR MISNFLFNVC KLEKNWKIGD LVEEKIRHIK ETIGNKKAIL ALSGGVDSSV AAVLVHRAIG KNLVCVFVDH GLLRKNEREE VERVFKEHFD MNLVVVDARK RFLEKLRGVT DPEKKRKIIG EEFIRVFEEE AKKHDVEFLV QGTIYSDVIE SAASGKTTAK IKSHHNVGGL PEKMNLKLVE PLRDLFKDEV RKVGKYLGIP DRIINRHPFP GPGLAVRVLG EVTEEKLEIL READYIFIET LRKHDYYDKV WQAFAVLLPI KSVGVKGDAR AYEYVVALRA VNSVEGMTAD WSRIPHDILD EAARRITREV KGVGRVVYDI TSKPPATIEW E // ID GYRA_THEMA Reviewed; 804 AA. AC O33926; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 117. DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_01897}; GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; Synonyms=top2A; GN OrderedLocusNames=TM_1084; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9380682; DOI=10.1073/pnas.94.20.10606; RA Guipaud O., Marguet E., Noll K.M., Bouthier de la Tour C., RA Forterre P.; RT "Both DNA gyrase and reverse gyrase are present in the RT hyperthermophilic bacterium Thermotoga maritima."; RL Proc. Natl. Acad. Sci. U.S.A. 94:10606-10611(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: A type II topoisomerase that negatively supercoils CC closed circular double-stranded (ds) DNA in an ATP-dependent CC manner to modulate DNA topology and maintain chromosomes in an CC underwound state. Negative supercoiling favors strand separation, CC and DNA replication, transcription, recombination and repair, all CC of which involve strand separation. Also able to catalyze the CC interconversion of other topological isomers of dsDNA rings, CC including catenanes and knotted rings. Type II topoisomerases CC break and join 2 DNA strands simultaneously in an ATP-dependent CC manner. {ECO:0000255|HAMAP-Rule:MF_01897}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_01897}. CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. CC In the heterotetramer, GyrA contains the active site tyrosine that CC forms a transient covalent intermediate with DNA, while GyrB binds CC cofactors and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP- CC Rule:MF_01897}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}. CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming CC negative supercoils. Not all organisms have 2 type II CC topoisomerases; in organisms with a single type II topoisomerase CC this enzyme also has to decatenate newly replicated chromosomes. CC {ECO:0000255|HAMAP-Rule:MF_01897}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit CC family. {ECO:0000255|HAMAP-Rule:MF_01897}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U76417; AAB87144.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36161.1; -; Genomic_DNA. DR PIR; D72297; D72297. DR RefSeq; NP_228890.1; NC_000853.1. DR RefSeq; WP_004080399.1; NZ_CP011107.1. DR ProteinModelPortal; O33926; -. DR STRING; 243274.TM1084; -. DR EnsemblBacteria; AAD36161; AAD36161; TM_1084. DR GeneID; 897026; -. DR KEGG; tma:TM1084; -. DR PATRIC; 23937097; VBITheMar51294_1097. DR eggNOG; ENOG4105C24; Bacteria. DR eggNOG; COG0188; LUCA. DR InParanoid; O33926; -. DR KO; K02469; -. DR OMA; ETVDWVP; -. DR OrthoDB; EOG661H5V; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009295; C:nucleoid; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.90.199.10; -; 2. DR HAMAP; MF_01897; GyrA; 1. DR InterPro; IPR024946; Arg_repress_C-like. DR InterPro; IPR005743; GyrA. DR InterPro; IPR006691; GyrA/parC_pinwhl. DR InterPro; IPR013760; Topo_IIA-like_dom. DR InterPro; IPR002205; Topo_IIA_A/C. DR InterPro; IPR013758; Topo_IIA_A/C_ab. DR Pfam; PF03989; DNA_gyraseA_C; 6. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR TIGRFAMs; TIGR01063; gyrA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase; KW Nucleotide-binding; Reference proteome; Topoisomerase. FT CHAIN 1 804 DNA gyrase subunit A. FT /FTId=PRO_0000145270. FT MOTIF 522 528 GyrA-box. {ECO:0000255|HAMAP- FT Rule:MF_01897}. FT ACT_SITE 119 119 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01897}. FT CONFLICT 91 91 Q -> H (in Ref. 1; AAB87144). FT {ECO:0000305}. FT CONFLICT 153 153 P -> T (in Ref. 1; AAB87144). FT {ECO:0000305}. SQ SEQUENCE 804 AA; 90448 MW; 0ED421407D35949F CRC64; MPEILINKPV EDELVESYLL YSMSVIVGRA IPDVRDGLKP VQRRILYGMY ELGLKHNSPT KKSARIVGEV MGKYHPHGDA PVYDALVRMA QPFTMRYPLI EGQGNFGSID RDPPAAMRYT EARLTRLAEE MLEDIEKNTV NMIDNFDGTL KEPEVLPSKV PNLIINGASG IAVGMATNIP PHNLSETVDA LIYLIDHPEA TVEELMQFIK GPDFPTGAVV VNASELKKVY EEGRGRIIVR GKVHVEDGKR VKRIVITEIP YGVSKAGLIE QIAKIAKDDE SLPIRNIRDE SDKRGMRIVI EIPKDANEEV IINNLYKRTA LQDYFNVQML VIDKHKRPRL MNLKGLMEAF LEHRFEVIRR RARYEYEQYT RRAHVVEGLL KAARAIGVVV DIVRNSKDVE SARQSLMETL EITEEQAKAI LDMRLSRLTS LEIENLQNEY SDLVRKISEV KEILEKDEKV KEIMKKEFLY LKQQYGDPRR TEVTDQSIEY NEEELIVEED VVITLSHKGY LKSTPLNSYR SQKRGGKGIT VSKLSEDDEV EFVVVAKNTS STLFITNLGR AYVLKNYQLE TTGRNTRGRH ITAFLNLEDT EKIVALASLN GEGRDLVIAT KSGKIKRTAL KEFENATSNR GVRAIKIEPG DEIVSARVVN SEKETLIVAT KMGMAIRFPV SDVRRMGRNA AGVQAIKLQP GDEVVSVDVI PPGEEGEILT VTEKGFGKRT PVQLYRIQRR GGTGLRNISD VNKTGYVVAV RYVRGDEEIV VVTRNGMMIR FPVSEIGVIG RVTKGVKLIE LGDDTISKVA VVKD // ID HFQ_THEMA Reviewed; 92 AA. AC Q9WYZ6; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436}; GN Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=TM_0526; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: RNA chaperone that binds small regulatory RNA (sRNAs) CC and mRNAs to facilitate mRNA translational regulation in response CC to envelope stress, environmental stress and changes in metabolite CC concentrations. Also binds with high specificity to tRNAs. CC {ECO:0000255|HAMAP-Rule:MF_00436}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00436}. CC -!- SIMILARITY: Belongs to the Hfq family. {ECO:0000255|HAMAP- CC Rule:MF_00436}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35611.1; -; Genomic_DNA. DR PIR; D72366; D72366. DR RefSeq; NP_228336.1; NC_000853.1. DR RefSeq; WP_010865141.1; NC_000853.1. DR PDB; 4Y91; X-ray; 2.66 A; A/B/C/D/E/F/G/H/I/J/K/L=1-92. DR PDBsum; 4Y91; -. DR ProteinModelPortal; Q9WYZ6; -. DR STRING; 243274.TM0526; -. DR EnsemblBacteria; AAD35611; AAD35611; TM_0526. DR GeneID; 897578; -. DR KEGG; tma:TM0526; -. DR PATRIC; 23935959; VBITheMar51294_0534. DR eggNOG; ENOG4105KW8; Bacteria. DR eggNOG; COG1923; LUCA. DR InParanoid; Q9WYZ6; -. DR KO; K03666; -. DR OMA; DNFTVIM; -. DR OrthoDB; EOG68SW3W; -. DR BioCyc; TMAR243274:GC6P-550-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR HAMAP; MF_00436; Hfq; 1. DR InterPro; IPR005001; Hfq. DR InterPro; IPR010920; LSM_dom. DR SUPFAM; SSF50182; SSF50182; 1. DR TIGRFAMs; TIGR02383; Hfq; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; RNA-binding; KW Stress response. FT CHAIN 1 92 RNA-binding protein Hfq. FT /FTId=PRO_0000095664. SQ SEQUENCE 92 AA; 10516 MW; 3E7D5B48E570C561 CRC64; MALAEKFNLQ DRFLNHLRVN KIEVKVYLVN GFQTKGFIRS FDSYTVLLES GNQQSLIYKH AISTIIPSSY VMLMPKKQET AQEAETSENE GS // ID HIS1_THEMA Reviewed; 208 AA. AC Q9X0D2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 121. DE RecName: Full=ATP phosphoribosyltransferase; DE Short=ATP-PRT; DE Short=ATP-PRTase; DE EC=2.4.2.17; GN Name=hisG; OrderedLocusNames=TM_1042; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- CC diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a CC crucial role in the pathway because the rate of histidine CC biosynthesis seems to be controlled primarily by regulation of CC HisG enzymatic activity (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate CC = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced CC by HisZ. CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. CC Short subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36119.1; -; Genomic_DNA. DR PIR; A72305; A72305. DR RefSeq; NP_228848.1; NC_000853.1. DR RefSeq; WP_004080478.1; NZ_CP011107.1. DR PDB; 1O63; X-ray; 2.00 A; A/B=2-208. DR PDB; 1O64; X-ray; 2.10 A; A/B=2-208. DR PDB; 1USY; X-ray; 2.52 A; E/F/G/H=1-208. DR PDBsum; 1O63; -. DR PDBsum; 1O64; -. DR PDBsum; 1USY; -. DR ProteinModelPortal; Q9X0D2; -. DR SMR; Q9X0D2; 1-203. DR STRING; 243274.TM1042; -. DR EnsemblBacteria; AAD36119; AAD36119; TM_1042. DR GeneID; 898709; -. DR KEGG; tma:TM1042; -. DR PATRIC; 23937013; VBITheMar51294_1055. DR eggNOG; ENOG4105E21; Bacteria. DR eggNOG; COG0040; LUCA. DR InParanoid; Q9X0D2; -. DR KO; K00765; -. DR OMA; VATKFPR; -. DR OrthoDB; EOG66MQT3; -. DR UniPathway; UPA00031; UER00006. DR EvolutionaryTrace; Q9X0D2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01018; HisG_Short; 1. DR InterPro; IPR013820; ATP_PRibTrfase_cat. DR InterPro; IPR018198; ATP_PRibTrfase_CS. DR InterPro; IPR001348; ATP_PRibTrfase_HisG. DR InterPro; IPR024893; ATP_PRibTrfase_HisG_short. DR PANTHER; PTHR21403; PTHR21403; 1. DR Pfam; PF01634; HisG; 1. DR TIGRFAMs; TIGR00070; hisG; 1. DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Complete proteome; KW Cytoplasm; Glycosyltransferase; Histidine biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 208 ATP phosphoribosyltransferase. FT /FTId=PRO_0000151944. FT STRAND 3 7 {ECO:0000244|PDB:1O63}. FT HELIX 12 22 {ECO:0000244|PDB:1O63}. FT STRAND 26 29 {ECO:0000244|PDB:1O63}. FT STRAND 31 36 {ECO:0000244|PDB:1O63}. FT STRAND 39 44 {ECO:0000244|PDB:1O63}. FT HELIX 46 48 {ECO:0000244|PDB:1O63}. FT HELIX 49 54 {ECO:0000244|PDB:1O63}. FT STRAND 59 64 {ECO:0000244|PDB:1O63}. FT HELIX 65 70 {ECO:0000244|PDB:1O63}. FT STRAND 79 93 {ECO:0000244|PDB:1O63}. FT TURN 94 96 {ECO:0000244|PDB:1O63}. FT STRAND 103 108 {ECO:0000244|PDB:1O63}. FT HELIX 110 119 {ECO:0000244|PDB:1O63}. FT STRAND 124 128 {ECO:0000244|PDB:1O63}. FT HELIX 135 138 {ECO:0000244|PDB:1O63}. FT STRAND 139 141 {ECO:0000244|PDB:1USY}. FT STRAND 143 152 {ECO:0000244|PDB:1O63}. FT HELIX 153 157 {ECO:0000244|PDB:1O63}. FT STRAND 160 175 {ECO:0000244|PDB:1O63}. FT HELIX 177 182 {ECO:0000244|PDB:1O63}. FT HELIX 184 203 {ECO:0000244|PDB:1O63}. SQ SEQUENCE 208 AA; 23511 MW; A3629EF262F48A80 CRC64; MLKLAIPKGR LEEKVMTYLK KTGVIFERES SILREGKDIV CFMVRPFDVP TYLVHGVADI GFCGTDVLLE KETSLIQPFF IPTNISRMVL AGPKGRGIPE GEKRIATKFP NVTQRYCESK GWHCRIIPLK GSVELAPIAG LSDLIVDITE TGRTLKENNL EILDEIFVIR THVVVNPVSY RTKREEVVSF LEKLQEVIEH DSNEQSRG // ID HIS4_THEMA Reviewed; 241 AA. AC Q9X0C7; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; DE EC=5.3.1.16; DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; GN Name=hisA; OrderedLocusNames=TM_1037; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP ACTIVE SITES, SUBUNIT, AND MUTAGENESIS OF ASP-8; HIS-48; ASP-51; RP ARG-83; ASP-127 AND THR-164. RX PubMed=12356303; DOI=10.1021/bi026092h; RA Henn-Sax M., Thoma R., Schmidt S., Hennig M., Kirschner K., RA Sterner R.; RT "Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan RT biosynthesis have similar reaction mechanisms and common strategies RT for protecting their labile substrates."; RL Biochemistry 41:12032-12042(2002). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). RX PubMed=10968789; DOI=10.1126/science.289.5484.1546; RA Lang D., Thoma R., Henn-Sax M., Sterner R., Wilmanns M.; RT "Structural evidence for evolution of the beta/alpha barrel scaffold RT by gene duplication and fusion."; RL Science 289:1546-1550(2000). CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho- CC beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide = 5- CC ((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5- CC phospho-beta-D-ribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12356303}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36114.1; -; Genomic_DNA. DR PIR; D72304; D72304. DR RefSeq; NP_228843.1; NC_000853.1. DR RefSeq; WP_004080485.1; NZ_CP011107.1. DR PDB; 1QO2; X-ray; 1.85 A; A/B=1-241. DR PDB; 2CFF; X-ray; 2.50 A; A/B=1-241. DR PDB; 2W79; X-ray; 1.85 A; A/B=1-241. DR PDBsum; 1QO2; -. DR PDBsum; 2CFF; -. DR PDBsum; 2W79; -. DR ProteinModelPortal; Q9X0C7; -. DR SMR; Q9X0C7; 1-241. DR STRING; 243274.TM1037; -. DR EnsemblBacteria; AAD36114; AAD36114; TM_1037. DR GeneID; 897150; -. DR KEGG; tma:TM1037; -. DR PATRIC; 23937003; VBITheMar51294_1050. DR eggNOG; ENOG4105CJV; Bacteria. DR eggNOG; COG0106; LUCA. DR InParanoid; Q9X0C7; -. DR KO; K01814; -. DR OMA; KKENTIF; -. DR OrthoDB; EOG6H1Q3W; -. DR UniPathway; UPA00031; UER00009. DR EvolutionaryTrace; Q9X0C7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IBA:GO_Central. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01014; HisA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR006063; HisA. DR InterPro; IPR023016; Isoase_HisA. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00977; His_biosynth; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00007; TIGR00007; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Isomerase; Reference proteome. FT CHAIN 1 241 1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] FT imidazole-4-carboxamide isomerase. FT /FTId=PRO_0000142068. FT ACT_SITE 8 8 Proton acceptor. FT {ECO:0000305|PubMed:12356303}. FT ACT_SITE 127 127 Proton donor. FT {ECO:0000305|PubMed:12356303}. FT MUTAGEN 8 8 D->N: Loss of activity. FT {ECO:0000269|PubMed:12356303}. FT MUTAGEN 48 48 H->A: Decrease in activity. FT {ECO:0000269|PubMed:12356303}. FT MUTAGEN 51 51 D->N: Decrease in activity. FT {ECO:0000269|PubMed:12356303}. FT MUTAGEN 83 83 R->N: Decrease in activity. FT {ECO:0000269|PubMed:12356303}. FT MUTAGEN 127 127 D->N: Almost no activity. FT {ECO:0000269|PubMed:12356303}. FT MUTAGEN 164 164 T->A: Strong decrease in activity. FT {ECO:0000269|PubMed:12356303}. FT STRAND 2 10 {ECO:0000244|PDB:1QO2}. FT STRAND 13 17 {ECO:0000244|PDB:1QO2}. FT HELIX 18 20 {ECO:0000244|PDB:1QO2}. FT HELIX 22 24 {ECO:0000244|PDB:1QO2}. FT STRAND 25 30 {ECO:0000244|PDB:1QO2}. FT HELIX 32 41 {ECO:0000244|PDB:1QO2}. FT STRAND 47 51 {ECO:0000244|PDB:1QO2}. FT HELIX 52 57 {ECO:0000244|PDB:1QO2}. FT HELIX 63 68 {ECO:0000244|PDB:1QO2}. FT HELIX 69 75 {ECO:0000244|PDB:1QO2}. FT STRAND 76 81 {ECO:0000244|PDB:1QO2}. FT HELIX 85 93 {ECO:0000244|PDB:1QO2}. FT STRAND 98 101 {ECO:0000244|PDB:1QO2}. FT HELIX 103 107 {ECO:0000244|PDB:1QO2}. FT HELIX 111 116 {ECO:0000244|PDB:1QO2}. FT TURN 117 119 {ECO:0000244|PDB:1QO2}. FT STRAND 121 129 {ECO:0000244|PDB:1QO2}. FT HELIX 141 144 {ECO:0000244|PDB:2W79}. FT HELIX 146 154 {ECO:0000244|PDB:1QO2}. FT TURN 155 157 {ECO:0000244|PDB:1QO2}. FT STRAND 160 165 {ECO:0000244|PDB:1QO2}. FT HELIX 168 171 {ECO:0000244|PDB:1QO2}. FT HELIX 177 187 {ECO:0000244|PDB:1QO2}. FT STRAND 190 196 {ECO:0000244|PDB:1QO2}. FT HELIX 200 212 {ECO:0000244|PDB:1QO2}. FT TURN 213 215 {ECO:0000244|PDB:1QO2}. FT STRAND 216 222 {ECO:0000244|PDB:1QO2}. FT HELIX 224 227 {ECO:0000244|PDB:1QO2}. FT HELIX 233 240 {ECO:0000244|PDB:1QO2}. SQ SEQUENCE 241 AA; 27028 MW; B1ABDDE5A4D5213D CRC64; MLVVPAIDLF RGKVARMIKG RKENTIFYEK DPVELVEKLI EEGFTLIHVV DLSNAIENSG ENLPVLEKLS EFAEHIQIGG GIRSLDYAEK LRKLGYRRQI VSSKVLEDPS FLKSLREIDV EPVFSLDTRG GRVAFKGWLA EEEIDPVSLL KRLKEYGLEE IVHTEIEKDG TLQEHDFSLT KKIAIEAEVK VLAAGGISSE NSLKTAQKVH TETNGLLKGV IVGRAFLEGI LTVEVMKRYA R // ID HCP_THEMA Reviewed; 431 AA. AC Q9X0Q4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 111. DE RecName: Full=Hydroxylamine reductase {ECO:0000255|HAMAP-Rule:MF_00069}; DE EC=1.7.99.1 {ECO:0000255|HAMAP-Rule:MF_00069}; DE AltName: Full=Hybrid-cluster protein {ECO:0000255|HAMAP-Rule:MF_00069}; DE Short=HCP {ECO:0000255|HAMAP-Rule:MF_00069}; DE AltName: Full=Prismane protein {ECO:0000255|HAMAP-Rule:MF_00069}; GN Name=hcp {ECO:0000255|HAMAP-Rule:MF_00069}; OrderedLocusNames=TM_1172; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the reduction of hydroxylamine to form NH(3) CC and H(2)O. {ECO:0000255|HAMAP-Rule:MF_00069}. CC -!- CATALYTIC ACTIVITY: NH(3) + H(2)O + acceptor = hydroxylamine + CC reduced acceptor. {ECO:0000255|HAMAP-Rule:MF_00069}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00069}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00069}; CC -!- COFACTOR: CC Name=hybrid [4Fe-2O-2S] cluster; Xref=ChEBI:CHEBI:60519; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00069}; CC Note=Binds 1 hybrid [4Fe-2O-2S] cluster. {ECO:0000255|HAMAP- CC Rule:MF_00069}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00069}. CC -!- SIMILARITY: Belongs to the HCP family. {ECO:0000255|HAMAP- CC Rule:MF_00069}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36247.1; -; Genomic_DNA. DR PIR; G72285; G72285. DR RefSeq; NP_228977.2; NC_000853.1. DR RefSeq; WP_004080194.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0Q4; -. DR STRING; 243274.TM1172; -. DR DNASU; 898314; -. DR EnsemblBacteria; AAD36247; AAD36247; TM_1172. DR GeneID; 898314; -. DR KEGG; tma:TM1172; -. DR PATRIC; 23937284; VBITheMar51294_1190. DR eggNOG; ENOG4105EJ7; Bacteria. DR eggNOG; COG1151; LUCA. DR InParanoid; Q9X0Q4; -. DR KO; K05601; -. DR OMA; CAYAQGM; -. DR OrthoDB; EOG69WFJT; -. DR BioCyc; TMAR243274:GC6P-1201-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0050418; F:hydroxylamine reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.20.1270.20; -; 1. DR Gene3D; 3.40.50.2030; -; 2. DR HAMAP; MF_00069; Hydroxylam_reduct; 1. DR InterPro; IPR004137; HCP/CODH. DR InterPro; IPR010048; Hydroxylam_reduct. DR InterPro; IPR011254; Prismane-like. DR InterPro; IPR016099; Prismane-like_a/b-sand. DR InterPro; IPR016100; Prismane_a-bundle. DR Pfam; PF03063; Prismane; 2. DR SUPFAM; SSF56821; SSF56821; 1. DR TIGRFAMs; TIGR01703; hybrid_clust; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1 431 Hydroxylamine reductase. FT /FTId=PRO_0000151684. FT METAL 5 5 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 8 8 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 17 17 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 23 23 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 73 73 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 131 131 Iron-oxo-sulfur (4Fe-2O-2S); via tele FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 155 155 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT METAL 199 199 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT METAL 286 286 Iron-oxo-sulfur (4Fe-2O-2S); via FT persulfide group. {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 314 314 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT METAL 339 339 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT METAL 373 373 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT METAL 375 375 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT MOD_RES 286 286 Cysteine persulfide. {ECO:0000255|HAMAP- FT Rule:MF_00069}. SQ SEQUENCE 431 AA; 47958 MW; 6D9E224F0F7706A4 CRC64; MQMFCYQCSQ TANGTGCTEY GVCGKSPTVA RLQDNLVFAI KGISAYYYHA RELGYDDPEI AGFLDEALYS TLTNVNFDAQ SFVEYALEAG RMNLKAMQLL KKAHIETYGE PTPVEVETGT KKGKGIIVTG HNLKALEELL KQVEGTNVYV YTHSEMLPAH GYPGLRKYKN LIGNLGKAWY DQRKLFAEYP VAILGTSNCV LIPSESYRDR MFTTSIARLP GVKHIDGYDY TEVIEKAKSL PDLEEKPGSY KLRTGFSTSV VVSLADKIKE LVEAGKIKHF LVVGGCDVPF KRNEYYREFV QKLPKETVVI TLACGKFRIN DLDLGDIDGI PRLIDVGQCN DTIVAIEIAQ ALAKVFGVEV TELPLTLVLT WMEQKAVAIL WTLLALGLKN IYVGPVLPAW VNEDILKVLT AEFGLKTISE PEKDIKEILK V // ID HISZ_THEMA Reviewed; 275 AA. AC Q9X0D3; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit; GN Name=hisZ; OrderedLocusNames=TM_1043; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Required for the first step of histidine biosynthesis. CC May allow the feedback regulation of ATP phosphoribosyltransferase CC activity by histidine (By similarity). {ECO:0000250}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: This function is generally fulfilled by the C- CC terminal part of HisG, which is missing in some bacteria such as CC this one. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. HisZ subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36120.1; -; Genomic_DNA. DR PIR; B72305; B72305. DR RefSeq; NP_228849.1; NC_000853.1. DR RefSeq; WP_010865251.1; NC_000853.1. DR PDB; 1USY; X-ray; 2.52 A; A/B/C/D=1-275. DR PDBsum; 1USY; -. DR ProteinModelPortal; Q9X0D3; -. DR SMR; Q9X0D3; 1-275. DR STRING; 243274.TM1043; -. DR EnsemblBacteria; AAD36120; AAD36120; TM_1043. DR GeneID; 897251; -. DR KEGG; tma:TM1043; -. DR KEGG; tmi:THEMA_09145; -. DR PATRIC; 23937015; VBITheMar51294_1056. DR eggNOG; COG0124; LUCA. DR InParanoid; Q9X0D3; -. DR KO; K01892; -. DR OMA; IEDSIYR; -. DR OrthoDB; EOG6F2956; -. DR BioCyc; TMAR243274:GC6P-1072-MONOMER; -. DR UniPathway; UPA00031; UER00006. DR EvolutionaryTrace; Q9X0D3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00125; HisZ; 1. DR InterPro; IPR004517; HisZ. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Reference proteome. FT CHAIN 1 275 ATP phosphoribosyltransferase regulatory FT subunit. FT /FTId=PRO_0000171072. FT HELIX 6 18 {ECO:0000244|PDB:1USY}. FT STRAND 28 31 {ECO:0000244|PDB:1USY}. FT STRAND 40 42 {ECO:0000244|PDB:1USY}. FT STRAND 47 50 {ECO:0000244|PDB:1USY}. FT HELIX 54 62 {ECO:0000244|PDB:1USY}. FT STRAND 65 67 {ECO:0000244|PDB:1USY}. FT STRAND 71 74 {ECO:0000244|PDB:1USY}. FT STRAND 77 83 {ECO:0000244|PDB:1USY}. FT STRAND 86 99 {ECO:0000244|PDB:1USY}. FT HELIX 103 120 {ECO:0000244|PDB:1USY}. FT STRAND 125 131 {ECO:0000244|PDB:1USY}. FT HELIX 134 139 {ECO:0000244|PDB:1USY}. FT STRAND 140 142 {ECO:0000244|PDB:1USY}. FT HELIX 144 146 {ECO:0000244|PDB:1USY}. FT HELIX 147 155 {ECO:0000244|PDB:1USY}. FT HELIX 159 168 {ECO:0000244|PDB:1USY}. FT HELIX 175 185 {ECO:0000244|PDB:1USY}. FT HELIX 189 193 {ECO:0000244|PDB:1USY}. FT HELIX 199 215 {ECO:0000244|PDB:1USY}. FT STRAND 217 223 {ECO:0000244|PDB:1USY}. FT HELIX 228 232 {ECO:0000244|PDB:1USY}. FT STRAND 235 243 {ECO:0000244|PDB:1USY}. FT TURN 244 247 {ECO:0000244|PDB:1USY}. FT STRAND 248 258 {ECO:0000244|PDB:1USY}. FT STRAND 261 274 {ECO:0000244|PDB:1USY}. SQ SEQUENCE 275 AA; 31289 MW; CFE7716DF9177EC1 CRC64; MDFLDFEKVF SFYSKATKKG FSPFFVPALE KAEEPAGNFF LDRKGNLFSI REDFTKTVLN HRKRYSPDSQ IKVWYADFVY RYSGSDLVAE YQLGLEKVPR NSLDDSLEVL EIIVESASEF FEGPVIVEIG HTGVYEDLLK EIPKDLHEKV LNLIDTKNLA EIEFLSHMKK IDLSRVEKII EDSIYRRSPE HLKTMDLPLS VREDLLSASS FLQEKFPTVS VEIDLTLART IEEYCGLIFT IYDTSSSRLV AAGGEYTVNG EKGVGGSIFL EGKTC // ID HIS2_THEMA Reviewed; 197 AA. AC Q9X0C5; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Histidine biosynthesis bifunctional protein HisIE; DE Includes: DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase; DE Short=PRA-CH; DE EC=3.5.4.19; DE Includes: DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase; DE Short=PRA-PH; DE EC=3.6.1.31; GN Name=hisI; Synonyms=hisIE; OrderedLocusNames=TM_1035; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + H(2)O = 1- CC (5-phospho-beta-D-ribosyl)-AMP + diphosphate. CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-AMP + H(2)O = 1- CC (5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D- CC ribosylamino)methylideneamino)imidazole-4-carboxamide. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH CC family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36112.1; -; Genomic_DNA. DR PIR; B72304; B72304. DR RefSeq; NP_228841.1; NC_000853.1. DR RefSeq; WP_010865250.1; NC_000853.1. DR ProteinModelPortal; Q9X0C5; -. DR STRING; 243274.TM1035; -. DR DNASU; 897097; -. DR EnsemblBacteria; AAD36112; AAD36112; TM_1035. DR GeneID; 897097; -. DR KEGG; tma:TM1035; -. DR KEGG; tmi:THEMA_09185; -. DR PATRIC; 23936999; VBITheMar51294_1048. DR eggNOG; ENOG4105K8F; Bacteria. DR eggNOG; COG0139; LUCA. DR eggNOG; COG0140; LUCA. DR InParanoid; Q9X0C5; -. DR KO; K11755; -. DR OMA; ERSCFHQ; -. DR OrthoDB; EOG6PGKB6; -. DR BioCyc; TMAR243274:GC6P-1064-MONOMER; -. DR UniPathway; UPA00031; UER00007. DR UniPathway; UPA00031; UER00008. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01019; HisIE; 1. DR HAMAP; MF_01020; HisE; 1. DR InterPro; IPR023019; His_synth_HisIE. DR InterPro; IPR008179; PRib-ATP_PPHydrolase. DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like. DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom. DR Pfam; PF01502; PRA-CH; 1. DR Pfam; PF01503; PRA-PH; 1. DR ProDom; PD002610; PRA_CycHdrlase; 1. DR TIGRFAMs; TIGR03188; histidine_hisI; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase; Multifunctional enzyme; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 197 Histidine biosynthesis bifunctional FT protein HisIE. FT /FTId=PRO_0000136442. FT REGION 1 108 Phosphoribosyl-AMP cyclohydrolase. FT REGION 109 197 Phosphoribosyl-ATP pyrophosphohydrolase. SQ SEQUENCE 197 AA; 23130 MW; 1E8222C406EC2D82 CRC64; MMTLYPVVVQ ERTTGEVLML AYANEEALEL TKKTGYAHFF SRERQKIWKK GETSGNTMRV VEIRRDCDDD AYLYIVDFPE DKVACHTGNR SCFFKVEHRF EETGSPTFWL ELYRLVRKRK EEMPEGSYTV KLFKEGKGKI AKKFGEEAVE VITGYLQNDR ENLVWEIADM MYHLTVLMAD AGVTVQDVMR ELEKRRK // ID HIS8_THEMA Reviewed; 335 AA. AC Q9X0D0; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 118. DE RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01023}; DE EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023}; DE AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000255|HAMAP-Rule:MF_01023}; GN Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023}; GN OrderedLocusNames=TM_1040; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 6-335, AND SUBUNIT. RX PubMed=15007066; DOI=10.1074/jbc.M400291200; RA Fernandez F.J., Vega M.C., Lehmann F., Sandmeier E., Gehring H., RA Christen P., Wilmanns M.; RT "Structural studies of the catalytic reaction pathway of a RT hyperthermophilic histidinol-phosphate aminotransferase."; RL J. Biol. Chem. 279:21478-21488(2004). CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3- CC (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_01023}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01023}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. CC {ECO:0000255|HAMAP-Rule:MF_01023}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023, CC ECO:0000269|PubMed:15007066}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. Histidinol-phosphate aminotransferase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36117.1; -; Genomic_DNA. DR PIR; G72304; G72304. DR RefSeq; NP_228846.1; NC_000853.1. DR RefSeq; WP_004080482.1; NZ_CP011107.1. DR PDB; 1H1C; X-ray; 2.85 A; A/B/C/D=1-335. DR PDB; 1UU0; X-ray; 2.85 A; A/B/C/D=1-335. DR PDB; 1UU1; X-ray; 2.38 A; A/B/C/D=1-335. DR PDB; 1UU2; X-ray; 2.80 A; A/B=1-335. DR PDB; 2F8J; X-ray; 2.40 A; A/B/C/D=1-335. DR PDBsum; 1H1C; -. DR PDBsum; 1UU0; -. DR PDBsum; 1UU1; -. DR PDBsum; 1UU2; -. DR PDBsum; 2F8J; -. DR ProteinModelPortal; Q9X0D0; -. DR SMR; Q9X0D0; 1-335. DR STRING; 243274.TM1040; -. DR DNASU; 897350; -. DR EnsemblBacteria; AAD36117; AAD36117; TM_1040. DR GeneID; 897350; -. DR KEGG; tma:TM1040; -. DR PATRIC; 23937009; VBITheMar51294_1053. DR eggNOG; ENOG4105CIH; Bacteria. DR eggNOG; COG0079; LUCA. DR InParanoid; Q9X0D0; -. DR KO; K00817; -. DR OMA; CYRIFAK; -. DR OrthoDB; EOG651SWW; -. DR BRENDA; 2.6.1.9; 6331. DR SABIO-RK; Q9X0D0; -. DR UniPathway; UPA00031; UER00012. DR EvolutionaryTrace; Q9X0D0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_01023; HisC_aminotrans_2; 1. DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR005861; HisP_aminotrans. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01141; hisC; 1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aminotransferase; KW Complete proteome; Histidine biosynthesis; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 335 Histidinol-phosphate aminotransferase. FT /FTId=PRO_0000153470. FT MOD_RES 202 202 N6-(pyridoxal phosphate)lysine. FT HELIX 2 5 {ECO:0000244|PDB:1UU1}. FT STRAND 21 26 {ECO:0000244|PDB:1UU1}. FT HELIX 35 43 {ECO:0000244|PDB:1UU1}. FT HELIX 47 51 {ECO:0000244|PDB:1UU1}. FT HELIX 59 69 {ECO:0000244|PDB:1UU1}. FT HELIX 76 78 {ECO:0000244|PDB:1UU1}. FT STRAND 79 84 {ECO:0000244|PDB:1UU1}. FT HELIX 85 95 {ECO:0000244|PDB:1UU1}. FT STRAND 96 101 {ECO:0000244|PDB:1UU1}. FT STRAND 103 105 {ECO:0000244|PDB:1UU1}. FT HELIX 108 116 {ECO:0000244|PDB:1UU1}. FT STRAND 119 122 {ECO:0000244|PDB:1UU1}. FT STRAND 140 147 {ECO:0000244|PDB:1UU1}. FT TURN 149 151 {ECO:0000244|PDB:1UU1}. FT HELIX 157 165 {ECO:0000244|PDB:1UU1}. FT STRAND 169 173 {ECO:0000244|PDB:1UU1}. FT HELIX 177 180 {ECO:0000244|PDB:1UU1}. FT HELIX 185 189 {ECO:0000244|PDB:1UU1}. FT STRAND 192 200 {ECO:0000244|PDB:1UU1}. FT TURN 201 204 {ECO:0000244|PDB:1UU1}. FT HELIX 207 209 {ECO:0000244|PDB:1UU1}. FT STRAND 212 216 {ECO:0000244|PDB:1UU1}. FT HELIX 218 227 {ECO:0000244|PDB:1UU1}. FT HELIX 235 246 {ECO:0000244|PDB:1UU1}. FT HELIX 248 272 {ECO:0000244|PDB:1UU1}. FT STRAND 281 287 {ECO:0000244|PDB:1UU1}. FT HELIX 291 302 {ECO:0000244|PDB:1UU1}. FT STRAND 305 310 {ECO:0000244|PDB:1UU1}. FT STRAND 313 317 {ECO:0000244|PDB:1UU1}. FT HELIX 321 332 {ECO:0000244|PDB:1UU1}. SQ SEQUENCE 335 AA; 39298 MW; D7CA1B807825376A CRC64; MNPLDLIAKR AYPYETEKRD KTYLALNENP FPFPEDLVDE VFRRLNSDAL RIYYDSPDEE LIEKILSYLD TDFLSKNNVS VGNGADEIIY VMMLMFDRSV FFPPTYSCYR IFAKAVGAKF LEVPLTKDLR IPEVNVGEGD VVFIPNPNNP TGHVFEREEI ERILKTGAFV ALDEAYYEFH GESYVDFLKK YENLAVIRTF SKAFSLAAQR VGYVVASEKF IDAYNRVRLP FNVSYVSQMF AKVALDHREI FEERTKFIVE ERERMKSALR EMGYRITDSR GNFVFVFMEK EEKERLLEHL RTKNVAVRSF REGVRITIGK REENDMILRE LEVFK // ID HIS5_THEMA Reviewed; 201 AA. AC Q9X0C8; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 126. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH; DE EC=2.4.2.-; DE AltName: Full=IGP synthase glutamine amidotransferase subunit; DE AltName: Full=IGP synthase subunit HisH; DE AltName: Full=ImGP synthase subunit HisH; DE Short=IGPS subunit HisH; DE AltName: Full=TmHisH; GN Name=hisH; OrderedLocusNames=TM_1038; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF N-TERMINUS, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=11264293; DOI=10.1074/jbc.M102012200; RA Beismann-Driemeyer S., Sterner R.; RT "Imidazole glycerol phosphate synthase from Thermotoga maritima. RT Quaternary structure, steady-state kinetics, and reaction mechanism of RT the bienzyme complex."; RL J. Biol. Chem. 276:20387-20396(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=12360532; DOI=10.1002/prot.10161; RA Korolev S., Skarina T., Evdokimova E., Beasley S., Edwards A., RA Joachimiak A., Savchenko A.; RT "Crystal structure of glutamine amidotransferase from Thermotoga RT maritima."; RL Proteins 49:420-422(2002). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=11839304; DOI=10.1016/S0969-2126(02)00702-5; RA Douangamath A., Walker M., Beismann-Driemeyer S., Vega-Fernandez M.C., RA Sterner R., Wilmanns M.; RT "Structural evidence for ammonia tunneling across the (beta alpha)(8) RT barrel of the imidazole glycerol phosphate synthase bienzyme RT complex."; RL Structure 10:185-193(2002). CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to CC IGP, AICAR and glutamate. The HisH subunit provides the glutamine CC amidotransferase activity that produces the ammonia necessary to CC HisF for the synthesis of IGP and AICAR. CC -!- CATALYTIC ACTIVITY: 5-[(5-phospho-1-deoxyribulos-1- CC ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4- CC carboxamide + L-glutamine = imidazole-glycerol phosphate + 5- CC aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H(2)O. CC -!- ENZYME REGULATION: Activated by the binding of either IGP or PRFAR CC to the active site of HisF. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.32 mM for glutamine {ECO:0000269|PubMed:11264293}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC -!- SUBUNIT: Heterodimer of HisH and HisF. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36115.1; -; Genomic_DNA. DR PIR; E72304; E72304. DR RefSeq; NP_228844.1; NC_000853.1. DR RefSeq; WP_004080484.1; NZ_CP011107.1. DR PDB; 1GPW; X-ray; 2.40 A; B/D/F=1-201. DR PDB; 1K9V; X-ray; 2.40 A; F=1-201. DR PDB; 1KXJ; X-ray; 2.80 A; A/B=1-201. DR PDB; 2WJZ; X-ray; 2.60 A; B/D/F=1-201. DR PDB; 3ZR4; X-ray; 2.41 A; B/D/F=1-201. DR PDBsum; 1GPW; -. DR PDBsum; 1K9V; -. DR PDBsum; 1KXJ; -. DR PDBsum; 2WJZ; -. DR PDBsum; 3ZR4; -. DR ProteinModelPortal; Q9X0C8; -. DR SMR; Q9X0C8; 1-201. DR DIP; DIP-59019N; -. DR STRING; 243274.TM1038; -. DR MEROPS; C26.965; -. DR EnsemblBacteria; AAD36115; AAD36115; TM_1038. DR GeneID; 897045; -. DR KEGG; tma:TM1038; -. DR PATRIC; 23937005; VBITheMar51294_1051. DR eggNOG; ENOG4108UJE; Bacteria. DR eggNOG; COG0118; LUCA. DR InParanoid; Q9X0C8; -. DR KO; K02501; -. DR OMA; STIAQCH; -. DR OrthoDB; EOG69KV05; -. DR BioCyc; MetaCyc:MONOMER-468; -. DR BRENDA; 4.3.1.B2; 6331. DR UniPathway; UPA00031; UER00010. DR EvolutionaryTrace; Q9X0C8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00278; HisH; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR010139; Imidazole-glycPsynth_HisH. DR Pfam; PF00117; GATase; 1. DR PIRSF; PIRSF000495; Amidotransf_hisH; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01855; IMP_synth_hisH; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Direct protein sequencing; Glutamine amidotransferase; KW Histidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 201 Imidazole glycerol phosphate synthase FT subunit HisH. FT /FTId=PRO_0000152437. FT DOMAIN 2 201 Glutamine amidotransferase type-1. FT ACT_SITE 84 84 Nucleophile. FT ACT_SITE 178 178 FT ACT_SITE 180 180 FT STRAND 2 6 {ECO:0000244|PDB:1GPW}. FT STRAND 9 11 {ECO:0000244|PDB:1GPW}. FT HELIX 14 23 {ECO:0000244|PDB:1GPW}. FT TURN 24 26 {ECO:0000244|PDB:1K9V}. FT STRAND 27 29 {ECO:0000244|PDB:1GPW}. FT STRAND 31 35 {ECO:0000244|PDB:1GPW}. FT STRAND 44 48 {ECO:0000244|PDB:1GPW}. FT HELIX 55 63 {ECO:0000244|PDB:1GPW}. FT HELIX 67 75 {ECO:0000244|PDB:1GPW}. FT STRAND 79 83 {ECO:0000244|PDB:1GPW}. FT HELIX 85 88 {ECO:0000244|PDB:1GPW}. FT STRAND 91 94 {ECO:0000244|PDB:1GPW}. FT STRAND 97 101 {ECO:0000244|PDB:1GPW}. FT STRAND 105 112 {ECO:0000244|PDB:1GPW}. FT STRAND 119 132 {ECO:0000244|PDB:1GPW}. FT STRAND 135 147 {ECO:0000244|PDB:1GPW}. FT HELIX 149 151 {ECO:0000244|PDB:1GPW}. FT STRAND 152 158 {ECO:0000244|PDB:1GPW}. FT STRAND 161 169 {ECO:0000244|PDB:1GPW}. FT STRAND 172 177 {ECO:0000244|PDB:1GPW}. FT HELIX 179 181 {ECO:0000244|PDB:1GPW}. FT HELIX 183 196 {ECO:0000244|PDB:1GPW}. SQ SEQUENCE 201 AA; 23097 MW; 10957D075094F778 CRC64; MRIGIISVGP GNIMNLYRGV KRASENFEDV SIELVESPRN DLYDLLFIPG VGHFGEGMRR LRENDLIDFV RKHVEDERYV VGVCLGMQLL FEESEEAPGV KGLSLIEGNV VKLRSRRLPH MGWNEVIFKD TFPNGYYYFV HTYRAVCEEE HVLGTTEYDG EIFPSAVRKG RILGFQFHPE KSSKIGRKLL EKVIECSLSR R // ID HPPA_THEMA Reviewed; 726 AA. AC Q9S5X0; O51935; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=K(+)-stimulated pyrophosphate-energized sodium pump; DE EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_01129}; DE AltName: Full=Membrane-bound sodium-translocating pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01129}; DE AltName: Full=Pyrophosphate-energized inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01129}; DE Short=Na(+)-PPase {ECO:0000255|HAMAP-Rule:MF_01129}; DE AltName: Full=Tm-PPase; GN Name=hppA {ECO:0000255|HAMAP-Rule:MF_01129}; GN OrderedLocusNames=TM_0174; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-276. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9440516; RA Bouthier de la Tour C., Portemer C., Kaltoum H., Duguet M.; RT "Reverse gyrase from the hyperthermophilic bacterium Thermotoga RT maritima: properties and gene structure."; RL J. Bacteriol. 180:274-281(1998). RN [3] RP CHARACTERIZATION, FUNCTION, COFACTOR, ENZYME REGULATION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=11343697; DOI=10.1016/S0014-5793(01)02390-0; RA Perez-Castineira J.R., Lopez-Marques R.L., Losada M., Serrano A.; RT "A thermostable K(+)-stimulated vacuolar-type pyrophosphatase from the RT hyperthermophilic bacterium Thermotoga maritima."; RL FEBS Lett. 496:6-11(2001). RN [4] RP CATALYTIC ACTIVITY, ENZYME REGULATION, AND MUTAGENESIS OF ASP-190 AND RP ASP-703. RX PubMed=15697234; DOI=10.1021/bi048429g; RA Belogurov G.A., Malinen A.M., Turkina M.V., Jalonen U., Rytkonen K., RA Baykov A.A., Lahti R.; RT "Membrane-bound pyrophosphatase of Thermotoga maritima requires sodium RT for activity."; RL Biochemistry 44:2088-2096(2005). RN [5] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=16182234; DOI=10.1016/j.bbamem.2005.08.004; RA Lopez-Marques R.L., Perez-Castineira J.R., Buch-Pedersen M.J., RA Marco S., Rigaud J.L., Palmgren M.G., Serrano A.; RT "Large-scale purification of the proton pumping pyrophosphatase from RT Thermotoga maritima: a 'Hot-Solve' method for isolation of recombinant RT thermophilic membrane proteins."; RL Biochim. Biophys. Acta 1716:69-76(2005). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=17605473; DOI=10.1021/bi700564b; RA Malinen A.M., Belogurov G.A., Baykov A.A., Lahti R.; RT "Na+-pyrophosphatase: a novel primary sodium pump."; RL Biochemistry 46:8872-8878(2007). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH CALCIUM AND RP MAGNESIUM, TOPOLOGY, FUNCTION, SUBUNIT, METAL-BINDING SITES, ENZYME RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=22837527; DOI=10.1126/science.1222505; RA Kellosalo J., Kajander T., Kogan K., Pokharel K., Goldman A.; RT "The structure and catalytic cycle of a sodium-pumping RT pyrophosphatase."; RL Science 337:473-476(2012). CC -!- FUNCTION: Sodium pump that utilizes the energy of pyrophosphate CC hydrolysis as the driving force for Na(+) movement across the CC membrane. {ECO:0000255|HAMAP-Rule:MF_01129, CC ECO:0000269|PubMed:11343697, ECO:0000269|PubMed:17605473, CC ECO:0000269|PubMed:22837527}. CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000269|PubMed:15697234, CC ECO:0000269|PubMed:17605473}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01129, CC ECO:0000269|PubMed:11343697}; CC -!- ENZYME REGULATION: Inhibited by GdCl3. Requires K(+) for maximal CC activity. K(+) greatly stimulates Na(+) binding. Thermostability CC depends on the binding of Mg(2+). {ECO:0000269|PubMed:11343697, CC ECO:0000269|PubMed:15697234, ECO:0000269|PubMed:22837527}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 70 degrees Celsius. CC {ECO:0000269|PubMed:11343697, ECO:0000269|PubMed:22837527}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01129, CC ECO:0000269|PubMed:16182234, ECO:0000269|PubMed:22837527}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01129, ECO:0000269|PubMed:16182234}; Multi-pass membrane CC protein {ECO:0000255|HAMAP-Rule:MF_01129, CC ECO:0000269|PubMed:16182234}. CC -!- DOMAIN: Has 16 transmembrane helices and a cytoplasmic domain that CC contains the active site. Pyrophosphate binding is thought to CC trigger a conformation change that allows Na(+) release. Has at CC least two binding sites for Na(+) (PubMed:22837527). CC {ECO:0000269|PubMed:22837527}. CC -!- SIMILARITY: Belongs to the H(+)-translocating pyrophosphatase CC (TC 3.A.10) family. K(+)-stimulated subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01129}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35267.1; -; Genomic_DNA. DR EMBL; AF013268; AAC01564.2; -; Genomic_DNA. DR PIR; D72409; D72409. DR RefSeq; NP_227989.1; NC_000853.1. DR RefSeq; WP_004082809.1; NZ_CP011107.1. DR PDB; 4AV3; X-ray; 2.60 A; A/B=2-726. DR PDB; 4AV6; X-ray; 4.00 A; A/B=2-726. DR PDBsum; 4AV3; -. DR PDBsum; 4AV6; -. DR STRING; 243274.TM0174; -. DR TCDB; 3.A.10.1.4; the h(+), na(+)-translocating pyrophosphatase (m(+)-ppase) family. DR EnsemblBacteria; AAD35267; AAD35267; TM_0174. DR GeneID; 897014; -. DR KEGG; tma:TM0174; -. DR PATRIC; 23935196; VBITheMar51294_0175. DR eggNOG; ENOG4105EAY; Bacteria. DR eggNOG; COG3808; LUCA. DR InParanoid; Q9S5X0; -. DR KO; K15987; -. DR OMA; FLAHETK; -. DR OrthoDB; EOG6TXQSF; -. DR BRENDA; 3.6.1.1; 6331. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0009678; F:hydrogen-translocating pyrophosphatase activity; IEA:InterPro. DR GO; GO:0004427; F:inorganic diphosphatase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015992; P:proton transport; IEA:InterPro. DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB. DR HAMAP; MF_01129; PPase_energized_pump; 1. DR InterPro; IPR004131; PPase-energised_H-pump. DR Pfam; PF03030; H_PPase; 1. DR PIRSF; PIRSF001265; H+-PPase; 1. DR TIGRFAMs; TIGR01104; V_PPase; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cell membrane; Complete proteome; Hydrolase; KW Ion transport; Magnesium; Membrane; Metal-binding; Potassium; KW Reference proteome; Sodium; Sodium transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 726 K(+)-stimulated pyrophosphate-energized FT sodium pump. FT /FTId=PRO_0000217005. FT TOPO_DOM 1 1 Periplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 2 22 Helical. FT TOPO_DOM 23 46 Cytoplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 47 71 Helical. FT TOPO_DOM 72 73 Periplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 74 97 Helical. FT TOPO_DOM 98 122 Cytoplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 123 153 Helical. FT TOPO_DOM 154 168 Periplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 169 197 Helical. FT TOPO_DOM 198 235 Cytoplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 236 261 Helical. FT TOPO_DOM 262 284 Periplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 285 309 Helical. FT TOPO_DOM 310 320 Cytoplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 321 343 Helical. FT TOPO_DOM 344 358 Periplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 359 379 Helical. FT TOPO_DOM 380 405 Cytoplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 406 430 Helical. FT TOPO_DOM 431 436 Periplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 437 463 Helical. FT TOPO_DOM 464 492 Cytoplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 493 520 Helical. FT TOPO_DOM 521 541 Periplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 542 571 Helical. FT TOPO_DOM 572 601 Cytoplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 602 629 Helical. FT TOPO_DOM 630 630 Periplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 631 658 Helical. FT TOPO_DOM 659 697 Cytoplasmic. FT {ECO:0000269|PubMed:22837527}. FT TRANSMEM 698 722 Helical. FT TOPO_DOM 723 726 Periplasmic. FT {ECO:0000269|PubMed:22837527}. FT METAL 202 202 Magnesium 1. {ECO:0000250}. FT METAL 206 206 Magnesium 1. {ECO:0000250}. FT METAL 229 229 Magnesium 2. FT {ECO:0000269|PubMed:22837527}. FT METAL 232 232 Magnesium 2. FT {ECO:0000269|PubMed:22837527}. FT METAL 465 465 Magnesium 2. FT {ECO:0000269|PubMed:22837527}. FT METAL 660 660 Calcium or magnesium. FT {ECO:0000269|PubMed:22837527}. FT METAL 688 688 Calcium or magnesium. FT {ECO:0000269|PubMed:22837527}. FT METAL 692 692 Calcium or magnesium. FT {ECO:0000269|PubMed:22837527}. FT BINDING 199 199 Substrate. FT BINDING 695 695 Substrate. FT SITE 191 191 Important for ion transport. FT {ECO:0000250}. FT SITE 236 236 Important for ion transport. FT {ECO:0000250}. FT SITE 243 243 Important for ion transport. FT {ECO:0000250}. FT SITE 495 495 Important for potassium dependence. FT {ECO:0000305}. FT SITE 696 696 Important for ion transport. FT {ECO:0000250}. FT SITE 707 707 Important for ion transport. FT {ECO:0000250}. FT MUTAGEN 190 190 D->A: No change in activity. FT {ECO:0000269|PubMed:15697234}. FT MUTAGEN 703 703 D->N: Silences the K(+)-independent FT activating Na(+)-binding site. FT {ECO:0000269|PubMed:15697234}. FT HELIX 3 8 {ECO:0000244|PDB:4AV3}. FT HELIX 10 26 {ECO:0000244|PDB:4AV3}. FT HELIX 33 71 {ECO:0000244|PDB:4AV3}. FT HELIX 74 108 {ECO:0000244|PDB:4AV3}. FT TURN 109 112 {ECO:0000244|PDB:4AV3}. FT HELIX 116 147 {ECO:0000244|PDB:4AV3}. FT TURN 148 152 {ECO:0000244|PDB:4AV3}. FT HELIX 154 157 {ECO:0000244|PDB:4AV3}. FT HELIX 171 192 {ECO:0000244|PDB:4AV3}. FT HELIX 194 205 {ECO:0000244|PDB:4AV3}. FT HELIX 226 236 {ECO:0000244|PDB:4AV3}. FT HELIX 238 265 {ECO:0000244|PDB:4AV3}. FT STRAND 267 270 {ECO:0000244|PDB:4AV3}. FT STRAND 273 278 {ECO:0000244|PDB:4AV3}. FT HELIX 280 310 {ECO:0000244|PDB:4AV3}. FT HELIX 317 344 {ECO:0000244|PDB:4AV3}. FT HELIX 350 353 {ECO:0000244|PDB:4AV3}. FT HELIX 358 360 {ECO:0000244|PDB:4AV3}. FT HELIX 361 384 {ECO:0000244|PDB:4AV3}. FT HELIX 389 397 {ECO:0000244|PDB:4AV3}. FT HELIX 398 400 {ECO:0000244|PDB:4AV3}. FT HELIX 402 416 {ECO:0000244|PDB:4AV3}. FT HELIX 418 447 {ECO:0000244|PDB:4AV3}. FT TURN 448 450 {ECO:0000244|PDB:4AV3}. FT HELIX 451 474 {ECO:0000244|PDB:4AV3}. FT HELIX 479 519 {ECO:0000244|PDB:4AV3}. FT HELIX 524 526 {ECO:0000244|PDB:4AV3}. FT STRAND 527 529 {ECO:0000244|PDB:4AV3}. FT HELIX 531 533 {ECO:0000244|PDB:4AV3}. FT HELIX 542 574 {ECO:0000244|PDB:4AV3}. FT HELIX 577 583 {ECO:0000244|PDB:4AV3}. FT TURN 584 587 {ECO:0000244|PDB:4AV3}. FT HELIX 597 609 {ECO:0000244|PDB:4AV3}. FT HELIX 612 629 {ECO:0000244|PDB:4AV3}. FT HELIX 631 667 {ECO:0000244|PDB:4AV3}. FT STRAND 671 673 {ECO:0000244|PDB:4AV3}. FT STRAND 676 678 {ECO:0000244|PDB:4AV3}. FT HELIX 679 696 {ECO:0000244|PDB:4AV3}. FT HELIX 698 723 {ECO:0000244|PDB:4AV3}. SQ SEQUENCE 726 AA; 77046 MW; 492243F8C320BF93 CRC64; MYVAALFFLI PLVALGFAAA NFAAVVRKPE GTERMKEISS YIRSGADSFL AHETKAIFKV AIVIAILLMI FTTWQTGVAF LLGAVMSASA GIVGMKMATR ANVRVAEAAR TTKKIGPALK VAYQGGSVMG LSVGGFALLG LVLVYLIFGK WMGQVDNLNI YTNWLGINFV PFAMTVSGYA LGCSIIAMFD RVGGGVYTKA ADMAADLVGK TELNLPEDDP RNPATIADNV GDNVGDVAGL GADLLESFVG AIVSSIILAS YMFPIYVQKI GENLVHQVPK ETIQALISYP IFFALVGLGC SMLGILYVIV KKPSDNPQRE LNISLWTSAL LTVVLTAFLT YFYLKDLQGL DVVGFRFGAI SPWFSAIIGI FSGILIGFWA EYYTSYRYKP TQFLSKSSIE GTGMVISNGL SLGMKSVFPP TLTLVLGILF ADYFAGLYGV AIAALGMLSF VATSVSVDSY GPIADNAGGI SEMCELDPEV RKITDHLDAV GNTTAAIGKG FAIGSAIFAA LSLFASYMFS QISPSDIGKP PSLVLLLNML DARVIAGALL GAAITYYFSG YLISAVTKAA MKMVDEIRRQ AREIPGLLEG KAKPDYNRCI EITSDNALKQ MGYPAFIAIL TPLVTGFLLG AEFVGGVLIG TVLSGAMLAI LTANSGGAWD NAKKYLEAGN LEGYGKGSEP HKALVIGDTV GDPLKDTVGP SLDILIKIMS VVSVIAVSIF KHVHLF // ID HPR_THEMA Reviewed; 306 AA. AC Q9X1C1; G4FFD7; DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Hydroxypyruvate reductase; DE Short=HPR; DE EC=1.1.1.81; GN OrderedLocusNames=TM_1401; ORFNames=THEMA_07310, Tmari_1408; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RG DOE Joint Genome Institute; RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18156253; DOI=10.1128/JB.01469-07; RA Yang C., Rodionov D.A., Rodionova I.A., Li X., Osterman A.L.; RT "Glycerate 2-kinase of Thermotoga maritima and genomic reconstruction RT of related metabolic pathways."; RL J. Bacteriol. 190:1773-1782(2008). CC -!- FUNCTION: Involved in the degradation of L-serine via 3- CC hydroxypyruvate. Catalyzes the non-reversible reduction of 3- CC hydroxypyruvate to yield D-glycerate. CC {ECO:0000269|PubMed:18156253}. CC -!- CATALYTIC ACTIVITY: D-glycerate + NAD(P)(+) = hydroxypyruvate + CC NAD(P)H. {ECO:0000269|PubMed:18156253}. CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36472.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50332.1; -; Genomic_DNA. DR EMBL; CP007013; AHD18703.1; -; Genomic_DNA. DR PIR; B72257; B72257. DR RefSeq; NP_229202.1; NC_000853.1. DR RefSeq; WP_004081620.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1C1; -. DR SMR; Q9X1C1; 5-301. DR STRING; 243274.TM1401; -. DR EnsemblBacteria; AAD36472; AAD36472; TM_1401. DR EnsemblBacteria; AGL50332; AGL50332; Tmari_1408. DR EnsemblBacteria; AHD18703; AHD18703; THEMA_07310. DR GeneID; 898075; -. DR KEGG; tma:TM1401; -. DR KEGG; tmi:THEMA_07310; -. DR KEGG; tmm:Tmari_1408; -. DR KEGG; tmw:THMA_1430; -. DR PATRIC; 23937748; VBITheMar51294_1413. DR eggNOG; ENOG4108JQ1; Bacteria. DR eggNOG; COG0111; LUCA. DR InParanoid; Q9X1C1; -. DR KO; K00058; -. DR OMA; AKCKQGV; -. DR OrthoDB; EOG6VXFC3; -. DR BioCyc; TMAR243274:GC6P-1438-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IBA:GO_Central. DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR029753; D-isomer_DH_CS. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1. PE 1: Evidence at protein level; KW Complete proteome; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 306 Hydroxypyruvate reductase. FT /FTId=PRO_0000428996. FT NP_BIND 152 153 NAD. {ECO:0000250}. FT NP_BIND 228 230 NAD. {ECO:0000250}. FT NP_BIND 280 283 NAD. {ECO:0000250}. FT ACT_SITE 230 230 {ECO:0000250}. FT ACT_SITE 259 259 {ECO:0000250}. FT ACT_SITE 280 280 Proton donor. {ECO:0000250}. FT BINDING 172 172 NAD. {ECO:0000250}. FT BINDING 254 254 NAD. {ECO:0000250}. SQ SEQUENCE 306 AA; 33451 MW; 49896899D111C039 CRC64; MARYRVHVND PLDKEATQLL MNKEELEVTS EHLEKDELMK IIPEVDVLVV RSATKVTADI IEAGKNLKII ARAGIGLDNI DVQKAKEKGI KVLNTPGASA PSVAELAMGL MLACARHIAR ATVSLKEGKW EKKALKGKEL LGKTLGLIGF GNIGQEVAKR ALAFGMKIIA YDPAKPETDL PVEYVDLDTL FKESDFISLH VPLTESTRHI INRESIAKMK DGVIIVNTAR GGTIDEEALY EEVVSGKVYA AGLDVFEVEP PTDEIRRKLL SLDNVVATPH IGASTAEAQR RVGIELVEKI FKELGI // ID HIS6_THEMA Reviewed; 253 AA. AC Q9X0C6; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 123. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF; DE EC=4.1.3.-; DE AltName: Full=IGP synthase cyclase subunit; DE AltName: Full=IGP synthase subunit HisF; DE AltName: Full=ImGP synthase subunit HisF; DE Short=IGPS subunit HisF; GN Name=hisF; OrderedLocusNames=TM_1036; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF N-TERMINUS, MUTAGENESIS OF CYS-9; ASP-11; LYS-19; RP ASP-51; ASN-103; ASP-130; ASP-176 AND ASP-183, BIOPHYSICOCHEMICAL RP PROPERTIES, AND REACTION MECHANISM. RX PubMed=11264293; DOI=10.1074/jbc.M102012200; RA Beismann-Driemeyer S., Sterner R.; RT "Imidazole glycerol phosphate synthase from Thermotoga maritima. RT Quaternary structure, steady-state kinetics, and reaction mechanism of RT the bienzyme complex."; RL J. Biol. Chem. 276:20387-20396(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS). RX PubMed=10968789; DOI=10.1126/science.289.5484.1546; RA Lang D., Thoma R., Henn-Sax M., Sterner R., Wilmanns M.; RT "Structural evidence for evolution of the beta/alpha barrel scaffold RT by gene duplication and fusion."; RL Science 289:1546-1550(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=11839304; DOI=10.1016/S0969-2126(02)00702-5; RA Douangamath A., Walker M., Beismann-Driemeyer S., Vega-Fernandez M.C., RA Sterner R., Wilmanns M.; RT "Structural evidence for ammonia tunneling across the (beta alpha)(8) RT barrel of the imidazole glycerol phosphate synthase bienzyme RT complex."; RL Structure 10:185-193(2002). CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to CC IGP, AICAR and glutamate. The HisF subunit catalyzes the CC cyclization activity that produces IGP and AICAR from PRFAR using CC the ammonia provided by the HisH subunit. CC -!- CATALYTIC ACTIVITY: 5-[(5-phospho-1-deoxyribulos-1- CC ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4- CC carboxamide + L-glutamine = imidazole-glycerol phosphate + 5- CC aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H(2)O. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.5 uM for PRFAR {ECO:0000269|PubMed:11264293}; CC KM=2.2 mM for NH(3) {ECO:0000269|PubMed:11264293}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC -!- SUBUNIT: Heterodimer of HisH and HisF. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36113.1; -; Genomic_DNA. DR PIR; C72304; C72304. DR RefSeq; NP_228842.1; NC_000853.1. DR RefSeq; WP_004080486.1; NZ_CP011107.1. DR PDB; 1GPW; X-ray; 2.40 A; A/C/E=1-253. DR PDB; 1THF; X-ray; 1.45 A; D=1-253. DR PDB; 1VH7; X-ray; 1.90 A; A=2-253. DR PDB; 2A0N; X-ray; 1.64 A; A=1-253. DR PDB; 2LLE; NMR; -; A=103-247. DR PDB; 2W6R; X-ray; 2.10 A; A=123-253. DR PDB; 2WJZ; X-ray; 2.60 A; A/C/E=1-253. DR PDB; 3CWO; X-ray; 3.10 A; X=103-253. DR PDB; 3OG3; X-ray; 2.08 A; A=43-221. DR PDB; 3ZR4; X-ray; 2.41 A; A/C/E=1-253. DR PDB; 4EWN; X-ray; 1.90 A; D=1-253. DR PDB; 4FX7; X-ray; 2.08 A; A/B/C/D=99-219. DR PDB; 4J9J; X-ray; 2.30 A; A=91-220. DR PDBsum; 1GPW; -. DR PDBsum; 1THF; -. DR PDBsum; 1VH7; -. DR PDBsum; 2A0N; -. DR PDBsum; 2LLE; -. DR PDBsum; 2W6R; -. DR PDBsum; 2WJZ; -. DR PDBsum; 3CWO; -. DR PDBsum; 3OG3; -. DR PDBsum; 3ZR4; -. DR PDBsum; 4EWN; -. DR PDBsum; 4FX7; -. DR PDBsum; 4J9J; -. DR ProteinModelPortal; Q9X0C6; -. DR SMR; Q9X0C6; 1-251. DR DIP; DIP-59020N; -. DR STRING; 243274.TM1036; -. DR EnsemblBacteria; AAD36113; AAD36113; TM_1036. DR GeneID; 897046; -. DR KEGG; tma:TM1036; -. DR PATRIC; 23937001; VBITheMar51294_1049. DR eggNOG; ENOG4105C0S; Bacteria. DR eggNOG; COG0107; LUCA. DR InParanoid; Q9X0C6; -. DR KO; K02500; -. DR OMA; KGTNFVN; -. DR OrthoDB; EOG6H1Q3W; -. DR BioCyc; MetaCyc:MONOMER-467; -. DR BRENDA; 4.3.1.B2; 6331. DR UniPathway; UPA00031; UER00010. DR EvolutionaryTrace; Q9X0C6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01013; HisF; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR004651; HisF. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00977; His_biosynth; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00735; hisF; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Direct protein sequencing; Histidine biosynthesis; Lyase; KW Reference proteome. FT CHAIN 1 253 Imidazole glycerol phosphate synthase FT subunit HisF. FT /FTId=PRO_0000142253. FT ACT_SITE 11 11 {ECO:0000255}. FT ACT_SITE 130 130 {ECO:0000255}. FT MUTAGEN 9 9 C->A: No change in activity. FT {ECO:0000269|PubMed:11264293}. FT MUTAGEN 11 11 D->X: Loss of activity. FT {ECO:0000269|PubMed:11264293}. FT MUTAGEN 19 19 K->S: Decrease in activity. FT {ECO:0000269|PubMed:11264293}. FT MUTAGEN 51 51 D->N: No change in activity. FT {ECO:0000269|PubMed:11264293}. FT MUTAGEN 103 103 N->A: No change in activity. FT {ECO:0000269|PubMed:11264293}. FT MUTAGEN 130 130 D->A,C,F,G,H,I,K,L,M,N,P,Q,R,S,T,V,W,Y: FT Complete loss of activity. FT {ECO:0000269|PubMed:11264293}. FT MUTAGEN 130 130 D->E: Weak activity. FT {ECO:0000269|PubMed:11264293}. FT MUTAGEN 176 176 D->N: Decrease in activity. FT {ECO:0000269|PubMed:11264293}. FT MUTAGEN 183 183 D->N: No change in activity. FT {ECO:0000269|PubMed:11264293}. FT STRAND 5 13 {ECO:0000244|PDB:1THF}. FT STRAND 16 23 {ECO:0000244|PDB:1GPW}. FT HELIX 32 41 {ECO:0000244|PDB:1THF}. FT STRAND 46 53 {ECO:0000244|PDB:1THF}. FT STRAND 55 57 {ECO:0000244|PDB:1THF}. FT HELIX 58 70 {ECO:0000244|PDB:1THF}. FT STRAND 77 82 {ECO:0000244|PDB:1THF}. FT HELIX 86 94 {ECO:0000244|PDB:1THF}. FT STRAND 98 103 {ECO:0000244|PDB:1THF}. FT HELIX 104 108 {ECO:0000244|PDB:1THF}. FT HELIX 111 120 {ECO:0000244|PDB:1THF}. FT HELIX 122 124 {ECO:0000244|PDB:1THF}. FT STRAND 125 134 {ECO:0000244|PDB:1THF}. FT STRAND 137 142 {ECO:0000244|PDB:1THF}. FT TURN 143 146 {ECO:0000244|PDB:1THF}. FT STRAND 147 152 {ECO:0000244|PDB:1THF}. FT HELIX 153 162 {ECO:0000244|PDB:1THF}. FT STRAND 166 172 {ECO:0000244|PDB:1THF}. FT TURN 173 177 {ECO:0000244|PDB:1THF}. FT HELIX 184 190 {ECO:0000244|PDB:1THF}. FT HELIX 191 193 {ECO:0000244|PDB:1THF}. FT STRAND 198 202 {ECO:0000244|PDB:1THF}. FT HELIX 207 215 {ECO:0000244|PDB:1THF}. FT STRAND 219 224 {ECO:0000244|PDB:1THF}. FT HELIX 225 228 {ECO:0000244|PDB:1THF}. FT STRAND 229 232 {ECO:0000244|PDB:1GPW}. FT HELIX 234 243 {ECO:0000244|PDB:1THF}. FT STRAND 250 253 {ECO:0000244|PDB:3CWO}. SQ SEQUENCE 253 AA; 27719 MW; FE0F97F0C57E9025 CRC64; MLAKRIIACL DVKDGRVVKG TNFENLRDSG DPVELGKFYS EIGIDELVFL DITASVEKRK TMLELVEKVA EQIDIPFTVG GGIHDFETAS ELILRGADKV SINTAAVENP SLITQIAQTF GSQAVVVAID AKRVDGEFMV FTYSGKKNTG ILLRDWVVEV EKRGAGEILL TSIDRDGTKS GYDTEMIRFV RPLTTLPIIA SGGAGKMEHF LEAFLAGADA ALAASVFHFR EIDVRELKEY LKKHGVNVRL EGL // ID HIS9_THEMA Reviewed; 233 AA. AC Q9WZR1; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=Probable histidinol-phosphatase; DE Short=HolPase; DE EC=3.1.3.15; GN Name=hisK; OrderedLocusNames=TM_0804; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + H(2)O = L-histidinol CC + phosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9. CC -!- SIMILARITY: Belongs to the PHP hydrolase family. HisK subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35886.1; -; Genomic_DNA. DR PIR; E72330; E72330. DR RefSeq; NP_228613.1; NC_000853.1. DR RefSeq; WP_004080859.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZR1; -. DR STRING; 243274.TM0804; -. DR EnsemblBacteria; AAD35886; AAD35886; TM_0804. DR GeneID; 898472; -. DR KEGG; tma:TM0804; -. DR PATRIC; 23936528; VBITheMar51294_0816. DR eggNOG; ENOG4107RU2; Bacteria. DR eggNOG; COG1387; LUCA. DR InParanoid; Q9WZR1; -. DR KO; K04486; -. DR OMA; HIHSNFS; -. DR OrthoDB; EOG69975M; -. DR UniPathway; UPA00031; UER00013. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR010140; Histidinol_P_phosphatase_HisJ. DR InterPro; IPR004013; PHP_dom. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR PANTHER; PTHR21039; PTHR21039; 1. DR Pfam; PF02811; PHP; 1. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; SSF89550; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Hydrolase; Reference proteome. FT CHAIN 1 233 Probable histidinol-phosphatase. FT /FTId=PRO_0000122320. SQ SEQUENCE 233 AA; 27144 MW; E0CE3D245E0EDA30 CRC64; MIDMHLHSTF SYDGKAEIDD IISQVQKLGI EHFCITDHYE YENGELVHDF NVEEYFLTME KYDLPKGAEI SWDGVGEAVF PDGFDYLLLG IHRYDENLPP DELARDYLER TLFVMERVKF HTLAHLDYPA RYAKADFKAN RDLIEKILVF LVKNEKALEI NTAGLFKHGK PNPDYWIVEM YYDLGGRVVT IGSDAHESQH IGRGIEEVMR ELKKFNFEYL AVDGKKLVTV KLR // ID HRCA_THEMA Reviewed; 338 AA. AC Q9WZV5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Heat-inducible transcription repressor HrcA {ECO:0000255|HAMAP-Rule:MF_00081}; GN Name=hrcA {ECO:0000255|HAMAP-Rule:MF_00081}; GN OrderedLocusNames=TM_0851; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Negative regulator of class I heat shock genes (grpE- CC dnaK-dnaJ and groELS operons). Prevents heat-shock induction of CC these operons. {ECO:0000255|HAMAP-Rule:MF_00081}. CC -!- SIMILARITY: Belongs to the HrcA family. {ECO:0000255|HAMAP- CC Rule:MF_00081}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35933.1; -; Genomic_DNA. DR PIR; D72327; D72327. DR RefSeq; NP_228660.1; NC_000853.1. DR RefSeq; WP_004080775.1; NZ_CP011107.1. DR PDB; 1STZ; X-ray; 2.20 A; A/B/C=1-338. DR PDBsum; 1STZ; -. DR ProteinModelPortal; Q9WZV5; -. DR SMR; Q9WZV5; 14-336. DR STRING; 243274.TM0851; -. DR EnsemblBacteria; AAD35933; AAD35933; TM_0851. DR GeneID; 898522; -. DR KEGG; tma:TM0851; -. DR PATRIC; 23936628; VBITheMar51294_0864. DR eggNOG; ENOG4105CI8; Bacteria. DR eggNOG; COG1420; LUCA. DR InParanoid; Q9WZV5; -. DR KO; K03705; -. DR OMA; LNWEEIE; -. DR OrthoDB; EOG632D4G; -. DR EvolutionaryTrace; Q9WZV5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.390.60; -; 1. DR HAMAP; MF_00081; HrcA; 1. DR InterPro; IPR029016; GAF_dom-like. DR InterPro; IPR002571; HrcA. DR InterPro; IPR021153; HrcA_C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR InterPro; IPR023120; WHTH_transcript_rep_HrcA_IDD. DR Pfam; PF01628; HrcA; 1. DR PIRSF; PIRSF005485; HrcA; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF55781; SSF55781; 1. DR TIGRFAMs; TIGR00331; hrcA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; Repressor; KW Stress response; Transcription; Transcription regulation. FT CHAIN 1 338 Heat-inducible transcription repressor FT HrcA. FT /FTId=PRO_0000182552. FT HELIX 17 33 {ECO:0000244|PDB:1STZ}. FT HELIX 39 45 {ECO:0000244|PDB:1STZ}. FT HELIX 52 64 {ECO:0000244|PDB:1STZ}. FT STRAND 67 69 {ECO:0000244|PDB:1STZ}. FT STRAND 77 79 {ECO:0000244|PDB:1STZ}. FT HELIX 81 94 {ECO:0000244|PDB:1STZ}. FT TURN 95 97 {ECO:0000244|PDB:1STZ}. FT HELIX 103 106 {ECO:0000244|PDB:1STZ}. FT HELIX 116 131 {ECO:0000244|PDB:1STZ}. FT STRAND 134 138 {ECO:0000244|PDB:1STZ}. FT HELIX 142 144 {ECO:0000244|PDB:1STZ}. FT STRAND 149 154 {ECO:0000244|PDB:1STZ}. FT STRAND 156 166 {ECO:0000244|PDB:1STZ}. FT STRAND 169 177 {ECO:0000244|PDB:1STZ}. FT HELIX 184 195 {ECO:0000244|PDB:1STZ}. FT HELIX 200 205 {ECO:0000244|PDB:1STZ}. FT HELIX 209 212 {ECO:0000244|PDB:1STZ}. FT HELIX 215 224 {ECO:0000244|PDB:1STZ}. FT STRAND 230 234 {ECO:0000244|PDB:1STZ}. FT HELIX 236 241 {ECO:0000244|PDB:1STZ}. FT HELIX 247 256 {ECO:0000244|PDB:1STZ}. FT HELIX 260 266 {ECO:0000244|PDB:1STZ}. FT STRAND 269 275 {ECO:0000244|PDB:1STZ}. FT HELIX 276 279 {ECO:0000244|PDB:1STZ}. FT HELIX 282 284 {ECO:0000244|PDB:1STZ}. FT STRAND 287 296 {ECO:0000244|PDB:1STZ}. FT STRAND 299 312 {ECO:0000244|PDB:1STZ}. FT HELIX 314 334 {ECO:0000244|PDB:1STZ}. SQ SEQUENCE 338 AA; 39307 MW; 02A505A546C313AE CRC64; MRRLNRKNNE ALKKLNDRQR KVLYCIVREY IENKKPVSSQ RVLEVSNIEF SSATIRNDMK KLEYLGYIYQ PHTSAGRIPT DKGLRFYYEE MLKISKETSE ADLAVETFKS MPLADPEKVL FLAGNLLARL TEGYVLIERP NTRDLKILRV MLIPVSEDYL IFSILTEFGV SKVTPIKTQE RLNWEEIERQ LNFLLRGRTV GEVLMGKIES LKGSGFLRLI ESLIGETVER YLDAGLENLL KDETLTLEDI RNLLEEVKDQ KFLESLVGEG ITVRIGREIG RKKLEKFAVF SGKYFKGESP IGSVYLFTSK VTKYDRNHRV FEYILNRLSE YFTSTSRR // ID HISX_THEMA Reviewed; 428 AA. AC Q9X0D1; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Histidinol dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01024}; DE Short=HDH {ECO:0000255|HAMAP-Rule:MF_01024}; DE EC=1.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01024}; GN Name=hisD {ECO:0000255|HAMAP-Rule:MF_01024}; GN OrderedLocusNames=TM_1041; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- CC histidinol to L-histidinaldehyde and then to L-histidine. CC {ECO:0000255|HAMAP-Rule:MF_01024}. CC -!- CATALYTIC ACTIVITY: L-histidinol + H(2)O + 2 NAD(+) = L-histidine CC + 2 NADH. {ECO:0000255|HAMAP-Rule:MF_01024}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01024}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01024}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC {ECO:0000255|HAMAP-Rule:MF_01024}. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_01024}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36118.1; -; Genomic_DNA. DR PIR; H72304; H72304. DR RefSeq; NP_228847.1; NC_000853.1. DR RefSeq; WP_004080480.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0D1; -. DR STRING; 243274.TM1041; -. DR EnsemblBacteria; AAD36118; AAD36118; TM_1041. DR GeneID; 897023; -. DR KEGG; tma:TM1041; -. DR PATRIC; 23937011; VBITheMar51294_1054. DR eggNOG; ENOG4105CEK; Bacteria. DR eggNOG; COG0141; LUCA. DR InParanoid; Q9X0D1; -. DR KO; K00013; -. DR OMA; TEIYRVG; -. DR OrthoDB; EOG6CVVCR; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01024; HisD; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR001692; Histidinol_DH_CS. DR InterPro; IPR022695; Histidinol_DH_monofunct. DR InterPro; IPR012131; Hstdl_DH. DR Pfam; PF00815; Histidinol_dh; 1. DR PIRSF; PIRSF000099; Histidinol_dh; 1. DR PRINTS; PR00083; HOLDHDRGNASE. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR00069; hisD; 1. DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 428 Histidinol dehydrogenase. FT /FTId=PRO_0000135869. FT ACT_SITE 324 324 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT ACT_SITE 325 325 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT METAL 254 254 Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}. FT METAL 257 257 Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}. FT METAL 358 358 Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}. FT METAL 417 417 Zinc. {ECO:0000255|HAMAP-Rule:MF_01024}. FT BINDING 232 232 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 254 254 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 257 257 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 325 325 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 358 358 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 412 412 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. FT BINDING 417 417 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01024}. SQ SEQUENCE 428 AA; 47749 MW; A7A765F2C298B45C CRC64; MILMNNPGDK EVLRLLKQRM ESVSQVEETV KEIIRRVKEE GDRALEEFLK RFEKHPVGIE NLRVTEKEIS EAQVEEEFVE TIKIVIEDLK EFHRRQEERS FFFTTKGGSF LGEMVVPLES VGIYVPGGKV PYFSTLLMCA VPAIVAGVER IAVTTPPNEN GGISPYILKT CEILGLKEIY RMGGAHAVAA LTYGTETVKP VDKIVGPGGV FVTLAKKHVY GDVGIDSIAG PSEIAIVTDG SADLDLIAAD FLSQAEHDEN AMSVVITTSK EVFEKLPQVI ERHLEALPEE RRKTARISTE NFGTIILTDS LKRAFEISNL IAPEHLEVLV ENPFEPLGHI KNAGSVFLGK YTCESVGDYG AGPNHVLPTF RSARFSSGLR VSDFTKKIFI THLSEEDFRR KSELYSKMAR WEGFEAHARA IDVRREKL // ID HIS7_THEMA Reviewed; 195 AA. AC Q9X0C9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_00076}; DE Short=IGPD {ECO:0000255|HAMAP-Rule:MF_00076}; DE EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_00076}; GN Name=hisB {ECO:0000255|HAMAP-Rule:MF_00076}; GN OrderedLocusNames=TM_1039; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: D-erythro-1-(imidazol-4-yl)glycerol 3- CC phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00076}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9. CC {ECO:0000255|HAMAP-Rule:MF_00076}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00076}. CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase CC family. {ECO:0000255|HAMAP-Rule:MF_00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36116.1; -; Genomic_DNA. DR PIR; F72304; F72304. DR RefSeq; NP_228845.1; NC_000853.1. DR RefSeq; WP_004080483.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0C9; -. DR STRING; 243274.TM1039; -. DR EnsemblBacteria; AAD36116; AAD36116; TM_1039. DR GeneID; 897766; -. DR KEGG; tma:TM1039; -. DR PATRIC; 23937007; VBITheMar51294_1052. DR eggNOG; ENOG4105ECC; Bacteria. DR eggNOG; COG0131; LUCA. DR InParanoid; Q9X0C9; -. DR KO; K01693; -. DR OMA; IQREANI; -. DR OrthoDB; EOG60PHGP; -. DR UniPathway; UPA00031; UER00011. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00076; HisB; 1. DR InterPro; IPR000807; ImidazoleglycerolP_deHydtase. DR InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR PANTHER; PTHR23133:SF2; PTHR23133:SF2; 1. DR Pfam; PF00475; IGPD; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Lyase; Reference proteome. FT CHAIN 1 195 Imidazoleglycerol-phosphate dehydratase. FT /FTId=PRO_0000158180. SQ SEQUENCE 195 AA; 21997 MW; 719E6B5A6F610E73 CRC64; MTVERLENGV IVQRNTNEIE ISITLDTVHG KLEGSTGVNF FDHLLNTFCH YSGLGLRVST CESKDGILHH LIEDFGISLG LAFRELFDYT KVRRFGEATV PMNEALVGCY VDLSGRPFFQ KNFEFSVEKI EDMPVEGFEE FMCGFVNHAR ITVHFFKFFG KNDHHISESA MKSFGLAIAK ALESSEKKTT KGVID // ID HSLO_THEMA Reviewed; 290 AA. AC Q9X1B4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=33 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00117}; DE AltName: Full=Heat shock protein 33 homolog {ECO:0000255|HAMAP-Rule:MF_00117}; DE Short=HSP33 {ECO:0000255|HAMAP-Rule:MF_00117}; GN Name=hslO {ECO:0000255|HAMAP-Rule:MF_00117}; GN OrderedLocusNames=TM_1394; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Redox regulated molecular chaperone. Protects both CC thermally unfolding and oxidatively damaged proteins from CC irreversible aggregation. Plays an important role in the bacterial CC defense system toward oxidative stress. {ECO:0000255|HAMAP- CC Rule:MF_00117}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00117}. CC -!- PTM: Under oxidizing conditions two disulfide bonds are formed CC involving the reactive cysteines. Under reducing conditions zinc CC is bound to the reactive cysteines and the protein is inactive. CC {ECO:0000255|HAMAP-Rule:MF_00117}. CC -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000255|HAMAP- CC Rule:MF_00117}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36465.1; -; Genomic_DNA. DR PIR; C72259; C72259. DR RefSeq; NP_229195.1; NC_000853.1. DR RefSeq; WP_004081604.1; NZ_CP011107.1. DR PDB; 1VQ0; X-ray; 2.20 A; A/B=1-290. DR PDBsum; 1VQ0; -. DR ProteinModelPortal; Q9X1B4; -. DR SMR; Q9X1B4; 1-287. DR STRING; 243274.TM1394; -. DR EnsemblBacteria; AAD36465; AAD36465; TM_1394. DR GeneID; 898082; -. DR KEGG; tma:TM1394; -. DR PATRIC; 23937734; VBITheMar51294_1406. DR eggNOG; ENOG4107S82; Bacteria. DR eggNOG; COG1281; LUCA. DR InParanoid; Q9X1B4; -. DR KO; K04083; -. DR OMA; YLWQSEQ; -. DR OrthoDB; EOG651SSJ; -. DR EvolutionaryTrace; Q9X1B4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 3.55.30.10; -; 1. DR Gene3D; 3.90.1280.10; -; 1. DR HAMAP; MF_00117; HslO; 1. DR InterPro; IPR000397; Heat_shock_Hsp33. DR InterPro; IPR016154; Heat_shock_Hsp33_C. DR InterPro; IPR016153; Heat_shock_Hsp33_N. DR Pfam; PF01430; HSP33; 1. DR PIRSF; PIRSF005261; Heat_shock_Hsp33; 1. DR SUPFAM; SSF118352; SSF118352; 1. DR SUPFAM; SSF64397; SSF64397; 1. PE 1: Evidence at protein level; KW 3D-structure; Chaperone; Complete proteome; Cytoplasm; Disulfide bond; KW Redox-active center; Reference proteome; Zinc. FT CHAIN 1 290 33 kDa chaperonin. FT /FTId=PRO_0000192220. FT DISULFID 231 233 Redox-active. {ECO:0000255|HAMAP- FT Rule:MF_00117}. FT DISULFID 263 266 Redox-active. {ECO:0000255|HAMAP- FT Rule:MF_00117}. FT STRAND 1 7 {ECO:0000244|PDB:1VQ0}. FT TURN 8 11 {ECO:0000244|PDB:1VQ0}. FT STRAND 12 18 {ECO:0000244|PDB:1VQ0}. FT HELIX 20 30 {ECO:0000244|PDB:1VQ0}. FT HELIX 34 50 {ECO:0000244|PDB:1VQ0}. FT HELIX 51 53 {ECO:0000244|PDB:1VQ0}. FT STRAND 59 68 {ECO:0000244|PDB:1VQ0}. FT STRAND 72 78 {ECO:0000244|PDB:1VQ0}. FT STRAND 81 88 {ECO:0000244|PDB:1VQ0}. FT HELIX 104 108 {ECO:0000244|PDB:1VQ0}. FT STRAND 110 118 {ECO:0000244|PDB:1VQ0}. FT STRAND 120 123 {ECO:0000244|PDB:1VQ0}. FT STRAND 125 130 {ECO:0000244|PDB:1VQ0}. FT STRAND 132 136 {ECO:0000244|PDB:1VQ0}. FT HELIX 137 147 {ECO:0000244|PDB:1VQ0}. FT STRAND 152 161 {ECO:0000244|PDB:1VQ0}. FT STRAND 164 176 {ECO:0000244|PDB:1VQ0}. FT HELIX 182 193 {ECO:0000244|PDB:1VQ0}. FT HELIX 198 201 {ECO:0000244|PDB:1VQ0}. FT TURN 202 204 {ECO:0000244|PDB:1VQ0}. FT HELIX 207 215 {ECO:0000244|PDB:1VQ0}. FT STRAND 223 226 {ECO:0000244|PDB:1VQ0}. FT HELIX 235 243 {ECO:0000244|PDB:1VQ0}. FT HELIX 247 256 {ECO:0000244|PDB:1VQ0}. FT STRAND 259 262 {ECO:0000244|PDB:1VQ0}. FT TURN 264 266 {ECO:0000244|PDB:1VQ0}. FT STRAND 269 272 {ECO:0000244|PDB:1VQ0}. FT HELIX 274 286 {ECO:0000244|PDB:1VQ0}. SQ SEQUENCE 290 AA; 32541 MW; 22CD6658EA62692F CRC64; MIYYGTMFDH KVRFSIVRMR EVVEEARNRH ALSYLATVVL GRALIGAALV TPWLAEKERW TLDIEGNGPI RRVVAQSTSE FTVRGYVANP KVELPLNEKG KFDVAGAIGQ GVLRVVRDLG LKTPFVSQVP LVSGEIAEDL AYYFAVSEQI PSAFSIGVLV DSDGVKIAGG FAVQIIDRTL EQEKVEMIEK NIKNLPSISK LFQEAEPLDV LERIFGEKVG FVETAEIKYK CDCNREKAKN ALLVLDKKEL EDMRKEGKGE VVCKWCNTRY VFSEEELEEL LKFKVDDSGS // ID HYDE_THEMA Reviewed; 348 AA. AC Q9X0Z6; G4FE79; DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=[FeFe] hydrogenase maturase subunit HydE {ECO:0000305}; DE EC=1.8.-.- {ECO:0000305}; GN OrderedLocusNames=TM_1269 {ECO:0000312|EMBL:AAD36344.1}; GN ORFNames=THEMA_07990 {ECO:0000312|EMBL:AHD18826.1}, GN Tmari_1274 {ECO:0000312|EMBL:AGL50198.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000312|EMBL:AAD36344.1}; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000312|EMBL:AGL50198.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). RN [3] RP FUNCTION, SUBUNIT, COFACTOR, AND MUTAGENESIS OF CYS-63; CYS-67 AND RP CYS-70. RX PubMed=16137685; DOI=10.1016/j.febslet.2005.07.092; RA Rubach J.K., Brazzolotto X., Gaillard J., Fontecave M.; RT "Biochemical characterization of the HydE and HydG iron-only RT hydrogenase maturation enzymes from Thermatoga maritima."; RL FEBS Lett. 579:5055-5060(2005). RN [4] {ECO:0000244|PDB:3CIW, ECO:0000244|PDB:3CIX} RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR RP (2FE-2S); IRON-SULFUR (4FE-4S-S-ADOMET), SUBUNIT, AND COFACTOR. RX PubMed=18400755; DOI=10.1074/jbc.M801161200; RA Nicolet Y., Rubach J.K., Posewitz M.C., Amara P., Mathevon C., RA Atta M., Fontecave M., Fontecilla-Camps J.C.; RT "X-ray structure of the [FeFe]-hydrogenase maturase HydE from RT Thermotoga maritima."; RL J. Biol. Chem. 283:18861-18872(2008). RN [5] {ECO:0000244|PDB:3IIX, ECO:0000244|PDB:3IIZ} RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR RP (2FE-2S) AND IRON-SULFUR (4FE-4S-S-ADOMET), AND COFACTOR. RX PubMed=19706452; DOI=10.1073/pnas.0904385106; RA Nicolet Y., Amara P., Mouesca J.M., Fontecilla-Camps J.C.; RT "Unexpected electron transfer mechanism upon AdoMet cleavage in RT radical SAM proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 106:14867-14871(2009). RN [6] {ECO:0000244|PDB:4JXC, ECO:0000244|PDB:4JY8, ECO:0000244|PDB:4JY9} RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR RP (2FE-2S) AND IRON-SULFUR (4FE-4S-S-ADOMET), AND COFACTOR. RX PubMed=23596207; DOI=10.1073/pnas.1302388110; RA Nicolet Y., Rohac R., Martin L., Fontecilla-Camps J.C.; RT "X-ray snapshots of possible intermediates in the time course of RT synthesis and degradation of protein-bound Fe4S4 clusters."; RL Proc. Natl. Acad. Sci. U.S.A. 110:7188-7192(2013). CC -!- FUNCTION: Required for the maturation of the [FeFe]-hydrogenase CC HydA (By similarity). Catalyzes the reductive cleavage of S- CC adenosyl-L-methionine (in vitro), suggesting it may contribute to CC the biosynthesis of an essential sulfur-containing ligand that CC binds to the hydrogenase active site [2Fe-2S] cluster CC (PubMed:16137685). {ECO:0000250|UniProtKB:Q97IK9, CC ECO:0000269|PubMed:16137685, ECO:0000305}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|PIRSR:PIRSR004762-1, CC ECO:0000269|PubMed:16137685, ECO:0000269|PubMed:18400755, CC ECO:0000269|PubMed:19706452, ECO:0000269|PubMed:23596207}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|PIRSR:PIRSR004762-1, ECO:0000269|PubMed:18400755, CC ECO:0000269|PubMed:19706452, ECO:0000269|PubMed:23596207}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000269|PubMed:18400755, CC ECO:0000269|PubMed:19706452, ECO:0000269|PubMed:23596207}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:18400755, CC ECO:0000269|PubMed:19706452, ECO:0000269|PubMed:23596207}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16137685, CC ECO:0000269|PubMed:18400755}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. HydE family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36344.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50198.1; -; Genomic_DNA. DR EMBL; CP007013; AHD18826.1; -; Genomic_DNA. DR PIR; D72274; D72274. DR RefSeq; NP_229074.1; NC_000853.1. DR RefSeq; WP_004079975.1; NZ_CP011107.1. DR PDB; 3CIW; X-ray; 1.35 A; A=1-348. DR PDB; 3CIX; X-ray; 1.70 A; A=1-348. DR PDB; 3IIX; X-ray; 1.25 A; A=1-348. DR PDB; 3IIZ; X-ray; 1.62 A; A=1-348. DR PDB; 4JXC; X-ray; 1.50 A; A=1-348. DR PDB; 4JY8; X-ray; 2.90 A; A=2-348. DR PDB; 4JY9; X-ray; 1.60 A; A=1-348. DR PDB; 4JYD; X-ray; 1.71 A; A=1-348. DR PDB; 4JYE; X-ray; 1.65 A; A=1-348. DR PDB; 4JYF; X-ray; 1.45 A; A=1-348. DR PDBsum; 3CIW; -. DR PDBsum; 3CIX; -. DR PDBsum; 3IIX; -. DR PDBsum; 3IIZ; -. DR PDBsum; 4JXC; -. DR PDBsum; 4JY8; -. DR PDBsum; 4JY9; -. DR PDBsum; 4JYD; -. DR PDBsum; 4JYE; -. DR PDBsum; 4JYF; -. DR ProteinModelPortal; Q9X0Z6; -. DR SMR; Q9X0Z6; 2-347. DR STRING; 243274.TM1269; -. DR EnsemblBacteria; AAD36344; AAD36344; TM_1269. DR EnsemblBacteria; AGL50198; AGL50198; Tmari_1274. DR EnsemblBacteria; AHD18826; AHD18826; THEMA_07990. DR GeneID; 898214; -. DR KEGG; tma:TM1269; -. DR KEGG; tmi:THEMA_07990; -. DR KEGG; tmm:Tmari_1274; -. DR KEGG; tmw:THMA_1294; -. DR PATRIC; 23937478; VBITheMar51294_1285. DR eggNOG; ENOG4107QW8; Bacteria. DR eggNOG; COG0502; LUCA. DR KO; K01012; -. DR OMA; FLLRHET; -. DR OrthoDB; EOG6FJNBQ; -. DR BioCyc; TMAR243274:GC6P-1300-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro. DR GO; GO:0051188; P:cofactor biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR010722; BATS_dom. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR024021; FeFe-hyd_HydE_rSAM. DR InterPro; IPR005244; FO_synthase_su2-like. DR InterPro; IPR007197; rSAM. DR Pfam; PF06968; BATS; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004762; CHP00423; 1. DR SMART; SM00876; BATS; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR03956; rSAM_HydE; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; 4Fe-4S; Complete proteome; Iron; Iron-sulfur; KW Metal-binding; Oxidoreductase; Reference proteome; KW S-adenosyl-L-methionine. FT CHAIN 1 348 [FeFe] hydrogenase maturase subunit HydE. FT /FTId=PRO_0000433230. FT METAL 63 63 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000244|PDB:3CIW, FT ECO:0000244|PDB:3CIX, FT ECO:0000244|PDB:3IIX, FT ECO:0000255|PIRSR:PIRSR004762-1, FT ECO:0000269|PubMed:16137685, FT ECO:0000269|PubMed:18400755, FT ECO:0000269|PubMed:19706452}. FT METAL 67 67 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000244|PDB:3CIW, FT ECO:0000244|PDB:3CIX, FT ECO:0000244|PDB:3IIX, FT ECO:0000255|PIRSR:PIRSR004762-1, FT ECO:0000269|PubMed:16137685}. FT METAL 70 70 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000244|PDB:3CIW, FT ECO:0000244|PDB:3CIX, FT ECO:0000244|PDB:3IIX, FT ECO:0000255|PIRSR:PIRSR004762-1, FT ECO:0000269|PubMed:16137685}. FT METAL 311 311 Iron-sulfur (2Fe-2S). FT {ECO:0000244|PDB:3CIX, FT ECO:0000244|PDB:3IIZ, FT ECO:0000244|PDB:4JXC, FT ECO:0000244|PDB:4JY8, FT ECO:0000244|PDB:4JY9, FT ECO:0000244|PDB:4JYE}. FT METAL 319 319 Iron-sulfur (2Fe-2S). FT {ECO:0000244|PDB:3CIX, FT ECO:0000244|PDB:4JY8, FT ECO:0000244|PDB:4JY9, FT ECO:0000244|PDB:4JYE}. FT METAL 322 322 Iron-sulfur (2Fe-2S). FT {ECO:0000244|PDB:3CIX, FT ECO:0000244|PDB:4JY8, FT ECO:0000244|PDB:4JY9, FT ECO:0000244|PDB:4JYE}. FT MUTAGEN 63 63 C->A: Eliminates binding of one iron- FT sulfur cluster; when associated with A-67 FT and A-70. {ECO:0000269|PubMed:16137685}. FT MUTAGEN 67 67 C->A: Eliminates binding of one iron- FT sulfur cluster; when associated with A-63 FT and A-70. {ECO:0000269|PubMed:16137685}. FT MUTAGEN 70 70 C->A: Eliminates binding of one iron- FT sulfur cluster; when associated with A-63 FT and A-67. {ECO:0000269|PubMed:16137685}. FT HELIX 3 11 {ECO:0000244|PDB:3IIX}. FT HELIX 17 25 {ECO:0000244|PDB:3IIX}. FT HELIX 29 47 {ECO:0000244|PDB:3IIX}. FT STRAND 49 60 {ECO:0000244|PDB:3IIX}. FT HELIX 86 98 {ECO:0000244|PDB:3IIX}. FT STRAND 102 109 {ECO:0000244|PDB:3IIX}. FT HELIX 112 114 {ECO:0000244|PDB:3IIX}. FT HELIX 117 127 {ECO:0000244|PDB:3IIX}. FT TURN 128 130 {ECO:0000244|PDB:3CIW}. FT STRAND 132 136 {ECO:0000244|PDB:3IIX}. FT HELIX 142 151 {ECO:0000244|PDB:3IIX}. FT STRAND 155 157 {ECO:0000244|PDB:3IIX}. FT HELIX 165 171 {ECO:0000244|PDB:3IIX}. FT HELIX 177 189 {ECO:0000244|PDB:3IIX}. FT STRAND 193 196 {ECO:0000244|PDB:3IIX}. FT STRAND 198 201 {ECO:0000244|PDB:3IIX}. FT HELIX 207 220 {ECO:0000244|PDB:3IIX}. FT STRAND 223 225 {ECO:0000244|PDB:3IIX}. FT TURN 237 240 {ECO:0000244|PDB:3IIX}. FT HELIX 246 259 {ECO:0000244|PDB:3IIX}. FT HELIX 269 274 {ECO:0000244|PDB:3IIX}. FT HELIX 278 283 {ECO:0000244|PDB:3IIX}. FT TURN 284 286 {ECO:0000244|PDB:3IIX}. FT TURN 297 299 {ECO:0000244|PDB:3IIX}. FT HELIX 300 302 {ECO:0000244|PDB:3IIX}. FT STRAND 305 307 {ECO:0000244|PDB:3IIX}. FT TURN 310 313 {ECO:0000244|PDB:3IIX}. FT HELIX 319 329 {ECO:0000244|PDB:3IIX}. SQ SEQUENCE 348 AA; 39799 MW; 472505213FF63799 CRC64; MTGREILEKL ERREFTREVL KEALSINDRG FNEALFKLAD EIRRKYVGDE VHIRAIIEFS NVCRKNCLYC GLRRDNKNLK RYRMTPEEIV ERARLAVQFG AKTIVLQSGE DPYYMPDVIS DIVKEIKKMG VAVTLSLGEW PREYYEKWKE AGADRYLLRH ETANPVLHRK LRPDTSFENR LNCLLTLKEL GYETGAGSMV GLPGQTIDDL VDDLLFLKEH DFDMVGIGPF IPHPDTPLAN EKKGDFTLTL KMVALTRILL PDSNIPATTA MGTIVPGGRE ITLRCGANVI MPNWTPSPYR QLYQLYPGKI CVFEKDTACI PCVMKMIELL GRKPGRDWGG RKRVFETV // ID HSLU_THEMA Reviewed; 463 AA. AC Q9WYZ2; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 117. DE RecName: Full=ATP-dependent protease ATPase subunit HslU; DE AltName: Full=Unfoldase HslU; GN Name=hslU; OrderedLocusNames=TM_0522; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12646382; DOI=10.1016/S0301-4622(02)00297-1; RA Song H.K., Bochtler M., Azim M.K., Hartmann C., Huber R., RA Ramachandran R.; RT "Isolation and characterization of the prokaryotic proteasome homolog RT HslVU (ClpQY) from Thermotoga maritima and the crystal structure of RT HslV."; RL Biophys. Chem. 100:437-452(2003). CC -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex; CC this subunit has chaperone activity. The binding of ATP and its CC subsequent hydrolysis by HslU are essential for unfolding of CC protein substrates subsequently hydrolyzed by HslV. HslU CC recognizes the N-terminal part of its protein substrates and CC unfolds these before they are guided to HslV for hydrolysis. CC {ECO:0000269|PubMed:12646382}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 75 degrees Celsius. CC {ECO:0000269|PubMed:12646382}; CC -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on CC each side by a ring-shaped HslU homohexamer. The assembly of the CC HslU/HslV complex is dependent on binding of ATP (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35607.1; -; Genomic_DNA. DR PIR; H72365; H72365. DR RefSeq; NP_228332.1; NC_000853.1. DR RefSeq; WP_004081401.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYZ2; -. DR SMR; Q9WYZ2; 6-463. DR STRING; 243274.TM0522; -. DR EnsemblBacteria; AAD35607; AAD35607; TM_0522. DR GeneID; 897573; -. DR KEGG; tma:TM0522; -. DR PATRIC; 23935949; VBITheMar51294_0529. DR eggNOG; ENOG4105C4N; Bacteria. DR eggNOG; COG1220; LUCA. DR InParanoid; Q9WYZ2; -. DR KO; K03667; -. DR OMA; RLHTTIE; -. DR OrthoDB; EOG6NPM7G; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070011; F:peptidase activity, acting on L-amino acid peptides; IEA:InterPro. DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00249; HslU; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004491; HslU. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11262:SF3; PTHR11262:SF3; 2. DR Pfam; PF00004; AAA; 1. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF10431; ClpB_D2-small; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM01086; ClpB_D2-small; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00390; hslU; 1. PE 1: Evidence at protein level; KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 463 ATP-dependent protease ATPase subunit FT HslU. FT /FTId=PRO_0000160555. FT NP_BIND 63 68 ATP. {ECO:0000250}. FT BINDING 21 21 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT BINDING 276 276 ATP. {ECO:0000250}. FT BINDING 341 341 ATP. {ECO:0000250}. FT BINDING 413 413 ATP. {ECO:0000250}. SQ SEQUENCE 463 AA; 53052 MW; F871CD909FCBA5CA CRC64; MKSFDEMTPK EIVQELDKYI VGQYEAKKAV AIAVRNRIRR QKLPEEWRKE VLPKNILMIG PTGVGKTEIA RRLAQLSGSP FLKVEATRFT EVGYVGKNVD SMIRDLVEIS VNMVKQEKIK EVERQAEELV EERILDALVP ESKAMPVVTN PFINLITGGQ QQQYTPEDRR RFRAKREEMR EKLRKGELED EEIEIELEET VSPFMGIFGP GMEDLGIEIT NMFSGMLPKR KKKRKMKVSE ARKVLLPLEA EKLIDMDKVV QEALDRAQNR GIIFIDEIDK IAGKESAVGP DVSRQGVQRD LLPIVEGTTI MTKYGPVRTD FILFIAAGAF HVSRPSDLIP ELQGRFPIRV ELSPLTEEDF VRILKEPENA IIKQYQALLS TEGVELVFTE DGIREMARIA YQLNQRLENI GARRLYTVAE KVLEEISFEA PDIPEKRVVV DAEYVRRRLE KIVQDEDLSA YIL // ID HSLV_THEMA Reviewed; 176 AA. AC Q9WYZ1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=ATP-dependent protease subunit HslV; DE EC=3.4.25.2; DE Flags: Precursor; GN Name=hslV; OrderedLocusNames=TM_0521; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 6-176 IN COMPLEX WITH SODIUM, RP FUNCTION, PROPEPTIDE, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=12646382; DOI=10.1016/S0301-4622(02)00297-1; RA Song H.K., Bochtler M., Azim M.K., Hartmann C., Huber R., RA Ramachandran R.; RT "Isolation and characterization of the prokaryotic proteasome homolog RT HslVU (ClpQY) from Thermotoga maritima and the crystal structure of RT HslV."; RL Biophys. Chem. 100:437-452(2003). CC -!- FUNCTION: Protease subunit of a proteasome-like degradation CC complex believed to be a general protein degrading machinery. CC {ECO:0000269|PubMed:12646382}. CC -!- CATALYTIC ACTIVITY: ATP-dependent cleavage of peptide bonds with CC broad specificity. {ECO:0000269|PubMed:12646382}. CC -!- ENZYME REGULATION: Allosterically activated by HslU binding. CC {ECO:0000250}. CC -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on CC each side by a ring-shaped HslU homohexamer. The assembly of the CC HslU/HslV complex is dependent on binding of ATP. CC {ECO:0000269|PubMed:12646382}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: According to PubMed:12646382 the propeptide is CC autoprocessed in 20% of the cases in the expression system CC (E.coli). CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35606.1; -; Genomic_DNA. DR PIR; G72365; G72365. DR RefSeq; NP_228331.1; NC_000853.1. DR RefSeq; WP_004081403.1; NZ_CP011107.1. DR PDB; 1M4Y; X-ray; 2.10 A; A/B/C=6-176. DR PDBsum; 1M4Y; -. DR ProteinModelPortal; Q9WYZ1; -. DR SMR; Q9WYZ1; 6-176. DR STRING; 243274.TM0521; -. DR MEROPS; T01.006; -. DR EnsemblBacteria; AAD35606; AAD35606; TM_0521. DR GeneID; 897572; -. DR KEGG; tma:TM0521; -. DR PATRIC; 23935947; VBITheMar51294_0528. DR eggNOG; ENOG4108R5P; Bacteria. DR eggNOG; COG5405; LUCA. DR InParanoid; Q9WYZ1; -. DR KO; K01419; -. DR OMA; IMKGNAR; -. DR OrthoDB; EOG6ND0PJ; -. DR EvolutionaryTrace; Q9WYZ1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:InterPro. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_00248; HslV; 1. DR InterPro; IPR022281; ATP-dep_Prtase_HsIV_su. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR Pfam; PF00227; Proteasome; 1. DR PIRSF; PIRSF039093; HslV; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR03692; ATP_dep_HslV; 1. DR PROSITE; PS51476; PROTEASOME_BETA_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Complete proteome; Cytoplasm; KW Hydrolase; Metal-binding; Protease; Reference proteome; Sodium; KW Threonine protease. FT PROPEP 1 5 Removed in mature form. {ECO:0000305}. FT /FTId=PRO_0000395618. FT CHAIN 6 176 ATP-dependent protease subunit HslV. FT /FTId=PRO_0000148154. FT ACT_SITE 6 6 {ECO:0000250}. FT METAL 161 161 Sodium; via carbonyl oxygen. FT {ECO:0000269|PubMed:12646382}. FT METAL 164 164 Sodium; via carbonyl oxygen. FT {ECO:0000269|PubMed:12646382}. FT METAL 167 167 Sodium; via carbonyl oxygen. FT {ECO:0000269|PubMed:12646382}. FT STRAND 8 13 {ECO:0000244|PDB:1M4Y}. FT STRAND 16 21 {ECO:0000244|PDB:1M4Y}. FT STRAND 25 27 {ECO:0000244|PDB:1M4Y}. FT STRAND 30 34 {ECO:0000244|PDB:1M4Y}. FT STRAND 39 42 {ECO:0000244|PDB:1M4Y}. FT TURN 43 46 {ECO:0000244|PDB:1M4Y}. FT STRAND 47 53 {ECO:0000244|PDB:1M4Y}. FT HELIX 55 71 {ECO:0000244|PDB:1M4Y}. FT TURN 72 74 {ECO:0000244|PDB:1M4Y}. FT HELIX 76 89 {ECO:0000244|PDB:1M4Y}. FT HELIX 93 95 {ECO:0000244|PDB:1M4Y}. FT STRAND 99 103 {ECO:0000244|PDB:1M4Y}. FT STRAND 108 111 {ECO:0000244|PDB:1M4Y}. FT STRAND 121 128 {ECO:0000244|PDB:1M4Y}. FT HELIX 131 144 {ECO:0000244|PDB:1M4Y}. FT HELIX 149 163 {ECO:0000244|PDB:1M4Y}. FT STRAND 172 175 {ECO:0000244|PDB:1M4Y}. SQ SEQUENCE 176 AA; 18933 MW; ECE369602A0ABD02 CRC64; MKFHGTTILV VRRNGQTVMG GDGQVTFGST VLKGNARKVR KLGEGKVLAG FAGSVADAMT LFDRFEAKLR EWGGNLTKAA VELAKDWRTD RVLRRLEALL LVADKENIFI ISGNGEVIQP DDDAAAIGSG GPYALAAAKA LLRNTDLSAR EIVEKAMTIA GEICIYTNQN IVIEEV // ID IF3_THEMA Reviewed; 172 AA. AC Q9X1S6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 98. DE RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080}; GN Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; GN OrderedLocusNames=TM_1590; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: IF-3 binds to the 30S ribosomal subunit and shifts the CC equilibrum between 70S ribosomes and their 50S and 30S subunits in CC favor of the free subunits, thus enhancing the availability of 30S CC subunits on which protein synthesis initiation begins. CC {ECO:0000255|HAMAP-Rule:MF_00080}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00080}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00080}. CC -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000255|HAMAP- CC Rule:MF_00080}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD36657.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36657.1; ALT_INIT; Genomic_DNA. DR PIR; B72233; B72233. DR RefSeq; NP_229390.1; NC_000853.1. DR RefSeq; WP_004082027.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1S6; -. DR SMR; Q9X1S6; 8-82. DR STRING; 243274.TM1590; -. DR EnsemblBacteria; AAD36657; AAD36657; TM_1590. DR GeneID; 897946; -. DR KEGG; tma:TM1590; -. DR PATRIC; 23938154; VBITheMar51294_1609. DR eggNOG; ENOG4108UUX; Bacteria. DR eggNOG; COG0290; LUCA. DR InParanoid; Q9X1S6; -. DR KO; K02520; -. DR OMA; HDFNVKV; -. DR OrthoDB; EOG63JRGJ; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.20.80; -; 1. DR Gene3D; 3.30.110.10; -; 1. DR HAMAP; MF_00080; IF_3; 1. DR InterPro; IPR019813; Translation_initiation_fac3_CS. DR InterPro; IPR001288; Translation_initiation_fac_3. DR InterPro; IPR019815; Translation_initiation_fac_3_C. DR InterPro; IPR019814; Translation_initiation_fac_3_N. DR PANTHER; PTHR10938; PTHR10938; 1. DR Pfam; PF00707; IF3_C; 1. DR Pfam; PF05198; IF3_N; 1. DR SUPFAM; SSF54364; SSF54364; 1. DR SUPFAM; SSF55200; SSF55200; 1. DR TIGRFAMs; TIGR00168; infC; 1. DR PROSITE; PS00938; IF3; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Initiation factor; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 172 Translation initiation factor IF-3. FT /FTId=PRO_0000177597. SQ SEQUENCE 172 AA; 20047 MW; C14AFE51DD03C7EF CRC64; MGIGVNTDLP RNEQIKAPKV RVVDENGKMI GVMPTRKALE LAREKGLDLV LVAPNENPPV ARIMDYGKYK YQLTKKQKEN KKKPVQMKQM KFRLKIDEHD YQTKVKHIRR FLEDGHKVRV VVMFIGREMM FAEKGKEILE RVIKDTEDLA TVESPPKMEG RDMWMVLKPK NS // ID IF2_THEMA Reviewed; 690 AA. AC Q9WZN3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 117. DE RecName: Full=Translation initiation factor IF-2; GN Name=infB; OrderedLocusNames=TM_0775; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: One of the essential components for the initiation of CC protein synthesis. Protects formylmethionyl-tRNA from spontaneous CC hydrolysis and promotes its binding to the 30S ribosomal subunits. CC Also involved in the hydrolysis of GTP during the formation of the CC 70S ribosomal complex (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. IF-2 CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35857.1; -; Genomic_DNA. DR PIR; E72337; E72337. DR RefSeq; NP_228584.1; NC_000853.1. DR RefSeq; WP_004080913.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZN3; -. DR STRING; 243274.TM0775; -. DR EnsemblBacteria; AAD35857; AAD35857; TM_0775. DR GeneID; 898443; -. DR KEGG; tma:TM0775; -. DR PATRIC; 23936472; VBITheMar51294_0788. DR eggNOG; ENOG4107QHU; Bacteria. DR eggNOG; COG0532; LUCA. DR InParanoid; Q9WZN3; -. DR KO; K02519; -. DR OMA; MGLKADP; -. DR OrthoDB; EOG67HJSV; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.10050; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00100_B; IF_2_B; 1. DR InterPro; IPR006847; IF2_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR000178; TF_IF2_bacterial-like. DR InterPro; IPR023115; TIF_IF2_dom3. DR InterPro; IPR009000; Transl_B-barrel. DR Pfam; PF11987; IF-2; 1. DR Pfam; PF04760; IF2_N; 1. DR SUPFAM; SSF50447; SSF50447; 2. DR SUPFAM; SSF52156; SSF52156; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00487; IF-2; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Initiation factor; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 690 Translation initiation factor IF-2. FT /FTId=PRO_0000137272. FT DOMAIN 178 346 tr-type G. FT NP_BIND 187 194 GTP. {ECO:0000250}. FT NP_BIND 233 237 GTP. {ECO:0000250}. FT NP_BIND 287 290 GTP. {ECO:0000250}. FT REGION 187 194 G1. {ECO:0000250}. FT REGION 212 216 G2. {ECO:0000250}. FT REGION 233 236 G3. {ECO:0000250}. FT REGION 287 290 G4. {ECO:0000250}. FT REGION 324 326 G5. {ECO:0000250}. FT COMPBIAS 79 84 Poly-Lys. SQ SEQUENCE 690 AA; 77774 MW; 8673FFFA20C37B60 CRC64; MARLRVYELA RKLNMSPKEL LQELEELGVN VKSHMSYVDE EMANIIIDLL EEDNRKAKQP SKPKKEKGEE EVEKEVVEKK KKKKITLKPD ELKLDIIAEK IGVPQNKIIQ DMFVKRGIAL RPGQILKLEE VEQILKEYKI EIEIEEEQQT SVEEVDEFEL LEKRYQELYE KEKDKLVPRP PVVTVMGHVD HGKTTLLDRI RSTRVAEREE GGITQSIGAY QVEVNGKKIT FIDTPGHELF TEMRARGAQA TDIVVLVVAA DDGVMPQTIE AYNHAKAANV PIIVAINKID KPNANVEKTK QELVEKLGLI PEEWGGDTIV VPISARTGQG VDELLEMILL VAEMNEIKCY PEGPARAVII ESKLDKKMGP VASAIVKDGV LKVGDAVVAS NTYGRVRNLF DDNMRPIREA YPSQPVMILG FEDVPDVHSN VYVVESAEKA KEIVEKRLQR LEAQKQSRKH INLEELMKMM QEKEKKVLNL ILKADTYGSV AALKNAINKL QSKEIELNIV HAGVGEISTS DVMLAAAVDG VILGFRVKVN NQARRLAEQE GVDVRTYSII YKLVEDLKLA LEGMLEPEEV EEVIGHGEIR KVFKISKVGK VAGVQMLDGK ADRNGFVRIY RNGQLVFGGK IESLKHYKED VSVVEAPQEC GIKFAGFDDI HEGDELEFYV IRKVKRKPTF VEEQADQEQK // ID IF1_THEMA Reviewed; 74 AA. AC P56866; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075}; GN Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; GN OrderedLocusNames=TM_1477; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: One of the essential components for the initiation of CC protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the CC 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently CC binds. Helps modulate mRNA selection, yielding the 30S pre- CC initiation complex (PIC). Upon addition of the 50S ribosomal CC subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S CC translation initation complex. {ECO:0000255|HAMAP-Rule:MF_00075}. CC -!- SUBUNIT: Component of the 30S ribosomal translation pre-initiation CC complex which assembles on the 30S ribosome in the order IF-2 and CC IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can CC occur at any time during PIC assembly. {ECO:0000255|HAMAP- CC Rule:MF_00075}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00075}. CC -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000255|HAMAP- CC Rule:MF_00075}. CC -!- SIMILARITY: Contains 1 S1-like domain. {ECO:0000255|HAMAP- CC Rule:MF_00075}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_229277.1; NC_000853.1. DR RefSeq; WP_010865349.1; NC_000853.1. DR STRING; 243274.TM1477; -. DR GeneID; 897590; -. DR KEGG; tma:TM1477; -. DR eggNOG; ENOG4105K9U; Bacteria. DR eggNOG; COG0361; LUCA. DR InParanoid; P56866; -. DR KO; K02518; -. DR OMA; KGRIIWR; -. DR OrthoDB; EOG6384SC; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00075; IF_1; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR006196; RNA-binding_domain_S1_IF1. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR004368; TIF_IF1. DR Pfam; PF01176; eIF-1a; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00008; infA; 1. DR PROSITE; PS50832; S1_IF1_TYPE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Initiation factor; Protein biosynthesis; KW Reference proteome; RNA-binding; rRNA-binding. FT CHAIN 1 74 Translation initiation factor IF-1. FT /FTId=PRO_0000095891. FT DOMAIN 1 72 S1-like. {ECO:0000255|HAMAP- FT Rule:MF_00075}. SQ SEQUENCE 74 AA; 8589 MW; A9E7FD07C8F45610 CRC64; MGKEDVIRME GTIIEALPNA MFRVELDNGH KVLAHVSXRM RKNFIRLVPG DRVIVELSVY DLTRGRIVYR KKPE // ID ILVD_THEMA Reviewed; 554 AA. AC Q9WZ21; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 111. DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0000255|HAMAP-Rule:MF_00012}; DE Short=DAD {ECO:0000255|HAMAP-Rule:MF_00012}; DE EC=4.2.1.9 {ECO:0000255|HAMAP-Rule:MF_00012}; GN Name=ilvD {ECO:0000255|HAMAP-Rule:MF_00012}; GN OrderedLocusNames=TM_0551; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2- CC oxobutanoate + H(2)O. {ECO:0000255|HAMAP-Rule:MF_00012}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00012}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP- CC Rule:MF_00012}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012}. CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP- CC Rule:MF_00012}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35636.1; -; Genomic_DNA. DR PIR; E72362; E72362. DR RefSeq; NP_228361.1; NC_000853.1. DR RefSeq; WP_004081337.1; NZ_CP011107.1. DR STRING; 243274.TM0551; -. DR EnsemblBacteria; AAD35636; AAD35636; TM_0551. DR GeneID; 897608; -. DR KEGG; tma:TM0551; -. DR PATRIC; 23936009; VBITheMar51294_0559. DR eggNOG; ENOG4105C01; Bacteria. DR eggNOG; COG0129; LUCA. DR InParanoid; Q9WZ21; -. DR KO; K01687; -. DR OMA; QGRNMAG; -. DR OrthoDB; EOG6MSS24; -. DR UniPathway; UPA00047; UER00057. DR UniPathway; UPA00049; UER00061. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IBA:GO_Central. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00012; IlvD; 1. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR004404; DihydroxyA_deHydtase. DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase. DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS. DR PANTHER; PTHR21000; PTHR21000; 1. DR Pfam; PF00920; ILVD_EDD; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR TIGRFAMs; TIGR00110; ilvD; 1. DR PROSITE; PS00886; ILVD_EDD_1; 1. DR PROSITE; PS00887; ILVD_EDD_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Lyase; Metal-binding; Reference proteome. FT CHAIN 1 554 Dihydroxy-acid dehydratase. FT /FTId=PRO_0000103521. FT METAL 119 119 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00012}. FT METAL 191 191 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00012}. SQ SEQUENCE 554 AA; 59781 MW; FD50487294FC355B CRC64; MRSDVIKKGL ERVPHRSLLK ALGITDDEMR RPFIGIVSSW NEIIPGHVHL DKVVEAVKAG VRMAGGVPFV FPTIGICDGI AMDHRGMKFS LPSRELIADS IEIVASGFPF DGLVFVPNCD KITPGMMMAM GRLNIPSVLI SGGPMLAGRY NGRDIDLITV FEAVGGYKVG KVDEETLKAI EDLACPGAGS CAGLFTANTM NSLAEALGIA PRGNGTVPAV HAKRLRMAKE AGMLVVELVK RDVKPRDIVT LDSFMNAVMV DLATGGSTNT VLHLKAIAES FGIDFDIKLF DELSRKIPHI CNISPVGPYH IQDLDDAGGI YAVMKRLQEN GLLKEDVMTI YLRKIGDLVR EAKILNEDVI RPFDNPYHKE GGLGILFGNL APEGAVAKLS GVPEKMMHHV GPAVVFEDGE EATKAILSGK IKKGDVVVIR YEGPKGGPGM REMLSPTSAI VGMGLAEDVA LITDGRFSGG SHGAVIGHVS PEAAEGGPIG IVKDGDLIEI DFEKRTLNLL ISDEEFERRM KEFTPLVKEV DSDYLRRYAF FVQSASKGAI FRKP // ID ISCU_THEMA Reviewed; 142 AA. AC Q9X192; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU; DE AltName: Full=Sulfur acceptor protein IscU; GN Name=iscU; Synonyms=nifU; OrderedLocusNames=TM_1372; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: A scaffold on which IscS assembles Fe-S clusters. CC Subsequently gives the nascent cluster to other proteins. It is CC likely that Fe-S cluster coordination is flexible as the role of CC this complex is to build and then hand off Fe-S clusters (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Forms a heterotetramer with IscS; each subunit of the CC IscS dimer contacts an IscU monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36442.1; -; Genomic_DNA. DR PIR; E72260; E72260. DR RefSeq; NP_229173.1; NC_000853.1. DR RefSeq; WP_010865327.1; NC_000853.1. DR ProteinModelPortal; Q9X192; -. DR STRING; 243274.TM1372; -. DR EnsemblBacteria; AAD36442; AAD36442; TM_1372. DR GeneID; 898107; -. DR KEGG; tma:TM1372; -. DR KEGG; tmi:THEMA_07475; -. DR PATRIC; 23937684; VBITheMar51294_1384. DR eggNOG; ENOG4107YH3; Bacteria. DR eggNOG; COG0822; LUCA. DR InParanoid; Q9X192; -. DR KO; K04488; -. DR OMA; NKFPARI; -. DR OrthoDB; EOG6GFGQT; -. DR BioCyc; TMAR243274:GC6P-1406-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central. DR GO; GO:0036455; F:iron-sulfur transferase activity; IBA:GO_Central. DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IBA:GO_Central. DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central. DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central. DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N. DR Pfam; PF01592; NifU_N; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 142 Iron-sulfur cluster assembly scaffold FT protein IscU. FT /FTId=PRO_0000166190. SQ SEQUENCE 142 AA; 16071 MW; FC2935B469D2CCBE CRC64; MVFKMMYSEA ILDYANSKKF RGKLDDATVI EEGKNISCGD EITLYLKVED GVVKDAKFEG MGCVISQASA SLMLERIIGE RVEEIFSLIE EAEKMSRGEN FDEGKLKNVT LMSDIKNYPA RVKCFILAWK TLKEALKKIS RP // ID ISPG_THEMA Reviewed; 344 AA. AC Q9WZZ3; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) {ECO:0000255|HAMAP-Rule:MF_00159}; DE EC=1.17.7.3 {ECO:0000255|HAMAP-Rule:MF_00159}; DE AltName: Full=1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00159}; GN Name=ispG {ECO:0000255|HAMAP-Rule:MF_00159}; GN OrderedLocusNames=TM_0891; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate CC (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_00159}. CC -!- CATALYTIC ACTIVITY: (E)-4-hydroxy-3-methylbut-2-en-1-yl CC diphosphate + H(2)O + oxidized flavodoxin = 2-C-methyl-D- CC erythritol 2,4-cyclodiphosphate + reduced flavodoxin. CC {ECO:0000255|HAMAP-Rule:MF_00159}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00159}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00159}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 5/6. {ECO:0000255|HAMAP- CC Rule:MF_00159}. CC -!- SIMILARITY: Belongs to the IspG family. {ECO:0000255|HAMAP- CC Rule:MF_00159}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35972.1; -; Genomic_DNA. DR PIR; D72321; D72321. DR RefSeq; NP_228699.1; NC_000853.1. DR RefSeq; WP_004080695.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZZ3; -. DR STRING; 243274.TM0891; -. DR EnsemblBacteria; AAD35972; AAD35972; TM_0891. DR GeneID; 898565; -. DR KEGG; tma:TM0891; -. DR PATRIC; 23936713; VBITheMar51294_0905. DR eggNOG; ENOG4105C4E; Bacteria. DR eggNOG; COG0821; LUCA. DR InParanoid; Q9WZZ3; -. DR KO; K03526; -. DR OMA; HNGMKIA; -. DR OrthoDB; EOG67Q96Z; -. DR UniPathway; UPA00056; UER00096. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046429; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IBA:GO_Central. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00159; IspG; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR016425; IspG_bac. DR InterPro; IPR004588; IspG_bac-typ. DR Pfam; PF04551; GcpE; 1. DR PIRSF; PIRSF004640; IspG; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR TIGRFAMs; TIGR00612; ispG_gcpE; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Isoprene biosynthesis; KW Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1 344 4-hydroxy-3-methylbut-2-en-1-yl FT diphosphate synthase (flavodoxin). FT /FTId=PRO_0000190642. FT METAL 253 253 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. FT METAL 256 256 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. FT METAL 288 288 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. FT METAL 295 295 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. SQ SEQUENCE 344 AA; 37760 MW; 3F0871F1BB065694 CRC64; MRKSVKVGKV VIGGEAPVSV QSMTTTKTAD VEKTVSQIKS LERAGCEIVR VAVQDEEDAK AIRRIKEQIE IPLVADIQFD YRLAILSIEN GADKIRINPG NMSRDRLKDV VAAAKGKGIP IRVGANVGSI KRRTSERWKD LAESALEEVR LLEKEGFYDI IVSVKSSDVL ETIKANEYIA EKVEYPIHLG VTEAGVSETA IVKSSIAIGH LLLKNIGDTI RVSISGDPVR EVIVGKKILI ALGLREGVEV IACPTCGRAE IDVENMAKMI EENFFHVQKR LKIAVMGCVV NGIGEGKDAD LGVAGLRDGA VIFVKGEIKE RVSKEFVLER LKYYLNELLE EVER // ID ISPH_THEMA Reviewed; 275 AA. AC Q9X1F7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000255|HAMAP-Rule:MF_00191}; DE EC=1.17.7.4 {ECO:0000255|HAMAP-Rule:MF_00191}; GN Name=ispH {ECO:0000255|HAMAP-Rule:MF_00191}; Synonyms=lytB; GN OrderedLocusNames=TM_1444; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate CC into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate CC (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + 2 oxidized CC ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3- CC methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron- CC sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + 2 oxidized CC ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3- CC methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron- CC sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00191}; CC Note=Binds 1 [3Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00191}; CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate CC biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3- CC methylbutenyl diphosphate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 6/6. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36513.1; -; Genomic_DNA. DR PIR; A72253; A72253. DR RefSeq; NP_229243.1; NC_000853.1. DR RefSeq; WP_004081718.1; NZ_CP011107.1. DR STRING; 243274.TM1444; -. DR DNASU; 898031; -. DR EnsemblBacteria; AAD36513; AAD36513; TM_1444. DR GeneID; 898031; -. DR KEGG; tma:TM1444; -. DR PATRIC; 23937838; VBITheMar51294_1457. DR eggNOG; ENOG4105C48; Bacteria. DR eggNOG; COG0761; LUCA. DR InParanoid; Q9X1F7; -. DR KO; K03527; -. DR OMA; QGPDTRD; -. DR OrthoDB; EOG6HF624; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-HAMAP. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00191; IspH; 1. DR InterPro; IPR003451; LytB/IspH. DR Pfam; PF02401; LYTB; 1. DR TIGRFAMs; TIGR00216; ispH_lytB; 1. PE 3: Inferred from homology; KW 3Fe-4S; Complete proteome; Iron; Iron-sulfur; Isoprene biosynthesis; KW Metal-binding; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 275 4-hydroxy-3-methylbut-2-enyl diphosphate FT reductase. FT /FTId=PRO_0000128881. FT REGION 209 211 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 12 12 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 92 92 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 181 181 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 40 40 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 70 70 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 119 119 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 151 151 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 251 251 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. SQ SEQUENCE 275 AA; 30921 MW; FAE3A7810E98495A CRC64; MKIVVAKNIG FCFGVERAIR TVEELLDEGK KVVTDGEIVH NKQVMEQLTK KGLKVSSEMT DGEVFVVRAH GIPKDRLEEL KKIFPEVVDL TCPIVSQLFK TAQRYAKERK VIVFGKEDHP EMVALRGYAP AIVTKVPFKL EEKKVVFLSQ TTSSLEEYKE FVAAMIRMNE FEEAVFLNTI CPVTVNRERE VEELSKICDL SIVVGGKHSS NTGKLFRIAS KHSKTIWIES PDELPADVVK YGTVCVFSGT STPNSLIENV VRKLKEMEGK RDGTI // ID ILVC_THEMA Reviewed; 336 AA. AC Q9WZ20; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 113. DE RecName: Full=Ketol-acid reductoisomerase; DE EC=1.1.1.86; DE AltName: Full=Acetohydroxy-acid isomeroreductase; DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase; GN Name=ilvC; OrderedLocusNames=TM_0550; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) CC = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. CC -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + CC NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 2/4. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35635.1; -; Genomic_DNA. DR PIR; D72362; D72362. DR RefSeq; NP_228360.1; NC_000853.1. DR RefSeq; WP_004081338.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ20; -. DR SMR; Q9WZ20; 3-328. DR STRING; 243274.TM0550; -. DR EnsemblBacteria; AAD35635; AAD35635; TM_0550. DR GeneID; 897607; -. DR KEGG; tma:TM0550; -. DR PATRIC; 23936007; VBITheMar51294_0558. DR eggNOG; ENOG4105C6M; Bacteria. DR eggNOG; COG0059; LUCA. DR InParanoid; Q9WZ20; -. DR KO; K00053; -. DR OMA; EPNIKQG; -. DR OrthoDB; EOG625K07; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1040.10; -; 1. DR HAMAP; MF_00435; IlvC; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR000506; AcH_isomrdctse_C. DR InterPro; IPR013116; IlvN. DR InterPro; IPR013023; Ketol-acid_reductoisomrdctse. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR21371; PTHR21371; 1. DR Pfam; PF01450; IlvC; 1. DR Pfam; PF07991; IlvN; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00465; ilvC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 336 Ketol-acid reductoisomerase. FT /FTId=PRO_0000151373. FT ACT_SITE 108 108 {ECO:0000255}. SQ SEQUENCE 336 AA; 38047 MW; F4ED4C853BAE536E CRC64; MAVIYYDKDA DLNLIKDKKI AIIGYGSQGH AHALNLKDSG LNVVVGLREG SKSWKKAEEQ GLTVKTIEEA AKEADIIMIL IPDEHQPEIY KKYIEKHLTE GKMLMFAHGF NIHYHQIIPP KNVDVTMIAP KSPGHIVRRE YVEGRGVPAL VAVYQDYTGK AKDIALAYAK GIGVTRAGVI ETTFKEETET DLFGEQAVLC GGVTALIKAG FETLVDAGYQ PEIAYFECLN ELKLIVDLIY EGGLSFMRYS VSNTAEYGDY ISQEKIVTKE VRENMKQMLK DIQTGKFAKD WILENQAGRP YFYTMRKKES EHLIEKVGKE LRKMMPWLKE RNVDEE // ID ILVE_THEMA Reviewed; 273 AA. AC P74921; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 116. DE RecName: Full=Probable branched-chain-amino-acid aminotransferase; DE Short=BCAT; DE EC=2.6.1.42; GN Name=ilvE; OrderedLocusNames=TM_0831; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-273. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8863738; DOI=10.1016/0378-1119(96)00508-2; RA Guipaud O., Labedan B., Forterre P.; RT "A gyrB-like gene from the hyperthermophilic bacterion Thermotoga RT maritima."; RL Gene 174:121-128(1996). CC -!- FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-leucine + 2-oxoglutarate = 4-methyl-2- CC oxopentanoate + L-glutamate. CC -!- CATALYTIC ACTIVITY: L-isoleucine + 2-oxoglutarate = (S)-3-methyl- CC 2-oxopentanoate + L-glutamate. CC -!- CATALYTIC ACTIVITY: L-valine + 2-oxoglutarate = 3-methyl-2- CC oxobutanoate + L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 4/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 4/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 4/4. CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35913.1; -; Genomic_DNA. DR EMBL; U49692; AAC44497.1; -; Genomic_DNA. DR PIR; C72328; C72328. DR RefSeq; NP_228640.1; NC_000853.1. DR RefSeq; WP_004080810.1; NZ_CP011107.1. DR PDB; 3CSW; X-ray; 2.15 A; A/B/C/D=2-273. DR PDBsum; 3CSW; -. DR ProteinModelPortal; P74921; -. DR SMR; P74921; 1-273. DR STRING; 243274.TM0831; -. DR EnsemblBacteria; AAD35913; AAD35913; TM_0831. DR GeneID; 898501; -. DR KEGG; tma:TM0831; -. DR PATRIC; 23936588; VBITheMar51294_0844. DR eggNOG; ENOG4107Z5F; Bacteria. DR eggNOG; COG0115; LUCA. DR InParanoid; P74921; -. DR KO; K00826; -. DR OMA; VCEGSFS; -. DR OrthoDB; EOG6G4VTJ; -. DR UniPathway; UPA00047; UER00058. DR UniPathway; UPA00048; UER00073. DR UniPathway; UPA00049; UER00062. DR EvolutionaryTrace; P74921; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR001544; Aminotrans_IV. DR InterPro; IPR018300; Aminotrans_IV_CS. DR PANTHER; PTHR11825; PTHR11825; 1. DR Pfam; PF01063; Aminotran_4; 1. DR SUPFAM; SSF56752; SSF56752; 1. DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aminotransferase; KW Branched-chain amino acid biosynthesis; Complete proteome; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 273 Probable branched-chain-amino-acid FT aminotransferase. FT /FTId=PRO_0000103287. FT MOD_RES 133 133 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. FT CONFLICT 77 77 A -> R (in Ref. 2; AAC44497). FT {ECO:0000305}. FT STRAND 2 5 {ECO:0000244|PDB:3CSW}. FT STRAND 8 18 {ECO:0000244|PDB:3CSW}. FT HELIX 19 25 {ECO:0000244|PDB:3CSW}. FT STRAND 30 37 {ECO:0000244|PDB:3CSW}. FT HELIX 44 56 {ECO:0000244|PDB:3CSW}. FT TURN 57 59 {ECO:0000244|PDB:3CSW}. FT HELIX 66 77 {ECO:0000244|PDB:3CSW}. FT STRAND 84 90 {ECO:0000244|PDB:3CSW}. FT TURN 92 94 {ECO:0000244|PDB:3CSW}. FT STRAND 97 103 {ECO:0000244|PDB:3CSW}. FT STRAND 113 117 {ECO:0000244|PDB:3CSW}. FT TURN 125 127 {ECO:0000244|PDB:3CSW}. FT HELIX 138 144 {ECO:0000244|PDB:3CSW}. FT STRAND 148 156 {ECO:0000244|PDB:3CSW}. FT STRAND 160 174 {ECO:0000244|PDB:3CSW}. FT STRAND 177 181 {ECO:0000244|PDB:3CSW}. FT HELIX 183 185 {ECO:0000244|PDB:3CSW}. FT HELIX 191 202 {ECO:0000244|PDB:3CSW}. FT STRAND 207 210 {ECO:0000244|PDB:3CSW}. FT HELIX 214 218 {ECO:0000244|PDB:3CSW}. FT STRAND 221 227 {ECO:0000244|PDB:3CSW}. FT TURN 228 230 {ECO:0000244|PDB:3CSW}. FT STRAND 231 238 {ECO:0000244|PDB:3CSW}. FT STRAND 241 243 {ECO:0000244|PDB:3CSW}. FT STRAND 245 247 {ECO:0000244|PDB:3CSW}. FT HELIX 250 264 {ECO:0000244|PDB:3CSW}. FT HELIX 267 269 {ECO:0000244|PDB:3CSW}. FT TURN 270 272 {ECO:0000244|PDB:3CSW}. SQ SEQUENCE 273 AA; 31158 MW; 2162B705612E90E3 CRC64; MLIWWRGKFR RADEISLDFS LFEKSLQGAV YETLRTYSRA PFAAYKHYTR LKRSADFFNL PLSLSFDEFT KVLKAGADEF KQEVRIKVYL FPDSGEVLFV FSPLNIPDLE TGVEVKISNV RRIPDLSTPP ALKITGRTDI VLARREIVDC YDVILLGLNG QVCEGSFSNV FLVKEGKLIT PSLDSGILDG ITRENVIKLA KSLEIPVEER VVWVWELFEA DEMFLTHTSA GVVPVRRLNE HSFFEEEPGP VTATLMENFE PFVLNLEENW VGI // ID KAD_THEMA Reviewed; 220 AA. AC Q9X1I8; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00235}; DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00235}; DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00235}; DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00235}; GN Name=adk {ECO:0000255|HAMAP-Rule:MF_00235}; OrderedLocusNames=TM_1479; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal CC phosphate group between ATP and AMP. Plays an important role in CC cellular energy homeostasis and in adenine nucleotide metabolism. CC {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000255|HAMAP- CC Rule:MF_00235}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- DOMAIN: Consists of three domains, a large central CORE domain and CC two small peripheral domains, NMPbind and LID, which undergo CC movements during catalysis. The LID domain closes over the site of CC phosphoryl transfer upon ATP binding. Assembling and dissambling CC the active center during each catalytic cycle provides an CC effective means to prevent ATP hydrolysis. Some bacteria have CC evolved a zinc-coordinating structure that stabilizes the LID CC domain. {ECO:0000255|HAMAP-Rule:MF_00235}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00235}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36545.1; -; Genomic_DNA. DR PIR; G72247; G72247. DR RefSeq; NP_229279.1; NC_000853.1. DR RefSeq; WP_004081793.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1I8; -. DR STRING; 243274.TM1479; -. DR EnsemblBacteria; AAD36545; AAD36545; TM_1479. DR GeneID; 897080; -. DR KEGG; tma:TM1479; -. DR KEGG; tmi:THEMA_06905; -. DR KEGG; tmw:THMA_1511; -. DR PATRIC; 23937916; VBITheMar51294_1496. DR eggNOG; ENOG4105CC8; Bacteria. DR eggNOG; COG0563; LUCA. DR InParanoid; Q9X1I8; -. DR KO; K00939; -. DR OMA; PHISTGA; -. DR OrthoDB; EOG679TH4; -. DR UniPathway; UPA00588; UER00649. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR InterPro; IPR006259; Adenyl_kin_sub. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR007862; Adenylate_kinase_lid-dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23359; PTHR23359; 1. DR Pfam; PF05191; ADK_lid; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01351; adk; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Metal-binding; KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome; KW Transferase; Zinc. FT CHAIN 1 220 Adenylate kinase. FT /FTId=PRO_0000158873. FT NP_BIND 12 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 60 62 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 88 91 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 139 140 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT REGION 32 62 NMPbind. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT REGION 129 166 LID. {ECO:0000255|HAMAP-Rule:MF_00235}. FT METAL 133 133 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT METAL 136 136 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT METAL 153 153 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT METAL 156 156 Zinc; structural. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT BINDING 33 33 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 38 38 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 95 95 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 130 130 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 163 163 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 174 174 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 202 202 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00235}. SQ SEQUENCE 220 AA; 25169 MW; 42C2C22D44A15DDB CRC64; MMAYLVFLGP PGAGKGTYAK RLQEITGIPH ISTGDIFRDI VKKENDELGK KIKEIMERGE LVPDELVNEV VKRRLSEKDC ERGFILDGYP RTVAQAEFLD GFLKTQNKEL TAAVLFEVPE EVVVQRLTAR RICPKCGRIY NLISLPPKED ELCDDCKVKL VQREDDKEET VRHRYKVYLE KTQPVIDYYD KKGILKRVDG TIGIDNVIAE VLKIIGWSDK // ID ISPE_THEMA Reviewed; 271 AA. AC Q9X1A3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061}; DE Short=CMK {ECO:0000255|HAMAP-Rule:MF_00061}; DE EC=2.7.1.148 {ECO:0000255|HAMAP-Rule:MF_00061}; DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061}; GN Name=ispE {ECO:0000255|HAMAP-Rule:MF_00061}; GN OrderedLocusNames=TM_1383; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy CC group of 4-diphosphocytidyl-2C-methyl-D-erythritol. CC {ECO:0000255|HAMAP-Rule:MF_00061}. CC -!- CATALYTIC ACTIVITY: ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D- CC erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl- CC D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 3/6. {ECO:0000255|HAMAP- CC Rule:MF_00061}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00061}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36453.1; -; Genomic_DNA. DR PIR; H72261; H72261. DR RefSeq; NP_229184.1; NC_000853.1. DR RefSeq; WP_004081581.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1A3; -. DR STRING; 243274.TM1383; -. DR DNASU; 898095; -. DR EnsemblBacteria; AAD36453; AAD36453; TM_1383. DR GeneID; 898095; -. DR KEGG; tma:TM1383; -. DR PATRIC; 23937708; VBITheMar51294_1395. DR eggNOG; ENOG4107SJN; Bacteria. DR eggNOG; COG1947; LUCA. DR InParanoid; Q9X1A3; -. DR KO; K00919; -. DR OMA; DGYHEIV; -. DR OrthoDB; EOG62VNQ2; -. DR UniPathway; UPA00056; UER00094. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; -; 1. DR HAMAP; MF_00061; IspE; 1. DR InterPro; IPR013750; GHMP_kinase_C_dom. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR004424; IspE. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR20861:SF2; PTHR20861:SF2; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF010376; IspE; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55060; SSF55060; 1. DR TIGRFAMs; TIGR00154; ispE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Isoprene biosynthesis; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 271 4-diphosphocytidyl-2-C-methyl-D- FT erythritol kinase. FT /FTId=PRO_0000189277. FT NP_BIND 97 107 ATP. {ECO:0000255|HAMAP-Rule:MF_00061}. FT ACT_SITE 17 17 {ECO:0000255|HAMAP-Rule:MF_00061}. FT ACT_SITE 137 137 {ECO:0000255|HAMAP-Rule:MF_00061}. SQ SEQUENCE 271 AA; 30056 MW; 3E9E47FDAB0F336D CRC64; MVENIGSGSA ELVSYAKLNL YLDVLGKRSD GYHEIVGLFQ TISLHDTLTV EICDRGFYLE SSVALPSDNT IKRAWEMFRK NTGKEFGLKV TLKKEIPVGS GLGGGSSNAA AVLRYLGEVF KIPLEDLLNI AAQVGSDVPF FLYGGTALVR GRGEIVEKLE DIEGYSVDLF FPGIHSSTKE MYLSLTPEMY RKGPGRVEEL HRAYLERNYE KIKELSYNVF EKVFLEKHPE VMDGLRNFGD GSIVKMMTGS GSVFFALYPL DKGNYSFVGG V // ID ISPD_THEMA Reviewed; 222 AA. AC Q9X1B3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108}; DE EC=2.7.7.60 {ECO:0000255|HAMAP-Rule:MF_00108}; DE AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000255|HAMAP-Rule:MF_00108}; DE AltName: Full=MEP cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108}; DE Short=MCT {ECO:0000255|HAMAP-Rule:MF_00108}; GN Name=ispD {ECO:0000255|HAMAP-Rule:MF_00108}; GN OrderedLocusNames=TM_1393; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C- CC methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4- CC phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}. CC -!- CATALYTIC ACTIVITY: CTP + 2-C-methyl-D-erythritol 4-phosphate = CC diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. CC {ECO:0000255|HAMAP-Rule:MF_00108}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 2/6. {ECO:0000255|HAMAP- CC Rule:MF_00108}. CC -!- SIMILARITY: Belongs to the IspD family. {ECO:0000255|HAMAP- CC Rule:MF_00108}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36464.1; -; Genomic_DNA. DR PIR; B72259; B72259. DR RefSeq; NP_229194.1; NC_000853.1. DR RefSeq; WP_004081602.1; NZ_CP011107.1. DR PDB; 1VPA; X-ray; 2.67 A; A/B=1-222. DR PDBsum; 1VPA; -. DR ProteinModelPortal; Q9X1B3; -. DR SMR; Q9X1B3; 1-219. DR STRING; 243274.TM1393; -. DR EnsemblBacteria; AAD36464; AAD36464; TM_1393. DR GeneID; 898083; -. DR KEGG; tma:TM1393; -. DR PATRIC; 23937732; VBITheMar51294_1405. DR eggNOG; ENOG4105CE5; Bacteria. DR eggNOG; COG1211; LUCA. DR InParanoid; Q9X1B3; -. DR KO; K00991; -. DR OMA; PQVFDAD; -. DR OrthoDB; EOG6B3662; -. DR UniPathway; UPA00056; UER00093. DR EvolutionaryTrace; Q9X1B3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_00108; IspD; 1. DR InterPro; IPR001228; IspD. DR InterPro; IPR018294; ISPD_synthase_CS. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF01128; IspD; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR00453; ispD; 1. DR PROSITE; PS01295; ISPD; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isoprene biosynthesis; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 222 2-C-methyl-D-erythritol 4-phosphate FT cytidylyltransferase. FT /FTId=PRO_0000075638. FT SITE 14 14 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00108}. FT SITE 21 21 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00108}. FT SITE 149 149 Positions MEP for the nucleophilic FT attack. {ECO:0000255|HAMAP- FT Rule:MF_00108}. FT SITE 201 201 Positions MEP for the nucleophilic FT attack. {ECO:0000255|HAMAP- FT Rule:MF_00108}. FT STRAND 2 8 {ECO:0000244|PDB:1VPA}. FT HELIX 13 15 {ECO:0000244|PDB:1VPA}. FT HELIX 21 23 {ECO:0000244|PDB:1VPA}. FT HELIX 33 41 {ECO:0000244|PDB:1VPA}. FT STRAND 46 52 {ECO:0000244|PDB:1VPA}. FT HELIX 54 56 {ECO:0000244|PDB:1VPA}. FT HELIX 57 61 {ECO:0000244|PDB:1VPA}. FT STRAND 69 74 {ECO:0000244|PDB:1VPA}. FT HELIX 79 90 {ECO:0000244|PDB:1VPA}. FT HELIX 91 93 {ECO:0000244|PDB:1VPA}. FT STRAND 96 102 {ECO:0000244|PDB:1VPA}. FT HELIX 110 123 {ECO:0000244|PDB:1VPA}. FT STRAND 124 131 {ECO:0000244|PDB:1VPA}. FT STRAND 134 140 {ECO:0000244|PDB:1VPA}. FT STRAND 143 147 {ECO:0000244|PDB:1VPA}. FT STRAND 152 162 {ECO:0000244|PDB:1VPA}. FT HELIX 163 170 {ECO:0000244|PDB:1VPA}. FT STRAND 177 179 {ECO:0000244|PDB:1VPA}. FT HELIX 180 184 {ECO:0000244|PDB:1VPA}. FT TURN 185 187 {ECO:0000244|PDB:1VPA}. FT STRAND 191 194 {ECO:0000244|PDB:1VPA}. FT HELIX 197 199 {ECO:0000244|PDB:1VPA}. FT HELIX 207 218 {ECO:0000244|PDB:1VPA}. SQ SEQUENCE 222 AA; 25370 MW; 51D5E945D078ACEC CRC64; MNVAILLAAG KGERMSENVP KQFLEIEGRM LFEYPLSTFL KSEAIDGVVI VTRREWFEVV EKRVFHEKVL GIVEGGDTRS QSVRSALEFL EKFSPSYVLV HDSARPFLRK KHVSEVLRRA RETGAATLAL KNSDALVRVE NDRIEYIPRK GVYRILTPQA FSYEILKKAH ENGGEWADDT EPVQKLGVKI ALVEGDPLCF KVTFKEDLEL ARIIAREWER IP // ID ISPF_THEMA Reviewed; 165 AA. AC Q9WZB5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 104. DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00107}; DE Short=MECDP-synthase {ECO:0000255|HAMAP-Rule:MF_00107}; DE Short=MECPP-synthase {ECO:0000255|HAMAP-Rule:MF_00107}; DE Short=MECPS {ECO:0000255|HAMAP-Rule:MF_00107}; DE EC=4.6.1.12 {ECO:0000255|HAMAP-Rule:MF_00107}; GN Name=ispF {ECO:0000255|HAMAP-Rule:MF_00107}; GN OrderedLocusNames=TM_0647; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate CC (IPP) and dimethylallyl diphosphate (DMAPP), two major building CC blocks of isoprenoid compounds. Catalyzes the conversion of 4- CC diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to CC 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a CC corresponding release of cytidine 5-monophosphate (CMP). CC {ECO:0000255|HAMAP-Rule:MF_00107}. CC -!- CATALYTIC ACTIVITY: 2-phospho-4-(cytidine 5'-diphospho)-2-C- CC methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate CC + CMP. {ECO:0000255|HAMAP-Rule:MF_00107}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00107}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00107}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 4/6. {ECO:0000255|HAMAP- CC Rule:MF_00107}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00107}. CC -!- SIMILARITY: Belongs to the IspF family. {ECO:0000255|HAMAP- CC Rule:MF_00107}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35731.1; -; Genomic_DNA. DR PIR; F72351; F72351. DR RefSeq; NP_228456.1; NC_000853.1. DR RefSeq; WP_010865174.1; NC_000853.1. DR ProteinModelPortal; Q9WZB5; -. DR STRING; 243274.TM0647; -. DR DNASU; 897752; -. DR EnsemblBacteria; AAD35731; AAD35731; TM_0647. DR GeneID; 897752; -. DR KEGG; tma:TM0647; -. DR PATRIC; 23936208; VBITheMar51294_0657. DR eggNOG; ENOG41082Q0; Bacteria. DR eggNOG; COG0245; LUCA. DR InParanoid; Q9WZB5; -. DR KO; K01770; -. DR OMA; IRIGNGY; -. DR OrthoDB; EOG6J48RZ; -. DR BioCyc; TMAR243274:GC6P-672-MONOMER; -. DR UniPathway; UPA00056; UER00095. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.50; -; 1. DR HAMAP; MF_00107; IspF; 1. DR InterPro; IPR003526; MECDP_synthase. DR InterPro; IPR020555; MECDP_synthase_CS. DR Pfam; PF02542; YgbB; 1. DR SUPFAM; SSF69765; SSF69765; 1. DR TIGRFAMs; TIGR00151; ispF; 1. DR PROSITE; PS01350; ISPF; 1. PE 3: Inferred from homology; KW Complete proteome; Isoprene biosynthesis; Lyase; Metal-binding; KW Reference proteome. FT CHAIN 1 165 2-C-methyl-D-erythritol 2,4- FT cyclodiphosphate synthase. FT /FTId=PRO_0000189509. FT REGION 13 15 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00107}. FT REGION 39 40 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00107}. FT REGION 43 51 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00107}. FT REGION 61 63 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00107}. FT METAL 13 13 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00107}. FT METAL 15 15 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00107}. FT METAL 47 47 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00107}. FT BINDING 71 71 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00107}. FT BINDING 141 141 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00107}. FT SITE 39 39 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00107}. FT SITE 135 135 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00107}. SQ SEQUENCE 165 AA; 17833 MW; 6F112BC8296B742A CRC64; MESDPMFIGF GYDRHPLVEG RRLVLAGVEI DAPLGSLGHS DGDVLSHAII DALLGAGCLG DIGTWFPETK EYKDANSLDL LKETVKILEE RGFSVVNVDA TVVASIVKLS PYREKIVENL KSALETSRVN VKFKSGNTLG FEGEERGISA YAVCLVEEKG CTKST // ID KCY_THEMA Reviewed; 220 AA. AC Q9X1F6; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_00238}; DE Short=CK {ECO:0000255|HAMAP-Rule:MF_00238}; DE EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238}; DE AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00238}; DE Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_00238}; GN Name=cmk {ECO:0000255|HAMAP-Rule:MF_00238}; OrderedLocusNames=TM_1443; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + (d)CMP = ADP + (d)CDP. CC {ECO:0000255|HAMAP-Rule:MF_00238}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00238}. CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00238}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36512.1; -; Genomic_DNA. DR PIR; H72252; H72252. DR RefSeq; NP_229242.1; NC_000853.1. DR RefSeq; WP_004081716.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1F6; -. DR STRING; 243274.TM1443; -. DR EnsemblBacteria; AAD36512; AAD36512; TM_1443. DR GeneID; 898032; -. DR KEGG; tma:TM1443; -. DR PATRIC; 23937836; VBITheMar51294_1456. DR eggNOG; ENOG4107RB4; Bacteria. DR eggNOG; COG0283; LUCA. DR InParanoid; Q9X1F6; -. DR KO; K00945; -. DR OMA; LKIFMTA; -. DR OrthoDB; EOG6Z6FZ4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00238; Cytidyl_kinase_type1; 1. DR InterPro; IPR003136; Cytidylate_kin. DR InterPro; IPR011994; Cytidylate_kinase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF02224; Cytidylate_kin; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00017; cmk; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 220 Cytidylate kinase. FT /FTId=PRO_0000131993. FT NP_BIND 9 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00238}. SQ SEQUENCE 220 AA; 24702 MW; 2B15B70F21B9FCE4 CRC64; MGFQIAIDGP AASGKSTIAK LLAEKLGFDH LNTGATYRAV AVYLHEKGLS SSSAEEEIEN VLKDLKIDYV NGRVYINGED YTEKIQSPEA GVLASNFARL EVVRRHLVRI QREICDDKNI VVEGRDIGTV VLPNAHLKIF LTASLEARVE RKLKEYQKRG LKVTKEEVER ELISRDEQDS KRNVAPLKPA EDAVIIDTTS MSVEEVLDRI LKLVRERMNT // ID ISPT_THEMA Reviewed; 233 AA. AC Q9X1B8; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Isoprenyl transferase {ECO:0000255|HAMAP-Rule:MF_01139}; DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01139}; GN Name=uppS {ECO:0000255|HAMAP-Rule:MF_01139}; GN OrderedLocusNames=TM_1398; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate CC (IPP) with allylic pyrophosphates generating different type of CC terpenoids. {ECO:0000255|HAMAP-Rule:MF_01139}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01139}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01139}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01139}. CC -!- SIMILARITY: Belongs to the UPP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01139}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36469.1; -; Genomic_DNA. DR PIR; G72259; G72259. DR RefSeq; NP_229199.1; NC_000853.1. DR RefSeq; WP_004081614.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1B8; -. DR STRING; 243274.TM1398; -. DR EnsemblBacteria; AAD36469; AAD36469; TM_1398. DR GeneID; 898078; -. DR KEGG; tma:TM1398; -. DR PATRIC; 23937742; VBITheMar51294_1410. DR eggNOG; ENOG4105CR3; Bacteria. DR eggNOG; COG0020; LUCA. DR InParanoid; Q9X1B8; -. DR KO; K00806; -. DR OMA; WAKLKNK; -. DR OrthoDB; EOG68H89T; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1180.10; -; 1. DR HAMAP; MF_01139; ISPT; 1. DR InterPro; IPR001441; UPP_synth-like. DR InterPro; IPR018520; UPP_synth-like_CS. DR PANTHER; PTHR10291; PTHR10291; 1. DR Pfam; PF01255; Prenyltransf; 1. DR SUPFAM; SSF64005; SSF64005; 1. DR TIGRFAMs; TIGR00055; uppS; 1. DR PROSITE; PS01066; UPP_SYNTHASE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Transferase. FT CHAIN 1 233 Isoprenyl transferase. FT /FTId=PRO_0000123701. FT REGION 13 16 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT REGION 57 59 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT REGION 184 186 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT ACT_SITE 12 12 {ECO:0000255|HAMAP-Rule:MF_01139}. FT ACT_SITE 60 60 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT METAL 12 12 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT METAL 197 197 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 17 17 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 25 25 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 29 29 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 61 61 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 63 63 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 178 178 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. SQ SEQUENCE 233 AA; 27859 MW; 22D43CC79F98E074 CRC64; MRIPQHVAII MDGNGRWAKK RGLPRIKGHQ RGAEVLHNTV KWSLELGIKY LTAFSFSTEN WKRPKEEVEF LMDLFVQMID REMELLRRER VRVRILGRKE GLPEKVLKKW QEVEEKTKEF DRMTLIIAFN YGGRREILDA VEFILKDVSH GKKIELTEET FRQYLYLPDV PDPDLIIRTS GEMRLSNFLL WQSAYSELYF FKKLWPDFTK RDFLRAIESY SKRERRFGGL ING // ID KHSE_THEMA Reviewed; 281 AA. AC Q9WZ15; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 113. DE RecName: Full=Homoserine kinase {ECO:0000255|HAMAP-Rule:MF_00384}; DE Short=HK {ECO:0000255|HAMAP-Rule:MF_00384}; DE Short=HSK {ECO:0000255|HAMAP-Rule:MF_00384}; DE EC=2.7.1.39 {ECO:0000255|HAMAP-Rule:MF_00384}; GN Name=thrB {ECO:0000255|HAMAP-Rule:MF_00384}; GN OrderedLocusNames=TM_0545; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L- CC homoserine to L-homoserine phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00384}. CC -!- CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L- CC homoserine. {ECO:0000255|HAMAP-Rule:MF_00384}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 4/5. {ECO:0000255|HAMAP- CC Rule:MF_00384}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00384}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00384}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35630.1; -; Genomic_DNA. DR PIR; F72364; F72364. DR RefSeq; NP_228355.1; NC_000853.1. DR RefSeq; WP_004081349.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ15; -. DR STRING; 243274.TM0545; -. DR DNASU; 897599; -. DR EnsemblBacteria; AAD35630; AAD35630; TM_0545. DR GeneID; 897599; -. DR KEGG; tma:TM0545; -. DR PATRIC; 23935997; VBITheMar51294_0553. DR eggNOG; ENOG4105D5I; Bacteria. DR eggNOG; COG0083; LUCA. DR InParanoid; Q9WZ15; -. DR KO; K00872; -. DR OMA; HQNYRIN; -. DR OrthoDB; EOG6DG2WK; -. DR UniPathway; UPA00050; UER00064. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; -; 1. DR HAMAP; MF_00384; Homoser_kinase; 1. DR InterPro; IPR013750; GHMP_kinase_C_dom. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS. DR InterPro; IPR000870; Homoserine_kinase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF000676; Homoser_kin; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55060; SSF55060; 1. DR TIGRFAMs; TIGR00191; thrB; 1. DR PROSITE; PS00627; GHMP_KINASES_ATP; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Reference proteome; KW Threonine biosynthesis; Transferase. FT CHAIN 1 281 Homoserine kinase. FT /FTId=PRO_0000156625. FT NP_BIND 83 93 ATP. {ECO:0000255|HAMAP-Rule:MF_00384}. SQ SEQUENCE 281 AA; 31296 MW; EFF08A5359F445CC CRC64; MKVLVPATTT NLGAGFDVFG LALDLFNEVE FSFDTKETTI ESTGKYASDL KDHNLFFEVL RFFERKTGYR VPPVRIKQTC NIPVSSGLGS SAAVIVAALH IANEGTGRNL SREDLMKLAV ELEGHPDNVV PAFTGGLVVC YQNGSHLDFE KFEIDLSLTF LVPNFPVCTN EMRKILPEKV PFEDAVFNIK NSCQFLAKIA AGKIKEALKY VGDRLHQNYR INGNKKMKEF VEAILSKNPE YWFVSGSGPS VCSNINDFEG IPYLKDVLKL RVNNRGMIVS E // ID KPRS_THEMA Reviewed; 315 AA. AC Q9X1W3; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583}; DE EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583}; GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583}; OrderedLocusNames=TM_1628; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in the biosynthesis of ribose 1,5-bisphosphate. CC Catalyzes the transfer of pyrophosphoryl group from ATP to ribose- CC 5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP. CC {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00583}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D- CC ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1- CC diphosphate from D-ribose 5-phosphate (route I): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. {ECO:0000255|HAMAP-Rule:MF_00583}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36695.1; -; Genomic_DNA. DR PIR; D72229; D72229. DR RefSeq; NP_229428.1; NC_000853.1. DR RefSeq; WP_004082104.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1W3; -. DR SMR; Q9X1W3; 6-315. DR STRING; 243274.TM1628; -. DR EnsemblBacteria; AAD36695; AAD36695; TM_1628. DR GeneID; 897927; -. DR KEGG; tma:TM1628; -. DR PATRIC; 23938230; VBITheMar51294_1647. DR eggNOG; ENOG4105C5T; Bacteria. DR eggNOG; COG0462; LUCA. DR InParanoid; Q9X1W3; -. DR KO; K00948; -. DR OMA; HENVRGQ; -. DR OrthoDB; EOG6Z99XQ; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.2020; -; 2. DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1. DR InterPro; IPR000842; PRib_PP_synth_CS. DR InterPro; IPR029099; Pribosyltran_N. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005946; Rib-P_diPkinase. DR Pfam; PF14572; Pribosyl_synth; 1. DR Pfam; PF13793; Pribosyltran_N; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. DR PROSITE; PS00114; PRPP_SYNTHASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide biosynthesis; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 315 Ribose-phosphate pyrophosphokinase. FT /FTId=PRO_0000141219. FT NP_BIND 40 42 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT NP_BIND 99 102 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 198 200 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 225 232 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 309 311 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT METAL 131 131 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 133 133 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 142 142 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 146 146 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 107 107 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 133 133 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 138 138 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 175 175 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 315 AA; 34952 MW; 9570508E420D8CF3 CRC64; MSFSNEMKVF SGNANRPLAE KIANYLNLQL GDCEVGRFAD GEINVRINET VRGHDIFLIQ PTSPPVNENL MELLIMIDAF KRASANTIAV VIPYYGYARQ DRKAKGRDPI SAKLVANLIT VAGATRVLTV DLHAEQIQGF FDIPVDNLWS YPVFAEELLK RENIVPEETV VVSPDVGGVR RARRMAERLG TSLAILDKRR PSDNVAEVVN IIGEVEDKVV IMFDDIIDTA HSIVKGAEAL KNAGAKRIIA CATHGVFSDR ALERIENSSI DTVYITDTIY HENLPEKVKV ISVANLIGEA IMRIRKHLSV STLFR // ID KITH_THEMA Reviewed; 184 AA. AC Q9WYN2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Thymidine kinase; DE EC=2.7.1.21; GN Name=tdk; OrderedLocusNames=TM_0401; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS; RP THYMIDINE AND ATP ANALOGS, AND SUBUNIT. RX PubMed=17407781; DOI=10.1016/j.jmb.2007.02.104; RA Segura-Pena D., Lutz S., Monnerjahn C., Konrad M., Lavie A.; RT "Binding of ATP to TK1-like enzymes is associated with a RT conformational change in the quaternary structure."; RL J. Mol. Biol. 369:129-141(2007). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND RP THYMIDINE, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF RP HIS-53; GLY-55 AND LEU-129. RX PubMed=18073106; DOI=10.1016/j.str.2007.09.025; RA Segura-Pena D., Lichter J., Trani M., Konrad M., Lavie A., Lutz S.; RT "Quaternary structure change as a mechanism for the regulation of RT thymidine kinase 1-like enzymes."; RL Structure 15:1555-1566(2007). CC -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'- CC phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=40 uM for ATP {ECO:0000269|PubMed:18073106}; CC KM=0.5 uM for thymidine {ECO:0000269|PubMed:18073106}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17407781, CC ECO:0000269|PubMed:18073106}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35486.1; -; Genomic_DNA. DR PIR; B72383; B72383. DR RefSeq; NP_228211.1; NC_000853.1. DR RefSeq; WP_004083238.1; NZ_CP011107.1. DR PDB; 2ORW; X-ray; 1.50 A; A/B=1-184. DR PDB; 2QPO; X-ray; 1.95 A; A/B/C/D=1-184. DR PDB; 2QQ0; X-ray; 1.50 A; A/B=1-184. DR PDB; 2QQE; X-ray; 1.90 A; A/B=1-184. DR PDBsum; 2ORW; -. DR PDBsum; 2QPO; -. DR PDBsum; 2QQ0; -. DR PDBsum; 2QQE; -. DR ProteinModelPortal; Q9WYN2; -. DR SMR; Q9WYN2; 2-182. DR DIP; DIP-29527N; -. DR STRING; 243274.TM0401; -. DR EnsemblBacteria; AAD35486; AAD35486; TM_0401. DR GeneID; 897394; -. DR KEGG; tma:TM0401; -. DR PATRIC; 23935685; VBITheMar51294_0406. DR eggNOG; ENOG4107104; Bacteria. DR eggNOG; COG1435; LUCA. DR InParanoid; Q9WYN2; -. DR KO; K00857; -. DR OMA; KEQFGWI; -. DR OrthoDB; EOG69D3J2; -. DR EvolutionaryTrace; Q9WYN2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00124; Thymidine_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001267; Thymidine_kinase. DR InterPro; IPR020633; Thymidine_kinase_CS. DR PANTHER; PTHR11441; PTHR11441; 1. DR Pfam; PF00265; TK; 1. DR PIRSF; PIRSF035805; TK_cell; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; KW DNA synthesis; Kinase; Metal-binding; Nucleotide-binding; KW Reference proteome; Transferase; Zinc. FT CHAIN 1 184 Thymidine kinase. FT /FTId=PRO_0000175040. FT NP_BIND 10 17 ATP. FT NP_BIND 83 86 ATP. {ECO:0000250}. FT REGION 161 164 Substrate binding. FT ACT_SITE 84 84 Proton acceptor. {ECO:0000255}. FT METAL 140 140 Zinc. FT METAL 143 143 Zinc. FT METAL 173 173 Zinc. FT METAL 176 176 Zinc. FT BINDING 53 53 ATP. FT BINDING 115 115 Substrate; via amide nitrogen. FT BINDING 169 169 Substrate. FT MUTAGEN 53 53 H->A: Reduced affinity for ATP. FT {ECO:0000269|PubMed:18073106}. FT MUTAGEN 55 55 G->W: Reduced affinity for ATP. FT {ECO:0000269|PubMed:18073106}. FT MUTAGEN 129 129 L->W: Reduced affinity for thymidine. FT {ECO:0000269|PubMed:18073106}. FT STRAND 5 11 {ECO:0000244|PDB:2ORW}. FT HELIX 16 29 {ECO:0000244|PDB:2ORW}. FT STRAND 33 39 {ECO:0000244|PDB:2ORW}. FT STRAND 61 65 {ECO:0000244|PDB:2ORW}. FT HELIX 66 72 {ECO:0000244|PDB:2ORW}. FT STRAND 77 82 {ECO:0000244|PDB:2ORW}. FT HELIX 85 87 {ECO:0000244|PDB:2ORW}. FT HELIX 92 101 {ECO:0000244|PDB:2ORW}. FT STRAND 105 113 {ECO:0000244|PDB:2ORW}. FT HELIX 121 129 {ECO:0000244|PDB:2ORW}. FT STRAND 131 135 {ECO:0000244|PDB:2ORW}. FT TURN 141 143 {ECO:0000244|PDB:2ORW}. FT STRAND 146 148 {ECO:0000244|PDB:2QQE}. FT STRAND 150 153 {ECO:0000244|PDB:2ORW}. FT TURN 166 168 {ECO:0000244|PDB:2ORW}. FT STRAND 169 172 {ECO:0000244|PDB:2ORW}. FT HELIX 174 180 {ECO:0000244|PDB:2ORW}. SQ SEQUENCE 184 AA; 20654 MW; 906B2C1BE3A7EDDA CRC64; MSGKLTVITG PMYSGKTTEL LSFVEIYKLG KKKVAVFKPK IDSRYHSTMI VSHSGNGVEA HVIERPEEMR KYIEEDTRGV FIDEVQFFNP SLFEVVKDLL DRGIDVFCAG LDLTHKQNPF ETTALLLSLA DTVIKKKAVC HRCGEYNATL TLKVAGGEEE IDVGGQEKYI AVCRDCYNTL KKRV // ID KGUA_THEMA Reviewed; 207 AA. AC Q9X215; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Guanylate kinase; DE EC=2.7.4.8; DE AltName: Full=GMP kinase; GN Name=gmk; OrderedLocusNames=TM_1689; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + GMP = ADP + GDP. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36756.1; -; Genomic_DNA. DR PIR; C72223; C72223. DR RefSeq; NP_229489.1; NC_000853.1. DR RefSeq; WP_004082205.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X215; -. DR STRING; 243274.TM1689; -. DR EnsemblBacteria; AAD36756; AAD36756; TM_1689. DR GeneID; 897895; -. DR KEGG; tma:TM1689; -. DR PATRIC; 23938352; VBITheMar51294_1706. DR eggNOG; ENOG4108UHA; Bacteria. DR eggNOG; COG0194; LUCA. DR InParanoid; Q9X215; -. DR KO; K00942; -. DR OMA; DYCVIND; -. DR OrthoDB; EOG6CP410; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004385; F:guanylate kinase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 3. DR HAMAP; MF_00328; Guanylate_kinase; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR017665; Guanylate_kinase. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00625; Guanylate_kin; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00072; GuKc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03263; guanyl_kin; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 207 Guanylate kinase. FT /FTId=PRO_0000170630. FT DOMAIN 3 181 Guanylate kinase-like. FT NP_BIND 10 17 ATP. {ECO:0000250}. SQ SEQUENCE 207 AA; 24037 MW; E38375CFF2E26963 CRC64; MKGQLFVICG PSGAGKTSII KEVLKRLDNV VFSVSCTTRP KRPHEEDGKD YFFITEEEFL KRVERGEFLE WARVHGHLYG TLRSFVESHI NEGKDVVLDI DVQGALSVKK KYSNTVFIYV APPSYADLRE RILKRGTEKE ADVLVRLENA KWELMFMDEF DYIVVNENLE DAVEMVVSIV RSERAKVTRN QDKIERFKME VKGWKKL // ID KPYK_THEMA Reviewed; 466 AA. AC Q9WY51; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OrderedLocusNames=TM_0208; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, AND REGULATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=12654928; DOI=10.1074/jbc.M210288200; RA Johnsen U., Hansen T., Schoenheit P.; RT "Comparative analysis of pyruvate kinases from the hyperthermophilic RT archaea Archaeoglobus fulgidus, Aeropyrum pernix, and Pyrobaculum RT aerophilum and the hyperthermophilic bacterium Thermotoga maritima: RT unusual regulatory properties in hyperthermophilic archaea."; RL J. Biol. Chem. 278:25417-25427(2003). CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000269|PubMed:12654928}; CC -!- ENZYME REGULATION: Allosterically activated by AMP and inhibited CC by ATP. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Vmax=578 umol/min/mg enzyme (at 65 degrees Celsius) CC {ECO:0000269|PubMed:12654928}; CC pH dependence: CC Optimum pH is 5.9-6.0. {ECO:0000269|PubMed:12654928}; CC Temperature dependence: CC Optimum temperature is 80 degrees Celsius for the recombinant CC enzyme. Thermostable up to 85 degrees Celsius. CC {ECO:0000269|PubMed:12654928}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12654928}. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35300.1; -; Genomic_DNA. DR PIR; B72406; B72406. DR RefSeq; NP_228023.1; NC_000853.1. DR RefSeq; WP_008193903.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY51; -. DR STRING; 243274.TM0208; -. DR EnsemblBacteria; AAD35300; AAD35300; TM_0208. DR GeneID; 897079; -. DR KEGG; tma:TM0208; -. DR PATRIC; 23935288; VBITheMar51294_0210. DR eggNOG; ENOG4105CA9; Bacteria. DR eggNOG; COG0469; LUCA. DR InParanoid; Q9WY51; -. DR KO; K00873; -. DR OMA; GTHEEHK; -. DR OrthoDB; EOG6GBMB0; -. DR BioCyc; MetaCyc:MONOMER-4887; -. DR BioCyc; TMAR243274:GC6P-221-MONOMER; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro. DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC. DR Gene3D; 2.40.33.10; -; 1. DR Gene3D; 3.20.20.60; -; 2. DR Gene3D; 3.40.1380.20; -; 1. DR InterPro; IPR001697; Pyr_Knase. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom. DR InterPro; IPR015794; Pyrv_Knase_a/b. DR InterPro; IPR015793; Pyrv_Knase_brl. DR InterPro; IPR015795; Pyrv_Knase_C. DR InterPro; IPR015806; Pyrv_Knase_insert_dom. DR PANTHER; PTHR11817; PTHR11817; 1. DR Pfam; PF00224; PK; 1. DR Pfam; PF02887; PK_C; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR SUPFAM; SSF50800; SSF50800; 1. DR SUPFAM; SSF51621; SSF51621; 2. DR SUPFAM; SSF52935; SSF52935; 1. DR TIGRFAMs; TIGR01064; pyruv_kin; 1. PE 1: Evidence at protein level; KW Allosteric enzyme; ATP-binding; Complete proteome; Glycolysis; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Potassium; Pyruvate; KW Reference proteome; Transferase. FT CHAIN 1 466 Pyruvate kinase. FT /FTId=PRO_0000295179. FT METAL 34 34 Potassium. {ECO:0000250}. FT METAL 36 36 Potassium. {ECO:0000250}. FT METAL 66 66 Potassium. {ECO:0000250}. FT METAL 219 219 Magnesium. {ECO:0000250}. FT METAL 243 243 Magnesium. {ECO:0000250}. FT BINDING 32 32 Substrate. {ECO:0000250}. FT BINDING 242 242 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 243 243 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 275 275 Substrate. {ECO:0000250}. FT SITE 217 217 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 466 AA; 51892 MW; 5083B7B28A5D8DEF CRC64; MRSTKIVCTV GPRTDSYEMI EKMIDLGVNV FRINTSHGDW NEQEQKILKI KDLREKKKKP VAILIDLAGP KIRTGYLEKE FVELKEGQIF TLTTKEILGN EHIVSVNLSS LPKDVKKGDT ILLSDGEIVL EVIETTDTEV KTVVKVGGKI THRRGVNVPT ADLSVESITD RDREFIKLGT LHDVEFFALS FVRKPEDVLK AKEEIRKHGK EIPVISKIET KKALERLEEI IKVSDGIMVA RGDLGVEIPI EEVPIVQKEI IKLSKYYSKP VIVATQILES MIENPFPTRA EVTDIANAIF DGADALLLTA ETAVGKHPLE AIKVLSKVAK EAEKKLEFFR TIEYDTSDIS EAISHACWQL SESLNAKLII TPTISGSTAV RVSKYNVSQP IVALTPEEKT YYRLSLVRKV IPVLAEKCSQ ELEFIEKGLK KVEEMGLAEK GDLVVLTSGV PGKVGTTNTI RVLKVD // ID LEUC2_THEMA Reviewed; 417 AA. AC Q9WZ24; DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 110. DE RecName: Full=3-isopropylmalate dehydratase large subunit 2 {ECO:0000255|HAMAP-Rule:MF_01027}; DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01027}; DE AltName: Full=Alpha-IPM isomerase 2 {ECO:0000255|HAMAP-Rule:MF_01027}; DE Short=IPMI 2 {ECO:0000255|HAMAP-Rule:MF_01027}; DE AltName: Full=Isopropylmalate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_01027}; GN Name=leuC2 {ECO:0000255|HAMAP-Rule:MF_01027}; GN OrderedLocusNames=TM_0554; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate. CC {ECO:0000255|HAMAP-Rule:MF_01027}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. {ECO:0000255|HAMAP-Rule:MF_01027}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01027}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01027}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_01027}. CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP- CC Rule:MF_01027}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC CC type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_01027}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35639.1; -; Genomic_DNA. DR PIR; H72362; H72362. DR RefSeq; NP_228364.1; NC_000853.1. DR RefSeq; WP_004081330.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ24; -. DR STRING; 243274.TM0554; -. DR EnsemblBacteria; AAD35639; AAD35639; TM_0554. DR GeneID; 897612; -. DR KEGG; tma:TM0554; -. DR PATRIC; 23936015; VBITheMar51294_0562. DR eggNOG; ENOG4105CQI; Bacteria. DR eggNOG; COG0065; LUCA. DR InParanoid; Q9WZ24; -. DR KO; K01703; -. DR OMA; KIEPQVA; -. DR OrthoDB; EOG600DP5; -. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.499.10; -; 2. DR Gene3D; 3.40.1060.10; -; 1. DR HAMAP; MF_01027; LeuC_type2; 1. DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok. DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu. DR InterPro; IPR011823; IsopropMal_deHydtase_lsu_bac. DR PANTHER; PTHR11670; PTHR11670; 1. DR Pfam; PF00330; Aconitase; 1. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF53732; SSF53732; 1. DR TIGRFAMs; TIGR01343; hacA_fam; 1. DR TIGRFAMs; TIGR02086; IPMI_arch; 1. DR TIGRFAMs; TIGR02083; LEU2; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding; KW Reference proteome. FT CHAIN 1 417 3-isopropylmalate dehydratase large FT subunit 2. FT /FTId=PRO_0000076861. FT METAL 298 298 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. FT METAL 358 358 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. FT METAL 361 361 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. SQ SEQUENCE 417 AA; 45286 MW; FEC10AF1ECA78D49 CRC64; MTLAEKILSQ KAGRKVEPGE FLLLEPDIAL ANDITAPLAI KKFKEYGGKK VKYPDRVVLV PDHFTPNKDI KSAMQVKMMR EFAREQGIEK FFEIGRMGIE HVLLPEEGIV KSGDLVVGAD SHTCTYGALG AFATGVGSTD IAGFYLIGKV WFRVPESIKV TLRGKFKDLV TAKDLVLKLI SILGVDGANY KAIEFSGPGV KEISMDGRFT ISNMAIEAGG KTGLFPVDEI TIAYERERGI EVEEMYPDED AKYVREVEMD LSELEPQVAY PFLPSNAKDV SEAEKERIKI DQAVIGSCTN GRIEDLRLAA QILKGRTVSP DVRCIIIPGS QKVYKQALKE GLIDIFIDAG CAVSTPTCGP CLGGHMGVLA EGEVAISTTN RNFVGRMGHP NSKVFLASPA VAAASAIKGY IADPRKL // ID KTHY_THEMA Reviewed; 197 AA. AC Q9X0I3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=Thymidylate kinase; DE EC=2.7.4.9; DE AltName: Full=dTMP kinase; GN Name=tmk; OrderedLocusNames=TM_1099; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and CC salvage pathways of dTTP synthesis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + dTMP = ADP + dTDP. CC -!- SIMILARITY: Belongs to the thymidylate kinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36175.1; -; Genomic_DNA. DR PIR; E72294; E72294. DR RefSeq; NP_228905.1; NC_000853.1. DR RefSeq; WP_004080341.1; NZ_CP011107.1. DR PDB; 3HJN; X-ray; 2.10 A; A/B=1-197. DR PDBsum; 3HJN; -. DR ProteinModelPortal; Q9X0I3; -. DR SMR; Q9X0I3; 1-192. DR STRING; 243274.TM1099; -. DR EnsemblBacteria; AAD36175; AAD36175; TM_1099. DR GeneID; 898666; -. DR KEGG; tma:TM1099; -. DR PATRIC; 23937131; VBITheMar51294_1114. DR eggNOG; ENOG4108ZMD; Bacteria. DR eggNOG; COG0125; LUCA. DR InParanoid; Q9X0I3; -. DR KO; K00943; -. DR OMA; GGIDIAE; -. DR OrthoDB; EOG64JFSH; -. DR EvolutionaryTrace; Q9X0I3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central. DR GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central. DR GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central. DR GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central. DR GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central. DR GO; GO:0046939; P:nucleotide phosphorylation; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00165; Thymidylate_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR018095; Thymidylate_kin_CS. DR InterPro; IPR018094; Thymidylate_kinase. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00041; DTMP_kinase; 1. DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Kinase; KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 197 Thymidylate kinase. FT /FTId=PRO_0000155359. FT NP_BIND 7 14 ATP. {ECO:0000255}. FT STRAND 2 6 {ECO:0000244|PDB:3HJN}. FT HELIX 13 26 {ECO:0000244|PDB:3HJN}. FT STRAND 31 37 {ECO:0000244|PDB:3HJN}. FT HELIX 41 52 {ECO:0000244|PDB:3HJN}. FT HELIX 57 79 {ECO:0000244|PDB:3HJN}. FT TURN 80 82 {ECO:0000244|PDB:3HJN}. FT STRAND 84 89 {ECO:0000244|PDB:3HJN}. FT HELIX 91 98 {ECO:0000244|PDB:3HJN}. FT TURN 99 102 {ECO:0000244|PDB:3HJN}. FT HELIX 106 117 {ECO:0000244|PDB:3HJN}. FT STRAND 123 129 {ECO:0000244|PDB:3HJN}. FT HELIX 132 138 {ECO:0000244|PDB:3HJN}. FT HELIX 148 164 {ECO:0000244|PDB:3HJN}. FT TURN 166 168 {ECO:0000244|PDB:3HJN}. FT STRAND 169 173 {ECO:0000244|PDB:3HJN}. FT HELIX 178 189 {ECO:0000244|PDB:3HJN}. SQ SEQUENCE 197 AA; 22849 MW; 302D2EF3BAB6658E CRC64; MFITFEGIDG SGKSTQIQLL AQYLEKRGKK VILKREPGGT ETGEKIRKIL LEEEVTPKAE LFLFLASRNL LVTEIKQYLS EGYAVLLDRY TDSSVAYQGF GRNLGKEIVE ELNDFATDGL IPDLTFYIDV DVETALKRKG ELNRFEKREF LERVREGYLV LAREHPERIV VLDGKRSIEE IHRDVVREVK RRWKLDV // ID LEUC1_THEMA Reviewed; 418 AA. AC Q9WYC7; DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=3-isopropylmalate dehydratase large subunit 1 {ECO:0000255|HAMAP-Rule:MF_01027}; DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01027}; DE AltName: Full=Alpha-IPM isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01027}; DE Short=IPMI 1 {ECO:0000255|HAMAP-Rule:MF_01027}; DE AltName: Full=Isopropylmalate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01027}; GN Name=leuC1 {ECO:0000255|HAMAP-Rule:MF_01027}; GN OrderedLocusNames=TM_0291; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate. CC {ECO:0000255|HAMAP-Rule:MF_01027}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. {ECO:0000255|HAMAP-Rule:MF_01027}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01027}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01027}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_01027}. CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP- CC Rule:MF_01027}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC CC type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_01027}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35379.1; -; Genomic_DNA. DR PIR; C72394; C72394. DR RefSeq; NP_228103.1; NC_000853.1. DR RefSeq; WP_004083007.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYC7; -. DR STRING; 243274.TM0291; -. DR EnsemblBacteria; AAD35379; AAD35379; TM_0291. DR GeneID; 897215; -. DR KEGG; tma:TM0291; -. DR PATRIC; 23935461; VBITheMar51294_0296. DR eggNOG; ENOG4105CQI; Bacteria. DR eggNOG; COG0065; LUCA. DR InParanoid; Q9WYC7; -. DR KO; K01703; -. DR OMA; GADALMF; -. DR OrthoDB; EOG600DP5; -. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.499.10; -; 2. DR Gene3D; 3.40.1060.10; -; 1. DR HAMAP; MF_01027; LeuC_type2; 1. DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok. DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu. DR PANTHER; PTHR11670; PTHR11670; 1. DR Pfam; PF00330; Aconitase; 1. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF53732; SSF53732; 1. DR TIGRFAMs; TIGR01343; hacA_fam; 1. DR TIGRFAMs; TIGR02086; IPMI_arch; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding; KW Reference proteome. FT CHAIN 1 418 3-isopropylmalate dehydratase large FT subunit 1. FT /FTId=PRO_0000076860. FT METAL 298 298 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. FT METAL 358 358 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. FT METAL 361 361 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. SQ SEQUENCE 418 AA; 45447 MW; 18D41B4BFAA825BF CRC64; MGKTLAEKIF SEHVGRDVKA GEIVLARVDI AMAQDGTGPL MINEFRELGF KEVKVPKAFL FIDHASPSPR KELSNSQKMM REFGKEMGVK VFDAGDGISH QILAEKYVKP GDLVAGADSH TCTAGGLGAF GTGMGSTDVA IIFGLGQNWF KVPETIKVVV NGKLQDGVYA KDIILEIARI LGSDGATYKA LEFHGSCIEN MNVEDRLTIS NMAVEVGAKA GLMPSDEKTR EFLKKMGREE DFRELKADPD AVYETEIEID ATTLEPLVSL PHYVDNVRKV SEVEKEKIKI DQVFIGTCTN GRLQDLEIAL KILEKHGKHP DVRLIVGPAS RKVYMDALEK GIIKKFVELG AAVIPPGCGP CVGIHMGVLG DGERVLSTQN RNFKGRMGNP NAEIYLASPA TAAATAVTGY ITDPRRFI // ID LDH_THEMA Reviewed; 319 AA. AC P16115; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 13-APR-2016, entry version 139. DE RecName: Full=L-lactate dehydrogenase; DE Short=L-LDH; DE EC=1.1.1.27; GN Name=ldh; OrderedLocusNames=TM_1867; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8404889; DOI=10.1111/j.1432-1033.1993.tb18190.x; RA Ostendorp R., Liebl W., Schurig H., Jaenicke R.; RT "The L-lactate dehydrogenase gene of the hyperthermophilic bacterium RT Thermotoga maritima cloned by complementation in Escherichia coli."; RL Eur. J. Biochem. 216:709-715(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP PROTEIN SEQUENCE OF 1-31. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=2318202; DOI=10.1111/j.1432-1033.1990.tb15388.x; RA Wrba A., Jaenicke R., Huber R., Stetter K.O.; RT "Lactate dehydrogenase from the extreme thermophile Thermotoga RT maritima."; RL Eur. J. Biochem. 188:195-201(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NAD. RX PubMed=9655830; DOI=10.1016/S0969-2126(98)00078-1; RA Auerbach G., Ostendorp R., Prade L., Korndorfer I., Dams T., Huber R., RA Jaenicke R.; RT "Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga RT maritima: the crystal structure at 2.1-A resolution reveals strategies RT for intrinsic protein stabilization."; RL Structure 6:769-781(1998). CC -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)- CC lactate from pyruvate: step 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9655830}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X74302; CAA52355.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36929.1; -; Genomic_DNA. DR PIR; S36863; S36863. DR RefSeq; NP_229663.1; NC_000853.1. DR RefSeq; WP_004082418.1; NZ_CP011107.1. DR PDB; 1A5Z; X-ray; 2.10 A; A=1-319. DR PDBsum; 1A5Z; -. DR ProteinModelPortal; P16115; -. DR SMR; P16115; 1-312. DR STRING; 243274.TM1867; -. DR EnsemblBacteria; AAD36929; AAD36929; TM_1867. DR GeneID; 897800; -. DR KEGG; tma:TM1867; -. DR PATRIC; 23938723; VBITheMar51294_1888. DR eggNOG; ENOG4105C80; Bacteria. DR eggNOG; COG0039; LUCA. DR InParanoid; P16115; -. DR KO; K00016; -. DR OMA; AGDYEDC; -. DR OrthoDB; EOG6091FG; -. DR UniPathway; UPA00554; UER00611. DR EvolutionaryTrace; P16115; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR HAMAP; MF_00488; Lactate_dehydrog; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR011304; L-lactate_DH. DR InterPro; IPR018177; L-lactate_DH_AS. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR011275; Malate_DH_type3. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11540; PTHR11540; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF56327; SSF56327; 1. DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1. DR PROSITE; PS00064; L_LDH; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1 319 L-lactate dehydrogenase. FT /FTId=PRO_0000168406. FT NP_BIND 9 37 NAD. {ECO:0000269|PubMed:9655830}. FT ACT_SITE 172 172 Proton acceptor. FT BINDING 85 85 Substrate. {ECO:0000250}. FT BINDING 117 117 NAD or substrate. {ECO:0000250}. FT BINDING 148 148 Substrate. {ECO:0000250}. FT BINDING 226 226 Substrate. {ECO:0000250}. FT MOD_RES 217 217 Phosphotyrosine. {ECO:0000250}. FT CONFLICT 14 14 Missing (in Ref. 3; AA sequence). FT {ECO:0000305}. FT STRAND 2 6 {ECO:0000244|PDB:1A5Z}. FT HELIX 10 22 {ECO:0000244|PDB:1A5Z}. FT STRAND 26 31 {ECO:0000244|PDB:1A5Z}. FT HELIX 35 48 {ECO:0000244|PDB:1A5Z}. FT HELIX 49 51 {ECO:0000244|PDB:1A5Z}. FT STRAND 56 59 {ECO:0000244|PDB:1A5Z}. FT HELIX 62 65 {ECO:0000244|PDB:1A5Z}. FT STRAND 69 73 {ECO:0000244|PDB:1A5Z}. FT HELIX 85 106 {ECO:0000244|PDB:1A5Z}. FT STRAND 111 114 {ECO:0000244|PDB:1A5Z}. FT STRAND 116 118 {ECO:0000244|PDB:1A5Z}. FT HELIX 119 130 {ECO:0000244|PDB:1A5Z}. FT TURN 134 136 {ECO:0000244|PDB:1A5Z}. FT STRAND 137 139 {ECO:0000244|PDB:1A5Z}. FT HELIX 143 157 {ECO:0000244|PDB:1A5Z}. FT HELIX 161 163 {ECO:0000244|PDB:1A5Z}. FT STRAND 168 170 {ECO:0000244|PDB:1A5Z}. FT HELIX 180 182 {ECO:0000244|PDB:1A5Z}. FT HELIX 190 194 {ECO:0000244|PDB:1A5Z}. FT STRAND 197 199 {ECO:0000244|PDB:1A5Z}. FT HELIX 202 223 {ECO:0000244|PDB:1A5Z}. FT HELIX 228 242 {ECO:0000244|PDB:1A5Z}. FT STRAND 247 258 {ECO:0000244|PDB:1A5Z}. FT STRAND 263 273 {ECO:0000244|PDB:1A5Z}. FT STRAND 276 280 {ECO:0000244|PDB:1A5Z}. FT HELIX 287 308 {ECO:0000244|PDB:1A5Z}. SQ SEQUENCE 319 AA; 34994 MW; A1FB9B97CDCF290B CRC64; MKIGIVGLGR VGSSTAFALL MKGFAREMVL IDVDKKRAEG DALDLIHGTP FTRRANIYAG DYADLKGSDV VIVAAGVPQK PGETRLQLLG RNARVMKEIA RNVSKYAPDS IVIVVTNPVD VLTYFFLKES GMDPRKVFGS GTVLDTARLR TLIAQHCGFS PRSVHVYVIG EHGDSEVPVW SGAMIGGIPL QNMCQICQKC DSKILENFAE KTKRAAYEII ERKGATHYAI ALAVADIVES IFFDEKRVLT LSVYLEDYLG VKDLCISVPV TLGKHGVERI LELNLNEEEL EAFRKSASIL KNAINEITAE ENKHQNTSG // ID LEPA_THEMA Reviewed; 621 AA. AC Q9X1V8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 108. DE RecName: Full=Elongation factor 4 {ECO:0000255|HAMAP-Rule:MF_00071}; DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_00071}; DE EC=3.6.5.n1 {ECO:0000255|HAMAP-Rule:MF_00071}; DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000255|HAMAP-Rule:MF_00071}; GN Name=lepA {ECO:0000255|HAMAP-Rule:MF_00071}; GN OrderedLocusNames=TM_1623; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Required for accurate and efficient protein synthesis CC under certain stress conditions. May act as a fidelity factor of CC the translation reaction, by catalyzing a one-codon backward CC translocation of tRNAs on improperly translocated ribosomes. Back- CC translocation proceeds from a post-translocation (POST) complex to CC a pre-translocation (PRE) complex, thus giving elongation factor G CC a second chance to translocate the tRNAs correctly. Binds to CC ribosomes in a GTP-dependent manner. {ECO:0000255|HAMAP- CC Rule:MF_00071}. CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00071}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00071}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00071}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_00071}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. LepA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00071}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36690.1; -; Genomic_DNA. DR PIR; A72233; A72233. DR RefSeq; NP_229423.1; NC_000853.1. DR RefSeq; WP_010865372.1; NC_000853.1. DR ProteinModelPortal; Q9X1V8; -. DR SMR; Q9X1V8; 20-567. DR STRING; 243274.TM1623; -. DR EnsemblBacteria; AAD36690; AAD36690; TM_1623. DR GeneID; 897378; -. DR KEGG; tma:TM1623; -. DR PATRIC; 23938220; VBITheMar51294_1642. DR eggNOG; ENOG4105C4S; Bacteria. DR eggNOG; COG0481; LUCA. DR InParanoid; Q9X1V8; -. DR KO; K03596; -. DR OMA; KPMVFCG; -. DR OrthoDB; EOG6ZKXQ4; -. DR BioCyc; TMAR243274:GC6P-1669-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00071; LepA; 1. DR InterPro; IPR006297; EF-4. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR013842; LepA_GTP-bd_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF06421; LepA_C; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR01393; lepA; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; GTP-binding; KW Hydrolase; Membrane; Nucleotide-binding; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 621 Elongation factor 4. FT /FTId=PRO_0000176362. FT DOMAIN 21 203 tr-type G. FT NP_BIND 33 38 GTP. {ECO:0000255|HAMAP-Rule:MF_00071}. FT NP_BIND 150 153 GTP. {ECO:0000255|HAMAP-Rule:MF_00071}. SQ SEQUENCE 621 AA; 70086 MW; 71571406B1A1BD72 CRC64; MVKFKREVNF SGGDRGVYRP DLIRNICIIA HIDHGKTTLV DRILEITNTV DRRKMREQYL DMMDIERERG ITIKAQPVKV MYTAEDGNTY EINIIDTPGH VDFSYEVGRS MAACEGAILL VDATQGVEAQ TVAHTYLAIE HDLEIIPVIN KIDLPNANIE ETALEIKDLL GVSENEILLV SAKEGTGVKE LLEAIVKRVP PPKGDINGKL KALIFDAKYD NYKGVIVHVR LFDGQVKPGD KIMTFSNKKV YEVQEVGVFL PEMEPVDSLS AGEVGYIIAG IKEVSDARVG DTITSANDPV DEALPGYREI KPMVFAGMFP GLPEYYEELR KALEKLKLND SALYFEPTMS PAMGFGFRCG FLGPLHMEVV RERIEREFDL AVILTAPNVR YRVKLRNGEE IEITDPSKFP DEGEILEAYE PYVDLSIITP SEYIGAIINL VQNEKRGELR ITENAGKNRV ILRFDAPLAE IIYDFFDRMK AVSRGYASMD YEFKEYRRSD LVKVTILVNK EPVDALSFIV HRSKAYQMAR KIVEKLKDLI PRHQFQIPIQ AKAGGRIIAR ADIKALRKDV LAKCYGGDVT RKMKLLEKQK EGKKKLREIG RVTIPQEAFL ALLKIGGEDE K // ID LEU3_THEMA Reviewed; 354 AA. AC Q9WZ26; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 123. DE RecName: Full=3-isopropylmalate dehydrogenase; DE EC=1.1.1.85; DE AltName: Full=3-IPM-DH; DE AltName: Full=Beta-IPM dehydrogenase; DE Short=IMDH; GN Name=leuB; OrderedLocusNames=TM_0556; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- CC methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- CC oxopentanoate. The product decarboxylates to 4-methyl-2 CC oxopentanoate. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl- CC 2-oxopentanoate + CO(2) + NADH. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 3/4. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35641.1; -; Genomic_DNA. DR PIR; B72363; B72363. DR RefSeq; NP_228366.1; NC_000853.1. DR RefSeq; WP_004081326.1; NZ_CP011107.1. DR PDB; 1VLC; X-ray; 1.90 A; A=1-354. DR PDBsum; 1VLC; -. DR ProteinModelPortal; Q9WZ26; -. DR SMR; Q9WZ26; 1-354. DR STRING; 243274.TM0556; -. DR EnsemblBacteria; AAD35641; AAD35641; TM_0556. DR GeneID; 897614; -. DR KEGG; tma:TM0556; -. DR PATRIC; 23936019; VBITheMar51294_0564. DR eggNOG; ENOG4105C0C; Bacteria. DR eggNOG; COG0473; LUCA. DR InParanoid; Q9WZ26; -. DR KO; K00052; -. DR OMA; RRPKQFD; -. DR OrthoDB; EOG65N1BN; -. DR UniPathway; UPA00048; UER00072. DR EvolutionaryTrace; Q9WZ26; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.718.10; -; 1. DR HAMAP; MF_01033; LeuB_type1; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR InterPro; IPR004429; Isopropylmalate_DH. DR PANTHER; PTHR11835; PTHR11835; 1. DR Pfam; PF00180; Iso_dh; 1. DR SMART; SM01329; Iso_dh; 1. DR TIGRFAMs; TIGR00169; leuB; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm; KW Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; KW Oxidoreductase; Reference proteome. FT CHAIN 1 354 3-isopropylmalate dehydrogenase. FT /FTId=PRO_0000083771. FT NP_BIND 74 87 NAD. {ECO:0000250}. FT NP_BIND 275 287 NAD. {ECO:0000250}. FT METAL 219 219 Magnesium or manganese. {ECO:0000250}. FT METAL 243 243 Magnesium or manganese. {ECO:0000250}. FT METAL 247 247 Magnesium or manganese. {ECO:0000250}. FT BINDING 95 95 Substrate. {ECO:0000250}. FT BINDING 105 105 Substrate. {ECO:0000250}. FT BINDING 134 134 Substrate. {ECO:0000250}. FT BINDING 219 219 Substrate. {ECO:0000250}. FT SITE 141 141 Important for catalysis. {ECO:0000250}. FT SITE 187 187 Important for catalysis. {ECO:0000250}. FT STRAND 1 9 {ECO:0000244|PDB:1VLC}. FT HELIX 11 30 {ECO:0000244|PDB:1VLC}. FT STRAND 33 38 {ECO:0000244|PDB:1VLC}. FT HELIX 43 49 {ECO:0000244|PDB:1VLC}. FT STRAND 50 53 {ECO:0000244|PDB:1VLC}. FT HELIX 55 63 {ECO:0000244|PDB:1VLC}. FT STRAND 64 71 {ECO:0000244|PDB:1VLC}. FT HELIX 75 77 {ECO:0000244|PDB:1VLC}. FT HELIX 86 89 {ECO:0000244|PDB:1VLC}. FT HELIX 91 97 {ECO:0000244|PDB:1VLC}. FT STRAND 102 108 {ECO:0000244|PDB:1VLC}. FT HELIX 111 116 {ECO:0000244|PDB:1VLC}. FT STRAND 117 119 {ECO:0000244|PDB:1VLC}. FT HELIX 121 124 {ECO:0000244|PDB:1VLC}. FT STRAND 129 135 {ECO:0000244|PDB:1VLC}. FT HELIX 139 141 {ECO:0000244|PDB:1VLC}. FT STRAND 143 148 {ECO:0000244|PDB:1VLC}. FT STRAND 153 156 {ECO:0000244|PDB:1VLC}. FT HELIX 161 176 {ECO:0000244|PDB:1VLC}. FT TURN 177 179 {ECO:0000244|PDB:1VLC}. FT STRAND 180 186 {ECO:0000244|PDB:1VLC}. FT TURN 188 190 {ECO:0000244|PDB:1VLC}. FT HELIX 192 205 {ECO:0000244|PDB:1VLC}. FT STRAND 211 217 {ECO:0000244|PDB:1VLC}. FT HELIX 218 227 {ECO:0000244|PDB:1VLC}. FT HELIX 229 231 {ECO:0000244|PDB:1VLC}. FT STRAND 233 237 {ECO:0000244|PDB:1VLC}. FT HELIX 239 249 {ECO:0000244|PDB:1VLC}. FT STRAND 252 254 {ECO:0000244|PDB:1VLC}. FT HELIX 256 258 {ECO:0000244|PDB:1VLC}. FT STRAND 260 274 {ECO:0000244|PDB:1VLC}. FT TURN 278 284 {ECO:0000244|PDB:1VLC}. FT HELIX 289 303 {ECO:0000244|PDB:1VLC}. FT HELIX 306 321 {ECO:0000244|PDB:1VLC}. FT HELIX 327 329 {ECO:0000244|PDB:1VLC}. FT HELIX 333 335 {ECO:0000244|PDB:1VLC}. FT HELIX 339 353 {ECO:0000244|PDB:1VLC}. SQ SEQUENCE 354 AA; 39190 MW; 2C93ACBF888A0D38 CRC64; MKIAVLPGDG IGPEVVREAL KVLEVVEKKT GKTFEKVFGH IGGDAIDRFG EPLPEETKKI CLEADAIFLG SVGGPKWDDL PPEKRPEIGG LLALRKMLNL YANIRPIKVY RSLVHVSPLK EKVIGSGVDL VTVRELSYGV YYGQPRGLDE EKGFDTMIYD RKTVERIART AFEIAKNRRK KVTSVDKANV LYSSMLWRKV VNEVAREYPD VELTHIYVDN AAMQLILKPS QFDVILTTNM FGDILSDESA ALPGSLGLLP SASFGDKNLY EPAGGSAPDI AGKNIANPIA QILSLAMMLE HSFGMVEEAR KIERAVELVI EEGYRTRDIA EDPEKAVSTS QMGDLICKKL EEIW // ID LEUD1_THEMA Reviewed; 166 AA. AC Q9WYC8; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=3-isopropylmalate dehydratase small subunit 1; DE EC=4.2.1.33; DE AltName: Full=Alpha-IPM isomerase 1; DE Short=IPMI 1; DE AltName: Full=Isopropylmalate isomerase 1; GN Name=leuD1; OrderedLocusNames=TM_0292; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35380.1; -; Genomic_DNA. DR PIR; D72394; D72394. DR RefSeq; NP_228104.1; NC_000853.1. DR RefSeq; WP_004083008.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYC8; -. DR STRING; 243274.TM0292; -. DR EnsemblBacteria; AAD35380; AAD35380; TM_0292. DR GeneID; 897216; -. DR KEGG; tma:TM0292; -. DR PATRIC; 23935463; VBITheMar51294_0297. DR eggNOG; ENOG4105MQS; Bacteria. DR eggNOG; COG0066; LUCA. DR InParanoid; Q9WYC8; -. DR KO; K01704; -. DR OMA; ARHVMED; -. DR OrthoDB; EOG6PZXB8; -. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.19.10; -; 1. DR HAMAP; MF_01032; LeuD_type2; 1. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl. DR InterPro; IPR011827; LeuD_type2/HacB/DmdB. DR PANTHER; PTHR11670; PTHR11670; 1. DR Pfam; PF00694; Aconitase_C; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR TIGRFAMs; TIGR02087; LEUD_arch; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Leucine biosynthesis; Lyase; Reference proteome. FT CHAIN 1 166 3-isopropylmalate dehydratase small FT subunit 1. FT /FTId=PRO_0000141927. SQ SEQUENCE 166 AA; 18734 MW; D8ACF340205111A4 CRC64; MIRGRVWKFG DNISTDHIAP GRYFHLRNNL EELAKHVLED AMEDFAKKVQ KGDIIVAGKN FGLGSSREHA ARIIKIAGVS CIVAKSFARI FYRNAINVGL PVIELKEVDE INQGDELEID LENGVLKNLT TGKEYRFTPI PKFLLEILKE DGIVNYLKKH GSFPKV // ID LGT_THEMA Reviewed; 293 AA. AC Q9WY05; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=Prolipoprotein diacylglyceryl transferase {ECO:0000255|HAMAP-Rule:MF_01147}; DE EC=2.4.99.- {ECO:0000255|HAMAP-Rule:MF_01147}; GN Name=lgt {ECO:0000255|HAMAP-Rule:MF_01147}; OrderedLocusNames=TM_0158; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Transfers the N-acyl diglyceride group on what will CC become the N-terminal cysteine of membrane lipoproteins. CC {ECO:0000255|HAMAP-Rule:MF_01147}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis CC (diacylglyceryl transfer). {ECO:0000255|HAMAP-Rule:MF_01147}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01147}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01147}. CC -!- SIMILARITY: Belongs to the Lgt family. {ECO:0000255|HAMAP- CC Rule:MF_01147}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35251.1; -; Genomic_DNA. DR PIR; D72410; D72410. DR RefSeq; NP_227973.1; NC_000853.1. DR RefSeq; WP_004082778.1; NZ_CP011107.1. DR STRING; 243274.TM0158; -. DR EnsemblBacteria; AAD35251; AAD35251; TM_0158. DR GeneID; 896996; -. DR KEGG; tma:TM0158; -. DR PATRIC; 23935162; VBITheMar51294_0158. DR eggNOG; ENOG4105C3B; Bacteria. DR eggNOG; COG0682; LUCA. DR InParanoid; Q9WY05; -. DR KO; K13292; -. DR OMA; FEYFHPT; -. DR OrthoDB; EOG6MH5CQ; -. DR UniPathway; UPA00664; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008961; F:phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009249; P:protein lipoylation; IEA:InterPro. DR HAMAP; MF_01147; Lgt; 1. DR InterPro; IPR001640; Prolipoprot_diAcglycer_Trfase. DR Pfam; PF01790; LGT; 1. DR TIGRFAMs; TIGR00544; lgt; 1. DR PROSITE; PS01311; LGT; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 293 Prolipoprotein diacylglyceryl FT transferase. FT /FTId=PRO_0000172701. FT TRANSMEM 4 26 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 47 66 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 81 103 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 115 137 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 205 224 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 231 249 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 264 283 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. SQ SEQUENCE 293 AA; 34001 MW; 98562A2D27AFDBEF CRC64; MKKILAFLLI AAGSTLFFVF LFIFLSKVFS GEILLSRYIF RIGGFELRWY STLILMGFLI SYFVARKRAK NEGINLEEFD ELIFYGVIAG IVGARLYYVL FNLKYYRSLW DALKIWEGGL AIHGAVIGAL LTGFLYVRLK KPSFTFLQAT DLFTSVLPLG QAIGRWGNFF NYEAFGVPTN LPWKMFVPEP YRPVVYKDYS FFHPTFLYES IWDLLVFFML SVYFKRYRKR HGEVTCLYFV LYSLGRIVIE RLRVDSLMIG NIKAAQLLSA VLILLGFTGF LILRSSQEPK RAF // ID LEU1_THEMA Reviewed; 513 AA. AC Q9WZ23; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=2-isopropylmalate synthase; DE EC=2.3.3.13; DE AltName: Full=Alpha-IPM synthase; DE AltName: Full=Alpha-isopropylmalate synthase; GN Name=leuA; OrderedLocusNames=TM_0553; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of CC acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form CC 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = CC (2S)-2-isopropylmalate + CoA. CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 1/4. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase CC family. LeuA type 1 subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35638.1; -; Genomic_DNA. DR PIR; G72362; G72362. DR RefSeq; NP_228363.1; NC_000853.1. DR RefSeq; WP_004081333.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ23; -. DR STRING; 243274.TM0553; -. DR EnsemblBacteria; AAD35638; AAD35638; TM_0553. DR GeneID; 897611; -. DR KEGG; tma:TM0553; -. DR PATRIC; 23936013; VBITheMar51294_0561. DR eggNOG; ENOG4105CYQ; Bacteria. DR eggNOG; COG0119; LUCA. DR InParanoid; Q9WZ23; -. DR KO; K01649; -. DR OMA; MAIKTRQ; -. DR OrthoDB; EOG6CGCF3; -. DR UniPathway; UPA00048; UER00070. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01025; LeuA_type1; 1. DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer. DR InterPro; IPR002034; AIPM/Hcit_synth_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005671; LeuA_bact_synth. DR InterPro; IPR000891; PYR_CT. DR Pfam; PF00682; HMGL-like; 1. DR Pfam; PF08502; LeuA_dimer; 1. DR SMART; SM00917; LeuA_dimer; 1. DR SUPFAM; SSF110921; SSF110921; 1. DR TIGRFAMs; TIGR00973; leuA_bact; 1. DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1. DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Leucine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 513 2-isopropylmalate synthase. FT /FTId=PRO_0000140391. SQ SEQUENCE 513 AA; 56805 MW; 08EBF526E5BD4502 CRC64; MRRIKIFDTT LRDGEQSPGA SMSIEEKVEM ALMLEDLGVD LIEAGFPVSS PVQFEAVKRV ASAVQKPIVV GLARCVEKDI DAAYEALKDR PKDKRMIHVF IATSPIHRKY KLRMEKEEIL ERIRRYVGYA KQFFDLVEFS AEDASRTEVP FLIEAYKTAI EAGATTINVP DTVGYALPDE FGELIKTLRE GVPGIENVDL SVHCHNDLGL AVANSLAAVQ NGATQVEVTL NGIGERAGNC ALEEFVMILK VRKDKLPYET GIKTELIYPA SRLLTHITGL IPSRNKPIVG ENVFLHESGI HQDGVLKHRE TYEIMKPSDI GRSSETLVLG RHSGKHALRK KLETYGIKLD EETFQKVFEK FTELADRKKE VYDDDLFSIV SEVLREPING YKLVHFHVHT GNTLLPTAAV VLQVGNEKRE AAEAGNGPVD AIFKAIDKAL GIQPKLEEYI IQAVGTGKNA QGEVKLTLRI DNELYSGRGV STDIVEASAI AYINAINKYL IAKGLLRKNG GAE // ID LEUD2_THEMA Reviewed; 166 AA. AC Q9WZ25; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=3-isopropylmalate dehydratase small subunit 2; DE EC=4.2.1.33; DE AltName: Full=Alpha-IPM isomerase 2; DE Short=IPMI 2; DE AltName: Full=Isopropylmalate isomerase 2; GN Name=leuD2; OrderedLocusNames=TM_0555; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35640.1; -; Genomic_DNA. DR PIR; A72363; A72363. DR RefSeq; NP_228365.1; NC_000853.1. DR RefSeq; WP_010865146.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ25; -. DR STRING; 243274.TM0555; -. DR EnsemblBacteria; AAD35640; AAD35640; TM_0555. DR GeneID; 897613; -. DR KEGG; tma:TM0555; -. DR KEGG; tmi:THEMA_01900; -. DR KEGG; tmw:THMA_0568; -. DR PATRIC; 23936017; VBITheMar51294_0563. DR eggNOG; ENOG4105MQS; Bacteria. DR eggNOG; COG0066; LUCA. DR InParanoid; Q9WZ25; -. DR KO; K01704; -. DR OMA; EYRIRPY; -. DR OrthoDB; EOG6PZXB8; -. DR BioCyc; TMAR243274:GC6P-579-MONOMER; -. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.19.10; -; 1. DR HAMAP; MF_01032; LeuD_type2; 1. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl. DR InterPro; IPR011824; LeuD/DmdB_bac. DR InterPro; IPR011827; LeuD_type2/HacB/DmdB. DR PANTHER; PTHR11670; PTHR11670; 1. DR Pfam; PF00694; Aconitase_C; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR TIGRFAMs; TIGR02084; leud; 1. DR TIGRFAMs; TIGR02087; LEUD_arch; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Leucine biosynthesis; Lyase; Reference proteome. FT CHAIN 1 166 3-isopropylmalate dehydratase small FT subunit 2. FT /FTId=PRO_0000141928. SQ SEQUENCE 166 AA; 18451 MW; BE56CDCEB6B0D22F CRC64; MVVKIKGKVF VFGDNVNTDE IIPARYLNTS DPQELAKYCM EDARPGFGRR DDIKGSIIVA GENFGCGSSR EHAPVAIKAA GISCVIAKSF ARIFFRNAIN IGLPIVELKE ADEFEEGDIA EVDLENGVVR NLTKGKEYRI RPYPEFLMKI MEAGGWLEYC LKEVGE // ID LEXA_THEMA Reviewed; 197 AA. AC O33927; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 13-APR-2016, entry version 125. DE RecName: Full=LexA repressor {ECO:0000255|HAMAP-Rule:MF_00015}; DE EC=3.4.21.88 {ECO:0000255|HAMAP-Rule:MF_00015}; GN Name=lexA {ECO:0000255|HAMAP-Rule:MF_00015}; GN OrderedLocusNames=TM_1082; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9380682; DOI=10.1073/pnas.94.20.10606; RA Guipaud O., Marguet E., Noll K.M., Bouthier de la Tour C., RA Forterre P.; RT "Both DNA gyrase and reverse gyrase are present in the RT hyperthermophilic bacterium Thermotoga maritima."; RL Proc. Natl. Acad. Sci. U.S.A. 94:10606-10611(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Represses a number of genes involved in the response to CC DNA damage (SOS response), including recA and lexA. In the CC presence of single-stranded DNA, RecA interacts with LexA causing CC an autocatalytic cleavage which disrupts the DNA-binding part of CC LexA, leading to derepression of the SOS regulon and eventually CC DNA repair. {ECO:0000255|HAMAP-Rule:MF_00015}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of Ala-|-Gly bond in repressor CC LexA. {ECO:0000255|HAMAP-Rule:MF_00015}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00015}. CC -!- MISCELLANEOUS: No consensus sequence similar to the SOS-box from CC E.coli or from B.subtilis was found upstream of the lexA gene, CC suggesting the presence of another target sequence specific for CC the Thermotogales. CC -!- SIMILARITY: Belongs to the peptidase S24 family. CC {ECO:0000255|HAMAP-Rule:MF_00015}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U76417; AAB87145.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36159.1; -; Genomic_DNA. DR PIR; B72297; B72297. DR RefSeq; NP_228888.1; NC_000853.1. DR RefSeq; WP_004080401.1; NZ_CP011107.1. DR PDB; 3K2Z; X-ray; 1.37 A; A/B=3-197. DR PDBsum; 3K2Z; -. DR ProteinModelPortal; O33927; -. DR STRING; 243274.TM1082; -. DR MEROPS; S24.001; -. DR DNASU; 897745; -. DR EnsemblBacteria; AAD36159; AAD36159; TM_1082. DR GeneID; 897745; -. DR KEGG; tma:TM1082; -. DR PATRIC; 23937093; VBITheMar51294_1095. DR eggNOG; ENOG4105DS7; Bacteria. DR eggNOG; COG1974; LUCA. DR InParanoid; O33927; -. DR KO; K01356; -. DR OMA; GVNDHLK; -. DR OrthoDB; EOG6JHRHJ; -. DR EvolutionaryTrace; O33927; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 2.10.109.10; -; 1. DR HAMAP; MF_00015; LexA; 1. DR InterPro; IPR006200; LexA. DR InterPro; IPR006199; LexA_DNA-bd_dom. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR006197; Peptidase_S24_LexA. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01726; LexA_DNA_bind; 1. DR Pfam; PF00717; Peptidase_S24; 1. DR PRINTS; PR00726; LEXASERPTASE. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF51306; SSF51306; 1. DR TIGRFAMs; TIGR00498; lexA; 1. PE 1: Evidence at protein level; KW 3D-structure; Autocatalytic cleavage; Complete proteome; DNA damage; KW DNA repair; DNA replication; DNA-binding; Hydrolase; KW Reference proteome; Repressor; SOS response; Transcription; KW Transcription regulation. FT CHAIN 1 197 LexA repressor. FT /FTId=PRO_0000170098. FT DNA_BIND 28 47 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00015}. FT ACT_SITE 119 119 For autocatalytic cleavage activity. FT {ECO:0000255|HAMAP-Rule:MF_00015}. FT ACT_SITE 156 156 For autocatalytic cleavage activity. FT {ECO:0000255|HAMAP-Rule:MF_00015}. FT SITE 83 84 Cleavage; by autolysis. FT {ECO:0000255|HAMAP-Rule:MF_00015}. FT HELIX 6 22 {ECO:0000244|PDB:3K2Z}. FT HELIX 28 35 {ECO:0000244|PDB:3K2Z}. FT HELIX 39 51 {ECO:0000244|PDB:3K2Z}. FT STRAND 54 56 {ECO:0000244|PDB:3K2Z}. FT HELIX 58 60 {ECO:0000244|PDB:3K2Z}. FT STRAND 66 69 {ECO:0000244|PDB:3K2Z}. FT STRAND 74 83 {ECO:0000244|PDB:3K2Z}. FT HELIX 85 87 {ECO:0000244|PDB:3K2Z}. FT STRAND 89 98 {ECO:0000244|PDB:3K2Z}. FT HELIX 101 103 {ECO:0000244|PDB:3K2Z}. FT STRAND 110 114 {ECO:0000244|PDB:3K2Z}. FT HELIX 121 123 {ECO:0000244|PDB:3K2Z}. FT STRAND 130 135 {ECO:0000244|PDB:3K2Z}. FT STRAND 144 149 {ECO:0000244|PDB:3K2Z}. FT STRAND 152 161 {ECO:0000244|PDB:3K2Z}. FT STRAND 164 168 {ECO:0000244|PDB:3K2Z}. FT STRAND 177 180 {ECO:0000244|PDB:3K2Z}. FT HELIX 181 183 {ECO:0000244|PDB:3K2Z}. FT STRAND 185 196 {ECO:0000244|PDB:3K2Z}. SQ SEQUENCE 197 AA; 22864 MW; A8093B0BB3D10BFB CRC64; MKDLTERQRK VLLFIEEFIE KNGYPPSVRE IARRFRITPR GALLHLIALE KKGYIERKNG KPRALRISKS IRNKIPLIGE IRAGEKREAI EYLEDYIEIP ESFLSSGYDH FLLKVKGESM IEEHICDGDL VLVRRQDWAQ NGDIVAAMVD GEVTLKKFYQ RGDTVELRPA NREMSSMFFR AEKVKILGKV VGVFRKL // ID LNT_THEMA Reviewed; 503 AA. AC Q9WZ43; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148}; DE Short=ALP N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_01148}; DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_01148}; GN Name=lnt {ECO:0000255|HAMAP-Rule:MF_01148}; OrderedLocusNames=TM_0573; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Transfers the fatty acyl group on membrane lipoproteins. CC {ECO:0000255|HAMAP-Rule:MF_01148}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl CC transfer). {ECO:0000255|HAMAP-Rule:MF_01148}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01148}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01148}. CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N- CC acyltransferase subfamily. {ECO:0000255|HAMAP-Rule:MF_01148}. CC -!- SIMILARITY: Contains 1 CN hydrolase domain. {ECO:0000255|HAMAP- CC Rule:MF_01148}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35658.1; -; Genomic_DNA. DR PIR; H72359; H72359. DR RefSeq; NP_228383.1; NC_000853.1. DR RefSeq; WP_010865149.1; NC_000853.1. DR ProteinModelPortal; Q9WZ43; -. DR STRING; 243274.TM0573; -. DR EnsemblBacteria; AAD35658; AAD35658; TM_0573. DR GeneID; 897638; -. DR KEGG; tma:TM0573; -. DR PATRIC; 23936055; VBITheMar51294_0582. DR eggNOG; ENOG4105CE8; Bacteria. DR eggNOG; COG0815; LUCA. DR InParanoid; Q9WZ43; -. DR KO; K03820; -. DR OMA; HYLINTL; -. DR OrthoDB; EOG6VTJXM; -. DR BioCyc; TMAR243274:GC6P-597-MONOMER; -. DR UniPathway; UPA00666; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0016410; F:N-acyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR Gene3D; 3.60.110.10; -; 1. DR HAMAP; MF_01148; Lnt; 1. DR InterPro; IPR004563; Apolipo_AcylTrfase. DR InterPro; IPR003010; C-N_Hydrolase. DR Pfam; PF00795; CN_hydrolase; 1. DR SUPFAM; SSF56317; SSF56317; 1. DR TIGRFAMs; TIGR00546; lnt; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. PE 3: Inferred from homology; KW Acyltransferase; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 503 Apolipoprotein N-acyltransferase. FT /FTId=PRO_0000178102. FT TRANSMEM 13 32 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 37 56 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 63 85 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 100 122 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 129 151 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 171 193 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 202 224 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 466 488 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01148}. FT DOMAIN 231 503 CN hydrolase. {ECO:0000255|HAMAP- FT Rule:MF_01148}. SQ SEQUENCE 503 AA; 57394 MW; 4924365E109AE30F CRC64; MNRRRWWRSS ERRWRGLVSL FLSVLSGFLT ALSMPGFLSG ALIWFSLIPL LYAVEGRGVW KRAFLSFVYF FTHVLISFFW VLPTLTENVP LVFGRYPSWL GIVVFVLMGI IEAVPFLGFG FLSYFAPQSI VLKTLYLASV YTIFEYLRGV GELGFTGGRI SEALYSHTGL IQIVSITGTL GLVFLIVSLN VLFYEFLRRR KGLLIFPVIF FVYLLNSSVV HLLPVPERGS FKVVALQPNV PTSLKYSVSS GEMLELLESM TKDFHGSIVI TPEAFFLEDV RYSQKLRELS EENTFVIGFP ADNQNSVFVL EGGRFRKVYS KVKLFPFVEK LPYPRVFGVF SFLKGLSYYE PGRNFSVFNV GESPPLSVQI CFESYFPEVS RAFVKNGSEL LIVVTNDGWF HYKAALLNHF VQGVFRAVET RRQFLQVANT GITGLVDEYG RIVDALPLRV RLAGEFHIKA RKGETFYVRY GDWFFYLSVI LAVVSVFISR MRGERNEGIG IRL // ID MCP1_THEMA Reviewed; 656 AA. AC Q9WYR0; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Methyl-accepting chemotaxis protein 1; GN Name=mcp1; OrderedLocusNames=TM_0429; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP METHYLATION AT GLU-401; GLU-407; GLU-590 AND GLU-596. RX PubMed=16707700; DOI=10.1128/JB.00181-06; RA Perez E., Zheng H., Stock A.M.; RT "Identification of methylation sites in Thermotoga maritima chemotaxis RT receptors."; RL J. Bacteriol. 188:4093-4100(2006). CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the CC concentration of attractants and repellents in the environment, CC transduce a signal from the outside to the inside of the cell, and CC facilitate sensory adaptation through the variation of the level CC of methylation. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HAMP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00102}. CC -!- SIMILARITY: Contains 1 methyl-accepting transducer domain. CC {ECO:0000255|PROSITE-ProRule:PRU00284}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35514.1; -; Genomic_DNA. DR PIR; E72379; E72379. DR RefSeq; NP_228239.1; NC_000853.1. DR RefSeq; WP_010865116.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYR0; -. DR STRING; 243274.TM0429; -. DR EnsemblBacteria; AAD35514; AAD35514; TM_0429. DR GeneID; 897437; -. DR KEGG; tma:TM0429; -. DR PATRIC; 23935743; VBITheMar51294_0435. DR eggNOG; ENOG4105C8Q; Bacteria. DR eggNOG; COG0840; LUCA. DR InParanoid; Q9WYR0; -. DR KO; K03406; -. DR OMA; FIHENVD; -. DR OrthoDB; EOG6RVFRP; -. DR BioCyc; TMAR243274:GC6P-444-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR004089; MCPsignal_dom. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF00015; MCPsignal; 1. DR SMART; SM00304; HAMP; 1. DR SMART; SM00283; MA; 1. DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1. DR PROSITE; PS50885; HAMP; 1. PE 1: Evidence at protein level; KW Cell membrane; Chemotaxis; Complete proteome; Membrane; Methylation; KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1 656 Methyl-accepting chemotaxis protein 1. FT /FTId=PRO_0000250993. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 276 296 Helical. {ECO:0000255}. FT DOMAIN 299 351 HAMP. {ECO:0000255|PROSITE- FT ProRule:PRU00102}. FT DOMAIN 370 606 Methyl-accepting transducer. FT {ECO:0000255|PROSITE-ProRule:PRU00284}. FT MOD_RES 401 401 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 407 407 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 590 590 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 596 596 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. SQ SEQUENCE 656 AA; 72217 MW; EB932E2C3505B143 CRC64; MSLRKKVFLL MIVVVAGLLL SFFLIYRSVS NSIINSVRSN TENQAKALSK FVVEKLNNVT NVARSAATYL GSQFFEAYMI TNQLKTTVEK EKSTFAFAFS ALSFNKSAAL TDGNRVDRVD FADYEKYIKA VEGKDIFFMP ETFQGTPVLT VVVPIETMNT RTGIVGFGIN LSENSDLWKA VVEEGKASKS GYGLLVTSDG KVLIHKDMGN FMKDVKELGG FEKAFEEAKS GGEKYVEYEY NGEKKYTVWE KVPGYDFYIF STGYLEELLA EGRKATLGTI VTYVVFGGVI FAVLFVSMMP VVKRMRQQVE KVKRFGEGDL TVEFEAKGRD ELTQIEESLK EAALSLKEMI VSIIEAAKEL SGASEEIKVL SEESHKMSEN LHEEAKKILD EANNMSSALT EVTSGVEEVA ASAQNISKIT QDLTERSEAV TKAAREGTER VEAVGGVINK LKGSAERQRD YLRELVDSAK TIGEIVDTIS SIAEQTNLLA LNAAIEAARA GEAGRGFAVV ADEIRKLAEE SQRATEDIAK MLSSLRTTIE HVENGSKEMF EGVDEIAVMG EEVTKRFREI LGRIEEINSM IENTAATAQE QGAAAEEMAS AMDNVTKIVE GVVESLNRME SLIEDQTTSA AKVSQAAERL SELSEQLSTL VQKFKV // ID MARIT_THEMA Reviewed; 265 AA. AC Q9WZP2; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 2. DT 13-APR-2016, entry version 78. DE RecName: Full=Maritimacin; DE EC=3.4.-.-; DE AltName: Full=Thermotoga bacteriocin; GN OrderedLocusNames=TM_0785; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF 1-15, PROTEASE ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9872409; DOI=10.1016/S0014-5793(98)01451-3; RA Hicks P.M., Rinker K.D., Baker J.R., Kelly R.M.; RT "Homomultimeric protease in the hyperthermophilic bacterium Thermotoga RT maritima has structural and amino acid sequence homology to RT bacteriocins in mesophilic bacteria."; RL FEBS Lett. 440:393-398(1998). RN [3] RP PROTEIN NAME, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=11210524; DOI=10.1016/S0076-6879(01)30397-X; RA Hicks P.M., Chang L.S., Kelly R.M.; RT "Homomultimeric protease and putative bacteriocin homolog from RT Thermotoga maritima."; RL Methods Enzymol. 330:455-460(2001). CC -!- FUNCTION: Protease that exhibits activity toward chymotrypsin and CC trypsin substrates. May have antibacterial activity. CC -!- ENZYME REGULATION: Activated by calcium and cobalt. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.1. {ECO:0000269|PubMed:11210524, CC ECO:0000269|PubMed:9872409}; CC Temperature dependence: CC Optimum temperature is 90-93 degrees Celsius. CC {ECO:0000269|PubMed:11210524, ECO:0000269|PubMed:9872409}; CC -!- SUBUNIT: Homomultimeric. {ECO:0000269|PubMed:9872409}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase U56 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35867.1; Type=Frameshift; Positions=252; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35867.1; ALT_FRAME; Genomic_DNA. DR PIR; B72333; B72333. DR RefSeq; NP_228594.1; NC_000853.1. DR RefSeq; WP_004080898.1; NZ_CP011107.1. DR PDB; 3DKT; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J=1-265. DR PDBsum; 3DKT; -. DR ProteinModelPortal; Q9WZP2; -. DR STRING; 243274.TM0785; -. DR MEROPS; U56.001; -. DR EnsemblBacteria; AAD35867; AAD35867; TM_0785. DR GeneID; 898453; -. DR KEGG; tma:TM0785; -. DR PATRIC; 23936490; VBITheMar51294_0797. DR eggNOG; ENOG41074CX; Bacteria. DR eggNOG; COG1659; LUCA. DR InParanoid; Q9WZP2; -. DR OMA; AGVNGPY; -. DR OrthoDB; EOG64XXKZ; -. DR BioCyc; TMAR243274:GC6P-812-MONOMER; -. DR EvolutionaryTrace; Q9WZP2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR InterPro; IPR007544; Linocin_M18. DR Pfam; PF04454; Linocin_M18; 1. DR PIRSF; PIRSF019254; CFP29; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin; Calcium; Cobalt; KW Complete proteome; Direct protein sequencing; Hydrolase; Protease; KW Reference proteome; Secreted. FT CHAIN 1 265 Maritimacin. FT /FTId=PRO_0000343950. FT HELIX 6 8 {ECO:0000244|PDB:3DKT}. FT HELIX 13 30 {ECO:0000244|PDB:3DKT}. FT HELIX 32 35 {ECO:0000244|PDB:3DKT}. FT STRAND 37 40 {ECO:0000244|PDB:3DKT}. FT STRAND 49 57 {ECO:0000244|PDB:3DKT}. FT STRAND 68 74 {ECO:0000244|PDB:3DKT}. FT STRAND 76 85 {ECO:0000244|PDB:3DKT}. FT HELIX 86 94 {ECO:0000244|PDB:3DKT}. FT HELIX 102 120 {ECO:0000244|PDB:3DKT}. FT TURN 124 127 {ECO:0000244|PDB:3DKT}. FT HELIX 135 137 {ECO:0000244|PDB:3DKT}. FT HELIX 145 160 {ECO:0000244|PDB:3DKT}. FT STRAND 166 173 {ECO:0000244|PDB:3DKT}. FT HELIX 174 183 {ECO:0000244|PDB:3DKT}. FT STRAND 184 188 {ECO:0000244|PDB:3DKT}. FT HELIX 190 197 {ECO:0000244|PDB:3DKT}. FT STRAND 202 208 {ECO:0000244|PDB:3DKT}. FT STRAND 210 216 {ECO:0000244|PDB:3DKT}. FT STRAND 219 228 {ECO:0000244|PDB:3DKT}. FT STRAND 230 237 {ECO:0000244|PDB:3DKT}. FT STRAND 239 255 {ECO:0000244|PDB:3DKT}. FT HELIX 257 259 {ECO:0000244|PDB:3DKT}. FT STRAND 260 263 {ECO:0000244|PDB:3DKT}. SQ SEQUENCE 265 AA; 30478 MW; 062B867B75CDA155 CRC64; MEFLKRSFAP LTEKQWQEID NRAREIFKTQ LYGRKFVDVE GPYGWEYAAH PLGEVEVLSD ENEVVKWGLR KSLPLIELRA TFTLDLWELD NLERGKPNVD LSSLEETVRK VAEFEDEVIF RGCEKSGVKG LLSFEERKIE CGSTPKDLLE AIVRALSIFS KDGIEGPYTL VINTDRWINF LKEEAGHYPL EKRVEECLRG GKIITTPRIE DALVVSERGG DFKLILGQDL SIGYEDREKD AVRLFITETF TFQVVNPEAL ILLKF // ID MAZG_THEMA Reviewed; 255 AA. AC Q9X015; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 78. DE RecName: Full=Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG; DE Short=NTP-PPase; DE EC=3.6.1.1; DE EC=3.6.1.19; GN Name=mazG; OrderedLocusNames=TM_0913; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION AS A PYROPHOSPHOHYDROLASE AND PYROPHOSPHATASE, CATALYTIC RP ACTIVITY, MUTAGENESIS OF GLU-41; GLU-42; GLU-45; GLU-61; ARG-97; RP ARG-98; LYS-118; GLU-173; GLU-176 AND 185-GLU-GLU-186, MASS RP SPECTROMETRY, ENZYME REGULATION, AND SUBSTRATE SPECIFICITY. RX PubMed=12657645; DOI=10.1074/jbc.M213294200; RA Zhang J., Zhang Y., Inouye M.; RT "Thermotoga maritima MazG protein has both nucleoside triphosphate RT pyrophosphohydrolase and pyrophosphatase activities."; RL J. Biol. Chem. 278:21408-21414(2003). CC -!- FUNCTION: Catalyzes the hydrolysis of all eight canonical CC ribonucleoside triphosphates (NTP) and deoxyribonucleoside CC triphosphates (dNTP) to their corresponding nucleoside CC monophosphates ((d)NMP) and PPi and subsequently hydrolyzes the CC resultant PPi to Pi. The NTPase activity with deoxyribonucleoside CC triphosphates as substrate is higher than corresponding CC ribonucleoside triphosphates. dGTP is the best substrate among the CC deoxyribonucleoside triphosphates, and GTP is the best among the CC ribonucleoside triphosphates. {ECO:0000269|PubMed:12657645}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {ECO:0000269|PubMed:12657645}. CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate. CC {ECO:0000269|PubMed:12657645}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ENZYME REGULATION: Inhibited by AMPCPP (alpha,beta- CC methyleneadenosine triphosphate). {ECO:0000269|PubMed:12657645}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.4 mM for CTP (at pH 8 and at 70 degrees Celsius); CC KM=1 mM for dGTP (at pH 8 and at 70 degrees Celsius); CC KM=1 mM for GTP (at pH 8 and at 70 degrees Celsius); CC KM=1 mM for ATP (at pH 8 and at 70 degrees Celsius); CC KM=1.1 mM for UTP (at pH 8 and at 70 degrees Celsius); CC KM=1.5 mM for dTTP (at pH 8 and at 70 degrees Celsius); CC KM=1.7 mM for dCTP (at pH 8 and at 70 degrees Celsius); CC KM=3.2 mM for dATP (at pH 8 and at 70 degrees Celsius); CC Vmax=0.22 nmol/min/ug enzyme with CTP as substrate (at pH 8 and CC at 70 degrees Celsius); CC Vmax=0.36 nmol/min/ug enzyme with UTP as substrate (at pH 8 and CC at 70 degrees Celsius); CC Vmax=0.39 nmol/min/ug enzyme with ATP as substrate (at pH 8 and CC at 70 degrees Celsius); CC Vmax=1.30 nmol/min/ug enzyme with dTTP as substrate (at pH 8 and CC at 70 degrees Celsius); CC Vmax=1.39 nmol/min/ug enzyme with GTP as substrate (at pH 8 and CC at 70 degrees Celsius); CC Vmax=1.90 nmol/min/ug enzyme with dGTP as substrate (at pH 8 and CC at 70 degrees Celsius); CC Vmax=2 nmol/min/ug enzyme with dCTP as substrate (at pH 8 and at CC 70 degrees Celsius); CC Vmax=2.25 nmol/min/ug enzyme with dATP as substrate (at pH 8 and CC at 70 degrees Celsius); CC Temperature dependence: CC Optimum temperature is about 80 degrees Celsius. MazG is very CC stable at high temperature, and no change is detected up to 85 CC degrees Celsius.; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- MASS SPECTROMETRY: Mass=29728; Method=Electrospray; Range=2-255; CC Evidence={ECO:0000269|PubMed:12657645}; CC -!- SIMILARITY: Belongs to the nucleoside triphosphate CC pyrophosphohydrolase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35994.1; -; Genomic_DNA. DR PIR; H72319; H72319. DR RefSeq; NP_228721.1; NC_000853.1. DR RefSeq; WP_004080649.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X015; -. DR STRING; 243274.TM0913; -. DR DNASU; 898587; -. DR EnsemblBacteria; AAD35994; AAD35994; TM_0913. DR GeneID; 898587; -. DR KEGG; tma:TM0913; -. DR PATRIC; 23936757; VBITheMar51294_0927. DR eggNOG; ENOG4105DXN; Bacteria. DR eggNOG; COG1694; LUCA. DR InParanoid; Q9X015; -. DR KO; K02499; -. DR OMA; RVGFDWE; -. DR OrthoDB; EOG67X1VS; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central. DR GO; GO:0046061; P:dATP catabolic process; IBA:GO_Central. DR GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central. DR GO; GO:0046076; P:dTTP catabolic process; IBA:GO_Central. DR GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central. DR GO; GO:0046047; P:TTP catabolic process; IBA:GO_Central. DR GO; GO:0046052; P:UTP catabolic process; IBA:GO_Central. DR InterPro; IPR004518; MazG_cat. DR InterPro; IPR011551; NTP_PyrPHydrolase_MazG. DR PANTHER; PTHR30522:SF0; PTHR30522:SF0; 1. DR Pfam; PF03819; MazG; 2. DR TIGRFAMs; TIGR00444; mazG; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 255 Nucleoside triphosphate FT pyrophosphohydrolase/pyrophosphatase FT MazG. FT /FTId=PRO_0000413417. FT NP_BIND 162 166 ATP 1. {ECO:0000250}. FT NP_BIND 182 185 ATP 1. {ECO:0000250}. FT NP_BIND 215 219 ATP 2. {ECO:0000250}. FT METAL 169 169 Magnesium. {ECO:0000250}. FT METAL 186 186 Magnesium. {ECO:0000250}. FT METAL 189 189 Magnesium. {ECO:0000250}. FT BINDING 169 169 ATP 1. {ECO:0000250}. FT BINDING 189 189 ATP 1. {ECO:0000250}. FT BINDING 246 246 ATP 2. {ECO:0000250}. FT MUTAGEN 41 41 E->Q: Reduces the NTPase activity to 10% FT of the wild-type activity; when FT associated with Q-42. FT {ECO:0000269|PubMed:12657645}. FT MUTAGEN 42 42 E->Q: Reduces the NTPase activity to 10% FT of the wild-type activity; when FT associated with Q-41. FT {ECO:0000269|PubMed:12657645}. FT MUTAGEN 45 45 E->Q: Reduces the NTPase activity to 10% FT of the wild-type activity. FT {ECO:0000269|PubMed:12657645}. FT MUTAGEN 61 61 E->Q: Reduces the NTPase activity to 10% FT of the wild-type activity. FT {ECO:0000269|PubMed:12657645}. FT MUTAGEN 97 97 R->A: Reduces the NTPase activity to 10% FT of the wild-type activity; when FT associated with A-98. FT {ECO:0000269|PubMed:12657645}. FT MUTAGEN 98 98 R->A: Reduces the NTPase activity to 10% FT of the wild-type activity; when FT associated with A-97. FT {ECO:0000269|PubMed:12657645}. FT MUTAGEN 118 118 K->E: Reduces the NTPase activity to 10% FT of the wild-type activity. FT {ECO:0000269|PubMed:12657645}. FT MUTAGEN 173 173 E->A: Has little effects on the NTPase FT activity. {ECO:0000269|PubMed:12657645}. FT MUTAGEN 176 176 E->A: Has little effects on the NTPase FT activity. {ECO:0000269|PubMed:12657645}. FT MUTAGEN 185 186 EE->AA: Has little effects on the NTPase FT activity. {ECO:0000269|PubMed:12657645}. SQ SEQUENCE 255 AA; 29805 MW; 92F4981444C70F42 CRC64; MKEAGILFEE LVSIMEKLRS PEGCEWDRKQ THESLKPYLI EECYELIEAI DEKNDDMMKE ELGDVLLQVV FHAQIARERG AFTIEDVIRT LNEKLIRRHP HVFGDSPGYS YKQWEDIKAQ EKGKKKSSRI GEINPLVPAL SMARRIQENA SQVGFDWKDP EGVYEKIEEE LKELKEAKDP RELEEEFGDL LFSIVNLSRF LNVDPESALR KATRKFVERF KKMEELIEKD GLVLEELPIE KLDEYWEKAK GGDET // ID MCP4_THEMA Reviewed; 566 AA. AC Q9X1E2; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 105. DE RecName: Full=Methyl-accepting chemotaxis protein 4; GN Name=mcp4; OrderedLocusNames=TM_1428; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP METHYLATION AT GLU-310; GLU-317; GLN-499 AND GLU-506, AND DEAMIDATION RP AT GLN-499. RX PubMed=16707700; DOI=10.1128/JB.00181-06; RA Perez E., Zheng H., Stock A.M.; RT "Identification of methylation sites in Thermotoga maritima chemotaxis RT receptors."; RL J. Bacteriol. 188:4093-4100(2006). CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the CC concentration of attractants and repellents in the environment, CC transduce a signal from the outside to the inside of the cell, and CC facilitate sensory adaptation through the variation of the level CC of methylation. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HAMP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00102}. CC -!- SIMILARITY: Contains 1 methyl-accepting transducer domain. CC {ECO:0000255|PROSITE-ProRule:PRU00284}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36498.1; -; Genomic_DNA. DR PIR; A72254; A72254. DR RefSeq; NP_229228.1; NC_000853.1. DR RefSeq; WP_004081682.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1E2; -. DR STRING; 243274.TM1428; -. DR EnsemblBacteria; AAD36498; AAD36498; TM_1428. DR GeneID; 898047; -. DR KEGG; tma:TM1428; -. DR PATRIC; 23937804; VBITheMar51294_1440. DR eggNOG; ENOG41080BE; Bacteria. DR eggNOG; COG0840; LUCA. DR InParanoid; Q9X1E2; -. DR KO; K03406; -. DR OMA; FNSIMER; -. DR OrthoDB; EOG6CK7NC; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR InterPro; IPR004010; Cache_domain. DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR004089; MCPsignal_dom. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF00015; MCPsignal; 1. DR Pfam; PF17200; sCache_2; 1. DR PRINTS; PR00260; CHEMTRNSDUCR. DR SMART; SM01049; Cache_2; 1. DR SMART; SM00304; HAMP; 1. DR SMART; SM00283; MA; 1. DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1. DR PROSITE; PS50885; HAMP; 1. PE 1: Evidence at protein level; KW Cell membrane; Chemotaxis; Complete proteome; Membrane; Methylation; KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1 566 Methyl-accepting chemotaxis protein 4. FT /FTId=PRO_0000250996. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 190 210 Helical. {ECO:0000255}. FT DOMAIN 209 261 HAMP. {ECO:0000255|PROSITE- FT ProRule:PRU00102}. FT DOMAIN 280 516 Methyl-accepting transducer. FT {ECO:0000255|PROSITE-ProRule:PRU00284}. FT MOD_RES 310 310 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 317 317 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 499 499 Glutamate methyl ester (Gln). FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 506 506 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. SQ SEQUENCE 566 AA; 63041 MW; BAA6BFB8F8A34ACF CRC64; MRSIASKVLV IGVVVVLAFF VTQYVLLNTT VFNSIMERKK EEAKHLVESV YGILERAYEM EQKGELTREQ AQELAKSLIG KIRYDDNNYF WINDTHPRMV FHPIKPEMNG QDLSNYKDPN GVYLFNEMVK VAKEKGEGFV SYSWPKAGSD KPEPKISYVK LFEPWGWIVG TGIYVDDVKV TVGNLIFRNV LTVSVIGIAV IIMIFFYGRV LSRKTKAVLS ALEKISSGDL SVSVDIKSKD EFGLIAQKLN ETVGNLRKMV QEIDKSQDEV ERVSEELFAL SQQLRSALEE IARASDTISK EVQNASASIE EVTSGSEEVS ANSQNISKLI QEISENADNI ADFARNGQRV LEEAVKKVED VSENSRETAD VVSNVTESAR NIEEIVRTIQ SIAEQTNLLA LNAAIEAARA GEAGRGFAVV ADEIRKLAEE SQKATEEISQ ILENIREGVE RTNEMSKKNV EITKDARRLV EESYESFNQI VTRIEDLAAR IEGIAASAQE LSAASEEMSS ALDAVAKTTT TVADEVEEVS ENITEQEKAA KRIADIGTEL KKLSDELKED VERFKI // ID META_THEMA Reviewed; 304 AA. AC Q9WZY3; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Homoserine O-succinyltransferase; DE EC=2.3.1.46; DE AltName: Full=Homoserine O-transsuccinylase; DE Short=HTS; GN Name=metA; OrderedLocusNames=TM_0881; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + L-homoserine = CoA + O- CC succinyl-L-homoserine. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HTS family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35962.1; -; Genomic_DNA. DR PIR; C72324; C72324. DR RefSeq; NP_228689.1; NC_000853.1. DR RefSeq; WP_004080711.1; NZ_CP011107.1. DR PDB; 2H2W; X-ray; 2.52 A; A=1-300. DR PDBsum; 2H2W; -. DR ProteinModelPortal; Q9WZY3; -. DR SMR; Q9WZY3; 2-296. DR STRING; 243274.TM0881; -. DR EnsemblBacteria; AAD35962; AAD35962; TM_0881. DR GeneID; 898555; -. DR KEGG; tma:TM0881; -. DR PATRIC; 23936693; VBITheMar51294_0895. DR eggNOG; ENOG4105CVG; Bacteria. DR eggNOG; COG1897; LUCA. DR InParanoid; Q9WZY3; -. DR KO; K00651; -. DR OMA; WRSHRNL; -. DR OrthoDB; EOG61P6ST; -. DR UniPathway; UPA00051; UER00075. DR EvolutionaryTrace; Q9WZY3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008899; F:homoserine O-succinyltransferase activity; IBA:GO_Central. DR GO; GO:0019281; P:L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00295; Homoser_O_succinyltr; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR005697; Homserine_suc_trans. DR PANTHER; PTHR20919; PTHR20919; 1. DR Pfam; PF04204; HTS; 1. DR PIRSF; PIRSF000450; H_ser_succinyltr; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01001; metA; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Amino-acid biosynthesis; KW Complete proteome; Cytoplasm; Methionine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 304 Homoserine O-succinyltransferase. FT /FTId=PRO_0000199763. FT ACT_SITE 142 142 {ECO:0000255}. FT HELIX 10 16 {ECO:0000244|PDB:2H2W}. FT TURN 17 19 {ECO:0000244|PDB:2H2W}. FT STRAND 36 41 {ECO:0000244|PDB:2H2W}. FT HELIX 47 59 {ECO:0000244|PDB:2H2W}. FT STRAND 60 63 {ECO:0000244|PDB:2H2W}. FT STRAND 65 70 {ECO:0000244|PDB:2H2W}. FT HELIX 82 88 {ECO:0000244|PDB:2H2W}. FT HELIX 92 94 {ECO:0000244|PDB:2H2W}. FT TURN 95 97 {ECO:0000244|PDB:2H2W}. FT STRAND 100 105 {ECO:0000244|PDB:2H2W}. FT HELIX 115 117 {ECO:0000244|PDB:2H2W}. FT HELIX 121 134 {ECO:0000244|PDB:2H2W}. FT STRAND 135 141 {ECO:0000244|PDB:2H2W}. FT HELIX 143 153 {ECO:0000244|PDB:2H2W}. FT STRAND 158 174 {ECO:0000244|PDB:2H2W}. FT HELIX 177 179 {ECO:0000244|PDB:2H2W}. FT STRAND 184 195 {ECO:0000244|PDB:2H2W}. FT HELIX 198 201 {ECO:0000244|PDB:2H2W}. FT STRAND 207 213 {ECO:0000244|PDB:2H2W}. FT TURN 214 216 {ECO:0000244|PDB:2H2W}. FT STRAND 217 231 {ECO:0000244|PDB:2H2W}. FT HELIX 241 251 {ECO:0000244|PDB:2H2W}. FT HELIX 264 266 {ECO:0000244|PDB:2H2W}. FT HELIX 277 290 {ECO:0000244|PDB:2H2W}. FT TURN 291 295 {ECO:0000244|PDB:2H2W}. SQ SEQUENCE 304 AA; 35759 MW; 3ED8226AA8F8044E CRC64; MPINVPSGLP AVKVLAKEGI FVMTEKRAIH QDIRPLEILI LNLMPDKIKT EIQLLRLLGN TPLQVNVTLL YTETHKPKHT PIEHILKFYT TFSAVKDRKF DGFIITGAPV ELLPFEEVDY WEELTEIMEW SRHNVYSTMF ICWAAQAGLY YFYGIPKYEL PQKLSGVYKH RVAKDSVLFR GHDDFFWAPH SRYTEVKKED IDKVPELEIL AESDEAGVYV VANKSERQIF VTGHPEYDRY TLRDEYYRDI GRNLKVPIPA NYFPNDDPTK TPILTWWSHA HLFFSNWLNY CIYQKTPYRL EDIH // ID MENG_THEMA Reviewed; 229 AA. AC Q9WZL2; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=Demethylmenaquinone methyltransferase {ECO:0000255|HAMAP-Rule:MF_01813}; DE EC=2.1.1.163 {ECO:0000255|HAMAP-Rule:MF_01813}; GN Name=menG {ECO:0000255|HAMAP-Rule:MF_01813}; GN OrderedLocusNames=TM_0753; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Methyltransferase required for the conversion of CC demethylmenaquinol (DMKH2) to menaquinol (MKH2). CC {ECO:0000255|HAMAP-Rule:MF_01813}. CC -!- CATALYTIC ACTIVITY: A demethylmenaquinol + S-adenosyl-L-methionine CC = a menaquinol + S-adenosyl-L-homocysteine. {ECO:0000255|HAMAP- CC Rule:MF_01813}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis; CC menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01813}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. MenG/UbiE family. CC {ECO:0000255|HAMAP-Rule:MF_01813}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35835.1; -; Genomic_DNA. DR PIR; G72337; G72337. DR RefSeq; NP_228562.1; NC_000853.1. DR RefSeq; WP_010865199.1; NC_000853.1. DR ProteinModelPortal; Q9WZL2; -. DR STRING; 243274.TM0753; -. DR DNASU; 898421; -. DR EnsemblBacteria; AAD35835; AAD35835; TM_0753. DR GeneID; 898421; -. DR KEGG; tma:TM0753; -. DR KEGG; tmi:THEMA_00885; -. DR PATRIC; 23936428; VBITheMar51294_0766. DR eggNOG; ENOG4107UA9; Bacteria. DR eggNOG; COG2226; LUCA. DR InParanoid; Q9WZL2; -. DR KO; K03183; -. DR OMA; SSKMLEI; -. DR OrthoDB; EOG6M6JSB; -. DR BioCyc; TMAR243274:GC6P-780-MONOMER; -. DR UniPathway; UPA00079; UER00169. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01813; MenG_UbiE_methyltr; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR004033; UbiE/COQ5_MeTrFase. DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS. DR Pfam; PF01209; Ubie_methyltran; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR01934; MenG_MenH_UbiE; 1. DR PROSITE; PS51608; SAM_MT_UBIE; 1. DR PROSITE; PS01183; UBIE_1; 1. PE 3: Inferred from homology; KW Complete proteome; Menaquinone biosynthesis; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 229 Demethylmenaquinone methyltransferase. FT /FTId=PRO_0000193343. FT REGION 100 101 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01813}. FT BINDING 58 58 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01813}. FT BINDING 78 78 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01813}. SQ SEQUENCE 229 AA; 26494 MW; DCF6227D22A46DD5 CRC64; MGGKTKKHAM RLFDRIAEKY DLLNRILSFG MDTKWRKRVV ELILEVNPEK VLDLATGTGD VARLLKRKAP HLEITGLDSS SKMLEIAEKR LKDGEFIVGD AHNLPFYDRS FDAITVAFGF RNFSDRRRVL RECRRVLKRK GRLVILELLP PNTKRFTGKI YSFYLKTWVP FVGGLFSGDF HAYRYLSTSV LNFLTPDQIV EMMKEEGFEV SFEPLFFSVA GIFIGDLIW // ID METK_THEMA Reviewed; 395 AA. AC Q9X1Y8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 113. DE RecName: Full=S-adenosylmethionine synthase; DE Short=AdoMet synthase; DE EC=2.5.1.6; DE AltName: Full=MAT; DE AltName: Full=Methionine adenosyltransferase; GN Name=metK; OrderedLocusNames=TM_1658; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from CC methionine and ATP. The overall synthetic reaction is composed of CC two sequential steps, AdoMet formation and the subsequent CC tripolyphosphate hydrolysis which occurs prior to release of CC AdoMet from the enzyme (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate + CC diphosphate + S-adenosyl-L-methionine. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; CC Note=Binds 2 divalent ions per subunit. Magnesium or cobalt. CC {ECO:0000250}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; CC Note=Binds 1 potassium ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine CC biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36725.1; -; Genomic_DNA. DR PIR; G72228; G72228. DR RefSeq; NP_229458.1; NC_000853.1. DR RefSeq; WP_004082170.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1Y8; -. DR STRING; 243274.TM1658; -. DR EnsemblBacteria; AAD36725; AAD36725; TM_1658. DR GeneID; 897911; -. DR KEGG; tma:TM1658; -. DR PATRIC; 23938290; VBITheMar51294_1677. DR eggNOG; ENOG4105CPH; Bacteria. DR eggNOG; COG0192; LUCA. DR InParanoid; Q9X1Y8; -. DR KO; K00789; -. DR OMA; DNFLAFD; -. DR OrthoDB; EOG68WR6M; -. DR UniPathway; UPA00315; UER00080. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004478; F:methionine adenosyltransferase activity; IBA:GO_Central. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00086; S_AdoMet_synth1; 1. DR InterPro; IPR022631; ADOMET_SYNTHASE_CS. DR InterPro; IPR022630; S-AdoMet_synt_C. DR InterPro; IPR022629; S-AdoMet_synt_central. DR InterPro; IPR022628; S-AdoMet_synt_N. DR InterPro; IPR002133; S-AdoMet_synthetase. DR InterPro; IPR022636; S-AdoMet_synthetase_sfam. DR PANTHER; PTHR11964; PTHR11964; 1. DR Pfam; PF02773; S-AdoMet_synt_C; 1. DR Pfam; PF02772; S-AdoMet_synt_M; 1. DR Pfam; PF00438; S-AdoMet_synt_N; 1. DR PIRSF; PIRSF000497; MAT; 1. DR SUPFAM; SSF55973; SSF55973; 3. DR TIGRFAMs; TIGR01034; metK; 1. DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1. DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cobalt; Complete proteome; Cytoplasm; Magnesium; KW Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium; KW Reference proteome; Transferase. FT CHAIN 1 395 S-adenosylmethionine synthase. FT /FTId=PRO_0000174613. FT NP_BIND 270 277 ATP. {ECO:0000255}. FT METAL 16 16 Magnesium. {ECO:0000250}. FT METAL 42 42 Potassium. {ECO:0000250}. FT METAL 274 274 Potassium. {ECO:0000250}. FT METAL 282 282 Magnesium. {ECO:0000250}. SQ SEQUENCE 395 AA; 43673 MW; 5ACA50F1DA60A9D5 CRC64; MRRLFTSESV TEGHPDKIAD QISDAILDAM LEQDPRSRVA VETLVTTGLV IIAGEVTTRA YVEIPDIARK TILEIGYTRA KYGFDGETCG VLTSIHSQSP DIALGVDKAL EVKTGEEVAD EFEALGAGDQ GIMFGYATNE TPEYMPLPIT LAHKLAMRLA EVRKNGTLPF LRPDGKTQVT IEYEDDKPVR VDTVLISTQH DPDISQADLR EAIIEHVINP VIPEQYRDDK MKILVNPTGR FVLGGPMADT GLTGRKIIVD TYGGWVPHGG GAFSGKDPTK VDRSAHYMAR YVAKNVVAAG LADKFLIQLS YAIGVAKPVS IMIDTYGTAK VDEDKLLKVI TELFDFRPGA IIKKLNLLRP IYRKTAAYGH FGRNEEEFTW EKLDMVDELK RAFNM // ID MGTA_THEMA Reviewed; 441 AA. AC P80099; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 135. DE RecName: Full=4-alpha-glucanotransferase; DE EC=2.4.1.25; DE AltName: Full=Amylomaltase; DE AltName: Full=Disproportionating enzyme; DE Short=D-enzyme; GN Name=mgtA; OrderedLocusNames=TM_0364; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF 1-23, AND CHARACTERIZATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1628664; DOI=10.1111/j.1432-1033.1992.tb17023.x; RA Liebl W., Feil R., Gabelsberger J., Kellermann J., Schleifer K.-H.; RT "Purification and characterization of a novel thermostable 4-alpha- RT glucanotransferase of Thermotoga maritima cloned in Escherichia RT coli."; RL Eur. J. Biochem. 207:81-88(1992). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=12139940; DOI=10.1016/S0022-2836(02)00570-3; RA Roujeinikova A., Raasch C., Sedelnikova S., Liebl W., Rice D.W.; RT "Crystal structure of Thermotoga maritima 4-alpha-glucanotransferase RT and its acarbose complex: implications for substrate specificity and RT catalysis."; RL J. Mol. Biol. 321:149-162(2002). CC -!- CATALYTIC ACTIVITY: Transfers a segment of a (1->4)-alpha-D-glucan CC to a new position in an acceptor, which may be glucose or a CC (1->4)-alpha-D-glucan. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 1 Ca(2+) ion per subunit.; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35451.1; -; Genomic_DNA. DR RefSeq; NP_228175.1; NC_000853.1. DR RefSeq; WP_004083169.1; NZ_CP011107.1. DR PDB; 1LWH; X-ray; 2.60 A; A/B=1-441. DR PDB; 1LWJ; X-ray; 2.50 A; A/B=1-441. DR PDBsum; 1LWH; -. DR PDBsum; 1LWJ; -. DR ProteinModelPortal; P80099; -. DR SMR; P80099; 1-441. DR STRING; 243274.TM0364; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR DNASU; 897323; -. DR EnsemblBacteria; AAD35451; AAD35451; TM_0364. DR GeneID; 897323; -. DR KEGG; tma:TM0364; -. DR PATRIC; 23935609; VBITheMar51294_0369. DR eggNOG; ENOG4105CG3; Bacteria. DR eggNOG; COG0366; LUCA. DR InParanoid; P80099; -. DR KO; K00705; -. DR OMA; WAEARMV; -. DR OrthoDB; EOG6RZB0T; -. DR EvolutionaryTrace; P80099; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.20.20.80; -; 2. DR InterPro; IPR015261; 4-alpha-glucanotransf_C. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR015902; Glyco_hydro_13. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10357; PTHR10357; 2. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF09178; DUF1945; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Carbohydrate metabolism; Complete proteome; KW Cytoplasm; Direct protein sequencing; Glycosyltransferase; KW Metal-binding; Reference proteome; Transferase. FT CHAIN 1 441 4-alpha-glucanotransferase. FT /FTId=PRO_0000054336. FT ACT_SITE 186 186 Nucleophile. FT ACT_SITE 216 216 Proton donor. FT METAL 13 13 Calcium. FT METAL 15 15 Calcium. FT METAL 17 17 Calcium. FT METAL 19 19 Calcium; via carbonyl oxygen. FT METAL 21 21 Calcium. FT SITE 278 278 Transition state stabilizer. FT {ECO:0000250}. FT CONFLICT 1 1 M -> A (in Ref. 2; AA sequence). FT {ECO:0000305}. FT STRAND 3 6 {ECO:0000244|PDB:1LWJ}. FT HELIX 8 11 {ECO:0000244|PDB:1LWJ}. FT STRAND 14 19 {ECO:0000244|PDB:1LWJ}. FT HELIX 22 27 {ECO:0000244|PDB:1LWJ}. FT HELIX 29 34 {ECO:0000244|PDB:1LWJ}. FT STRAND 39 42 {ECO:0000244|PDB:1LWJ}. FT STRAND 49 52 {ECO:0000244|PDB:1LWJ}. FT STRAND 57 62 {ECO:0000244|PDB:1LWJ}. FT TURN 64 66 {ECO:0000244|PDB:1LWJ}. FT HELIX 69 81 {ECO:0000244|PDB:1LWJ}. FT STRAND 85 90 {ECO:0000244|PDB:1LWJ}. FT HELIX 100 106 {ECO:0000244|PDB:1LWJ}. FT HELIX 110 113 {ECO:0000244|PDB:1LWJ}. FT STRAND 130 132 {ECO:0000244|PDB:1LWJ}. FT STRAND 137 139 {ECO:0000244|PDB:1LWJ}. FT STRAND 145 147 {ECO:0000244|PDB:1LWJ}. FT STRAND 159 161 {ECO:0000244|PDB:1LWJ}. FT HELIX 162 176 {ECO:0000244|PDB:1LWJ}. FT TURN 177 179 {ECO:0000244|PDB:1LWJ}. FT STRAND 182 185 {ECO:0000244|PDB:1LWJ}. FT HELIX 188 190 {ECO:0000244|PDB:1LWJ}. FT STRAND 191 194 {ECO:0000244|PDB:1LWJ}. FT HELIX 195 205 {ECO:0000244|PDB:1LWJ}. FT TURN 206 208 {ECO:0000244|PDB:1LWJ}. FT STRAND 211 215 {ECO:0000244|PDB:1LWJ}. FT HELIX 221 231 {ECO:0000244|PDB:1LWJ}. FT STRAND 232 235 {ECO:0000244|PDB:1LWJ}. FT HELIX 237 248 {ECO:0000244|PDB:1LWJ}. FT HELIX 253 262 {ECO:0000244|PDB:1LWJ}. FT STRAND 267 274 {ECO:0000244|PDB:1LWJ}. FT HELIX 282 284 {ECO:0000244|PDB:1LWJ}. FT TURN 285 287 {ECO:0000244|PDB:1LWJ}. FT HELIX 291 302 {ECO:0000244|PDB:1LWJ}. FT STRAND 304 311 {ECO:0000244|PDB:1LWJ}. FT TURN 312 317 {ECO:0000244|PDB:1LWJ}. FT HELIX 327 330 {ECO:0000244|PDB:1LWJ}. FT STRAND 336 340 {ECO:0000244|PDB:1LWJ}. FT STRAND 356 359 {ECO:0000244|PDB:1LWJ}. FT HELIX 362 365 {ECO:0000244|PDB:1LWJ}. FT HELIX 372 385 {ECO:0000244|PDB:1LWJ}. FT HELIX 387 389 {ECO:0000244|PDB:1LWJ}. FT STRAND 393 399 {ECO:0000244|PDB:1LWJ}. FT STRAND 401 410 {ECO:0000244|PDB:1LWJ}. FT STRAND 413 420 {ECO:0000244|PDB:1LWJ}. FT STRAND 422 424 {ECO:0000244|PDB:1LWJ}. FT STRAND 426 428 {ECO:0000244|PDB:1LWJ}. FT STRAND 431 433 {ECO:0000244|PDB:1LWJ}. FT STRAND 438 440 {ECO:0000244|PDB:1LWJ}. SQ SEQUENCE 441 AA; 51843 MW; 9FB4C2ABC9D3DF3A CRC64; MIGYQIYVRS FRDGNLDGVG DFRGLKNAVS YLKELGIDFV WLMPVFSSIS FHGYDVVDFY SFKAEYGSER EFKEMIEAFH DSGIKVVLDL PIHHTGFLHT WFQKALKGDP HYRDYYVWAN KETDLDERRE WDGEKIWHPL EDGRFYRGLF GPFSPDLNYD NPQVFDEMKR LVLHLLDMGV DGFRFDAAKH MRDTIEQNVR FWKYFLSDLK GIFLAEIWAE ARMVDEHGRI FGYMLNFDTS HCIKEAVWKE NTRVLIESIE RAVIGKDYLP VNFTSNHDMS RLASFEGGFS KEKIKLSISI LFTLPGVPLV FYGDELGMKG VYQKPNTEVV LDPFPWNESM CVEGQTFWKW PAYNGPFSGI SVEYQKRDPD SILSHTLGWT RFRKENQWID RAKLEFLCKE DKFLVYRLYD DQHSLKVFHN LSGEEVVFEG VKMKPYKTEV V // ID MIND_THEMA Reviewed; 271 AA. AC Q9X2I3; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Septum site-determining protein MinD; DE AltName: Full=Cell division inhibitor MinD; GN Name=minD; OrderedLocusNames=TM_1870; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: ATPase required for the correct placement of the CC division site. Cell division inhibitors MinC and MinD act in CC concert to form an inhibitor capable of blocking formation of the CC polar Z ring septums. Rapidly oscillates between the poles of the CC cell to destabilize FtsZ filaments that have formed before they CC mature into polar Z rings (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with MinC and FtsZ. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ParA family. MinD subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36932.1; -; Genomic_DNA. DR PIR; A72200; A72200. DR RefSeq; NP_229666.1; NC_000853.1. DR RefSeq; WP_004082421.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2I3; -. DR STRING; 243274.TM1870; -. DR EnsemblBacteria; AAD36932; AAD36932; TM_1870. DR GeneID; 897664; -. DR KEGG; tma:TM1870; -. DR KEGG; tmi:THEMA_04820; -. DR KEGG; tmw:THMA_1920; -. DR PATRIC; 23938729; VBITheMar51294_1891. DR eggNOG; ENOG4107U53; Bacteria. DR eggNOG; COG2894; LUCA. DR InParanoid; Q9X2I3; -. DR KO; K03609; -. DR OMA; VNRIRNH; -. DR OrthoDB; EOG6NPMB6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0000918; P:barrier septum site selection; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR025501; MinD. DR InterPro; IPR010223; MinD_bac-type. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR PIRSF; PIRSF003092; MinD; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01968; minD_bact; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell membrane; KW Complete proteome; Membrane; Nucleotide-binding; Reference proteome; KW Septation. FT CHAIN 1 271 Septum site-determining protein MinD. FT /FTId=PRO_0000201975. FT NP_BIND 10 17 ATP. {ECO:0000255}. SQ SEQUENCE 271 AA; 29483 MW; EC76D3F15D64A4CA CRC64; MGNVIVVTSG KGGVGKTTIT ANLGCALAKL GEKVCLIDAD IGLKNLDIVL GLENRIVYTM IDVVNGKVSP QEALVKHKML KNLYLLPASQ IATKEMISPN DMKAIVKELI PHFDYIIIDS PAGIERGFRN AVAPAERVLV VTTPELPAIS DADRVIGLLE NFGFSDEKIN VIINRFKPHM VKKGEMLTTD DIKHTLSLEI IAVIPDSEDI IVASNTGIPV SLNGNSRISK NFENLARRIR GEGVPLENDF VTVSKGLIDT LKDFFSKLKR G // ID MCP2_THEMA Reviewed; 530 AA. AC Q9X0M7; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=Methyl-accepting chemotaxis protein 2; GN Name=mcp2; OrderedLocusNames=TM_1143; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP METHYLATION AT GLN-274; GLU-281 AND GLU-505, AND DEAMIDATION AT RP GLN-274 AND GLN-498. RX PubMed=16707700; DOI=10.1128/JB.00181-06; RA Perez E., Zheng H., Stock A.M.; RT "Identification of methylation sites in Thermotoga maritima chemotaxis RT receptors."; RL J. Bacteriol. 188:4093-4100(2006). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 225-529. RX PubMed=16622408; DOI=10.1038/nsmb1085; RA Park S.-Y., Borbat P.P., Gonzalez-Bonet G., Bhatnagar J., RA Pollard A.M., Freed J.H., Bilwes A.M., Crane B.R.; RT "Reconstruction of the chemotaxis receptor-kinase assembly."; RL Nat. Struct. Mol. Biol. 13:400-407(2006). CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the CC concentration of attractants and repellents in the environment, CC transduce a signal from the outside to the inside of the cell, and CC facilitate sensory adaptation through the variation of the level CC of methylation. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HAMP domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 methyl-accepting transducer domain. CC {ECO:0000255|PROSITE-ProRule:PRU00284}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36219.1; -; Genomic_DNA. DR PIR; C72291; C72291. DR RefSeq; NP_228949.1; NC_000853.1. DR RefSeq; WP_004080253.1; NZ_CP011107.1. DR PDB; 2CH7; X-ray; 2.50 A; A/B=225-529. DR PDB; 3JA6; EM; 12.70 A; G/I/K/M/O/Q=225-529, H/J/L/N/P/R=225-528. DR PDBsum; 2CH7; -. DR PDBsum; 3JA6; -. DR ProteinModelPortal; Q9X0M7; -. DR SMR; Q9X0M7; 222-529. DR DIP; DIP-29072N; -. DR STRING; 243274.TM1143; -. DR EnsemblBacteria; AAD36219; AAD36219; TM_1143. DR GeneID; 898621; -. DR KEGG; tma:TM1143; -. DR PATRIC; 23937221; VBITheMar51294_1159. DR eggNOG; ENOG4105C8Q; Bacteria. DR eggNOG; COG0840; LUCA. DR InParanoid; Q9X0M7; -. DR KO; K03406; -. DR OMA; SEQASAM; -. DR OrthoDB; EOG6GN71H; -. DR EvolutionaryTrace; Q9X0M7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR004089; MCPsignal_dom. DR InterPro; IPR000727; T_SNARE_dom. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF00015; MCPsignal; 1. DR PRINTS; PR00260; CHEMTRNSDUCR. DR SMART; SM00283; MA; 1. DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Chemotaxis; Complete proteome; Membrane; KW Methylation; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1 530 Methyl-accepting chemotaxis protein 2. FT /FTId=PRO_0000250994. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 151 171 Helical. {ECO:0000255}. FT DOMAIN 152 222 HAMP. FT DOMAIN 244 480 Methyl-accepting transducer. FT {ECO:0000255|PROSITE-ProRule:PRU00284}. FT MOD_RES 274 274 Glutamate methyl ester (Gln). FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 281 281 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 498 498 Deamidated glutamine. FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 505 505 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. FT HELIX 225 341 {ECO:0000244|PDB:2CH7}. FT HELIX 344 372 {ECO:0000244|PDB:2CH7}. FT HELIX 378 414 {ECO:0000244|PDB:2CH7}. FT HELIX 417 432 {ECO:0000244|PDB:2CH7}. FT HELIX 435 518 {ECO:0000244|PDB:2CH7}. FT TURN 520 522 {ECO:0000244|PDB:2CH7}. FT HELIX 523 528 {ECO:0000244|PDB:2CH7}. SQ SEQUENCE 530 AA; 57929 MW; C04149A4F46890CE CRC64; MSLKGKTLLV STITLAAVVL VALLGGSVFL KAGQNVRKAF EEYELAVEAL DKLGELETKV ALFVNNAAKI EEVSSLFNEL KKVADKIPSL KEHMDALERN ISEIISGKTE VVSRIQSSVD QVKEDIMANL DRTRENLDKE ISYSSELIRN VLFIVLPIVA VASGVFLFVM ISRSLRLLKP VMEASRSLRN NDLTINIQEA KGKDEISTLL NEFKASIEYL RNNLKDVQTE TFSVAESIEE ISKANEEITN QLLGISKEMD NISTRIESIS ASVQETTAGS EEISSATKNI ADSAQQAASF ADQSTQLAKE AGDALKKVIE VTRMISNSAK DVERVVESFQ KGAEEITSFV ETINAIAEQT NLLALNAAIE AARAGEAGRG FAVVADEIRK LAEESQQASE NVRRVVNEIR SIAEDAGKVS SEITARVEEG TKLADEADEK LNSIVGAVER INEMLQNIAA AIEEQTAAVD EITTAMTENA KNAEEITNSV KEVNARLQEI SASTEEVTSR VQTIRENVQM LKEIVARYKI // ID MCP3_THEMA Reviewed; 539 AA. AC Q9X0N0; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=Methyl-accepting chemotaxis protein 3; GN Name=mcp3; OrderedLocusNames=TM_1146; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP METHYLATION AT GLU-255; GLU-284; GLU-479 AND GLU-515. RX PubMed=16707700; DOI=10.1128/JB.00181-06; RA Perez E., Zheng H., Stock A.M.; RT "Identification of methylation sites in Thermotoga maritima chemotaxis RT receptors."; RL J. Bacteriol. 188:4093-4100(2006). CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the CC concentration of attractants and repellents in the environment, CC transduce a signal from the outside to the inside of the cell, and CC facilitate sensory adaptation through the variation of the level CC of methylation. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HAMP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00102}. CC -!- SIMILARITY: Contains 1 methyl-accepting transducer domain. CC {ECO:0000255|PROSITE-ProRule:PRU00284}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36222.1; -; Genomic_DNA. DR PIR; F72288; F72288. DR RefSeq; NP_228952.1; NC_000853.1. DR RefSeq; WP_004080235.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0N0; -. DR STRING; 243274.TM1146; -. DR EnsemblBacteria; AAD36222; AAD36222; TM_1146. DR GeneID; 898550; -. DR KEGG; tma:TM1146; -. DR PATRIC; 23937229; VBITheMar51294_1163. DR eggNOG; ENOG4105C8Q; Bacteria. DR eggNOG; COG0840; LUCA. DR InParanoid; Q9X0N0; -. DR KO; K03406; -. DR OMA; EMIRITD; -. DR OrthoDB; EOG6KQ6J0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR004089; MCPsignal_dom. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF00015; MCPsignal; 1. DR PRINTS; PR00260; CHEMTRNSDUCR. DR SMART; SM00304; HAMP; 1. DR SMART; SM00283; MA; 1. DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1. DR PROSITE; PS50885; HAMP; 1. PE 1: Evidence at protein level; KW Cell membrane; Chemotaxis; Complete proteome; Membrane; Methylation; KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1 539 Methyl-accepting chemotaxis protein 3. FT /FTId=PRO_0000250995. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 160 180 Helical. {ECO:0000255}. FT DOMAIN 181 234 HAMP. {ECO:0000255|PROSITE- FT ProRule:PRU00102}. FT DOMAIN 253 489 Methyl-accepting transducer. FT {ECO:0000255|PROSITE-ProRule:PRU00284}. FT MOD_RES 255 255 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 284 284 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 479 479 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. FT MOD_RES 515 515 Glutamate methyl ester (Glu). FT {ECO:0000269|PubMed:16707700}. SQ SEQUENCE 539 AA; 58621 MW; 5330E1E48B1295BA CRC64; MKSVASKLLL GFGLVCAGLV LFGLLTFYNI LSLEKIVADT ANINRAIVEL AINQAGVLVA VQNKDKSLLS SSVEGLRTSL DDIKAYQSDF SGENLKLLQE SIAHLEEMIR ITDSLIVDGV DQSIYDRFVE LQAEIRNPLR KLVQNLGVEN VSMTKNIKRN IIFFLVVVCA AAMFIAIFTT RNLTTPLKKL AVLVENLSHG VLNVEIEKIR SKDEIGKAAM AVEKLREILL DIITGINKAS SEVSSSSEEL SATSEELSAN VNSISEALVS LNKEADENSA TLEEFTASIE ELSSTADSNS KSAQAMLEST QRVHEQVEKS TERIREITEK AHSTREMSEN TKQALNRLLS MAENINSIVD TINSIAEQTN LLALNAAIEA ARAGEAGRGF AVVADEIRKL AEESKAATQQ IGEILGKLRD EINNSSKIVE STASAIEETA SLVESIKDVF ESIRIAMEDV QSRVESVAAS TQEQSASLEE LSAGVTRLTE LLNKTRENTS SANSALQEAN AALEELSASA QSLAELAQEL QRRIEFFKI // ID MGSA_THEMA Reviewed; 155 AA. AC Q9X0R7; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 2. DT 11-NOV-2015, entry version 100. DE RecName: Full=Methylglyoxal synthase {ECO:0000255|HAMAP-Rule:MF_00549}; DE Short=MGS {ECO:0000255|HAMAP-Rule:MF_00549}; DE EC=4.2.3.3 {ECO:0000255|HAMAP-Rule:MF_00549}; GN Name=mgsA {ECO:0000255|HAMAP-Rule:MF_00549}; GN OrderedLocusNames=TM_1185; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: Glycerone phosphate = methylglyoxal + CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00549}. CC -!- SIMILARITY: Belongs to the methylglyoxal synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00549}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD36260.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36260.1; ALT_INIT; Genomic_DNA. DR PIR; G72284; G72284. DR RefSeq; NP_228990.1; NC_000853.1. DR PDB; 1VMD; X-ray; 2.06 A; A/B=1-155. DR PDBsum; 1VMD; -. DR ProteinModelPortal; Q9X0R7; -. DR SMR; Q9X0R7; 1-149. DR STRING; 243274.TM1185; -. DR EnsemblBacteria; AAD36260; AAD36260; TM_1185. DR GeneID; 898300; -. DR KEGG; tma:TM1185; -. DR PATRIC; 23937310; VBITheMar51294_1203. DR eggNOG; ENOG4108Z5K; Bacteria. DR eggNOG; COG1803; LUCA. DR InParanoid; Q9X0R7; -. DR KO; K01734; -. DR OMA; EPQPHDP; -. DR OrthoDB; EOG644ZN1; -. DR EvolutionaryTrace; Q9X0R7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008929; F:methylglyoxal synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019242; P:methylglyoxal biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1380; -; 1. DR HAMAP; MF_00549; Methylglyoxal_synth; 1. DR InterPro; IPR004363; Methylgl_synth. DR InterPro; IPR018148; Methylglyoxal_synth_AS. DR InterPro; IPR011607; MGS-like_dom. DR Pfam; PF02142; MGS; 1. DR PIRSF; PIRSF006614; Methylglyox_syn; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF52335; SSF52335; 1. DR TIGRFAMs; TIGR00160; MGSA; 1. DR PROSITE; PS01335; METHYLGLYOXAL_SYNTH; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Lyase; Reference proteome. FT CHAIN 1 155 Methylglyoxal synthase. FT /FTId=PRO_0000178648. FT ACT_SITE 64 64 {ECO:0000255|HAMAP-Rule:MF_00549}. FT STRAND 6 11 {ECO:0000244|PDB:1VMD}. FT HELIX 13 15 {ECO:0000244|PDB:1VMD}. FT HELIX 16 25 {ECO:0000244|PDB:1VMD}. FT HELIX 27 30 {ECO:0000244|PDB:1VMD}. FT STRAND 33 37 {ECO:0000244|PDB:1VMD}. FT HELIX 39 49 {ECO:0000244|PDB:1VMD}. FT HELIX 59 61 {ECO:0000244|PDB:1VMD}. FT HELIX 63 72 {ECO:0000244|PDB:1VMD}. FT STRAND 78 82 {ECO:0000244|PDB:1VMD}. FT STRAND 85 87 {ECO:0000244|PDB:1VMD}. FT HELIX 95 104 {ECO:0000244|PDB:1VMD}. FT STRAND 109 112 {ECO:0000244|PDB:1VMD}. FT HELIX 113 121 {ECO:0000244|PDB:1VMD}. FT HELIX 123 126 {ECO:0000244|PDB:1VMD}. FT STRAND 129 134 {ECO:0000244|PDB:1VMD}. FT HELIX 136 148 {ECO:0000244|PDB:1VMD}. SQ SEQUENCE 155 AA; 17641 MW; A60A600F5D144205 CRC64; MDKKKRIALI AHDRRKRDLL EWVSFNLGTL SKHELYATGT TGALLQEKLG LKVHRLKSGP LGGDQQIGAM IAEGKIDVLI FFWDPLEPQA HDVDVKALIR IATVYNIPVA ITRSTADFLI SSPLMNDVYE KIQIDYEEEL ERRIRKVVEG EEEET // ID MINC_THEMA Reviewed; 210 AA. AC Q9X0D7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 111. DE RecName: Full=Probable septum site-determining protein MinC; GN Name=minC; OrderedLocusNames=TM_1047; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Cell division inhibitor that blocks the formation of CC polar Z ring septums. Rapidly oscillates between the poles of the CC cell to destabilize FtsZ filaments that have formed before they CC mature into polar Z rings. Prevents FtsZ polymerization (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with MinD and FtsZ. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MinC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36124.1; -; Genomic_DNA. DR PIR; A72301; A72301. DR RefSeq; NP_228853.1; NC_000853.1. DR RefSeq; WP_008193407.1; NZ_CP011107.1. DR PDB; 1HF2; X-ray; 2.20 A; A/B/C/D=1-210. DR PDBsum; 1HF2; -. DR ProteinModelPortal; Q9X0D7; -. DR SMR; Q9X0D7; 2-207. DR STRING; 243274.TM1047; -. DR EnsemblBacteria; AAD36124; AAD36124; TM_1047. DR GeneID; 897677; -. DR KEGG; tma:TM1047; -. DR PATRIC; 23937023; VBITheMar51294_1060. DR eggNOG; ENOG4107YDG; Bacteria. DR eggNOG; COG0850; LUCA. DR InParanoid; Q9X0D7; -. DR KO; K03610; -. DR OMA; RISLMIE; -. DR OrthoDB; EOG606588; -. DR BioCyc; TMAR243274:GC6P-1076-MONOMER; -. DR EvolutionaryTrace; Q9X0D7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro. DR GO; GO:0051726; P:regulation of cell cycle; IEA:UniProtKB-HAMAP. DR GO; GO:0051302; P:regulation of cell division; IEA:InterPro. DR Gene3D; 2.160.20.70; -; 1. DR Gene3D; 3.30.750.50; -; 1. DR HAMAP; MF_00267; MinC; 1. DR InterPro; IPR016098; CAP/MinC_C. DR InterPro; IPR013033; MinC. DR InterPro; IPR007874; MinC_N. DR InterPro; IPR005526; Septum_form_inhib_MinC_C. DR Pfam; PF03775; MinC_C; 1. DR SUPFAM; SSF63848; SSF63848; 1. DR TIGRFAMs; TIGR01222; minC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Complete proteome; KW Reference proteome; Septation. FT CHAIN 1 210 Probable septum site-determining protein FT MinC. FT /FTId=PRO_0000189066. FT STRAND 2 7 {ECO:0000244|PDB:1HF2}. FT STRAND 10 15 {ECO:0000244|PDB:1HF2}. FT HELIX 21 34 {ECO:0000244|PDB:1HF2}. FT HELIX 36 38 {ECO:0000244|PDB:1HF2}. FT STRAND 44 49 {ECO:0000244|PDB:1HF2}. FT HELIX 52 55 {ECO:0000244|PDB:1HF2}. FT HELIX 56 58 {ECO:0000244|PDB:1HF2}. FT HELIX 59 68 {ECO:0000244|PDB:1HF2}. FT STRAND 72 77 {ECO:0000244|PDB:1HF2}. FT STRAND 80 82 {ECO:0000244|PDB:1HF2}. FT STRAND 85 89 {ECO:0000244|PDB:1HF2}. FT STRAND 94 97 {ECO:0000244|PDB:1HF2}. FT STRAND 102 104 {ECO:0000244|PDB:1HF2}. FT STRAND 112 118 {ECO:0000244|PDB:1HF2}. FT STRAND 120 124 {ECO:0000244|PDB:1HF2}. FT STRAND 131 136 {ECO:0000244|PDB:1HF2}. FT STRAND 138 144 {ECO:0000244|PDB:1HF2}. FT STRAND 146 150 {ECO:0000244|PDB:1HF2}. FT TURN 152 154 {ECO:0000244|PDB:1HF2}. FT STRAND 159 165 {ECO:0000244|PDB:1HF2}. FT STRAND 168 172 {ECO:0000244|PDB:1HF2}. FT STRAND 175 177 {ECO:0000244|PDB:1HF2}. FT STRAND 187 192 {ECO:0000244|PDB:1HF2}. FT STRAND 195 200 {ECO:0000244|PDB:1HF2}. FT HELIX 201 203 {ECO:0000244|PDB:1HF2}. SQ SEQUENCE 210 AA; 22727 MW; E900E42AE905D023 CRC64; MVDFKMTKEG LVLLIKDYQN LEEVLNAISA RITQMGGFFA KGDRISLMIE NHNKHSQDIP RIVSHLRNLG LEVSQILVGS TVEGKENDLK VQSRTTVEST GKVIKRNIRS GQTVVHSGDV IVFGNVNKGA EILAGGSVVV FGKAQGNIRA GLNEGGQAVV AALDLQTSLI QIAGFITHSK GEENVPSIAH VKGNRIVIEP FDKVSFERSE // ID METE_THEMA Reviewed; 734 AA. AC Q9X112; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 126. DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; DE EC=2.1.1.14; DE AltName: Full=Cobalamin-independent methionine synthase; DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme; GN Name=metE; OrderedLocusNames=TM_1286; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5- CC methyltetrahydrofolate to homocysteine resulting in methionine CC formation. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydropteroyltri-L-glutamate + L- CC homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetE route): step CC 1/1. CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine CC synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36360.1; -; Genomic_DNA. DR PIR; E72271; E72271. DR RefSeq; NP_229090.1; NC_000853.1. DR RefSeq; WP_004079949.1; NZ_CP011107.1. DR PDB; 1T7L; X-ray; 2.00 A; A/B=2-734. DR PDB; 1XDJ; X-ray; 2.20 A; A/B=2-734. DR PDB; 1XPG; X-ray; 2.59 A; A/B=2-732. DR PDB; 1XR2; X-ray; 2.35 A; A/B=2-734. DR PDB; 3BQ5; X-ray; 2.00 A; A/B=2-734. DR PDB; 3BQ6; X-ray; 2.10 A; A/B=2-734. DR PDBsum; 1T7L; -. DR PDBsum; 1XDJ; -. DR PDBsum; 1XPG; -. DR PDBsum; 1XR2; -. DR PDBsum; 3BQ5; -. DR PDBsum; 3BQ6; -. DR ProteinModelPortal; Q9X112; -. DR SMR; Q9X112; 2-733. DR STRING; 243274.TM1286; -. DR DNASU; 898197; -. DR EnsemblBacteria; AAD36360; AAD36360; TM_1286. DR GeneID; 898197; -. DR KEGG; tma:TM1286; -. DR PATRIC; 23937512; VBITheMar51294_1302. DR eggNOG; ENOG4105DSS; Bacteria. DR eggNOG; COG0620; LUCA. DR InParanoid; Q9X112; -. DR KO; K00549; -. DR OMA; RFGWVQS; -. DR OrthoDB; EOG6FFS3G; -. DR BRENDA; 2.1.1.14; 6331. DR UniPathway; UPA00051; UER00082. DR EvolutionaryTrace; Q9X112; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008705; F:methionine synthase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0050667; P:homocysteine metabolic process; IBA:GO_Central. DR HAMAP; MF_00172; Meth_synth; 1. DR InterPro; IPR013215; Cbl-indep_Met_Synth_N. DR InterPro; IPR006276; Cobalamin-indep_Met_synthase. DR InterPro; IPR002629; Met_Synth_C/arc. DR Pfam; PF08267; Meth_synt_1; 1. DR Pfam; PF01717; Meth_synt_2; 1. DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1. DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; KW Metal-binding; Methionine biosynthesis; Methyltransferase; KW Reference proteome; Repeat; Transferase; Zinc. FT CHAIN 1 734 5-methyltetrahydropteroyltriglutamate-- FT homocysteine methyltransferase. FT /FTId=PRO_0000098674. FT METAL 618 618 Zinc. {ECO:0000250}. FT METAL 620 620 Zinc. {ECO:0000250}. FT METAL 704 704 Zinc. {ECO:0000250}. FT STRAND 2 4 {ECO:0000244|PDB:3BQ5}. FT HELIX 16 25 {ECO:0000244|PDB:1T7L}. FT HELIX 31 52 {ECO:0000244|PDB:1T7L}. FT STRAND 57 59 {ECO:0000244|PDB:1T7L}. FT HELIX 66 73 {ECO:0000244|PDB:1T7L}. FT HELIX 79 81 {ECO:0000244|PDB:1T7L}. FT HELIX 87 94 {ECO:0000244|PDB:1T7L}. FT STRAND 101 104 {ECO:0000244|PDB:1T7L}. FT STRAND 111 114 {ECO:0000244|PDB:1T7L}. FT HELIX 128 137 {ECO:0000244|PDB:1T7L}. FT TURN 138 140 {ECO:0000244|PDB:1T7L}. FT STRAND 144 148 {ECO:0000244|PDB:1T7L}. FT HELIX 150 155 {ECO:0000244|PDB:1T7L}. FT HELIX 167 190 {ECO:0000244|PDB:1T7L}. FT STRAND 196 199 {ECO:0000244|PDB:1T7L}. FT HELIX 201 204 {ECO:0000244|PDB:1T7L}. FT HELIX 209 220 {ECO:0000244|PDB:1T7L}. FT TURN 221 224 {ECO:0000244|PDB:1T7L}. FT STRAND 227 230 {ECO:0000244|PDB:1T7L}. FT HELIX 239 243 {ECO:0000244|PDB:1T7L}. FT STRAND 248 253 {ECO:0000244|PDB:1T7L}. FT HELIX 259 267 {ECO:0000244|PDB:1T7L}. FT STRAND 273 280 {ECO:0000244|PDB:1T7L}. FT HELIX 290 300 {ECO:0000244|PDB:1T7L}. FT STRAND 303 309 {ECO:0000244|PDB:1T7L}. FT HELIX 311 313 {ECO:0000244|PDB:1T7L}. FT STRAND 323 325 {ECO:0000244|PDB:1T7L}. FT TURN 326 328 {ECO:0000244|PDB:1T7L}. FT HELIX 329 331 {ECO:0000244|PDB:1T7L}. FT HELIX 335 349 {ECO:0000244|PDB:1T7L}. FT TURN 362 365 {ECO:0000244|PDB:1T7L}. FT HELIX 368 375 {ECO:0000244|PDB:1T7L}. FT HELIX 379 381 {ECO:0000244|PDB:1T7L}. FT HELIX 388 399 {ECO:0000244|PDB:1T7L}. FT HELIX 416 426 {ECO:0000244|PDB:1T7L}. FT HELIX 432 453 {ECO:0000244|PDB:1T7L}. FT STRAND 456 458 {ECO:0000244|PDB:1T7L}. FT HELIX 468 473 {ECO:0000244|PDB:1T7L}. FT STRAND 476 480 {ECO:0000244|PDB:1T7L}. FT STRAND 487 490 {ECO:0000244|PDB:1T7L}. FT STRAND 493 495 {ECO:0000244|PDB:1T7L}. FT STRAND 499 505 {ECO:0000244|PDB:1T7L}. FT HELIX 512 520 {ECO:0000244|PDB:1T7L}. FT STRAND 526 531 {ECO:0000244|PDB:1T7L}. FT HELIX 533 538 {ECO:0000244|PDB:1T7L}. FT STRAND 540 542 {ECO:0000244|PDB:1T7L}. FT STRAND 544 546 {ECO:0000244|PDB:1T7L}. FT HELIX 548 568 {ECO:0000244|PDB:1T7L}. FT STRAND 573 577 {ECO:0000244|PDB:1T7L}. FT HELIX 580 583 {ECO:0000244|PDB:1T7L}. FT HELIX 589 591 {ECO:0000244|PDB:1T7L}. FT HELIX 592 606 {ECO:0000244|PDB:1T7L}. FT STRAND 613 618 {ECO:0000244|PDB:1T7L}. FT TURN 625 627 {ECO:0000244|PDB:1T7L}. FT HELIX 628 631 {ECO:0000244|PDB:1T7L}. FT STRAND 637 642 {ECO:0000244|PDB:1T7L}. FT TURN 644 648 {ECO:0000244|PDB:1T7L}. FT HELIX 649 651 {ECO:0000244|PDB:1T7L}. FT HELIX 652 655 {ECO:0000244|PDB:1T7L}. FT STRAND 662 667 {ECO:0000244|PDB:1T7L}. FT STRAND 673 675 {ECO:0000244|PDB:1XPG}. FT HELIX 679 689 {ECO:0000244|PDB:1T7L}. FT TURN 690 692 {ECO:0000244|PDB:1T7L}. FT HELIX 695 697 {ECO:0000244|PDB:1T7L}. FT STRAND 698 701 {ECO:0000244|PDB:1T7L}. FT HELIX 711 731 {ECO:0000244|PDB:1T7L}. SQ SEQUENCE 734 AA; 85571 MW; 34B19187480D443B CRC64; MKAYAFGFPK IGEKREFKKA LEDFWKGKIT EEQFEEEMNK LRMYMVENYR KNVDVIPSNE LSYYDFVLDT AVMVGAVPER FGEYRGLSTY FDMARGGKAL EMTKFFNTNY HYLVPEIETE EFYLLENKPL EDYLFFKSKG IETAPWVIGP FTFLYLSKRN GEWIRRPNQM EKLLESLVSV YKEVFEKLVE NGCKEILVNE PAFVCDLEKA HWDLILNVYR ELSEFPLTVF TYYDSVSDYE ACVSLPVKRL HFDFVSNEEN LKNLEKHGFP EDKKLVAGVI NGRQPWKVDL RKVASLVEKL GASAISNSCP LFHLPVTLEL ENNLPGGLKE KLAFAKEKLE ELKMLKDFLE GKTFDLPNVS FEDFAVDLQA VERVRNLPED SFRREKEYTE RDRIQRERLN LPLFPTTTIG SFPQTPEVRK MRSKYRKGEI SKEEYEAFIK EQIKKAIELQ EEIGLDVLVH GEFERTDMVE FFAEKLNGIA TTQNGWVLSY GSRCYRPPII YGTVTRPEPM TLKEITYAQS LTEKPVKGML TGPVTIMSWS YYREDIPERE IAYQIALAIN EEVKDLEEAG IKIVQIDEPA FREKAPIKKS KWPEYFEWAI NAFNLAANAR PETQIHAHMC YSDFNEIIEY IHQLEFDVIS IEASRSKGEI ISAFENFKGW IKQIGVGVWD IHSPAVPSIN EMREIVERVL RVLPKELIWI NPDCGLKTRN WDEVIPSLRN MVALAKEMRE KFES // ID MGGS_THEMA Reviewed; 427 AA. AC Q9X0V7; G4FEB6; DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Mannosylglucosylglycerate synthase {ECO:0000303|PubMed:20061481}; DE EC=2.4.1.- {ECO:0000269|PubMed:20061481}; GN Name=mggS {ECO:0000303|PubMed:20061481}; GN OrderedLocusNames=TM_1230 {ECO:0000312|EMBL:AAD36305.1}; GN ORFNames=THEMA_08180 {ECO:0000312|EMBL:AHD18863.1}, GN Tmari_1237 {ECO:0000312|EMBL:AGL50161.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RG DOE Joint Genome Institute; RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=20061481; DOI=10.1128/JB.01424-09; RA Fernandes C., Mendes V., Costa J., Empadinhas N., Jorge C., Lamosa P., RA Santos H., da Costa M.S.; RT "Two alternative pathways for the synthesis of the rare compatible RT solute mannosylglucosylglycerate in Petrotoga mobilis."; RL J. Bacteriol. 192:1624-1633(2010). CC -!- FUNCTION: Catalyzes the synthesis of mannosylglucosylglycerate CC (MGG) from glucosylglycerate (GG) and GDP-mannose. CC {ECO:0000269|PubMed:20061481}. CC -!- CATALYTIC ACTIVITY: GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-D- CC glycerate = GDP + 2-O-(2-O-(alpha-D-mannopranosyl)-alpha-D- CC glucopyranosyl)-3-D-glycerate. {ECO:0000269|PubMed:20061481}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:20061481}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:20061481}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:20061481}; CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000269|PubMed:20061481}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.0. {ECO:0000269|PubMed:20061481}; CC Temperature dependence: CC Optimum temperature is 60 degrees Celsius. CC {ECO:0000269|PubMed:20061481}; CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36305.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50161.1; -; Genomic_DNA. DR EMBL; CP007013; AHD18863.1; -; Genomic_DNA. DR PIR; G72278; G72278. DR RefSeq; NP_229035.1; NC_000853.1. DR RefSeq; WP_004080052.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0V7; -. DR STRING; 243274.TM1230; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAD36305; AAD36305; TM_1230. DR EnsemblBacteria; AGL50161; AGL50161; Tmari_1237. DR EnsemblBacteria; AHD18863; AHD18863; THEMA_08180. DR GeneID; 898254; -. DR KEGG; tma:TM1230; -. DR KEGG; tmi:THEMA_08180; -. DR KEGG; tmm:Tmari_1237; -. DR KEGG; tmw:THMA_1256; -. DR PATRIC; 23937402; VBITheMar51294_1248. DR eggNOG; ENOG4105IRK; Bacteria. DR eggNOG; ENOG410XSPD; LUCA. DR InParanoid; Q9X0V7; -. DR OMA; HVVINTI; -. DR OrthoDB; EOG60CWHV; -. DR BioCyc; MetaCyc:MONOMER-16144; -. DR BioCyc; TMAR243274:GC6P-1260-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 1: Evidence at protein level; KW Cobalt; Complete proteome; Glycosyltransferase; Magnesium; Manganese; KW Nickel; Reference proteome; Transferase. FT CHAIN 1 427 Mannosylglucosylglycerate synthase. FT /FTId=PRO_0000431558. SQ SEQUENCE 427 AA; 49702 MW; C3C1662ACA7D5AA5 CRC64; MKIALIHYRG GLMDGVSLEM EKWKKVLTKM GHEVHIVAEN KKEGVDLTLK EIGFENPDFE RVNRNFFGGI KDFLSEKEFL DFLKEKEEEL FHILNEALKD YDLIVPNNIW SLGLFPSLGL ALSRLEKNFV AHHHDFWWER KHLIPENRRF REILDKHFPP DLPNVKHVVI NTIAQRELKR RRNIDSVVVP NVMDFSSPIT SEEMYHRVRE ELQIAPGTIV ALQATRIDRR KTIELSIDVV SLLKETLTSK KEADLYNGER YSGEVILLFS GICEDEEYLK ELKEYASSKG VSLLVLSEEV RKNTSLFWKL YNAADFVTYP SILEGWGNQL LEAIAAKKPV VLFEYEVFKS DIKPAGLKYV SLGDRCFREN GLVKVDERIL KKAVEEISRL LFDPSLYRET VEHNFEVGKR HFSLERLEDI LSREVLP // ID MIAA_THEMA Reviewed; 305 AA. AC Q9WYZ5; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE EC=2.5.1.75 {ECO:0000255|HAMAP-Rule:MF_00185}; DE AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=DMAPP:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=DMATase {ECO:0000255|HAMAP-Rule:MF_00185}; DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPP transferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPPT {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPTase {ECO:0000255|HAMAP-Rule:MF_00185}; GN Name=miaA {ECO:0000255|HAMAP-Rule:MF_00185}; GN OrderedLocusNames=TM_0525; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the CC adenine at position 37 in tRNAs that read codons beginning with CC uridine, leading to the formation of N6-(dimethylallyl)adenosine CC (i(6)A). {ECO:0000255|HAMAP-Rule:MF_00185}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + adenine(37) in CC tRNA = diphosphate + N(6)-dimethylallyladenine(37) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_00185}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00185}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00185}. CC -!- SIMILARITY: Belongs to the IPP transferase family. CC {ECO:0000255|HAMAP-Rule:MF_00185}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35610.1; -; Genomic_DNA. DR PIR; C72366; C72366. DR RefSeq; NP_228335.1; NC_000853.1. DR RefSeq; WP_004081395.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYZ5; -. DR STRING; 243274.TM0525; -. DR DNASU; 897577; -. DR EnsemblBacteria; AAD35610; AAD35610; TM_0525. DR GeneID; 897577; -. DR KEGG; tma:TM0525; -. DR PATRIC; 23935957; VBITheMar51294_0533. DR eggNOG; ENOG4105DKX; Bacteria. DR eggNOG; COG0324; LUCA. DR InParanoid; Q9WYZ5; -. DR KO; K00791; -. DR OMA; TWFRNQT; -. DR OrthoDB; EOG661HB3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IBA:GO_Central. DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00185; IPP_trans; 1. DR InterPro; IPR018022; IPP_trans. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01715; IPPT; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00174; miaA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Nucleotide-binding; KW Reference proteome; Transferase; tRNA processing. FT CHAIN 1 305 tRNA dimethylallyltransferase. FT /FTId=PRO_0000163997. FT NP_BIND 8 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00185}. FT REGION 10 15 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00185}. FT REGION 33 36 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. FT SITE 99 99 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. FT SITE 121 121 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. SQ SEQUENCE 305 AA; 35926 MW; 59C3C845AEC64AC3 CRC64; MKIAIVGGPT AVGKTDIMIE VCEEIGAEII SMDSRQIYRY MDIGTAKPTP EQRKRVLHHM IDIIDPDEYY NAFMYRKDSL RAMEDVLRRG KIPVYVGGTG LYADALVRGI FEGVPADENI RKELRELERR EPGILRKMLE ELDPEAATRI HPNDLKRTIR ALEVYMKTGR RISELQKEAK GDDRFFIIVL TRERYELYER INKRVDKMIE MGLVDEVKRL LGMGYSKDLN SMKTIGYKEV IDYLEGKYDF DKMVHLIKRN TRHFARRQII WFKRYKEAVW YNLTFEDVGE VKEKLKKLIV ENFSV // ID MIAB_THEMA Reviewed; 443 AA. AC Q9WZC1; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000255|HAMAP-Rule:MF_01864}; DE EC=2.8.4.3 {ECO:0000255|HAMAP-Rule:MF_01864}; DE AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB {ECO:0000255|HAMAP-Rule:MF_01864}; DE AltName: Full=tRNA-i(6)A37 methylthiotransferase {ECO:0000255|HAMAP-Rule:MF_01864}; GN Name=miaB {ECO:0000255|HAMAP-Rule:MF_01864}; GN OrderedLocusNames=TM_0653; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION, COFACTOR, AND SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=12766153; DOI=10.1074/jbc.M301518200; RA Pierrel F., Hernandez H.L., Johnson M.K., Fontecave M., Atta M.; RT "MiaB protein from Thermotoga maritima. Characterization of an RT extremely thermophilic tRNA-methylthiotransferase."; RL J. Biol. Chem. 278:29515-29524(2003). RN [3] RP FUNCTION AS A METHYLTHIOTRANSFERASE. RX PubMed=15339930; DOI=10.1074/jbc.M408562200; RA Pierrel F., Douki T., Fontecave M., Atta M.; RT "MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme RT involved in thiolation and methylation of tRNA."; RL J. Biol. Chem. 279:47555-47563(2004). RN [4] RP COFACTOR, AND MUTAGENESIS OF CYS-10; CYS-150; CYS-154 AND CYS-157. RX PubMed=17407324; DOI=10.1021/bi7000449; RA Hernandez H.L., Pierrel F., Elleingand E., Garcia-Serres R., RA Huynh B.H., Johnson M.K., Fontecave M., Atta M.; RT "MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in RT the thiolation and methylation of tRNA, contains two essential [4Fe- RT 4S] clusters."; RL Biochemistry 46:5140-5147(2007). CC -!- FUNCTION: Catalyzes the methylthiolation of N6- CC (dimethylallyl)adenosine (i(6)A), leading to the formation of 2- CC methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 CC in tRNAs that read codons beginning with uridine. CC {ECO:0000255|HAMAP-Rule:MF_01864, ECO:0000269|PubMed:12766153, CC ECO:0000269|PubMed:15339930}. CC -!- CATALYTIC ACTIVITY: N(6)-dimethylallyladenine(37) in tRNA + CC sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced CC electron acceptor = 2-methylthio-N(6)-dimethylallyladenine(37) in CC tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine CC + 5'-deoxyadenosine + electron acceptor. {ECO:0000255|HAMAP- CC Rule:MF_01864}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01864, CC ECO:0000269|PubMed:12766153, ECO:0000269|PubMed:17407324}; CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01864, ECO:0000269|PubMed:12766153, CC ECO:0000269|PubMed:17407324}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01864, CC ECO:0000269|PubMed:12766153}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SIMILARITY: Contains 1 MTTase N-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|HAMAP- CC Rule:MF_01864}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35737.1; -; Genomic_DNA. DR PIR; D72352; D72352. DR RefSeq; NP_228462.1; NC_000853.1. DR RefSeq; WP_004081141.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZC1; -. DR STRING; 243274.TM0653; -. DR DNASU; 897761; -. DR EnsemblBacteria; AAD35737; AAD35737; TM_0653. DR GeneID; 897761; -. DR KEGG; tma:TM0653; -. DR PATRIC; 23936220; VBITheMar51294_0663. DR eggNOG; ENOG4105CIW; Bacteria. DR eggNOG; COG0621; LUCA. DR InParanoid; Q9WZC1; -. DR KO; K06168; -. DR OMA; IPMDLIL; -. DR OrthoDB; EOG6P5ZD8; -. DR BRENDA; 2.8.4.3; 6331. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0035597; F:N6-isopentenyladenosine methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GOC. DR Gene3D; 3.80.30.20; -; 1. DR HAMAP; MF_01864; tRNA_metthiotr_MiaB; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR005839; Methylthiotransferase. DR InterPro; IPR020612; Methylthiotransferase_CS. DR InterPro; IPR013848; Methylthiotransferase_N. DR InterPro; IPR006463; MiaB_methiolase. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR002792; TRAM_dom. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF01938; TRAM; 1. DR Pfam; PF00919; UPF0004; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00089; TIGR00089; 1. DR PROSITE; PS51449; MTTASE_N; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. DR PROSITE; PS50926; TRAM; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; S-adenosyl-L-methionine; KW Transferase; tRNA processing. FT CHAIN 1 443 tRNA-2-methylthio-N(6)- FT dimethylallyladenosine synthase. FT /FTId=PRO_0000359590. FT DOMAIN 1 114 MTTase N-terminal. {ECO:0000255|HAMAP- FT Rule:MF_01864}. FT DOMAIN 370 431 TRAM. {ECO:0000255|HAMAP-Rule:MF_01864}. FT METAL 10 10 Iron-sulfur (4Fe-4S). {ECO:0000305}. FT METAL 46 46 Iron-sulfur (4Fe-4S). {ECO:0000305}. FT METAL 79 79 Iron-sulfur (4Fe-4S). {ECO:0000305}. FT METAL 150 150 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000305}. FT METAL 154 154 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000305}. FT METAL 157 157 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000305}. FT MUTAGEN 10 10 C->A: Loss of activity. FT {ECO:0000269|PubMed:17407324}. FT MUTAGEN 150 150 C->A: Decreased iron content and loss of FT activity; when associated with A-154 and FT A-157. {ECO:0000269|PubMed:17407324}. FT MUTAGEN 154 154 C->A: Decreased iron content and loss of FT activity; when associated with A-150 and FT A-157. {ECO:0000269|PubMed:17407324}. FT MUTAGEN 157 157 C->A: Decreased iron content and loss of FT activity; when associated with A-150 and FT A-154. {ECO:0000269|PubMed:17407324}. SQ SEQUENCE 443 AA; 50742 MW; 2C738B79667C9895 CRC64; MRFYIKTFGC QMNENDSEAM AGLLVKEGFT PASSPEEADV VIINTCAVRR KSEEKAYSEL GQVLKLKKKK KIVVGVAGCV AEKEREKFLE KGADFVLGTR AVPRVTEAVK KALEGEKVAL FEDHLDEYTH ELPRIRTSRH HAWVTIIHGC DRFCTYCIVP YTRGRERSRP MADILEEVKK LAEQGYREVT FLGQNVDAYG KDLKDGSSLA KLLEEASKIE GIERIWFLTS YPTDFSDELI EVIAKNPKVA KSVHLPVQSG SNRILKLMNR RYTKEEYLAL LEKIRSKVPE VAISSDIIVG FPTETEEDFM ETVDLVEKAQ FERLNLAIYS PREGTVAWKY YKDDVPYEEK VRRMQFLMNL QKRINRKLNE RYRGKTVRII VEAQAKNGLF YGRDIRNKII AFEGEDWMIG RFADVKVEKI TAGPLYGKVV WVEKTPSPVS SSE // ID MNME_THEMA Reviewed; 450 AA. AC Q9WYA4; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 128. DE RecName: Full=tRNA modification GTPase MnmE {ECO:0000255|HAMAP-Rule:MF_00379}; DE EC=3.6.5.-; GN Name=mnmE {ECO:0000255|HAMAP-Rule:MF_00379}; GN Synonyms=trmE {ECO:0000255|HAMAP-Rule:MF_00379}; GN OrderedLocusNames=TM_0267; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP CHARACTERIZATION. RX PubMed=11092873; DOI=10.1128/JB.182.24.7078-7082.2000; RA Yamanaka K., Hwang J., Inouye M.; RT "Characterization of GTPase activity of TrmE, a member of a novel RT GTPase superfamily, from Thermotoga maritima."; RL J. Bacteriol. 182:7078-7082(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH RP FORMYLTETRAHYDROFOLATE; GTP-BINDING, AND SUBUNIT. RX PubMed=15616586; DOI=10.1038/sj.emboj.7600507; RA Scrima A., Vetter I.R., Armengod M.-E., Wittinghofer A.; RT "The structure of the TrmE GTP-binding protein and its implications RT for tRNA modification."; RL EMBO J. 24:23-33(2005). CC -!- FUNCTION: Exhibits a very high intrinsic GTPase hydrolysis rate. CC Involved in the addition of a carboxymethylaminomethyl (cmnm) CC group at the wobble position (U34) of certain tRNAs, forming tRNA- CC cmnm(5)s(2)U34. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00379}; CC Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00379}; CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG CC subunits. {ECO:0000255|HAMAP-Rule:MF_00379}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00379}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. TrmE GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00379}. CC -!- SIMILARITY: Contains 1 TrmE-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35356.1; -; Genomic_DNA. DR PIR; A72397; A72397. DR RefSeq; NP_228080.1; NC_000853.1. DR RefSeq; WP_004082971.1; NZ_CP011107.1. DR PDB; 1XZP; X-ray; 2.30 A; A=1-450, B=1-118. DR PDB; 1XZQ; X-ray; 2.90 A; A=1-450, B=1-117. DR PDBsum; 1XZP; -. DR PDBsum; 1XZQ; -. DR ProteinModelPortal; Q9WYA4; -. DR SMR; Q9WYA4; 1-450. DR STRING; 243274.TM0267; -. DR EnsemblBacteria; AAD35356; AAD35356; TM_0267. DR GeneID; 897178; -. DR KEGG; tma:TM0267; -. DR PATRIC; 23935411; VBITheMar51294_0271. DR eggNOG; ENOG4105C1H; Bacteria. DR eggNOG; COG0486; LUCA. DR InParanoid; Q9WYA4; -. DR KO; K03650; -. DR OMA; FTPRYAY; -. DR OrthoDB; EOG6DC6K1; -. DR EvolutionaryTrace; Q9WYA4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.120.430; -; 3. DR Gene3D; 3.30.1360.120; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00379; GTPase_MnmE; 1. DR InterPro; IPR031168; G_TrmE. DR InterPro; IPR018948; GTP-bd_TrmE_N. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR004520; GTPase_MnmE. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR027368; MnmE_dom2. DR InterPro; IPR025867; MnmE_helical. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR027266; TrmE/GcvT_dom1. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF12631; MnmE_helical; 1. DR Pfam; PF10396; TrmE_N; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51709; G_TRME; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; GTP-binding; Hydrolase; KW Magnesium; Metal-binding; Nucleotide-binding; Potassium; KW Reference proteome; tRNA processing. FT CHAIN 1 450 tRNA modification GTPase MnmE. FT /FTId=PRO_0000188939. FT DOMAIN 211 372 TrmE-type G. FT NP_BIND 221 226 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 240 246 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 265 268 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 326 329 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 353 355 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 221 221 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 225 225 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 240 240 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 242 242 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 245 245 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 246 246 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT BINDING 20 20 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379, FT ECO:0000269|PubMed:15616586}. FT BINDING 78 78 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379, FT ECO:0000269|PubMed:15616586}. FT BINDING 117 117 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379, FT ECO:0000269|PubMed:15616586}. FT BINDING 450 450 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379, FT ECO:0000269|PubMed:15616586}. FT STRAND 4 7 {ECO:0000244|PDB:1XZP}. FT STRAND 11 13 {ECO:0000244|PDB:1XZP}. FT STRAND 17 25 {ECO:0000244|PDB:1XZP}. FT HELIX 26 31 {ECO:0000244|PDB:1XZP}. FT STRAND 34 38 {ECO:0000244|PDB:1XZP}. FT STRAND 46 50 {ECO:0000244|PDB:1XZP}. FT STRAND 59 65 {ECO:0000244|PDB:1XZP}. FT STRAND 69 74 {ECO:0000244|PDB:1XZP}. FT STRAND 76 81 {ECO:0000244|PDB:1XZP}. FT HELIX 85 96 {ECO:0000244|PDB:1XZP}. FT TURN 97 99 {ECO:0000244|PDB:1XZP}. FT HELIX 107 114 {ECO:0000244|PDB:1XZP}. FT HELIX 120 131 {ECO:0000244|PDB:1XZP}. FT HELIX 135 145 {ECO:0000244|PDB:1XZP}. FT HELIX 148 172 {ECO:0000244|PDB:1XZP}. FT TURN 174 176 {ECO:0000244|PDB:1XZP}. FT HELIX 181 210 {ECO:0000244|PDB:1XZP}. FT STRAND 212 217 {ECO:0000244|PDB:1XZP}. FT HELIX 220 223 {ECO:0000244|PDB:1XZP}. FT HELIX 226 234 {ECO:0000244|PDB:1XZP}. FT STRAND 252 256 {ECO:0000244|PDB:1XZP}. FT STRAND 259 267 {ECO:0000244|PDB:1XZP}. FT HELIX 282 291 {ECO:0000244|PDB:1XZP}. FT STRAND 293 300 {ECO:0000244|PDB:1XZP}. FT HELIX 307 316 {ECO:0000244|PDB:1XZP}. FT STRAND 319 327 {ECO:0000244|PDB:1XZP}. FT HELIX 336 343 {ECO:0000244|PDB:1XZP}. FT STRAND 349 353 {ECO:0000244|PDB:1XZP}. FT HELIX 354 356 {ECO:0000244|PDB:1XZP}. FT HELIX 360 370 {ECO:0000244|PDB:1XZP}. FT HELIX 372 378 {ECO:0000244|PDB:1XZP}. FT HELIX 386 407 {ECO:0000244|PDB:1XZP}. FT HELIX 412 429 {ECO:0000244|PDB:1XZP}. FT STRAND 431 433 {ECO:0000244|PDB:1XZQ}. FT HELIX 436 443 {ECO:0000244|PDB:1XZP}. SQ SEQUENCE 450 AA; 50682 MW; 8DAD2D1EB8500CC0 CRC64; MDTIVAVATP PGKGAIAILR LSGPDSWKIV QKHLRTRSKI VPRKAIHGWI HENGEDVDEV VVVFYKSPKS YTGEDMVEVM CHGGPLVVKK LLDLFLKSGA RMAEPGEFTK RAFLNGKMDL TSAEAVRDLI EAKSETSLKL SLRNLKGGLR DFVDSLRREL IEVLAEIRVE LDYPDEIETN TGEVVTRLER IKEKLTEELK KADAGILLNR GLRMVIVGKP NVGKSTLLNR LLNEDRAIVT DIPGTTRDVI SEEIVIRGIL FRIVDTAGVR SETNDLVERL GIERTLQEIE KADIVLFVLD ASSPLDEEDR KILERIKNKR YLVVINKVDV VEKINEEEIK NKLGTDRHMV KISALKGEGL EKLEESIYRE TQEIFERGSD SLITNLRQKQ LLENVKGHLE DAIKSLKEGM PVDMASIDLE RALNLLDEVT GRSFREDLLD TIFSNFCVGK // ID MTAB_THEMA Reviewed; 434 AA. AC Q9WZT7; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=Threonylcarbamoyladenosine tRNA methylthiotransferase MtaB; DE EC=2.8.4.5; DE AltName: Full=tRNA-t(6)A37 methylthiotransferase; GN Name=mtaB; OrderedLocusNames=TM_0830; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the methylthiolation of N6- CC threonylcarbamoyladenosine (t(6)A), leading to the formation of 2- CC methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position CC 37 in tRNAs that read codons beginning with adenine. CC {ECO:0000250|UniProtKB:P54462}. CC -!- CATALYTIC ACTIVITY: N(6)-L-threonylcarbamoyladenine(37) in tRNA + CC sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced CC electron acceptor = 2-methylthio-N(6)-L- CC threonylcarbamoyladenine(37) in tRNA + S-adenosyl-L-homocysteine + CC (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron CC acceptor. {ECO:0000250|UniProtKB:P54462}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00780}; CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|PROSITE-ProRule:PRU00780}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE- CC ProRule:PRU00780}. CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MtaB CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 MTTase N-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00780}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35912.1; -; Genomic_DNA. DR PIR; B72328; B72328. DR RefSeq; NP_228639.1; NC_000853.1. DR RefSeq; WP_004080813.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZT7; -. DR STRING; 243274.TM0830; -. DR EnsemblBacteria; AAD35912; AAD35912; TM_0830. DR GeneID; 898500; -. DR KEGG; tma:TM0830; -. DR PATRIC; 23936586; VBITheMar51294_0843. DR eggNOG; ENOG4105CIW; Bacteria. DR eggNOG; COG0621; LUCA. DR InParanoid; Q9WZT7; -. DR KO; K18707; -. DR OMA; YLHVFTY; -. DR OrthoDB; EOG6P5ZD8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035598; F:N6-threonylcarbomyladenosine methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0061712; F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase; IEA:UniProtKB-EC. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GOC. DR Gene3D; 3.40.50.1110; -; 1. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR005839; Methylthiotransferase. DR InterPro; IPR020612; Methylthiotransferase_CS. DR InterPro; IPR013848; Methylthiotransferase_N. DR InterPro; IPR006467; MiaB-like_C. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR013830; SGNH_hydro. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF00919; UPF0004; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR01579; MiaB-like-C; 1. DR TIGRFAMs; TIGR00089; TIGR00089; 1. DR PROSITE; PS51449; MTTASE_N; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; S-adenosyl-L-methionine; KW Transferase; tRNA processing. FT CHAIN 1 434 Threonylcarbamoyladenosine tRNA FT methylthiotransferase MtaB. FT /FTId=PRO_0000141754. FT DOMAIN 2 112 MTTase N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00780}. FT METAL 11 11 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 46 46 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 77 77 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 147 147 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 151 151 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 154 154 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. SQ SEQUENCE 434 AA; 49324 MW; C33186CD10545B20 CRC64; MKTVRIETFG CKVNQYESEY MAEQLEKAGY VVLPDGNAAY YIVNSCAVTK EVEKKVKRLI KSIRNRNKNA KIILTGCFAQ LSPDEAKNLP VDMVLGIDEK KHIVDHINSL NGKQQVVVSE PGRPVYEKVK GSFEDRTRSY IKVEDGCDNT CTYCAIRLAR GTRIRSKPLE IFKEEFAEMV MKGYKEIVIT GVNLGKYGKD MGSSLAELLK VIEKVPGDYR VRLSSINVED VNDEIVKAFK RNPRLCPHLH ISVQSGSDDV LKRMGRKYKI SDFMRVVDKL RSIDPDFSIT TDIIVGFPGE TDADFQRTLE LVEKVEFSRV HIFRFSPRPG TPASRMEGGV PESKKKERLD VLKEKAKDVS IRYRKRIIGK ERKVLAEWYV MKGVLSGYDE YYVKHEFVGN RVGEFHSVRV KSLSEEGVIS CRADMVEGKV PARG // ID MNMA_THEMA Reviewed; 358 AA. AC Q9WYZ0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 104. DE RecName: Full=tRNA-specific 2-thiouridylase MnmA {ECO:0000255|HAMAP-Rule:MF_00144}; DE EC=2.8.1.13 {ECO:0000255|HAMAP-Rule:MF_00144}; GN Name=mnmA {ECO:0000255|HAMAP-Rule:MF_00144}; Synonyms=trmU; GN OrderedLocusNames=TM_0520; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble CC position (U34) of tRNA, leading to the formation of s(2)U34. CC {ECO:0000255|HAMAP-Rule:MF_00144}. CC -!- CATALYTIC ACTIVITY: A [protein]-S-sulfanyl-L-cysteine + CC uridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L- CC cysteine + 2-thiouridine(34) in tRNA + AMP + diphosphate + CC acceptor. {ECO:0000255|HAMAP-Rule:MF_00144}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00144}. CC -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000255|HAMAP- CC Rule:MF_00144}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35605.1; -; Genomic_DNA. DR PIR; F72365; F72365. DR RefSeq; NP_228330.1; NC_000853.1. DR RefSeq; WP_004081405.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYZ0; -. DR STRING; 243274.TM0520; -. DR EnsemblBacteria; AAD35605; AAD35605; TM_0520. DR GeneID; 897571; -. DR KEGG; tma:TM0520; -. DR PATRIC; 23935945; VBITheMar51294_0527. DR eggNOG; ENOG4105CCJ; Bacteria. DR eggNOG; COG0482; LUCA. DR InParanoid; Q9WYZ0; -. DR KO; K00566; -. DR OMA; NPQSFRT; -. DR OrthoDB; EOG6RZB5H; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central. DR Gene3D; 2.30.30.280; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1. DR InterPro; IPR023382; Adenine_a_hdrlase_dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR004506; tRNA-specific_2-thiouridylase. DR PANTHER; PTHR11933; PTHR11933; 1. DR TIGRFAMs; TIGR00420; trmU; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Disulfide bond; KW Nucleotide-binding; Reference proteome; RNA-binding; Transferase; KW tRNA processing; tRNA-binding. FT CHAIN 1 358 tRNA-specific 2-thiouridylase MnmA. FT /FTId=PRO_0000121693. FT NP_BIND 6 13 ATP. {ECO:0000255|HAMAP-Rule:MF_00144}. FT REGION 151 153 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT ACT_SITE 103 103 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00144}. FT ACT_SITE 201 201 Cysteine persulfide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT BINDING 32 32 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00144}. FT BINDING 127 127 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT SITE 128 128 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT SITE 337 337 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT DISULFID 103 201 Alternate. {ECO:0000255|HAMAP- FT Rule:MF_00144}. SQ SEQUENCE 358 AA; 40670 MW; C41D1C81BDE04416 CRC64; MKVGVALSGG VDSAVALYLL LKEGHEVKAF HMKTKEDEFF IKKEIKKKVC CSPSDTADAM RIAHFLGVEI EIVDVKEIFR EKVIEPFKRD LLKGLTPNPC AHCNRFVKFG YLMDYVLNQG FDAFASGHYA RIEFSEKYGR KVIKKGVDLK KDQSYFLARI EPWRIERLIF PNGIYTKEEI RKIAEEAGIH VAKKQESQDV CFIPDGSIEN FLKDEGITLK DGDIITPEGE VVGRHFGYPL YTIGQRKGFK IEKFGRRYYV RGKIPEKNVV VVSDLEDVFF SGLIAEDPVW HVEVPEEFRC VCRVRKKSEE APAVVKVKDN EVEVSFEKKV FAVTPGQIAA FYDGDTLLGG AIIKEGIR // ID MNMG_THEMA Reviewed; 629 AA. AC Q9WYA1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 20-JAN-2016, entry version 108. DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000255|HAMAP-Rule:MF_00129}; DE AltName: Full=Glucose-inhibited division protein A {ECO:0000255|HAMAP-Rule:MF_00129}; GN Name=mnmG {ECO:0000255|HAMAP-Rule:MF_00129}; GN Synonyms=gidA {ECO:0000255|HAMAP-Rule:MF_00129}; GN OrderedLocusNames=TM_0263; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: NAD-binding protein involved in the addition of a CC carboxymethylaminomethyl (cmnm) group at the wobble position (U34) CC of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000255|HAMAP- CC Rule:MF_00129}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00129}; CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG CC subunits. {ECO:0000255|HAMAP-Rule:MF_00129}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00129}. CC -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000255|HAMAP- CC Rule:MF_00129}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35351.1; -; Genomic_DNA. DR PIR; F72400; F72400. DR RefSeq; NP_228076.1; NC_000853.1. DR RefSeq; WP_010865084.1; NC_000853.1. DR ProteinModelPortal; Q9WYA1; -. DR STRING; 243274.TM0263; -. DR EnsemblBacteria; AAD35351; AAD35351; TM_0263. DR GeneID; 897174; -. DR KEGG; tma:TM0263; -. DR KEGG; tmi:THEMA_03410; -. DR PATRIC; 23935403; VBITheMar51294_0267. DR eggNOG; ENOG4105CWE; Bacteria. DR eggNOG; COG0445; LUCA. DR InParanoid; Q9WYA1; -. DR KO; K03495; -. DR OMA; FRPGYAI; -. DR OrthoDB; EOG6W9X6J; -. DR BioCyc; TMAR243274:GC6P-276-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 1. DR HAMAP; MF_00129; MnmG_GidA; 1. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR026904; GidA-assoc_3. DR InterPro; IPR004416; MnmG. DR InterPro; IPR002218; MnmG-rel. DR InterPro; IPR020595; MnmG-rel_CS. DR Pfam; PF01134; GIDA; 1. DR Pfam; PF13932; GIDA_assoc; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR TIGRFAMs; TIGR00136; gidA; 1. DR PROSITE; PS01280; GIDA_1; 1. DR PROSITE; PS01281; GIDA_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; KW Reference proteome; tRNA processing. FT CHAIN 1 629 tRNA uridine 5-carboxymethylaminomethyl FT modification enzyme MnmG. FT /FTId=PRO_0000117202. FT NP_BIND 18 23 FAD. {ECO:0000255|HAMAP-Rule:MF_00129}. FT NP_BIND 280 294 NAD. {ECO:0000255|HAMAP-Rule:MF_00129}. SQ SEQUENCE 629 AA; 71040 MW; 0D8052BB809C2999 CRC64; MIGLRPEDDR VYDVIVVGAG HAGIEAALAA ARMGFRVLVL TVNPDTVGWA PCNPAIGGPA KGVVVREIDA LGGEMAKTTD ETMINVRMLN VSKGPAVRAL RAQIDKISYS RTMKRKLETN PNIVLRHGIV ERILTEKGRV KGVVDNYGID YLGKAVIVTT GTFLRGKIFI GRSTFPAGRM GEFPATKLTE SLIELGFEVG RFKTGTPARV LKRSINFSVM ERQDTSDEPL AFSFFDEPRV LPKDYPCWLT RTNPETHSII KQYLEFSPLY GTVKLIEGIG PRYCPSIEDK VVKFKDKESH QVFVEPEGRD TEEYYLNGLS TSLPYEAQIK MIRSVKGLEN AIVTRPAYAI EYDYIDPRQL YPTLESKLVE NLYFAGQVNG TSGYEEAAGQ GIIAGINAAL KLRGEPPLIL KRSEAYIGVL IDDLVTKGVD EPYRLLTSRA EYRLLLRHDN AHLRLAKYGY RVGLIPKWFY EKVLSLERRI NEEIERLKKV IVKPSDRVND LLTSLRTSPL KEPVSFYQLL KRPQLSYSAL KFLDPNPIDD PEVVEQVEIN VKYEGYIQKM FEEVAVFEKY ENYEIPHDLD YDAVPNLSTE ARDKLKKIRP RSIGQAMRIP GINPSDISNL IIYLDRKKQ // ID MURB_THEMA Reviewed; 284 AA. AC Q9X239; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase; DE EC=1.3.1.98; DE AltName: Full=UDP-N-acetylmuramate dehydrogenase; GN Name=murB; OrderedLocusNames=TM_1714; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Cell wall formation. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP- CC N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36780.1; -; Genomic_DNA. DR PIR; C72222; C72222. DR RefSeq; NP_229513.1; NC_000853.1. DR RefSeq; WP_010865388.1; NC_000853.1. DR ProteinModelPortal; Q9X239; -. DR STRING; 243274.TM1714; -. DR EnsemblBacteria; AAD36780; AAD36780; TM_1714. DR GeneID; 897266; -. DR KEGG; tma:TM1714; -. DR KEGG; tmi:THEMA_05670; -. DR PATRIC; 23938404; VBITheMar51294_1732. DR eggNOG; ENOG4105D4A; Bacteria. DR eggNOG; COG0812; LUCA. DR InParanoid; Q9X239; -. DR KO; K00075; -. DR OMA; LAPLTWF; -. DR OrthoDB; EOG60CWQ3; -. DR BioCyc; TMAR243274:GC6P-1762-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.78.10; -; 1. DR HAMAP; MF_00037; MurB; 1. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR003170; MurB. DR InterPro; IPR011601; MurB_C. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR PANTHER; PTHR21071; PTHR21071; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR Pfam; PF02873; MurB_C; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR SUPFAM; SSF56194; SSF56194; 1. DR TIGRFAMs; TIGR00179; murB; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; FAD; KW Flavoprotein; NADP; Oxidoreductase; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 284 UDP-N-acetylenolpyruvoylglucosamine FT reductase. FT /FTId=PRO_0000179280. FT DOMAIN 12 174 FAD-binding PCMH-type. FT ACT_SITE 153 153 {ECO:0000250}. FT ACT_SITE 203 203 Proton donor. {ECO:0000250}. FT ACT_SITE 274 274 {ECO:0000250}. SQ SEQUENCE 284 AA; 32253 MW; 689D0DA9475A30DA CRC64; MFEKLSCHTS IKIGGRVKYL VLPNDVFSLE RAITVLKDLP FQIMGLGTNL LVQDEDLDIA VLKTERLNQI EIKGEKVLVE SGTPLKRLCL FLMEAELGGL EFAYGIPGSV GGAIYMNAGA YGGEIGEFVE AVEVLRDGEK TWLSRNEIFF GYRDSTFKRE KLIITRVMMS FKKEKKETIK AKMDDYMRRR LEKQPLDLPS AGSVFKRPRE DFYVGKAIES LGLKGYRIGG AQISEKHAGF IVNAGSATFD DVMKLIDFVR KKVKEKYGVE LETEVEIWWN GRRW // ID MRAY_THEMA Reviewed; 302 AA. AC Q9WY77; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 117. DE RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000255|HAMAP-Rule:MF_00038}; DE EC=2.7.8.13 {ECO:0000255|HAMAP-Rule:MF_00038}; DE AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00038}; GN Name=mraY {ECO:0000255|HAMAP-Rule:MF_00038}; GN OrderedLocusNames=TM_0235; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: First step of the lipid cycle reactions in the CC biosynthesis of the cell wall peptidoglycan. {ECO:0000255|HAMAP- CC Rule:MF_00038}. CC -!- CATALYTIC ACTIVITY: UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala- CC D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D- CC Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. {ECO:0000255|HAMAP- CC Rule:MF_00038}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00038}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00038}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00038}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00038}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35326.1; -; Genomic_DNA. DR PIR; E72402; E72402. DR RefSeq; NP_228049.1; NC_000853.1. DR RefSeq; WP_004082932.1; NZ_CP011107.1. DR STRING; 243274.TM0235; -. DR PRIDE; Q9WY77; -. DR DNASU; 897134; -. DR EnsemblBacteria; AAD35326; AAD35326; TM_0235. DR GeneID; 897134; -. DR KEGG; tma:TM0235; -. DR PATRIC; 23935345; VBITheMar51294_0238. DR eggNOG; ENOG4105CPY; Bacteria. DR eggNOG; COG0472; LUCA. DR InParanoid; Q9WY77; -. DR KO; K01000; -. DR OMA; RIGQYIR; -. DR OrthoDB; EOG69GZPZ; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051992; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00038; MraY; 1. DR InterPro; IPR000715; Glycosyl_transferase_4. DR InterPro; IPR003524; PNAcMuramoyl-5peptid_Trfase. DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS. DR PANTHER; PTHR22926; PTHR22926; 1. DR Pfam; PF00953; Glycos_transf_4; 1. DR Pfam; PF10555; MraY_sig1; 1. DR TIGRFAMs; TIGR00445; mraY; 1. DR PROSITE; PS01347; MRAY_1; 1. DR PROSITE; PS01348; MRAY_2; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Membrane; Peptidoglycan synthesis; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 302 Phospho-N-acetylmuramoyl-pentapeptide- FT transferase. FT /FTId=PRO_0000108917. FT TRANSMEM 1 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 42 62 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 67 87 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 95 115 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 123 143 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 154 174 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 178 198 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 204 224 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 229 249 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 279 299 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. SQ SEQUENCE 302 AA; 33814 MW; BB8FF74FEA9205CB CRC64; MIAANFLLNL FLYPILIKLF RRRRIGQYIR KEGPDLHGYK EGTPTMGGIL FVLTGFLFGM ISKTNTMVLL GMFLFFLIGF LDDFLSVARK DSTGLKTYQK ALLQTLAAFI MLLLIRPDTN VDFFGSTIEM GKWYYLFALL VIVGSSNAMN LTDGLDGLAG WIYVSGSIPY WFFLKERGVS EDILLILGVG VLAFLVFNSK PAKIFMGDTG SITLGGVLGT VSVLTKTEFY LVLFFMIPVI ETLSVILQVG SFKIFKRRIF KMSPLHHHFE LIGWSEEKIV AVFTVFNLIS SLVALEIFGV IG // ID MTAD_THEMA Reviewed; 406 AA. AC Q9X034; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=5-methylthioadenosine/S-adenosylhomocysteine deaminase; DE Short=MTA/SAH deaminase; DE EC=3.5.4.28; DE EC=3.5.4.31; GN Name=mtaD; OrderedLocusNames=TM_0936; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF 1-5, X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN RP COMPLEX WITH ZINC ION AND PRODUCT, FUNCTION, CATALYTIC ACTIVITY, RP SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND RP REACTION MECHANISM. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=17603473; DOI=10.1038/nature05981; RA Hermann J.C., Marti-Arbona R., Fedorov A.A., Fedorov E., Almo S.C., RA Shoichet B.K., Raushel F.M.; RT "Structure-based activity prediction for an enzyme of unknown RT function."; RL Nature 448:775-779(2007). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH NICKEL ION AND RP METHIONINE. RG New York structural genomics research consortium (NYSGRC); RT "Structure of the hypothetical protein TM0936 from Thermotoga maritima RT at 1.5 A bound to Ni and methionine."; RL Submitted (JAN-2005) to the PDB data bank. RN [4] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NICKEL ION. RG Joint center for structural genomics (JCSG); RT "Crystal structure of metal-dependent hydrolase of RT cytosinedemaniase/chlorohydrolase family (TM0936) from Thermotoga RT maritima at 1.9 A resolution."; RL Submitted (MAR-2006) to the PDB data bank. CC -!- FUNCTION: Catalyzes the deamination of 5-methylthioadenosine and CC S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L- CC homocysteine, respectively. Is also able to deaminate adenosine. CC Adenosine-5-monophosphate (AMP) and S-adenosyl-L-methionine (SAM) CC are not enzyme substrates. {ECO:0000269|PubMed:17603473}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = S-inosyl- CC L-homocysteine + NH(3). {ECO:0000269|PubMed:17603473}. CC -!- CATALYTIC ACTIVITY: S-methyl-5'-thioadenosine + H(2)O = S-methyl- CC 5'-thioinosine + NH(3). {ECO:0000269|PubMed:17603473}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:17603473}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17603473}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=210 uM for S-adenosyl-L-homocysteine CC {ECO:0000269|PubMed:17603473}; CC KM=44 uM for 5-methyl-thioadenosine CC {ECO:0000269|PubMed:17603473}; CC KM=250 uM for adenosine {ECO:0000269|PubMed:17603473}; CC -!- SIMILARITY: Belongs to the MTA/SAH deaminase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36017.1; -; Genomic_DNA. DR PIR; H72315; H72315. DR RefSeq; NP_228744.1; NC_000853.1. DR RefSeq; WP_004080626.1; NZ_CP011107.1. DR PDB; 1J6P; X-ray; 1.90 A; A=1-406. DR PDB; 1P1M; X-ray; 1.50 A; A=1-406. DR PDB; 2PLM; X-ray; 2.10 A; A=1-406. DR PDBsum; 1J6P; -. DR PDBsum; 1P1M; -. DR PDBsum; 2PLM; -. DR ProteinModelPortal; Q9X034; -. DR SMR; Q9X034; 1-405. DR STRING; 243274.TM0936; -. DR ChEMBL; CHEMBL1075031; -. DR EnsemblBacteria; AAD36017; AAD36017; TM_0936. DR GeneID; 898610; -. DR KEGG; tma:TM0936; -. DR PATRIC; 23936803; VBITheMar51294_0950. DR eggNOG; ENOG4105D6T; Bacteria. DR eggNOG; COG0402; LUCA. DR InParanoid; Q9X034; -. DR KO; K12960; -. DR OMA; CSEETYQ; -. DR OrthoDB; EOG65QWFB; -. DR BioCyc; MetaCyc:MONOMER-16147; -. DR BRENDA; 3.5.4.31; 6331. DR EvolutionaryTrace; Q9X034; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0090614; F:5'-methylthioadenosine deaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004000; F:adenosine deaminase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050270; F:S-adenosylhomocysteine deaminase activity; IDA:CACAO. DR GO; GO:0019700; P:organic phosphonate catabolic process; IBA:GO_Central. DR Gene3D; 2.30.40.10; -; 2. DR HAMAP; MF_01281; MTA_SAH_deamin; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR023512; Deaminase_MtaD/DadD. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51338; SSF51338; 2. DR SUPFAM; SSF51556; SSF51556; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; Hydrolase; KW Metal-binding; Reference proteome; Zinc. FT CHAIN 1 406 5-methylthioadenosine/S- FT adenosylhomocysteine deaminase. FT /FTId=PRO_0000312465. FT METAL 55 55 Zinc; via tele nitrogen. FT METAL 57 57 Zinc; via tele nitrogen. FT METAL 200 200 Zinc; via tele nitrogen. FT METAL 279 279 Zinc. FT BINDING 84 84 Substrate. FT BINDING 136 136 Substrate. FT BINDING 148 148 Substrate. FT BINDING 173 173 Substrate. FT BINDING 203 203 Substrate. FT BINDING 279 279 Substrate. FT STRAND 2 8 {ECO:0000244|PDB:1P1M}. FT STRAND 17 24 {ECO:0000244|PDB:1P1M}. FT STRAND 27 35 {ECO:0000244|PDB:1P1M}. FT STRAND 39 41 {ECO:0000244|PDB:1P1M}. FT STRAND 45 49 {ECO:0000244|PDB:1P1M}. FT STRAND 51 56 {ECO:0000244|PDB:1P1M}. FT HELIX 58 63 {ECO:0000244|PDB:1P1M}. FT HELIX 72 77 {ECO:0000244|PDB:1P1M}. FT HELIX 80 84 {ECO:0000244|PDB:1P1M}. FT HELIX 89 104 {ECO:0000244|PDB:1P1M}. FT TURN 105 107 {ECO:0000244|PDB:1P1M}. FT STRAND 108 117 {ECO:0000244|PDB:1P1M}. FT HELIX 118 128 {ECO:0000244|PDB:1P1M}. FT STRAND 131 138 {ECO:0000244|PDB:1P1M}. FT HELIX 148 159 {ECO:0000244|PDB:1P1M}. FT HELIX 162 164 {ECO:0000244|PDB:1P1M}. FT STRAND 166 172 {ECO:0000244|PDB:1P1M}. FT TURN 175 177 {ECO:0000244|PDB:1P1M}. FT HELIX 180 192 {ECO:0000244|PDB:1P1M}. FT STRAND 197 202 {ECO:0000244|PDB:1P1M}. FT HELIX 212 215 {ECO:0000244|PDB:1P1M}. FT TURN 216 221 {ECO:0000244|PDB:1P1M}. FT STRAND 224 228 {ECO:0000244|PDB:1P1M}. FT HELIX 234 236 {ECO:0000244|PDB:1P1M}. FT TURN 237 242 {ECO:0000244|PDB:1P1M}. FT STRAND 243 249 {ECO:0000244|PDB:1P1M}. FT HELIX 251 256 {ECO:0000244|PDB:1P1M}. FT HELIX 264 269 {ECO:0000244|PDB:1P1M}. FT STRAND 273 276 {ECO:0000244|PDB:1P1M}. FT TURN 281 284 {ECO:0000244|PDB:1P1M}. FT HELIX 289 301 {ECO:0000244|PDB:1P1M}. FT HELIX 310 317 {ECO:0000244|PDB:1P1M}. FT HELIX 319 325 {ECO:0000244|PDB:1P1M}. FT STRAND 340 344 {ECO:0000244|PDB:1P1M}. FT HELIX 348 350 {ECO:0000244|PDB:1P1M}. FT HELIX 353 355 {ECO:0000244|PDB:1P1M}. FT HELIX 356 362 {ECO:0000244|PDB:1P1M}. FT STRAND 369 373 {ECO:0000244|PDB:1P1M}. FT STRAND 376 380 {ECO:0000244|PDB:1P1M}. FT HELIX 389 403 {ECO:0000244|PDB:1P1M}. SQ SEQUENCE 406 AA; 45773 MW; 3437565703ECC544 CRC64; MIIGNCLILK DFSSEPFWGA VEIENGTIKR VLQGEVKVDL DLSGKLVMPA LFNTHTHAPM TLLRGVAEDL SFEEWLFSKV LPIEDRLTEK MAYYGTILAQ MEMARHGIAG FVDMYFHEEW IAKAVRDFGM RALLTRGLVD SNGDDGGRLE ENLKLYNEWN GFEGRIFVGF GPHSPYLCSE EYLKRVFDTA KSLNAPVTIH LYETSKEEYD LEDILNIGLK EVKTIAAHCV HLPERYFGVL KDIPFFVSHN PASNLKLGNG IAPVQRMIEH GMKVTLGTDG AASNNSLNLF FEMRLASLLQ KAQNPRNLDV NTCLKMVTYD GAQAMGFKSG KIEEGWNADL VVIDLDLPEM FPVQNIKNHL VHAFSGEVFA TMVAGKWIYF DGEYPTIDSE EVKRELARIE KELYSS // ID MURA_THEMA Reviewed; 421 AA. AC Q9WXW3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 119. DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00111}; DE EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111}; DE AltName: Full=Enoylpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_00111}; DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111}; DE Short=EPT {ECO:0000255|HAMAP-Rule:MF_00111}; GN Name=murA {ECO:0000255|HAMAP-Rule:MF_00111}; GN OrderedLocusNames=TM_0108; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- CC acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + UDP-N-acetyl-alpha-D- CC glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha- CC D-glucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00111}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35202.1; -; Genomic_DNA. DR PIR; C72416; C72416. DR RefSeq; NP_227924.1; NC_000853.1. DR RefSeq; WP_004082675.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXW3; -. DR STRING; 243274.TM0108; -. DR EnsemblBacteria; AAD35202; AAD35202; TM_0108. DR GeneID; 896935; -. DR KEGG; tma:TM0108; -. DR PATRIC; 23935056; VBITheMar51294_0106. DR eggNOG; ENOG4105CDF; Bacteria. DR eggNOG; COG0766; LUCA. DR InParanoid; Q9WXW3; -. DR KO; K00790; -. DR OMA; IRTAPHP; -. DR OrthoDB; EOG68M4GK; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.65.10.10; -; 2. DR HAMAP; MF_00111; MurA; 1. DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA. DR Pfam; PF00275; EPSP_synthase; 1. DR SUPFAM; SSF55205; SSF55205; 1. DR TIGRFAMs; TIGR01072; murA; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Peptidoglycan synthesis; Pyruvate; Reference proteome; Transferase. FT CHAIN 1 421 UDP-N-acetylglucosamine 1- FT carboxyvinyltransferase. FT /FTId=PRO_0000178943. FT ACT_SITE 116 116 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00111}. FT MOD_RES 116 116 2-(S-cysteinyl)pyruvic acid O- FT phosphothioketal. {ECO:0000255|HAMAP- FT Rule:MF_00111}. SQ SEQUENCE 421 AA; 45965 MW; 79CE853FA7116B18 CRC64; MGKLVVQGGA VLEGEVEISG SKNAALPIMA AAILCDEEVI LKNVPRLQDV FVMIDILRSI GFRVEFEENE LKIKRENDIS QEVPYELVRK MRASFNVLGP IAVRTGRAKV ALPGGCSIGV RPVDFHLEGL KKMGFSIKVE HGFVEACFER RIDYVTITLP FPSVGATEHL MTTAALLKGA RVVIENAAME PEIVDLQNFI NRMGGHIEGA GTSRIVIEGV EKMQGVEYSI IPDRIEAGTY LVAIAASRGK GLVKNVNPDH LTNFFEKLEE TGAKLKVLGN EVEIEMRERP KAVDVTTNPY PGFPTDLQPQ MMAYLSTASG VSVITENVFK TRFLHVDELK RMGADIEVSG NVAIVKGVEK LSGAPVEGTD LRATAALLIA GIIADGVTEI SNVEHIFRGY EDVIDKFSEL GAKIEYVEKE N // ID MUTL_THEMA Reviewed; 510 AA. AC P74925; Q9S5W9; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 110. DE RecName: Full=DNA mismatch repair protein MutL; GN Name=mutL; OrderedLocusNames=TM_0022; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Wetmur J.G., Rosenfeld A., Wong D.M.; RT "Expression and characterization of MutL proteins from thermophilic RT eubacteria."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: This protein is involved in the repair of mismatches in CC DNA. It is required for dam-dependent methyl-directed DNA mismatch CC repair. May act as a "molecular matchmaker", a protein that CC promotes the formation of a stable complex between two or more CC DNA-binding proteins in an ATP-dependent manner without itself CC being part of a final effector complex (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35116.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U71053; AAB09596.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35116.1; ALT_INIT; Genomic_DNA. DR PIR; H72427; H72427. DR RefSeq; NP_227838.1; NC_000853.1. DR RefSeq; WP_010865029.1; NZ_CP011107.1. DR ProteinModelPortal; P74925; -. DR STRING; 243274.TM0022; -. DR EnsemblBacteria; AAD35116; AAD35116; TM_0022. DR GeneID; 896837; -. DR KEGG; tma:TM0022; -. DR PATRIC; 23934884; VBITheMar51294_0020. DR eggNOG; ENOG4105DC6; Bacteria. DR eggNOG; COG0323; LUCA. DR InParanoid; P74925; -. DR KO; K03572; -. DR OMA; LCHPQVT; -. DR OrthoDB; EOG6P8TMH; -. DR BioCyc; TMAR243274:GC6P-22-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0032300; C:mismatch repair complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATPase activity; IBA:GO_Central. DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR HAMAP; MF_00149; DNA_mis_repair; 1. DR InterPro; IPR013507; DNA_mismatch_repair_C. DR InterPro; IPR014762; DNA_mismatch_repair_CS. DR InterPro; IPR002099; DNA_mismatch_repair_fam. DR InterPro; IPR020667; DNA_mismatch_repair_MutL. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR014790; MutL_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR Pfam; PF01119; DNA_mis_repair; 1. DR Pfam; PF08676; MutL_C; 1. DR SMART; SM01340; DNA_mis_repair; 1. DR SMART; SM00853; MutL_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR TIGRFAMs; TIGR00585; mutl; 1. DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; Reference proteome. FT CHAIN 1 510 DNA mismatch repair protein MutL. FT /FTId=PRO_0000177985. SQ SEQUENCE 510 AA; 59021 MW; 19FAE9EDE8986F47 CRC64; MRIKRLPESL VRKIAAGEVI HNPSFVLKEL VENSLDAQAD RIVVEIENGG KNMVRVSDNG IGMTREEALL AIEPYTTSKI ESEEDLHRIR TYGFRGEALA SIVQVSRAKI VTKTEKDALA TQLMIAGGKV EEISETHRDT GTTVEVRDLF FNLPVRRKSL KSSAIELRMC REMFERFVLV RNDVDFVFTS DGKIVHSFPR TQNIFERALL ILEDLRKGYI TFEEELSGLR IKGIVSSREV TRSSRTGEYF YVNGRFVVSE ELHEVLMKVY DLPKRSYPVA VLFIEVNPEE LDVNIHPSKI VVKFLNEEKV KKSLEETLKR NLARKWYRSV AYEEISSRAL SVAEAPSHRW FLVKGKYAVV EVEDGLLFVD LHALHERTIY EEILSKKSWG KRRVKRNITV VLSREEKQKL EEYGFSFQGE EGALKVIEIP EFLTEDVVEE FFRDFPVDEK LKERIALAAC KLATKSGEFD EEIASKLLDV FFKKRFERCP HGRPISFKIS YEDMDRFFER // ID MUTS2_THEMA Reviewed; 757 AA. AC Q9X105; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=Endonuclease MutS2 {ECO:0000255|HAMAP-Rule:MF_00092}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00092}; GN Name=mutS2 {ECO:0000255|HAMAP-Rule:MF_00092}; Synonyms=mutSB; GN OrderedLocusNames=TM_1278; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION, ATPASE ACTIVITY, NUCLEASE ACTIVITY, DNA-BINDING, ENZYME RP REGULATION, SUBUNIT, AND INTERACTION WITH MUTL. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=22545085; DOI=10.1371/journal.pone.0034529; RA Jeong E., Jo H., Kim T.G., Ban C.; RT "Characterization of multi-functional properties and conformational RT analysis of MutS2 from Thermotoga maritima MSB8."; RL PLoS ONE 7:E34529-E34529(2012). CC -!- FUNCTION: Endonuclease that is involved in the suppression of CC homologous recombination and may therefore have a key role in the CC control of bacterial genetic diversity (Probable). Has ATPase CC activity. Binds to DNA. {ECO:0000255|HAMAP-Rule:MF_00092, CC ECO:0000269|PubMed:22545085, ECO:0000305}. CC -!- ENZYME REGULATION: Nuclease activity is stimulated by interaction CC with MutL and inhibited in the presence of non-hydrolytic ATP CC (ADPnP). ATPase activity is stimulated by DNA. CC {ECO:0000269|PubMed:22545085}. CC -!- SUBUNIT: Homodimer. Interacts with MutL. {ECO:0000255|HAMAP- CC Rule:MF_00092, ECO:0000269|PubMed:22545085}. CC -!- DOMAIN: Contains an N-terminal DNA-binding domain, followed by a CC dimerization domain and a C-terminal domain, called the small CC MutS-related (Smr) domain, which is absent from MutS and contains CC the endonuclease activity. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00092}. CC -!- SIMILARITY: Contains 1 Smr domain. {ECO:0000255|HAMAP- CC Rule:MF_00092}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36353.1; -; Genomic_DNA. DR PIR; B72273; B72273. DR RefSeq; NP_229083.1; NC_000853.1. DR RefSeq; WP_004079958.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X105; -. DR STRING; 243274.TM1278; -. DR PRIDE; Q9X105; -. DR DNASU; 898205; -. DR EnsemblBacteria; AAD36353; AAD36353; TM_1278. DR GeneID; 898205; -. DR KEGG; tma:TM1278; -. DR PATRIC; 23937494; VBITheMar51294_1293. DR eggNOG; ENOG4105C98; Bacteria. DR eggNOG; COG1193; LUCA. DR InParanoid; Q9X105; -. DR KO; K07456; -. DR OMA; KLYGYNR; -. DR OrthoDB; EOG6P5ZC4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro. DR GO; GO:0006298; P:mismatch repair; IEA:InterPro. DR GO; GO:0045910; P:negative regulation of DNA recombination; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00092; MutS2; 1. DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C. DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core. DR InterPro; IPR005747; MutS2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR002625; Smr_dom. DR PANTHER; PTHR11361:SF14; PTHR11361:SF14; 1. DR Pfam; PF00488; MutS_V; 1. DR Pfam; PF01713; Smr; 1. DR PIRSF; PIRSF005814; MutS_YshD; 1. DR SMART; SM00534; MUTSac; 1. DR SMART; SM00533; MUTSd; 1. DR SMART; SM00463; SMR; 1. DR SUPFAM; SSF160443; SSF160443; 1. DR SUPFAM; SSF48334; SSF48334; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01069; mutS2; 1. DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1. DR PROSITE; PS50828; SMR; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; DNA-binding; Endonuclease; Hydrolase; KW Nuclease; Nucleotide-binding; Reference proteome. FT CHAIN 1 757 Endonuclease MutS2. FT /FTId=PRO_0000115238. FT DOMAIN 681 756 Smr. {ECO:0000255|HAMAP-Rule:MF_00092}. FT NP_BIND 321 328 ATP. {ECO:0000255|HAMAP-Rule:MF_00092}. SQ SEQUENCE 757 AA; 86626 MW; 818F8C4F5C20426B CRC64; MDYLESLDFP KVVEIVKKYA LSDLGRKHLD TLKPTVNPWD ELELVEELLN YFNRWGEPPI KGLNDISQEV EKVKSGSPLE PWELLRVSVF LEGCDILKKE FEKREYSRLK ETFSRLSSFR EFVEEVNRCI EQDGEISDRA SPRLREIRTE KKRLSSEIKR KADDFVRTHS QILQEQMYVY RDGRYLFPVK ASMKNAVRGI VHHLSSSGAT VFLEPDEFVE LNNRVRLLEE EERLEISRIL RQLTNILLSR LNDLERNVEL IARFDSLYAR VKFAREFNGT VVKPSSRIRL VNARHPLIPK ERVVPINLEL PPNKRGFIIT GPNMGGKTVT VKTVGLFTAL MMSGFPLPCD EGTELKVFPK IMADIGEEQS IEQSLSTFSS HMKKIVEIVK NADSDSLVIL DELGSGTDPV EGAALAIAII EDLLEKGATI FVTTHLTPVK VFAMNHPLLL NASMEFDPET LSPTYRVLVG VPGGSHAFQI AEKLGLDKRI IENARSRLSR EEMELEGLIR SLHEKISLLE EEKRKLQKER EEYMKLREKY EEDYKKLRRM KIEEFDKELR ELNDYIRKVK KELDQAIHVA KTGSVDEMRE AVKTIEKEKK DLEQKRIEEA TEEEIKPGDH VKMEGGTSVG KVVEVKSGTA LVDFGFLRLK VPVSKLRKTK KEEKKETSTF SYKPSSFRTE IDIRGMTVEE AEPVVKKFID DLMMNGISKG YIIHGKGTGK LASGVWEILR KDKRVVSFRF GTPSEGGTGV TVVEVKV // ID MTNN_THEMA Reviewed; 217 AA. AC Q9X0L3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; DE Short=MTA/SAH nucleosidase; DE Short=MTAN; DE EC=3.2.2.9; DE AltName: Full=5'-methylthioadenosine nucleosidase; DE Short=MTA nucleosidase; DE AltName: Full=S-adenosylhomocysteine nucleosidase; DE Short=AdoHcy nucleosidase; DE Short=SAH nucleosidase; DE Short=SRH nucleosidase; GN Name=mtnN; Synonyms=mtn; OrderedLocusNames=TM_1129; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the irreversible cleavage of the glycosidic CC bond in both 5'-methylthioadenosine (MTA) and S- CC adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding CC thioribose, 5'-methylthioribose and S-ribosylhomocysteine, CC respectively. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = S-(5- CC deoxy-D-ribos-5-yl)-L-homocysteine + adenine. CC -!- CATALYTIC ACTIVITY: S-methyl-5'-thioadenosine + H(2)O = S-methyl- CC 5-thio-D-ribose + adenine. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via CC salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from CC S-methyl-5'-thioadenosine (hydrolase route): step 1/2. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36205.1; -; Genomic_DNA. DR PIR; F72293; F72293. DR RefSeq; NP_228935.1; NC_000853.1. DR RefSeq; WP_004080281.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0L3; -. DR STRING; 243274.TM1129; -. DR DNASU; 898635; -. DR EnsemblBacteria; AAD36205; AAD36205; TM_1129. DR GeneID; 898635; -. DR KEGG; tma:TM1129; -. DR PATRIC; 23937193; VBITheMar51294_1145. DR eggNOG; ENOG41083B7; Bacteria. DR eggNOG; COG0775; LUCA. DR InParanoid; Q9X0L3; -. DR KO; K01243; -. DR OMA; CGRETEE; -. DR OrthoDB; EOG64JFVR; -. DR UniPathway; UPA00904; UER00871. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IEA:UniProtKB-EC. DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IEA:InterPro. DR GO; GO:0019509; P:L-methionine biosynthetic process from methylthioadenosine; IEA:UniProtKB-UniPathway. DR GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1580; -; 1. DR InterPro; IPR010049; MTA_SAH_Nsdase. DR InterPro; IPR018017; Nucleoside_phosphorylase. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR PANTHER; PTHR21234; PTHR21234; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; SSF53167; 1. DR TIGRFAMs; TIGR01704; MTA/SAH-Nsdase; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Hydrolase; KW Methionine biosynthesis; Reference proteome. FT CHAIN 1 217 5'-methylthioadenosine/S- FT adenosylhomocysteine nucleosidase. FT /FTId=PRO_0000164450. FT REGION 159 160 Substrate binding. {ECO:0000250}. FT ACT_SITE 11 11 Proton acceptor. {ECO:0000250}. FT ACT_SITE 183 183 Proton donor. {ECO:0000250}. FT BINDING 77 77 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 139 139 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000250}. SQ SEQUENCE 217 AA; 24166 MW; CF9AE5F0F0F4AA16 CRC64; MILVLGVFKI EVEPMLKEME VLEKGRLLKR YYQRGVVGRN EVVVSYGFIG KVEAALVTQA FLDRFNIDAV FLTGNAGGLE GVEVGDVVIG DSYVEYDFET ALGDEGIIVS GSEDLEDKVI AYSNREIKTG LIASGDAFVT VKEKAEEIKR RTGALCVDMD SAAVAKVCYE NEKKFLAIKT IVDICGRETE EEFRKNYERY GFLSNLILLD VLKKCVF // ID MURJ_THEMA Reviewed; 473 AA. AC Q9WXU1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Putative lipid II flippase MurJ; GN Name=murJ; Synonyms=mviN; OrderedLocusNames=TM_0086; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in peptidoglycan biosynthesis. Transports CC lipid-linked peptidoglycan precursors from the inner to the outer CC leaflet of the cytoplasmic membrane (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35180.1; -; Genomic_DNA. DR PIR; H72419; H72419. DR RefSeq; NP_227902.1; NC_000853.1. DR RefSeq; WP_004082614.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXU1; -. DR STRING; 243274.TM0086; -. DR EnsemblBacteria; AAD35180; AAD35180; TM_0086. DR GeneID; 896913; -. DR KEGG; tma:TM0086; -. DR PATRIC; 23935012; VBITheMar51294_0084. DR eggNOG; ENOG4105CJR; Bacteria. DR eggNOG; COG0728; LUCA. DR InParanoid; Q9WXU1; -. DR KO; K03980; -. DR OMA; IFAEGSF; -. DR OrthoDB; EOG6C0131; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0034204; P:lipid translocation; IBA:GO_Central. DR GO; GO:0015836; P:lipid-linked peptidoglycan transport; IBA:GOC. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR InterPro; IPR004268; MurJ. DR Pfam; PF03023; MVIN; 1. DR PIRSF; PIRSF002869; MviN; 1. DR PRINTS; PR01806; VIRFACTRMVIN. DR TIGRFAMs; TIGR01695; murJ_mviN; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Membrane; KW Peptidoglycan synthesis; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 473 Putative lipid II flippase MurJ. FT /FTId=PRO_0000182016. FT TRANSMEM 31 51 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. FT TRANSMEM 125 145 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TRANSMEM 177 197 Helical. {ECO:0000255}. FT TRANSMEM 215 235 Helical. {ECO:0000255}. FT TRANSMEM 253 273 Helical. {ECO:0000255}. FT TRANSMEM 300 320 Helical. {ECO:0000255}. FT TRANSMEM 328 348 Helical. {ECO:0000255}. FT TRANSMEM 360 380 Helical. {ECO:0000255}. FT TRANSMEM 382 402 Helical. {ECO:0000255}. FT TRANSMEM 414 434 Helical. {ECO:0000255}. FT TRANSMEM 439 459 Helical. {ECO:0000255}. SQ SEQUENCE 473 AA; 51850 MW; 6D02DAD2D3FEBE5A CRC64; MSSIKKTLAF SLGTFFSRIT GLVRDIILAK TFGASSTLDA YYVSIVFPFF LRRTFAEGAM SSAFMAIYKK LKNKEEKAQF TSAVLTSLGL VTLLIVFLSE VFPYFMASIF ATGADEEVKS LAADLIRLTA PFITIVFVWA VFYSVHNASH RYFLPALTPM FSNVGVIVGC LFGDVRWAAA GFTIGGLAAL LVLLPFGKFR YRPTFKGLGE FYRLFFGTFM TMAVSQVTTL IDVNVASFLD PGSLSLIQLS SRLYQLPLGI FGVAVSTVAL STLSESEGDF HENLKDFISK SLFLTLPSSI GLMALSERII SLLFGYGAFT HEDVKKSAQI LFMYAIGLCF VSLFNLLSRA YHASKEVKTP FFATLLVSAV NISLDVILGF TMGASGIALA TSVSYIAGFV FLTLRMKPSF DKKIFKISLA SAVMGTVILL LRGSFKGNLG TIFLVLIGVF VYVLFSKLLK IEELEEILRR GSH // ID MTNA_THEMA Reviewed; 343 AA. AC Q9X013; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 118. DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678}; DE Short=M1Pi {ECO:0000255|HAMAP-Rule:MF_01678}; DE Short=MTR-1-P isomerase {ECO:0000255|HAMAP-Rule:MF_01678}; DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_01678}; DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678}; GN Name=mtnA {ECO:0000255|HAMAP-Rule:MF_01678}; GN OrderedLocusNames=TM_0911; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SULFATE IONS. RG Midwest center for structural genomics (MCSG); RT "X-ray crystal structure of aif-2b translation initiation factor from RT Thermotoga maritima."; RL Submitted (JAN-2005) to the PDB data bank. CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1- CC phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1- CC P). {ECO:0000255|HAMAP-Rule:MF_01678}. CC -!- CATALYTIC ACTIVITY: S-methyl-5-thio-alpha-D-ribose 1-phosphate = CC S-methyl-5-thio-D-ribulose 1-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01678}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via CC salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose CC 1-phosphate: step 1/6. {ECO:0000255|HAMAP-Rule:MF_01678}. CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits CC family. MtnA subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35992.1; -; Genomic_DNA. DR PIR; F72319; F72319. DR RefSeq; NP_228719.1; NC_000853.1. DR RefSeq; WP_004080652.1; NZ_CP011107.1. DR PDB; 1T9K; X-ray; 2.60 A; A/B/C/D=1-343. DR PDBsum; 1T9K; -. DR ProteinModelPortal; Q9X013; -. DR SMR; Q9X013; 1-342. DR STRING; 243274.TM0911; -. DR EnsemblBacteria; AAD35992; AAD35992; TM_0911. DR GeneID; 898585; -. DR KEGG; tma:TM0911; -. DR PATRIC; 23936753; VBITheMar51294_0925. DR eggNOG; ENOG4105C35; Bacteria. DR eggNOG; COG0182; LUCA. DR InParanoid; Q9X013; -. DR KO; K08963; -. DR OMA; KVFNPAF; -. DR OrthoDB; EOG6CGCFN; -. DR UniPathway; UPA00904; UER00874. DR EvolutionaryTrace; Q9X013; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IBA:GO_Central. DR GO; GO:0019509; P:L-methionine biosynthetic process from methylthioadenosine; IBA:GO_Central. DR GO; GO:0019284; P:L-methionine biosynthetic process from S-adenosylmethionine; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.120.420; -; 1. DR HAMAP; MF_01678; Salvage_MtnA; 1. DR InterPro; IPR000649; IF-2B-related. DR InterPro; IPR005251; IF-M1Pi. DR InterPro; IPR011559; Initiation_fac_2B_a/b/d. DR InterPro; IPR027363; M1Pi_N. DR Pfam; PF01008; IF-2B; 1. DR TIGRFAMs; TIGR00524; eIF-2B_rel; 1. DR TIGRFAMs; TIGR00512; salvage_mtnA; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Isomerase; KW Methionine biosynthesis; Reference proteome. FT CHAIN 1 343 Methylthioribose-1-phosphate isomerase. FT /FTId=PRO_0000156094. FT REGION 48 50 Substrate binding. FT REGION 244 245 Substrate binding. FT ACT_SITE 234 234 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01678}. FT BINDING 88 88 Substrate. FT BINDING 193 193 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01678}. FT SITE 154 154 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_01678}. FT STRAND 6 10 {ECO:0000244|PDB:1T9K}. FT STRAND 15 18 {ECO:0000244|PDB:1T9K}. FT TURN 20 25 {ECO:0000244|PDB:1T9K}. FT STRAND 29 32 {ECO:0000244|PDB:1T9K}. FT HELIX 35 43 {ECO:0000244|PDB:1T9K}. FT HELIX 50 66 {ECO:0000244|PDB:1T9K}. FT HELIX 73 85 {ECO:0000244|PDB:1T9K}. FT HELIX 93 106 {ECO:0000244|PDB:1T9K}. FT TURN 107 110 {ECO:0000244|PDB:1T9K}. FT HELIX 114 141 {ECO:0000244|PDB:1T9K}. FT STRAND 148 152 {ECO:0000244|PDB:1T9K}. FT HELIX 158 160 {ECO:0000244|PDB:1T9K}. FT STRAND 161 164 {ECO:0000244|PDB:1T9K}. FT HELIX 167 176 {ECO:0000244|PDB:1T9K}. FT STRAND 181 186 {ECO:0000244|PDB:1T9K}. FT TURN 189 192 {ECO:0000244|PDB:1T9K}. FT HELIX 193 196 {ECO:0000244|PDB:1T9K}. FT HELIX 198 203 {ECO:0000244|PDB:1T9K}. FT TURN 204 206 {ECO:0000244|PDB:1T9K}. FT STRAND 208 212 {ECO:0000244|PDB:1T9K}. FT HELIX 214 216 {ECO:0000244|PDB:1T9K}. FT HELIX 217 222 {ECO:0000244|PDB:1T9K}. FT STRAND 227 231 {ECO:0000244|PDB:1T9K}. FT STRAND 234 237 {ECO:0000244|PDB:1T9K}. FT STRAND 242 245 {ECO:0000244|PDB:1T9K}. FT HELIX 248 257 {ECO:0000244|PDB:1T9K}. FT STRAND 262 265 {ECO:0000244|PDB:1T9K}. FT HELIX 268 270 {ECO:0000244|PDB:1T9K}. FT HELIX 278 280 {ECO:0000244|PDB:1T9K}. FT HELIX 289 292 {ECO:0000244|PDB:1T9K}. FT STRAND 309 314 {ECO:0000244|PDB:1T9K}. FT HELIX 316 318 {ECO:0000244|PDB:1T9K}. FT STRAND 320 324 {ECO:0000244|PDB:1T9K}. FT STRAND 327 329 {ECO:0000244|PDB:1T9K}. FT HELIX 333 341 {ECO:0000244|PDB:1T9K}. SQ SEQUENCE 343 AA; 38050 MW; 462EB159438C5BEF CRC64; MKLKTKTMEW SGNSLKLLDQ RKLPFIEEYV ECKTHEEVAH AIKEMIVRGA PAIGVAAAFG YVLGLRDYKT GSLTDWMKQV KETLARTRPT AVNLFWALNR MEKVFFENAD RENLFEILEN EALKMAYEDI EVNKAIGKNG AQLIKDGSTI LTHCNAGALA TVDYGTALGV IRAAVESGKR IRVFADETRP YLQGARLTAW ELMKDGIEVY VITDNMAGWL MKRGLIDAVV VGADRIALNG DTANKIGTYS LAVLAKRNNI PFYVAAPVST IDPTIRSGEE IPIEERRPEE VTHCGGNRIA PEGVKVLNPA FDVTENTLIT AIITEKGVIR PPFEENIKKI LEV // ID MURD_THEMA Reviewed; 430 AA. AC Q9WY76; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 113. DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_00639}; DE EC=6.3.2.9 {ECO:0000255|HAMAP-Rule:MF_00639}; DE AltName: Full=D-glutamic acid-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00639}; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_00639}; GN Name=murD {ECO:0000255|HAMAP-Rule:MF_00639}; GN OrderedLocusNames=TM_0234; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate CC to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). CC {ECO:0000255|HAMAP-Rule:MF_00639}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine CC + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- CC alanyl-D-glutamate. {ECO:0000255|HAMAP-Rule:MF_00639}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00639}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00639}. CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP- CC Rule:MF_00639}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35325.1; -; Genomic_DNA. DR PIR; D72402; D72402. DR RefSeq; NP_228048.1; NC_000853.1. DR RefSeq; WP_004082930.1; NZ_CP011107.1. DR PDB; 4BUC; X-ray; 2.17 A; A/B=1-430. DR PDBsum; 4BUC; -. DR ProteinModelPortal; Q9WY76; -. DR STRING; 243274.TM0234; -. DR EnsemblBacteria; AAD35325; AAD35325; TM_0234. DR GeneID; 897133; -. DR KEGG; tma:TM0234; -. DR PATRIC; 23935343; VBITheMar51294_0237. DR eggNOG; ENOG4105DMZ; Bacteria. DR eggNOG; COG0771; LUCA. DR InParanoid; Q9WY76; -. DR KO; K01925; -. DR OMA; SHKMEEF; -. DR OrthoDB; EOG6PKFCR; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00639; MurD; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR005762; UDP-N-AcMur-Glu_ligase. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01087; murD; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 430 UDP-N-acetylmuramoylalanine--D-glutamate FT ligase. FT /FTId=PRO_0000109113. FT NP_BIND 109 115 ATP. {ECO:0000255|HAMAP-Rule:MF_00639}. FT STRAND 2 7 {ECO:0000244|PDB:4BUC}. FT HELIX 10 20 {ECO:0000244|PDB:4BUC}. FT STRAND 25 30 {ECO:0000244|PDB:4BUC}. FT HELIX 37 45 {ECO:0000244|PDB:4BUC}. FT STRAND 49 51 {ECO:0000244|PDB:4BUC}. FT HELIX 57 61 {ECO:0000244|PDB:4BUC}. FT STRAND 63 67 {ECO:0000244|PDB:4BUC}. FT HELIX 76 83 {ECO:0000244|PDB:4BUC}. FT STRAND 87 89 {ECO:0000244|PDB:4BUC}. FT HELIX 91 98 {ECO:0000244|PDB:4BUC}. FT HELIX 101 103 {ECO:0000244|PDB:4BUC}. FT STRAND 104 108 {ECO:0000244|PDB:4BUC}. FT STRAND 110 112 {ECO:0000244|PDB:4BUC}. FT HELIX 113 126 {ECO:0000244|PDB:4BUC}. FT STRAND 131 135 {ECO:0000244|PDB:4BUC}. FT HELIX 141 145 {ECO:0000244|PDB:4BUC}. FT STRAND 150 155 {ECO:0000244|PDB:4BUC}. FT HELIX 158 162 {ECO:0000244|PDB:4BUC}. FT STRAND 170 174 {ECO:0000244|PDB:4BUC}. FT STRAND 179 181 {ECO:0000244|PDB:4BUC}. FT HELIX 188 201 {ECO:0000244|PDB:4BUC}. FT STRAND 206 211 {ECO:0000244|PDB:4BUC}. FT HELIX 212 216 {ECO:0000244|PDB:4BUC}. FT STRAND 225 237 {ECO:0000244|PDB:4BUC}. FT STRAND 239 244 {ECO:0000244|PDB:4BUC}. FT STRAND 247 250 {ECO:0000244|PDB:4BUC}. FT HELIX 257 274 {ECO:0000244|PDB:4BUC}. FT HELIX 278 284 {ECO:0000244|PDB:4BUC}. FT STRAND 295 300 {ECO:0000244|PDB:4BUC}. FT STRAND 303 307 {ECO:0000244|PDB:4BUC}. FT HELIX 314 321 {ECO:0000244|PDB:4BUC}. FT STRAND 325 334 {ECO:0000244|PDB:4BUC}. FT HELIX 340 347 {ECO:0000244|PDB:4BUC}. FT HELIX 348 350 {ECO:0000244|PDB:4BUC}. FT STRAND 351 358 {ECO:0000244|PDB:4BUC}. FT HELIX 360 364 {ECO:0000244|PDB:4BUC}. FT HELIX 365 367 {ECO:0000244|PDB:4BUC}. FT STRAND 373 375 {ECO:0000244|PDB:4BUC}. FT HELIX 379 389 {ECO:0000244|PDB:4BUC}. FT STRAND 395 403 {ECO:0000244|PDB:4BUC}. FT HELIX 414 424 {ECO:0000244|PDB:4BUC}. SQ SEQUENCE 430 AA; 49154 MW; 491D71CE4201B2C8 CRC64; MKIGFLGFGK SNRSLLKYLL NHQEAKFFVS EAKTLDGETK KFLEEHSVEY EEGGHTEKLL DCDVVYVSPG IKPDTSMIEL LSSRGVKLST ELQFFLDNVD PKKVVGITGT DGKSTATALM YHVLSGRGFK TFLGGNFGTP AVEALEGEYD YYVLEMSSFQ LFWSERPYLS NFLVLNISED HLDWHSSFKE YVDSKLKPAF LQTEGDLFVY NKHIERLRNL EGVRSRKIPF WTDENFATEK ELIVRGKKYT LPGNYPYQMR ENILAVSVLY MEMFNELESF LELLRDFKPL PHRMEYLGQI DGRHFYNDSK ATSTHAVLGA LSNFDKVVLI MCGIGKKENY SLFVEKASPK LKHLIMFGEI SKELAPFVGK IPHSIVENME EAFEKAMEVS EKGDVILLSP GGASFDMYEN YAKRGEHFRE IFKRHGGDEV // ID MURE_THEMA Reviewed; 490 AA. AC Q9WY79; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 124. DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligase; DE EC=6.3.2.37 {ECO:0000269|PubMed:16595662}; DE EC=6.3.2.7 {ECO:0000269|PubMed:16595662}; DE AltName: Full=D-lysine-adding enzyme; DE AltName: Full=L-lysine-adding enzyme; DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:LD-Lys ligase; DE AltName: Full=UDP-MurNAc-tripeptide synthetase; DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase; GN Name=murE; OrderedLocusNames=TM_0237; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16595662; DOI=10.1074/jbc.M506311200; RA Boniface A., Bouhss A., Mengin-Lecreulx D., Blanot D.; RT "The MurE synthetase from Thermotoga maritima is endowed with an RT unusual D-lysine adding activity."; RL J. Biol. Chem. 281:15680-15686(2006). CC -!- FUNCTION: Catalyzes the addition of both L- and D-lysine to the CC nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate CC (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. CC Is also able to use meso-diaminopimelate as the amino acid CC substrate in vitro, although much less efficiently. CC {ECO:0000269|PubMed:16595662}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl- CC D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetyl-alpha-D- CC muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine. CC {ECO:0000269|PubMed:16595662}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl- CC D-glutamate + D-lysine = ADP + phosphate + UDP-N-acetyl-alpha-D- CC muramoyl-L-alanyl-gamma-D-glutamyl-N(epsilon)-D-lysine. CC {ECO:0000269|PubMed:16595662}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.45 mM for UDP-N-acetylmuramoyl-L-Ala-D-Glu CC {ECO:0000269|PubMed:16595662}; CC KM=2.8 mM for L-lysine (at pH 9.4) CC {ECO:0000269|PubMed:16595662}; CC KM=0.65 mM for L-lysine (at pH 8) {ECO:0000269|PubMed:16595662}; CC KM=1.7 mM for D-lysine (at pH 9.4) CC {ECO:0000269|PubMed:16595662}; CC KM=1.0 mM for D-lysine (at pH 8) {ECO:0000269|PubMed:16595662}; CC KM=4.8 mM for meso-diaminopimelate (at pH 9.4) CC {ECO:0000269|PubMed:16595662}; CC KM=27 mM for L-ornithine (at pH 9.4) CC {ECO:0000269|PubMed:16595662}; CC KM=3.6 mM for ATP {ECO:0000269|PubMed:16595662}; CC Note=The catalytic efficiency for the L-lysine adding activity CC is 4-fold and 10-fold higher than that for the D-lysine and CC meso-diaminopimelate adding activity, respectively.; CC pH dependence: CC Optimum pH is 9.4 for the L-lysine adding activity. CC {ECO:0000269|PubMed:16595662}; CC Temperature dependence: CC Optimum temperature is 68 degrees Celsius for the L-lysine CC adding activity. {ECO:0000269|PubMed:16595662}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and, CC consequently, for the gamma-phosphate positioning of ATP. CC {ECO:0000250}. CC -!- MISCELLANEOUS: The peptidoglycan of T.maritima was shown to CC contain approximate amounts of both enantiomers of lysine and no CC diaminopimelate. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35328.1; -; Genomic_DNA. DR PIR; G72402; G72402. DR RefSeq; NP_228051.1; NC_000853.1. DR RefSeq; WP_004082936.1; NZ_CP011107.1. DR PDB; 4BUB; X-ray; 2.90 A; A/B=1-490. DR PDBsum; 4BUB; -. DR ProteinModelPortal; Q9WY79; -. DR STRING; 243274.TM0237; -. DR PRIDE; Q9WY79; -. DR EnsemblBacteria; AAD35328; AAD35328; TM_0237. DR GeneID; 897137; -. DR KEGG; tma:TM0237; -. DR PATRIC; 23935349; VBITheMar51294_0240. DR eggNOG; ENOG4107EEN; Bacteria. DR eggNOG; COG0769; LUCA. DR InParanoid; Q9WY79; -. DR KO; K01928; -. DR OMA; VIGCEGE; -. DR OrthoDB; EOG6PKFCR; -. DR BioCyc; MetaCyc:MONOMER-16146; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro. DR GO; GO:0047482; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.1390.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00208; MurE; 1. DR InterPro; IPR018109; Folylpolyglutamate_synth_CS. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR SUPFAM; SSF63418; SSF63418; 1. DR TIGRFAMs; TIGR01085; murE; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 490 UDP-N-acetylmuramoyl-L-alanyl-D- FT glutamate--LD-lysine ligase. FT /FTId=PRO_0000101962. FT NP_BIND 110 116 ATP. {ECO:0000255}. FT REGION 152 153 UDP-MurNAc-L-Ala-D-Glu binding. FT {ECO:0000250}. FT BINDING 32 32 UDP-MurNAc-L-Ala-D-Glu. {ECO:0000250}. FT BINDING 179 179 UDP-MurNAc-L-Ala-D-Glu. {ECO:0000250}. FT BINDING 185 185 UDP-MurNAc-L-Ala-D-Glu. {ECO:0000250}. FT BINDING 187 187 UDP-MurNAc-L-Ala-D-Glu. {ECO:0000250}. FT MOD_RES 219 219 N6-carboxylysine. {ECO:0000250}. FT HELIX 3 9 {ECO:0000244|PDB:4BUB}. FT TURN 10 13 {ECO:0000244|PDB:4BUB}. FT STRAND 14 19 {ECO:0000244|PDB:4BUB}. FT STRAND 27 32 {ECO:0000244|PDB:4BUB}. FT STRAND 37 43 {ECO:0000244|PDB:4BUB}. FT HELIX 54 60 {ECO:0000244|PDB:4BUB}. FT STRAND 64 70 {ECO:0000244|PDB:4BUB}. FT STRAND 74 76 {ECO:0000244|PDB:4BUB}. FT STRAND 78 82 {ECO:0000244|PDB:4BUB}. FT HELIX 84 95 {ECO:0000244|PDB:4BUB}. FT TURN 99 102 {ECO:0000244|PDB:4BUB}. FT STRAND 103 112 {ECO:0000244|PDB:4BUB}. FT HELIX 114 126 {ECO:0000244|PDB:4BUB}. FT STRAND 133 135 {ECO:0000244|PDB:4BUB}. FT HELIX 156 168 {ECO:0000244|PDB:4BUB}. FT STRAND 172 177 {ECO:0000244|PDB:4BUB}. FT HELIX 182 185 {ECO:0000244|PDB:4BUB}. FT TURN 186 188 {ECO:0000244|PDB:4BUB}. FT STRAND 193 198 {ECO:0000244|PDB:4BUB}. FT STRAND 203 207 {ECO:0000244|PDB:4BUB}. FT STRAND 209 211 {ECO:0000244|PDB:4BUB}. FT HELIX 212 220 {ECO:0000244|PDB:4BUB}. FT HELIX 221 223 {ECO:0000244|PDB:4BUB}. FT STRAND 226 235 {ECO:0000244|PDB:4BUB}. FT HELIX 236 238 {ECO:0000244|PDB:4BUB}. FT TURN 239 241 {ECO:0000244|PDB:4BUB}. FT STRAND 246 254 {ECO:0000244|PDB:4BUB}. FT STRAND 257 261 {ECO:0000244|PDB:4BUB}. FT STRAND 272 276 {ECO:0000244|PDB:4BUB}. FT STRAND 282 285 {ECO:0000244|PDB:4BUB}. FT HELIX 293 305 {ECO:0000244|PDB:4BUB}. FT TURN 306 308 {ECO:0000244|PDB:4BUB}. FT HELIX 311 315 {ECO:0000244|PDB:4BUB}. FT TURN 316 320 {ECO:0000244|PDB:4BUB}. FT STRAND 327 330 {ECO:0000244|PDB:4BUB}. FT HELIX 332 334 {ECO:0000244|PDB:4BUB}. FT TURN 335 338 {ECO:0000244|PDB:4BUB}. FT STRAND 340 343 {ECO:0000244|PDB:4BUB}. FT HELIX 349 362 {ECO:0000244|PDB:4BUB}. FT STRAND 367 371 {ECO:0000244|PDB:4BUB}. FT HELIX 383 392 {ECO:0000244|PDB:4BUB}. FT STRAND 394 398 {ECO:0000244|PDB:4BUB}. FT STRAND 404 406 {ECO:0000244|PDB:4BUB}. FT HELIX 409 416 {ECO:0000244|PDB:4BUB}. FT STRAND 425 427 {ECO:0000244|PDB:4BUB}. FT HELIX 431 441 {ECO:0000244|PDB:4BUB}. FT STRAND 447 450 {ECO:0000244|PDB:4BUB}. FT STRAND 458 462 {ECO:0000244|PDB:4BUB}. FT STRAND 465 468 {ECO:0000244|PDB:4BUB}. FT HELIX 471 484 {ECO:0000244|PDB:4BUB}. SQ SEQUENCE 490 AA; 54740 MW; 21A6FBE388D741A9 CRC64; MNISTIVSNL KDLILEVRAP YDLEITGVSN HSSKVKKGDL FICRRGEKFD SHEIIPEVME KGAVAVVVER EIDLDFPYIQ VFDSRYFEAK VASLFFEDPW KDVLTFGVTG TNGKTTTTMM IYHMLTSLGE RGSVLTTAVK RILGNSYYDD ITTPDAITIL SAMKENREGG GKFFALEVSS HALVQQRVEG VRFDVGIFTN ISRDHLDFHG TFENYLKAKL HLFDLLKDDG VAVLNESLAD AFNRKSRKIT FGTSKNADYR LGNIEVSWEG TQFVLETPDG LLKVFTRAIG DFNAYNAAAA IAALHQLGYD PKDLASSLET FTGVEGRFEV VRGAKKIGLN VVVDFAHSPD ALEKLLKNVR KISQGRVIVV FGAGGNSDRG KRPMMSEVAS KLADVVILTT DDPRGEDPEQ IMEDLIKGID KRKPYLVLFD RREAIETALT IANRGDSVVI AGRGHERYQI IDEEKKVPFQ DREVVEEIIR DKLKGRKYAQ // ID MURC_THEMA Reviewed; 457 AA. AC Q9WY73; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 130. DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase; DE EC=6.3.2.8; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase; GN Name=murC; OrderedLocusNames=TM_0231; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=15146505; DOI=10.1002/prot.20034; RA Spraggon G., Schwarzenbacher R., Kreusch A., Lee C.C., Abdubek P., RA Ambing E., Biorac T., Brinen L.S., Canaves J.M., Cambell J., RA Chiu H.-J., Dai X., Deacon A.M., DiDonato M., Elsliger M.-A., RA Eshagi S., Floyd R., Godzik A., Grittini C., Grzechnik S.K., RA Hampton E., Jaroszewski L., Karlak C., Klock H.E., Koesema E., RA Kovarik J.S., Kuhn P., Levin I., McMullan D., McPhillips T.M., RA Miller M.D., Morse A., Moy K., Ouyang J., Page R., Quijano K., RA Robb A., Stevens R.C., van den Bedem H., Velasquez J., Vincent J., RA von Delft F., Wang X., West B., Wolf G., Xu Q., Hodgson K.O., RA Wooley J., Lesley S.A., Wilson I.A.; RT "Crystal structure of an UDP-N-acetylmuramate-alanine ligase MurC RT (TM0231) from Thermotoga maritima at 2.3-A resolution."; RL Proteins 55:1078-1081(2004). CC -!- FUNCTION: Cell wall formation. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramate + L- CC alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- CC alanine. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35322.1; -; Genomic_DNA. DR PIR; A72402; A72402. DR RefSeq; NP_228045.1; NC_000853.1. DR RefSeq; WP_004082924.1; NZ_CP011107.1. DR PDB; 1J6U; X-ray; 2.30 A; A=1-457. DR PDBsum; 1J6U; -. DR ProteinModelPortal; Q9WY73; -. DR SMR; Q9WY73; 1-446. DR STRING; 243274.TM0231; -. DR EnsemblBacteria; AAD35322; AAD35322; TM_0231. DR GeneID; 897130; -. DR KEGG; tma:TM0231; -. DR PATRIC; 23935337; VBITheMar51294_0234. DR eggNOG; ENOG4105DFU; Bacteria. DR eggNOG; COG0773; LUCA. DR InParanoid; Q9WY73; -. DR KO; K01924; -. DR OMA; FHFIGIG; -. DR OrthoDB; EOG64BQ73; -. DR BRENDA; 6.3.2.8; 6331. DR UniPathway; UPA00219; -. DR EvolutionaryTrace; Q9WY73; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 2. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00046; MurC; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_murC. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01082; murC; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 457 UDP-N-acetylmuramate--L-alanine ligase. FT /FTId=PRO_0000182177. FT NP_BIND 109 115 ATP. {ECO:0000255}. FT STRAND 2 6 {ECO:0000244|PDB:1J6U}. FT TURN 7 9 {ECO:0000244|PDB:1J6U}. FT HELIX 11 22 {ECO:0000244|PDB:1J6U}. FT STRAND 26 30 {ECO:0000244|PDB:1J6U}. FT HELIX 36 43 {ECO:0000244|PDB:1J6U}. FT STRAND 48 51 {ECO:0000244|PDB:1J6U}. FT STRAND 61 65 {ECO:0000244|PDB:1J6U}. FT HELIX 74 81 {ECO:0000244|PDB:1J6U}. FT STRAND 86 88 {ECO:0000244|PDB:1J6U}. FT HELIX 89 100 {ECO:0000244|PDB:1J6U}. FT STRAND 104 108 {ECO:0000244|PDB:1J6U}. FT STRAND 110 112 {ECO:0000244|PDB:1J6U}. FT HELIX 113 126 {ECO:0000244|PDB:1J6U}. FT STRAND 132 134 {ECO:0000244|PDB:1J6U}. FT STRAND 145 148 {ECO:0000244|PDB:1J6U}. FT STRAND 154 158 {ECO:0000244|PDB:1J6U}. FT HELIX 163 167 {ECO:0000244|PDB:1J6U}. FT STRAND 171 175 {ECO:0000244|PDB:1J6U}. FT HELIX 183 186 {ECO:0000244|PDB:1J6U}. FT HELIX 190 202 {ECO:0000244|PDB:1J6U}. FT STRAND 205 210 {ECO:0000244|PDB:1J6U}. FT TURN 214 216 {ECO:0000244|PDB:1J6U}. FT HELIX 217 219 {ECO:0000244|PDB:1J6U}. FT STRAND 221 224 {ECO:0000244|PDB:1J6U}. FT STRAND 226 238 {ECO:0000244|PDB:1J6U}. FT STRAND 243 249 {ECO:0000244|PDB:1J6U}. FT STRAND 252 261 {ECO:0000244|PDB:1J6U}. FT HELIX 264 279 {ECO:0000244|PDB:1J6U}. FT HELIX 284 293 {ECO:0000244|PDB:1J6U}. FT STRAND 300 307 {ECO:0000244|PDB:1J6U}. FT TURN 308 311 {ECO:0000244|PDB:1J6U}. FT STRAND 312 317 {ECO:0000244|PDB:1J6U}. FT HELIX 322 335 {ECO:0000244|PDB:1J6U}. FT STRAND 337 345 {ECO:0000244|PDB:1J6U}. FT HELIX 359 364 {ECO:0000244|PDB:1J6U}. FT STRAND 367 372 {ECO:0000244|PDB:1J6U}. FT HELIX 388 397 {ECO:0000244|PDB:1J6U}. FT STRAND 402 404 {ECO:0000244|PDB:1J6U}. FT HELIX 408 410 {ECO:0000244|PDB:1J6U}. FT HELIX 411 414 {ECO:0000244|PDB:1J6U}. FT STRAND 419 426 {ECO:0000244|PDB:1J6U}. FT HELIX 431 445 {ECO:0000244|PDB:1J6U}. SQ SEQUENCE 457 AA; 51872 MW; 7D9AEDC50482351D CRC64; MKIHFVGIGG IGMSAVALHE FSNGNDVYGS NIEETERTAY LRKLGIPIFV PHSADNWYDP DLVIKTPAVR DDNPEIVRAR MERVPIENRL HYFRDTLKRE KKEEFAVTGT DGKTTTTAMV AHVLKHLRKS PTVFLGGIMD SLEHGNYEKG NGPVVYELDE SEEFFSEFSP NYLIITNARG DHLENYGNSL TRYRSAFEKI SRNTDLVVTF AEDELTSHLG DVTFGVKKGT YTLEMRSASR AEQKAMVEKN GKRYLELKLK VPGFHNVLNA LAVIALFDSL GYDLAPVLEA LEEFRGVHRR FSIAFHDPET NIYVIDDYAH TPDEIRNLLQ TAKEVFENEK IVVIFQPHRY SRLEREDGNF AKALQLADEV VVTEVYDAFE EKKNGISGKM IWDSLKSLGK EAYFVEKLPE LEKVISVSEN TVFLFVGAGD IIYSSRRFVE RYQSSKSSPS RVLGSNK // ID NADK_THEMA Reviewed; 258 AA. AC Q9X255; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361}; DE EC=2.7.1.23 {ECO:0000255|HAMAP-Rule:MF_00361}; DE AltName: Full=ATP-dependent NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361}; GN Name=NADK; OrderedLocusNames=TM_1733; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT. RX PubMed=16511117; DOI=10.1107/S1744309105019780; RA Oganesyan V., Huang C., Adams P.D., Jancarik J., Yokota H.A., Kim R., RA Kim S.H.; RT "Structure of a NAD kinase from Thermotoga maritima at 2.3 A RT resolution."; RL Acta Crystallogr. F 61:640-646(2005). CC -!- FUNCTION: Involved in the regulation of the intracellular balance CC between NAD(H) and NADP(H), and is a key enzyme in the CC biosynthesis of NADP. Catalyzes specifically the phosphorylation CC on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+). CC {ECO:0000255|HAMAP-Rule:MF_00361}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16511117}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}. CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00361}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36798.1; -; Genomic_DNA. DR PIR; D72217; D72217. DR RefSeq; NP_229531.1; NC_000853.1. DR RefSeq; WP_004082250.1; NZ_CP011107.1. DR PDB; 1YT5; X-ray; 2.30 A; A/B/C/D=1-258. DR PDBsum; 1YT5; -. DR ProteinModelPortal; Q9X255; -. DR SMR; Q9X255; 1-256. DR STRING; 243274.TM1733; -. DR EnsemblBacteria; AAD36798; AAD36798; TM_1733. DR GeneID; 897872; -. DR KEGG; tma:TM1733; -. DR PATRIC; 23938442; VBITheMar51294_1751. DR eggNOG; ENOG4105F91; Bacteria. DR eggNOG; COG0061; LUCA. DR InParanoid; Q9X255; -. DR KO; K00858; -. DR OMA; SGHFINE; -. DR OrthoDB; EOG6PZXDR; -. DR BRENDA; 2.7.1.23; 6331. DR EvolutionaryTrace; Q9X255; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro. DR GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.200.30; -; 1. DR Gene3D; 3.40.50.10330; -; 1. DR HAMAP; MF_00361; NAD_kinase; 1. DR InterPro; IPR017438; ATP-NAD_kinase_dom_1. DR InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b. DR InterPro; IPR016064; NAD/diacylglycerol_kinase. DR InterPro; IPR002504; NADK. DR PANTHER; PTHR20275; PTHR20275; 1. DR Pfam; PF01513; NAD_kinase; 1. DR SUPFAM; SSF111331; SSF111331; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; KW NADP; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 258 NAD kinase. FT /FTId=PRO_0000120680. FT NP_BIND 51 52 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT NP_BIND 119 120 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT NP_BIND 160 165 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT ACT_SITE 51 51 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00361}. FT BINDING 130 130 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT BINDING 149 149 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT BINDING 184 184 NAD; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00361}. FT STRAND 2 7 {ECO:0000244|PDB:1YT5}. FT HELIX 9 11 {ECO:0000244|PDB:1YT5}. FT HELIX 12 22 {ECO:0000244|PDB:1YT5}. FT TURN 23 25 {ECO:0000244|PDB:1YT5}. FT STRAND 26 36 {ECO:0000244|PDB:1YT5}. FT STRAND 43 49 {ECO:0000244|PDB:1YT5}. FT HELIX 51 58 {ECO:0000244|PDB:1YT5}. FT STRAND 66 74 {ECO:0000244|PDB:1YT5}. FT HELIX 83 85 {ECO:0000244|PDB:1YT5}. FT HELIX 86 94 {ECO:0000244|PDB:1YT5}. FT STRAND 99 110 {ECO:0000244|PDB:1YT5}. FT STRAND 113 124 {ECO:0000244|PDB:1YT5}. FT STRAND 132 138 {ECO:0000244|PDB:1YT5}. FT STRAND 144 154 {ECO:0000244|PDB:1YT5}. FT HELIX 157 160 {ECO:0000244|PDB:1YT5}. FT TURN 161 167 {ECO:0000244|PDB:1YT5}. FT STRAND 177 184 {ECO:0000244|PDB:1YT5}. FT STRAND 193 196 {ECO:0000244|PDB:1YT5}. FT STRAND 201 213 {ECO:0000244|PDB:1YT5}. FT STRAND 216 237 {ECO:0000244|PDB:1YT5}. FT HELIX 243 251 {ECO:0000244|PDB:1YT5}. SQ SEQUENCE 258 AA; 29242 MW; 45EBBCA0B6FD3EAB CRC64; MKIAILYREE REKEGEFLKE KISKEHEVIE FGEANAPGRV TADLIVVVGG DGTVLKAAKK AADGTPMVGF KAGRLGFLTS YTLDEIDRFL EDLRNWNFRE ETRWFIQIES ELGNHLALND VTLERDLSGK MVEIEVEVEH HSSMWFFADG VVISTPTGST AYSLSIGGPI IFPECEVLEI SPIAPQFFLT RSVVIPSNFK VVVESQRDIN MLVDGVLTGK TKRIEVKKSR RYVRILRPPE YDYVTVIRDK LGYGRRIE // ID MURG_THEMA Reviewed; 339 AA. AC Q9WY74; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 119. DE RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000255|HAMAP-Rule:MF_00033}; DE EC=2.4.1.227 {ECO:0000255|HAMAP-Rule:MF_00033}; DE AltName: Full=Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase {ECO:0000255|HAMAP-Rule:MF_00033}; GN Name=murG {ECO:0000255|HAMAP-Rule:MF_00033}; GN OrderedLocusNames=TM_0232; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc CC subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid CC intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- CC (pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP- CC Rule:MF_00033}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala- CC gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + CC GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- CC diphosphoundecaprenol. {ECO:0000255|HAMAP-Rule:MF_00033}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00033}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00033}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00033}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35323.1; -; Genomic_DNA. DR PIR; B72402; B72402. DR RefSeq; NP_228046.1; NC_000853.1. DR RefSeq; WP_004082926.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY74; -. DR STRING; 243274.TM0232; -. DR CAZy; GT28; Glycosyltransferase Family 28. DR DNASU; 897131; -. DR EnsemblBacteria; AAD35323; AAD35323; TM_0232. DR GeneID; 897131; -. DR KEGG; tma:TM0232; -. DR PATRIC; 23935339; VBITheMar51294_0235. DR eggNOG; ENOG4105DVQ; Bacteria. DR eggNOG; COG0707; LUCA. DR InParanoid; Q9WY74; -. DR KO; K02563; -. DR OMA; EQNALPG; -. DR OrthoDB; EOG61VZFD; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051991; F:UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity; IEA:UniProtKB-EC. DR GO; GO:0050511; F:undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0030259; P:lipid glycosylation; IEA:UniProtKB-HAMAP. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00033; MurG; 1. DR InterPro; IPR006009; GlcNAc_MurG. DR InterPro; IPR007235; Glyco_trans_28_C. DR InterPro; IPR004276; GlycoTrans_28_N. DR Pfam; PF04101; Glyco_tran_28_C; 1. DR Pfam; PF03033; Glyco_transf_28; 1. DR TIGRFAMs; TIGR01133; murG; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Glycosyltransferase; Membrane; Peptidoglycan synthesis; KW Reference proteome; Transferase. FT CHAIN 1 339 UDP-N-acetylglucosamine--N-acetylmuramyl- FT (pentapeptide) pyrophosphoryl- FT undecaprenol N-acetylglucosamine FT transferase. FT /FTId=PRO_0000109231. SQ SEQUENCE 339 AA; 37684 MW; BD7B7100F0851426 CRC64; MIKVAAAGGG TGGHLYPLLA ILETLAKRVD VKVLFFAVKG KIDERVVRKD HPEFETVSID VRGLLRPLHH PKNLWRTLKI GIATIEVKKH LKRFKPDLVV LTGGYISGVV GLAAKDLGIP IFVHEQNVVP GLAVKVLSQY AKKVFVSFER TRDYLREWQD KIVVTGCPVR ETEKEAPLKD FVLVLGGSLG SEAINELMEK VYPELQETQF VHSTGSDDWT ERLSVFPNVT ALTYIDPMGA YWKKAIASIS RAGASTIAEM MYYGVPGILI PWESSAESHQ LENALEAERL GYAIVIRENE ASPRKIIESI DKVVKKGKIE KMKENPASKI SKEILGEIM // ID MUTS_THEMA Reviewed; 793 AA. AC P74926; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 111. DE RecName: Full=DNA mismatch repair protein MutS; GN Name=mutS; OrderedLocusNames=TM_1719; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Wetmur J.G., Rosenfeld A., Wong D.M.; RT "Hyperthermophilic MutS proteins: isolation, characterization and RT enhancement of PCR specificity."; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: This protein is involved in the repair of mismatches in CC DNA. It is possible that it carries out the mismatch recognition CC step. This protein has a weak ATPase activity (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U71155; AAB16999.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36785.1; -; Genomic_DNA. DR PIR; C72219; C72219. DR RefSeq; NP_229518.1; NC_000853.1. DR RefSeq; WP_004082235.1; NZ_CP011107.1. DR ProteinModelPortal; P74926; -. DR STRING; 243274.TM1719; -. DR EnsemblBacteria; AAD36785; AAD36785; TM_1719. DR GeneID; 897879; -. DR KEGG; tma:TM1719; -. DR PATRIC; 23938414; VBITheMar51294_1737. DR eggNOG; ENOG4105D86; Bacteria. DR eggNOG; COG0249; LUCA. DR InParanoid; P74926; -. DR KO; K03555; -. DR OMA; CCTTMGS; -. DR OrthoDB; EOG6Q5NPV; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro. DR GO; GO:0006298; P:mismatch repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.110; -; 1. DR Gene3D; 3.40.1170.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00096; MutS; 1. DR InterPro; IPR005748; DNA_mismatch_repair_MutS-1. DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N. DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C. DR InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp. DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core. DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N. DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01624; MutS_I; 1. DR Pfam; PF05188; MutS_II; 1. DR Pfam; PF05192; MutS_III; 1. DR Pfam; PF05190; MutS_IV; 1. DR Pfam; PF00488; MutS_V; 1. DR SMART; SM00534; MUTSac; 1. DR SMART; SM00533; MUTSd; 1. DR SUPFAM; SSF48334; SSF48334; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF53150; SSF53150; 1. DR SUPFAM; SSF55271; SSF55271; 1. DR TIGRFAMs; TIGR01070; mutS1; 1. DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 793 DNA mismatch repair protein MutS. FT /FTId=PRO_0000115158. FT NP_BIND 589 596 ATP. {ECO:0000255}. FT CONFLICT 233 233 A -> G (in Ref. 1; AAB16999). FT {ECO:0000305}. FT CONFLICT 262 262 L -> W (in Ref. 1; AAB16999). FT {ECO:0000305}. FT CONFLICT 287 287 L -> G (in Ref. 1; AAB16999). FT {ECO:0000305}. FT CONFLICT 506 506 K -> T (in Ref. 1; AAB16999). FT {ECO:0000305}. SQ SEQUENCE 793 AA; 91066 MW; 1BCB2342E4F9B1BD CRC64; MKVTPLMEQY LRIKEQYKDS ILLFRLGDFY EAFFEDAKIV SKVLNIVLTR RQDAPMAGIP YHALNTYLKK LVEAGYKVAI CDQMEEPSKS KKLIRREVTR VVTPGSIVED EFLSETNNYM AVVSEEKGRY CTVFCDVSTG EVLVHESSDE QETLDLLKNY SISQIICPEH LKSSLKERFP GVYTETISEW YFSDLEEVEK AYNLKDIHHF ELSPLALKAL AALIKYVKYT MIAEDLNLKP PLLISQRDYM ILDSATVENL SLIPGDRGKN LFDVLNNTET PMGARLLKKW ILHPLVDRKQ IEERLKAVER LVNDRVSLEE MRNLLSNVRD VERIVSRVEY NRSVPRDLVA LRETLEIIPK LNEVLSTFGV FKKLAFPEGL VDLLRKAIED DPVGSPGEGK VIKRGFSSEL DEYRDLLEHA EERLKEFEEK ERERTGIQKL RVGYNQVFGY YIEVTKANLD KIPDDYERKQ TLVNSERFIT PELKEFETKI MAAKERIEEL EKELFKSVCE EVKKHKEVLL EISEDLAKID ALSTLAYDAI MYNYTKPVFS EDRLEIKGGR HPVVERFTQN FVENDIYMDN EKRFVVITGP NMSGKSTFIR QVGLISLMAQ IGSFVPAQKA ILPVFDRIFT RMGARDDLAG GRSTFLVEMN EMALILLKST NKSLVLLDEV GRGTSTQDGV SIAWAISEEL IKRGCKVLFA THFTELTELE KHFPQVQNKT ILVKEEGKNV IFTHKVVDGV ADRSYGIEVA KIAGIPDRVI NRAYEILERN FKNNTKKNGK SNRFSQQIPL FPV // ID NADD_THEMA Reviewed; 205 AA. AC Q9WXV2; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=Probable nicotinate-nucleotide adenylyltransferase; DE EC=2.7.7.18; DE AltName: Full=Deamido-NAD(+) diphosphorylase; DE AltName: Full=Deamido-NAD(+) pyrophosphorylase; DE AltName: Full=Nicotinate mononucleotide adenylyltransferase; DE Short=NaMN adenylyltransferase; GN Name=nadD; OrderedLocusNames=TM_0097; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate CC mononucleotide (NaMN) to nicotinic acid adenine dinucleotide CC (NaAD). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide = CC diphosphate + deamido-NAD(+). CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido- CC NAD(+) from nicotinate D-ribonucleotide: step 1/1. CC -!- SIMILARITY: Belongs to the NadD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35191.1; -; Genomic_DNA. DR PIR; A72418; A72418. DR RefSeq; NP_227913.1; NC_000853.1. DR RefSeq; WP_010865050.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXV2; -. DR STRING; 243274.TM0097; -. DR EnsemblBacteria; AAD35191; AAD35191; TM_0097. DR GeneID; 896924; -. DR KEGG; tma:TM0097; -. DR PATRIC; 23935034; VBITheMar51294_0095. DR eggNOG; ENOG4108Z1W; Bacteria. DR eggNOG; COG1057; LUCA. DR InParanoid; Q9WXV2; -. DR KO; K00969; -. DR OMA; PYHEHAR; -. DR OrthoDB; EOG6F55KJ; -. DR BioCyc; TMAR243274:GC6P-97-MONOMER; -. DR UniPathway; UPA00253; UER00332. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00244; NaMN_adenylyltr; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR005248; NAMN_adtrnsfrase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR TIGRFAMs; TIGR00482; TIGR00482; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; NAD; Nucleotide-binding; KW Nucleotidyltransferase; Pyridine nucleotide biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 205 Probable nicotinate-nucleotide FT adenylyltransferase. FT /FTId=PRO_0000181460. SQ SEQUENCE 205 AA; 23796 MW; CBC6518FC579753B CRC64; MLSGSETSSL NTGNRIGIFG GSFDPVHTGH VLVSVYTLEI LDLDRLIVVP VFNPPHKKTV APFEKRFEWL KKVFEGMEKM EVSDYEKRRG GVSYSIFTIE YFSEIYKTKP FFIVGEDALS YFEKWYRYRD ILKKSTLVVY PRYCGKPYHE HARRVLGDLS EIVFLDMPIV QISSTEIRER ARLGKTLKGF VPEEIRKEVE VFYGG // ID NADE2_THEMA Reviewed; 576 AA. AC Q9X0Y0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 113. DE RecName: Full=Probable glutamine-dependent NAD(+) synthetase; DE EC=6.3.5.1; DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing]; GN Name=nadE2; OrderedLocusNames=TM_1253; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Can use both glutamine or ammonia as a nitrogen source. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + L-glutamine + H(2)O = CC AMP + diphosphate + NAD(+) + L-glutamate. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC deamido-NAD(+) (L-Gln route): step 1/1. CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD CC synthetase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 CN hydrolase domain. {ECO:0000255|PROSITE- CC ProRule:PRU00054}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36328.1; -; Genomic_DNA. DR PIR; G72277; G72277. DR RefSeq; NP_229058.1; NC_000853.1. DR RefSeq; WP_004080010.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0Y0; -. DR STRING; 243274.TM1253; -. DR EnsemblBacteria; AAD36328; AAD36328; TM_1253. DR GeneID; 898230; -. DR KEGG; tma:TM1253; -. DR PATRIC; 23937446; VBITheMar51294_1269. DR eggNOG; ENOG4105C4K; Bacteria. DR eggNOG; COG0171; LUCA. DR eggNOG; COG0388; LUCA. DR InParanoid; Q9X0Y0; -. DR KO; K01950; -. DR OMA; LVYAHLV; -. DR OrthoDB; EOG6VB6S8; -. DR UniPathway; UPA00253; UER00334. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC. DR GO; GO:0008795; F:NAD+ synthase activity; IBA:GO_Central. DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.60.110.10; -; 1. DR InterPro; IPR003010; C-N_Hydrolase. DR InterPro; IPR014445; Gln-dep_NAD_synthase. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR003694; NAD_synthase. DR InterPro; IPR000132; Nitrilase/CN_hydratase_CS. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00795; CN_hydrolase; 1. DR Pfam; PF02540; NAD_synthase; 1. DR PIRSF; PIRSF006630; NADS_GAT; 1. DR SUPFAM; SSF56317; SSF56317; 1. DR TIGRFAMs; TIGR00552; nadE; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. DR PROSITE; PS00920; NITRIL_CHT_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 576 Probable glutamine-dependent NAD(+) FT synthetase. FT /FTId=PRO_0000152245. FT DOMAIN 4 264 CN hydrolase. {ECO:0000255|PROSITE- FT ProRule:PRU00054}. FT NP_BIND 321 328 ATP. {ECO:0000250}. FT REGION 292 576 Ligase. FT ACT_SITE 323 323 {ECO:0000255|PROSITE-ProRule:PRU00054}. SQ SEQUENCE 576 AA; 64920 MW; 208FDC77964C957F CRC64; MKRLRVTLAQ LNPTLGDFEG NLKKAIEALR VAEDRGSDLL VFPELFLPGY PPEDLMLRLS FLRENRKYLQ KFAQHTRNLG VTVLMGFIDS DEDAYNAAAV VKDGEILGVY RKISLPNYGV FDERRYFKPG EELLVVKIGN IKVGVTICED IWNPVEPSAS LSLGEGVHLI ANLSASPYHV GKPVLRKDYL SMKAYDYHVA MAYCNMVGGQ DELVFDGGSM VVDASGEVIN YGKLFEEEII TVDLDLDENL RVSLVDPRRR YMKTQNYPVK TVEAGNLREK SGHFEPVVNP LPVREEEMFR ALITGLRDYV RKNGFEKVVI GLSGGMDSSL VAVIATEALG KENVKGVLMP SMYTSKESIE DAQTLAKNLG IETFIIPITD VFHSYLETLK GVFAGREPDI TEENLQARIR GNYLMALSNK FGWLVLTTGN KSEMATGYAT LYGDMAGGFA VIKDVYKTDV YRIGRWYNSW RGKEIIPENI FVKPPTAELR PGQTDQEKLP PYEVLDEILR LYIEEGLDPE EIASKGFDRK TVLDVTEMIR KNEYKRKQAA IGVKISTRAF GKDWRMPITN RFKEPL // ID NADA_THEMA Reviewed; 298 AA. AC Q9X1X7; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Quinolinate synthase A {ECO:0000255|HAMAP-Rule:MF_00568}; DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00568}; GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00568}; GN OrderedLocusNames=TM_1644; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with CC dihydroxyacetone phosphate to form quinolinate. CC {ECO:0000255|HAMAP-Rule:MF_00568}. CC -!- CATALYTIC ACTIVITY: Glycerone phosphate + iminosuccinate = CC pyridine-2,3-dicarboxylate + 2 H(2)O + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00568}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00568}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate CC from iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00568}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00568}. CC -!- SIMILARITY: Belongs to the quinolinate synthase A family. Type 2 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00568}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36711.1; -; Genomic_DNA. DR PIR; A72227; A72227. DR RefSeq; NP_229444.1; NC_000853.1. DR RefSeq; WP_004082140.1; NZ_CP011107.1. DR PDB; 4P3X; X-ray; 1.65 A; A=1-298. DR PDBsum; 4P3X; -. DR ProteinModelPortal; Q9X1X7; -. DR STRING; 243274.TM1644; -. DR EnsemblBacteria; AAD36711; AAD36711; TM_1644. DR GeneID; 897919; -. DR KEGG; tma:TM1644; -. DR PATRIC; 23938262; VBITheMar51294_1663. DR eggNOG; ENOG4105D0I; Bacteria. DR eggNOG; COG0379; LUCA. DR InParanoid; Q9X1X7; -. DR KO; K03517; -. DR OMA; IAHPECE; -. DR OrthoDB; EOG6DJZ56; -. DR UniPathway; UPA00253; UER00327. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008987; F:quinolinate synthetase A activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00568; NadA_type2; 1. DR InterPro; IPR003473; NadA. DR InterPro; IPR023066; Quinolinate_synth_type2. DR Pfam; PF02445; NadA; 1. DR TIGRFAMs; TIGR00550; nadA; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Pyridine nucleotide biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 298 Quinolinate synthase A. FT /FTId=PRO_0000155798. FT BINDING 19 19 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00568}. FT BINDING 36 36 Iminoaspartate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00568}. FT BINDING 107 107 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00568}. FT BINDING 124 124 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00568}. FT BINDING 193 193 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00568}. FT BINDING 210 210 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00568}. FT HELIX 1 12 {ECO:0000244|PDB:4P3X}. FT STRAND 14 19 {ECO:0000244|PDB:4P3X}. FT HELIX 24 29 {ECO:0000244|PDB:4P3X}. FT STRAND 31 34 {ECO:0000244|PDB:4P3X}. FT HELIX 36 43 {ECO:0000244|PDB:4P3X}. FT STRAND 50 55 {ECO:0000244|PDB:4P3X}. FT HELIX 57 66 {ECO:0000244|PDB:4P3X}. FT STRAND 70 73 {ECO:0000244|PDB:4P3X}. FT HELIX 82 85 {ECO:0000244|PDB:4P3X}. FT HELIX 89 98 {ECO:0000244|PDB:4P3X}. FT STRAND 104 110 {ECO:0000244|PDB:4P3X}. FT HELIX 112 115 {ECO:0000244|PDB:4P3X}. FT STRAND 119 122 {ECO:0000244|PDB:4P3X}. FT TURN 124 126 {ECO:0000244|PDB:4P3X}. FT HELIX 127 133 {ECO:0000244|PDB:4P3X}. FT STRAND 137 143 {ECO:0000244|PDB:4P3X}. FT HELIX 145 155 {ECO:0000244|PDB:4P3X}. FT STRAND 158 163 {ECO:0000244|PDB:4P3X}. FT HELIX 169 171 {ECO:0000244|PDB:4P3X}. FT HELIX 175 184 {ECO:0000244|PDB:4P3X}. FT STRAND 189 192 {ECO:0000244|PDB:4P3X}. FT HELIX 198 203 {ECO:0000244|PDB:4P3X}. FT STRAND 204 207 {ECO:0000244|PDB:4P3X}. FT HELIX 210 219 {ECO:0000244|PDB:4P3X}. FT STRAND 223 229 {ECO:0000244|PDB:4P3X}. FT HELIX 232 240 {ECO:0000244|PDB:4P3X}. FT STRAND 244 250 {ECO:0000244|PDB:4P3X}. FT HELIX 257 259 {ECO:0000244|PDB:4P3X}. FT HELIX 262 271 {ECO:0000244|PDB:4P3X}. FT HELIX 280 296 {ECO:0000244|PDB:4P3X}. SQ SEQUENCE 298 AA; 33617 MW; 682510831BFF6D01 CRC64; MVDEILKLKK EKGYIILAHN YQIPELQDIA DFVGDSLQLA RKAMELSEKK ILFLGVDFMA ELVKILNPDK KVIVPDRSAT CPMANRLTPE IIREYREKFP DAPVVLYVNS TSECKTLADV ICTSANAVEV VKKLDSSVVI FGPDRNLGEY VAEKTGKKVI TIPENGHCPV HQFNAESIDA VRKKYPDAKV IVHPECPKPV RDKADYVGST GQMEKIPEKD PSRIFVIGTE IGMIHKLKKK FPDREFVPLE MAVCVNMKKN TLENTLHALQ TESFEVILPK EVIEKAKKPI LRMFELMG // ID NADE1_THEMA Reviewed; 281 AA. AC Q9WZB3; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=NH(3)-dependent NAD(+) synthetase; DE EC=6.3.1.5; GN Name=nadE1; OrderedLocusNames=TM_0645; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + NH(3) = AMP + CC diphosphate + NAD(+). CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC deamido-NAD(+) (ammonia route): step 1/1. CC -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35729.1; -; Genomic_DNA. DR PIR; D72351; D72351. DR RefSeq; NP_228454.1; NC_000853.1. DR RefSeq; WP_004081153.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZB3; -. DR STRING; 243274.TM0645; -. DR EnsemblBacteria; AAD35729; AAD35729; TM_0645. DR GeneID; 897750; -. DR KEGG; tma:TM0645; -. DR PATRIC; 23936204; VBITheMar51294_0655. DR eggNOG; ENOG4107S7H; Bacteria. DR eggNOG; COG0171; LUCA. DR InParanoid; Q9WZB3; -. DR KO; K01916; -. DR OMA; TGLYVKW; -. DR OrthoDB; EOG64JFM7; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0008795; F:NAD+ synthase activity; IBA:GO_Central. DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00193; NadE; 1. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR003694; NAD_synthase. DR InterPro; IPR022926; NH(3)-dep_NAD(+)_synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF02540; NAD_synthase; 2. DR TIGRFAMs; TIGR00552; nadE; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 281 NH(3)-dependent NAD(+) synthetase. FT /FTId=PRO_0000152212. FT NP_BIND 24 31 ATP. {ECO:0000250}. FT ACT_SITE 26 26 {ECO:0000250}. SQ SEQUENCE 281 AA; 32697 MW; CAF86CBF207752FA CRC64; MKESLISFIK EKIEEYNYRG AVVGVSGGVD SAVVLSLCVQ ALGKDRVFAL ILPERDSSKD SLKDAVDFCE RLGVEYRKRS ITPILRKIGV YRLFPPRLFL PDSIVKRYVL NRWNTLSKDP FLDDLRNTGP EEFLKGLAYY RIKHRIRMCL LYFEAEKRGY AVVGTTNRTE YLTGLYVKWG DEAVDIEPIM HLYKTQVFEL AKEMNVPEKI LKKPPSPDLI PGITDEMAFN MSYLELDRIL MKLEKNEDLS DEDPKKVERV KKILELSEKY RRDIPITFDR I // ID NFI_THEMA Reviewed; 225 AA. AC Q9X2H9; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Endonuclease V {ECO:0000255|HAMAP-Rule:MF_00801}; DE EC=3.1.21.7 {ECO:0000255|HAMAP-Rule:MF_00801}; DE AltName: Full=Deoxyinosine 3'endonuclease {ECO:0000255|HAMAP-Rule:MF_00801}; DE AltName: Full=Deoxyribonuclease V {ECO:0000255|HAMAP-Rule:MF_00801}; DE Short=DNase V {ECO:0000255|HAMAP-Rule:MF_00801}; GN Name=nfi {ECO:0000255|HAMAP-Rule:MF_00801}; OrderedLocusNames=TM_1865; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND MUTAGENESIS OF ASP-43; RP TYR-80; ARG-88; GLU-89; ASP-110; HIS-116; HIS-125 AND LYS-139. RX PubMed=12081482; DOI=10.1021/bi015960s; RA Huang J., Lu J., Barany F., Cao W.; RT "Mutational analysis of endonuclease V from Thermotoga maritima."; RL Biochemistry 41:8342-8350(2002). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEXES WITH HYPOXANTHINE RP LESION SUBSTRATE; DNA AND MAGNESIUM IONS. RX PubMed=19136958; DOI=10.1038/nsmb.1538; RA Dalhus B., Arvai A.S., Rosnes I., Olsen O.E., Backe P.H., Alseth I., RA Gao H., Cao W., Tainer J.A., Bjoras M.; RT "Structures of endonuclease V with DNA reveal initiation of deaminated RT adenine repair."; RL Nat. Struct. Mol. Biol. 16:138-143(2009). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-222. RA Utepbergenov D., Cooper D.R., Derewenda U., Derewenda Z.S.; RT "Crystal structure of Tm1865, an Endonuclease V from Thermotoga RT maritima."; RL Submitted (MAY-2009) to the PDB data bank. CC -!- FUNCTION: DNA repair enzyme involved in the repair of deaminated CC bases. Selectively cleaves double-stranded DNA at the second CC phosphodiester bond 3' to a deoxyinosine leaving behind the intact CC lesion on the nicked DNA. In vitro, can also cleave single- CC stranded substrates with inosine, double-stranded DNA with CC apurinic sites, or DNA sites with uracil or a mismatched base. CC When present in molar excess, two protein molecules can bind to CC the same DNA substrate and effect cleavage of both strands (in CC vitro). {ECO:0000255|HAMAP-Rule:MF_00801, CC ECO:0000269|PubMed:12081482}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage at apurinic or CC apyrimidinic sites to products with a 5'-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00801, ECO:0000269|PubMed:12081482}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00801, CC ECO:0000269|PubMed:12081482}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00801}. CC -!- SIMILARITY: Belongs to the endonuclease V family. CC {ECO:0000255|HAMAP-Rule:MF_00801}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36927.1; -; Genomic_DNA. DR PIR; B72202; B72202. DR RefSeq; NP_229661.1; NC_000853.1. DR RefSeq; WP_004082416.1; NZ_CP011107.1. DR PDB; 2W35; X-ray; 2.15 A; A/B=1-225. DR PDB; 2W36; X-ray; 2.10 A; A/B=1-225. DR PDB; 3HD0; X-ray; 2.70 A; A/B/D=1-222. DR PDB; 4B20; X-ray; 2.75 A; A/B=1-225. DR PDBsum; 2W35; -. DR PDBsum; 2W36; -. DR PDBsum; 3HD0; -. DR PDBsum; 4B20; -. DR DIP; DIP-48482N; -. DR STRING; 243274.TM1865; -. DR EnsemblBacteria; AAD36927; AAD36927; TM_1865. DR GeneID; 897801; -. DR KEGG; tma:TM1865; -. DR PATRIC; 23938719; VBITheMar51294_1886. DR eggNOG; ENOG4105Y7X; Bacteria. DR eggNOG; COG1515; LUCA. DR InParanoid; Q9X2H9; -. DR KO; K05982; -. DR OMA; REYPALM; -. DR OrthoDB; EOG6C0163; -. DR BRENDA; 3.1.21.7; 6331. DR EvolutionaryTrace; Q9X2H9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043737; F:deoxyribonuclease V activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00801; Endonuclease_5; 1. DR InterPro; IPR007581; Endonuclease-V. DR Pfam; PF04493; Endonuclease_5; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; DNA damage; DNA repair; KW Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Reference proteome. FT CHAIN 1 225 Endonuclease V. FT /FTId=PRO_0000159674. FT REGION 139 141 Interaction with target DNA. FT REGION 214 221 Interaction with target DNA. FT METAL 43 43 Magnesium. FT METAL 110 110 Magnesium. FT SITE 80 80 Interaction with target DNA. FT MUTAGEN 43 43 D->A: Complete loss of enzyme activity. FT {ECO:0000269|PubMed:12081482}. FT MUTAGEN 80 80 Y->A: Reduced affinity for DNA. No effect FT on cleavage of DNA containing inosine. FT Abolishes cleavage at apurinic sites. FT {ECO:0000269|PubMed:12081482}. FT MUTAGEN 88 88 R->A: Reduced affinity for DNA. No effect FT on cleavage of DNA containing inosine. FT Abolishes cleavage at apurinic sites. FT {ECO:0000269|PubMed:12081482}. FT MUTAGEN 89 89 E->A: Strongly reduced cleavage of DNA FT containing inosine. FT {ECO:0000269|PubMed:12081482}. FT MUTAGEN 105 105 D->A: No effect on cleavage of DNA FT containing inosine. FT MUTAGEN 110 110 D->A: Complete loss of enzyme activity. FT {ECO:0000269|PubMed:12081482}. FT MUTAGEN 116 116 H->A: Reduced affinity for DNA. No effect FT on cleavage of DNA containing inosine. FT Abolishes cleavage at apurinic sites. FT {ECO:0000269|PubMed:12081482}. FT MUTAGEN 125 125 H->A: No effect on cleavage of DNA FT containing inosine. FT {ECO:0000269|PubMed:12081482}. FT MUTAGEN 139 139 K->A: No effect on DNA binding. No effect FT on cleavage of DNA containing inosine. FT Strongly reduced cleavage at apurinic FT sites. {ECO:0000269|PubMed:12081482}. FT HELIX 13 23 {ECO:0000244|PDB:2W36}. FT HELIX 24 26 {ECO:0000244|PDB:2W36}. FT STRAND 37 48 {ECO:0000244|PDB:2W36}. FT STRAND 51 60 {ECO:0000244|PDB:2W36}. FT TURN 61 64 {ECO:0000244|PDB:2W36}. FT STRAND 65 75 {ECO:0000244|PDB:2W36}. FT HELIX 86 97 {ECO:0000244|PDB:2W36}. FT STRAND 105 111 {ECO:0000244|PDB:2W36}. FT STRAND 113 116 {ECO:0000244|PDB:2W36}. FT HELIX 122 130 {ECO:0000244|PDB:2W36}. FT STRAND 134 140 {ECO:0000244|PDB:2W36}. FT STRAND 143 145 {ECO:0000244|PDB:3HD0}. FT STRAND 151 154 {ECO:0000244|PDB:2W36}. FT STRAND 156 161 {ECO:0000244|PDB:2W36}. FT STRAND 164 170 {ECO:0000244|PDB:2W36}. FT STRAND 179 183 {ECO:0000244|PDB:2W36}. FT HELIX 189 199 {ECO:0000244|PDB:2W36}. FT HELIX 208 220 {ECO:0000244|PDB:2W36}. SQ SEQUENCE 225 AA; 25598 MW; 84250E645E410445 CRC64; MDYRQLHRWD LPPEEAIKVQ NELRKKIKLT PYEGEPEYVA GVDLSFPGKE EGLAVIVVLE YPSFKILEVV SERGEITFPY IPGLLAFREG PLFLKAWEKL RTKPDVVVFD GQGLAHPRKL GIASHMGLFI EIPTIGVAKS RLYGTFKMPE DKRCSWSYLY DGEEIIGCVI RTKEGSAPIF VSPGHLMDVE SSKRLIKAFT LPGRRIPEPT RLAHIYTQRL KKGLF // ID NIAR_THEMA Reviewed; 175 AA. AC Q9X1T8; DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 09-DEC-2015, entry version 93. DE RecName: Full=Probable transcription repressor NiaR; GN Name=niaR; OrderedLocusNames=TM_1602; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP DNA-BINDING. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=18276644; DOI=10.1093/nar/gkn046; RA Rodionov D.A., Li X., Rodionova I.A., Yang C., Sorci L., Dervyn E., RA Martynowski D., Zhang H., Gelfand M.S., Osterman A.L.; RT "Transcriptional regulation of NAD metabolism in bacteria: genomic RT reconstruction of NiaR (YrxA) regulon."; RL Nucleic Acids Res. 36:2032-2046(2008). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH NICKEL, AND RP SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=17256761; DOI=10.1002/prot.21221; RA Weekes D., Miller M.D., Krishna S.S., McMullan D., McPhillips T.M., RA Acosta C., Canaves J.M., Elsliger M.A., Floyd R., Grzechnik S.K., RA Jaroszewski L., Klock H.E., Koesema E., Kovarik J.S., Kreusch A., RA Morse A.T., Quijano K., Spraggon G., van den Bedem H., Wolf G., RA Hodgson K.O., Wooley J., Deacon A.M., Godzik A., Lesley S.A., RA Wilson I.A.; RT "Crystal structure of a transcription regulator (TM1602) from RT Thermotoga maritima at 2.3 A resolution."; RL Proteins 67:247-252(2007). CC -!- FUNCTION: Probably functions to regulate transcription of NAD CC metabolic genes. Binds to DNA upstream of the probable CC nadBII/nadA/nadC and niaRP operons in a nicotinic acid dependent CC fashion. Nicotinic acid may be a corepressor. CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Note=Binds 1 Ni(2+) ion per monomer; it is not certain this is the CC physiological metal.; CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:17256761}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36669.1; -; Genomic_DNA. DR PIR; F72234; F72234. DR RefSeq; NP_229402.1; NC_000853.1. DR RefSeq; WP_004082049.1; NZ_CP011107.1. DR PDB; 1J5Y; X-ray; 2.30 A; A=1-175. DR PDBsum; 1J5Y; -. DR ProteinModelPortal; Q9X1T8; -. DR SMR; Q9X1T8; 3-174. DR STRING; 243274.TM1602; -. DR EnsemblBacteria; AAD36669; AAD36669; TM_1602. DR GeneID; 897940; -. DR KEGG; tma:TM1602; -. DR KEGG; tmi:THEMA_06240; -. DR KEGG; tmw:THMA_1642; -. DR PATRIC; 23938178; VBITheMar51294_1621. DR eggNOG; ENOG4108Z3G; Bacteria. DR eggNOG; COG1827; LUCA. DR InParanoid; Q9X1T8; -. DR KO; K07105; -. DR OMA; IVEHPLY; -. DR OrthoDB; EOG6QCDFT; -. DR EvolutionaryTrace; Q9X1T8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0036094; F:small molecule binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.1340.20; -; 1. DR InterPro; IPR004173; 3H_domain. DR InterPro; IPR013196; HTH_11. DR InterPro; IPR026043; NadR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02829; 3H; 1. DR Pfam; PF08279; HTH_11; 1. DR PIRSF; PIRSF037847; NiaR; 1. DR ProDom; PD469575; 3H_domain; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF75500; SSF75500; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-binding; Metal-binding; Nickel; KW Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 175 Probable transcription repressor NiaR. FT /FTId=PRO_0000409021. FT METAL 79 79 Nickel; via tele nitrogen. FT {ECO:0000269|PubMed:17256761}. FT METAL 87 87 Nickel. {ECO:0000269|PubMed:17256761}. FT METAL 146 146 Nickel; via tele nitrogen. FT {ECO:0000269|PubMed:17256761}. FT METAL 148 148 Nickel; via tele nitrogen. FT {ECO:0000269|PubMed:17256761}. FT HELIX 4 20 {ECO:0000244|PDB:1J5Y}. FT HELIX 27 34 {ECO:0000244|PDB:1J5Y}. FT HELIX 38 51 {ECO:0000244|PDB:1J5Y}. FT STRAND 56 58 {ECO:0000244|PDB:1J5Y}. FT STRAND 61 63 {ECO:0000244|PDB:1J5Y}. FT TURN 66 68 {ECO:0000244|PDB:1J5Y}. FT STRAND 70 78 {ECO:0000244|PDB:1J5Y}. FT HELIX 81 83 {ECO:0000244|PDB:1J5Y}. FT HELIX 84 93 {ECO:0000244|PDB:1J5Y}. FT STRAND 97 105 {ECO:0000244|PDB:1J5Y}. FT TURN 106 108 {ECO:0000244|PDB:1J5Y}. FT STRAND 109 117 {ECO:0000244|PDB:1J5Y}. FT HELIX 120 132 {ECO:0000244|PDB:1J5Y}. FT HELIX 141 144 {ECO:0000244|PDB:1J5Y}. FT STRAND 145 154 {ECO:0000244|PDB:1J5Y}. FT HELIX 155 167 {ECO:0000244|PDB:1J5Y}. SQ SEQUENCE 175 AA; 19555 MW; 742C3C0DF51FE8A2 CRC64; MHMKTVRQER LKSIVRILER SKEPVSGAQL AEELSVSRQV IVQDIAYLRS LGYNIVATPR GYVLAGGKSG VSRLVAVKHA PEEIKEELLC VVRNGGRIVD VIVEHPVYGE IRGIIDVSSE EEVLKFVNLM EMAKTEPLLT LSGGVHLHTI EAPDEETMER IMRELKKKGF LIEEG // ID NPD_THEMA Reviewed; 246 AA. AC Q9WYW0; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 09-DEC-2015, entry version 105. DE RecName: Full=NAD-dependent protein deacetylase {ECO:0000255|HAMAP-Rule:MF_01968}; DE EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01968}; DE AltName: Full=Regulatory protein SIR2 homolog {ECO:0000255|HAMAP-Rule:MF_01968}; DE Short=Sir2Tm; GN Name=cobB {ECO:0000255|HAMAP-Rule:MF_01968}; Synonyms=sir2; GN OrderedLocusNames=TM_0490; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION. RX PubMed=17684016; DOI=10.1074/jbc.M704409200; RA Garrity J., Gardner J.G., Hawse W., Wolberger C., RA Escalante-Semerena J.C.; RT "N-lysine propionylation controls the activity of propionyl-CoA RT synthetase."; RL J. Biol. Chem. 282:30239-30245(2007). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH NICOTINAMIDE, RP ENZYME REGULATION, COFACTOR, AND MUTAGENESIS OF ASP-101. RX PubMed=15780941; DOI=10.1016/j.molcel.2005.02.022; RA Avalos J.L., Bever K.M., Wolberger C.; RT "Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) RT cosubstrate specificity of a Sir2 enzyme."; RL Mol. Cell 17:855-868(2005). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEX WITH PEPTIDE RP SUBSTRATES, COFACTOR, AND MUTAGENESIS OF ASN-165. RX PubMed=16768447; DOI=10.1021/bi0526332; RA Cosgrove M.S., Bever K., Avalos J.L., Muhammad S., Zhang X., RA Wolberger C.; RT "The structural basis of sirtuin substrate affinity."; RL Biochemistry 45:7511-7521(2006). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN TERNARY COMPLEX WITH NAD AND RP PEPTIDE SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND RP MUTAGENESIS OF HIS-116. RX PubMed=16905097; DOI=10.1016/j.str.2006.06.006; RA Hoff K.G., Avalos J.L., Sens K., Wolberger C.; RT "Insights into the sirtuin mechanism from ternary complexes containing RT NAD+ and acetylated peptide."; RL Structure 14:1231-1240(2006). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ANALOGS, AND RP MUTAGENESIS OF PHE-33. RX PubMed=18786399; DOI=10.1016/j.str.2008.05.015; RA Hawse W.F., Hoff K.G., Fatkins D.G., Daines A., Zubkova O.V., RA Schramm V.L., Zheng W., Wolberger C.; RT "Structural insights into intermediate steps in the Sir2 deacetylation RT reaction."; RL Structure 16:1368-1377(2008). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=21080423; DOI=10.1002/pro.544; RA Bheda P., Wang J.T., Escalante-Semerena J.C., Wolberger C.; RT "Structure of Sir2Tm bound to a propionylated peptide."; RL Protein Sci. 20:131-139(2011). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH PEPTIDE RP SUBSTRATES, FUNCTION, AND CHARACTERIZATION OF ADP-RIBOSYLATION RP ACTIVITY. RX PubMed=19801667; DOI=10.1074/jbc.M109.024521; RA Hawse W.F., Wolberger C.; RT "Structure-based mechanism of ADP-ribosylation by sirtuins."; RL J. Biol. Chem. 284:33654-33661(2009). CC -!- FUNCTION: NAD-dependent protein deacetylase which modulates the CC activities of several enzymes which are inactive in their CC acetylated form. Has also depropionylation activity in vitro. Also CC able to ADP-ribosylate peptide substrates with Arg or Lys in the CC +2 position. The role of this function in vivo is not clear. CC {ECO:0000255|HAMAP-Rule:MF_01968, ECO:0000269|PubMed:16905097, CC ECO:0000269|PubMed:17684016, ECO:0000269|PubMed:19801667}. CC -!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O- CC acetyl-ADP-ribose + a protein. {ECO:0000255|HAMAP-Rule:MF_01968, CC ECO:0000269|PubMed:16905097}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01968, CC ECO:0000269|PubMed:15780941, ECO:0000269|PubMed:16768447, CC ECO:0000269|PubMed:16905097}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01968, ECO:0000269|PubMed:15780941, CC ECO:0000269|PubMed:16768447, ECO:0000269|PubMed:16905097}; CC -!- ENZYME REGULATION: Non-competitively inhibited by nicotinamide but CC not by nicotinic acid. {ECO:0000269|PubMed:15780941}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01968}. CC -!- SIMILARITY: Belongs to the sirtuin family. Class U subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01968}. CC -!- SIMILARITY: Contains 1 deacetylase sirtuin-type domain. CC {ECO:0000255|HAMAP-Rule:MF_01968}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35575.1; -; Genomic_DNA. DR PIR; A72370; A72370. DR RefSeq; NP_228300.1; NC_000853.1. DR RefSeq; WP_010865133.1; NC_000853.1. DR PDB; 1YC5; X-ray; 1.40 A; A=1-246. DR PDB; 2H2D; X-ray; 1.70 A; A=1-246. DR PDB; 2H2F; X-ray; 2.20 A; A=1-246. DR PDB; 2H2G; X-ray; 1.63 A; A=1-246. DR PDB; 2H2H; X-ray; 2.20 A; A=1-246. DR PDB; 2H2I; X-ray; 1.80 A; A=1-246. DR PDB; 2H4F; X-ray; 2.00 A; A=1-246. DR PDB; 2H4H; X-ray; 1.99 A; A=1-246. DR PDB; 2H4J; X-ray; 2.10 A; A=1-246. DR PDB; 2H59; X-ray; 1.90 A; A/B=1-246. DR PDB; 3D4B; X-ray; 1.90 A; A=1-246. DR PDB; 3D81; X-ray; 2.50 A; A=1-246. DR PDB; 3JR3; X-ray; 1.50 A; A=1-246. DR PDB; 3PDH; X-ray; 1.80 A; A=1-246. DR PDB; 4BUZ; X-ray; 1.90 A; A=1-246. DR PDB; 4BV2; X-ray; 3.30 A; A/B=1-246. DR PDBsum; 1YC5; -. DR PDBsum; 2H2D; -. DR PDBsum; 2H2F; -. DR PDBsum; 2H2G; -. DR PDBsum; 2H2H; -. DR PDBsum; 2H2I; -. DR PDBsum; 2H4F; -. DR PDBsum; 2H4H; -. DR PDBsum; 2H4J; -. DR PDBsum; 2H59; -. DR PDBsum; 3D4B; -. DR PDBsum; 3D81; -. DR PDBsum; 3JR3; -. DR PDBsum; 3PDH; -. DR PDBsum; 4BUZ; -. DR PDBsum; 4BV2; -. DR ProteinModelPortal; Q9WYW0; -. DR SMR; Q9WYW0; 1-244. DR DIP; DIP-29141N; -. DR STRING; 243274.TM0490; -. DR ChEMBL; CHEMBL3217404; -. DR DNASU; 897531; -. DR EnsemblBacteria; AAD35575; AAD35575; TM_0490. DR GeneID; 897531; -. DR KEGG; tma:TM0490; -. DR PATRIC; 23935885; VBITheMar51294_0497. DR eggNOG; ENOG4105NDF; Bacteria. DR eggNOG; COG0846; LUCA. DR InParanoid; Q9WYW0; -. DR KO; K12410; -. DR OMA; VTEFHGN; -. DR OrthoDB; EOG6VQPX1; -. DR BioCyc; TMAR243274:GC6P-514-MONOMER; -. DR EvolutionaryTrace; Q9WYW0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-HAMAP. DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1600.10; -; 2. DR Gene3D; 3.40.50.1220; -; 3. DR HAMAP; MF_01968; Sirtuin_ClassU; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR003000; Sirtuin. DR InterPro; IPR026591; Sirtuin_cat_small_dom. DR InterPro; IPR028628; Sirtuin_class_U. DR InterPro; IPR026590; Ssirtuin_cat_dom. DR PANTHER; PTHR11085; PTHR11085; 1. DR Pfam; PF02146; SIR2; 1. DR SUPFAM; SSF52467; SSF52467; 1. DR PROSITE; PS50305; SIRTUIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; KW NAD; Reference proteome; Zinc. FT CHAIN 1 246 NAD-dependent protein deacetylase. FT /FTId=PRO_0000110362. FT DOMAIN 4 246 Deacetylase sirtuin-type. FT {ECO:0000255|HAMAP-Rule:MF_01968}. FT NP_BIND 21 40 NAD. FT NP_BIND 98 101 NAD. FT NP_BIND 188 190 NAD. FT NP_BIND 214 216 NAD. FT NP_BIND 231 232 NAD. FT ACT_SITE 116 116 Proton acceptor. {ECO:0000305}. FT METAL 124 124 Zinc. FT METAL 127 127 Zinc. FT METAL 148 148 Zinc. FT METAL 151 151 Zinc. FT MUTAGEN 33 33 F->A: Reduces kcat for NAD(+), greatly FT increases sensitivity to nicotinamide FT inhibition. FT {ECO:0000269|PubMed:18786399}. FT MUTAGEN 101 101 D->N: Alters cosubstrate specificity, FT decreases Km for NAD(+), enzyme unable to FT discriminate between NAD(+) and nicotinic FT acid adenine dinucleotide (NAAD). FT {ECO:0000269|PubMed:15780941}. FT MUTAGEN 116 116 H->A: 2-fold decrease in turnover and FT peptide affinity. FT {ECO:0000269|PubMed:16905097}. FT MUTAGEN 116 116 H->Y: 10-fold decrease in turnover and FT peptide affinity. FT {ECO:0000269|PubMed:16905097}. FT MUTAGEN 165 165 N->D: Increased affinity for substrate FT peptides with a lysine or arginine at FT position -1. FT {ECO:0000269|PubMed:16768447}. FT HELIX 4 12 {ECO:0000244|PDB:1YC5}. FT STRAND 14 20 {ECO:0000244|PDB:1YC5}. FT HELIX 22 24 {ECO:0000244|PDB:1YC5}. FT HELIX 26 28 {ECO:0000244|PDB:1YC5}. FT STRAND 33 35 {ECO:0000244|PDB:2H59}. FT HELIX 38 42 {ECO:0000244|PDB:2H2I}. FT TURN 45 48 {ECO:0000244|PDB:3JR3}. FT HELIX 50 55 {ECO:0000244|PDB:1YC5}. FT HELIX 57 67 {ECO:0000244|PDB:1YC5}. FT HELIX 69 73 {ECO:0000244|PDB:1YC5}. FT HELIX 78 88 {ECO:0000244|PDB:1YC5}. FT STRAND 93 97 {ECO:0000244|PDB:1YC5}. FT HELIX 103 106 {ECO:0000244|PDB:1YC5}. FT STRAND 112 114 {ECO:0000244|PDB:1YC5}. FT STRAND 117 124 {ECO:0000244|PDB:1YC5}. FT TURN 125 127 {ECO:0000244|PDB:1YC5}. FT STRAND 130 132 {ECO:0000244|PDB:1YC5}. FT HELIX 133 139 {ECO:0000244|PDB:1YC5}. FT TURN 140 142 {ECO:0000244|PDB:1YC5}. FT STRAND 143 145 {ECO:0000244|PDB:3D81}. FT TURN 149 151 {ECO:0000244|PDB:1YC5}. FT STRAND 154 159 {ECO:0000244|PDB:1YC5}. FT HELIX 168 180 {ECO:0000244|PDB:1YC5}. FT STRAND 182 188 {ECO:0000244|PDB:1YC5}. FT HELIX 196 198 {ECO:0000244|PDB:1YC5}. FT HELIX 199 206 {ECO:0000244|PDB:1YC5}. FT STRAND 209 213 {ECO:0000244|PDB:1YC5}. FT HELIX 221 223 {ECO:0000244|PDB:1YC5}. FT STRAND 225 228 {ECO:0000244|PDB:1YC5}. FT HELIX 232 243 {ECO:0000244|PDB:1YC5}. SQ SEQUENCE 246 AA; 27538 MW; 6BD2EF1B751C190D CRC64; MKMKEFLDLL NESRLTVTLT GAGISTPSGI PDFRGPNGIY KKYSQNVFDI DFFYSHPEEF YRFAKEGIFP MLQAKPNLAH VLLAKLEEKG LIEAVITQNI DRLHQRAGSK KVIELHGNVE EYYCVRCEKK YTVEDVIKKL ESSDVPLCDD CNSLIRPNIV FFGENLPQDA LREAIGLSSR ASLMIVLGSS LVVYPAAELP LITVRSGGKL VIVNLGETPF DDIATLKYNM DVVEFARRVM EEGGIS // ID NNR_THEMA Reviewed; 490 AA. AC Q9X024; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Bifunctional NAD(P)H-hydrate repair enzyme Nnr; DE AltName: Full=Nicotinamide nucleotide repair protein; DE Includes: DE RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase; DE EC=4.2.1.136; DE AltName: Full=ADP-dependent NAD(P)HX dehydratase; DE Includes: DE RecName: Full=NAD(P)H-hydrate epimerase; DE EC=5.1.99.6; DE AltName: Full=NAD(P)HX epimerase; GN Name=nnr; OrderedLocusNames=TM_0922; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS). RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of hypothetical protein (TM0922) from Thermotoga RT maritima at 2.27 A resolution."; RL Submitted (SEP-2005) to the PDB data bank. RN [3] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH POTASSIUM; RP ADP AND NAD(P)HX ANALOGS. RX PubMed=22940582; DOI=10.1016/j.str.2012.07.016; RA Shumilin I.A., Cymborowski M., Chertihin O., Jha K.N., Herr J.C., RA Lesley S.A., Joachimiak A., Minor W.; RT "Identification of unknown protein function using metabolite cocktail RT screening."; RL Structure 20:1715-1725(2012). CC -!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of CC the S- and R-forms of NAD(P)HX and the dehydration of the S-form CC of NAD(P)HX at the expense of ADP, which is converted to AMP. This CC allows the repair of both epimers of NAD(P)HX, a damaged form of CC NAD(P)H that is a result of enzymatic or heat-dependent hydration CC (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate + CC NADH. CC -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide adenine-dinucleotide phosphate = AMP + CC phosphate + NADPH. CC -!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy- CC 1,4,5,6-tetrahydronicotinamide-adenine dinucleotide. CC -!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6- CC beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide CC phosphate. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; CC Note=Binds 1 potassium ion per subunit. {ECO:0000250}; CC -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP CC family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 YjeF C-terminal domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 YjeF N-terminal domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36003.1; -; Genomic_DNA. DR PIR; C72317; C72317. DR RefSeq; NP_228730.1; NC_000853.1. DR RefSeq; WP_010865220.1; NC_000853.1. DR PDB; 2AX3; X-ray; 2.27 A; A=1-490. DR PDB; 3RRB; X-ray; 2.40 A; A=1-490. DR PDB; 3RRE; X-ray; 2.15 A; A=1-490. DR PDB; 3RRF; X-ray; 2.10 A; A=1-490. DR PDB; 3RRJ; X-ray; 2.50 A; A=1-490. DR PDB; 3RS8; X-ray; 2.10 A; A=1-490. DR PDB; 3RS9; X-ray; 2.10 A; A=1-490. DR PDB; 3RSF; X-ray; 2.30 A; A=1-490. DR PDB; 3RSG; X-ray; 2.10 A; A=1-490. DR PDB; 3RSQ; X-ray; 2.05 A; A=1-490. DR PDB; 3RSS; X-ray; 1.95 A; A=1-490. DR PDB; 3RT7; X-ray; 2.10 A; A=1-490. DR PDB; 3RT9; X-ray; 1.95 A; A=1-490. DR PDB; 3RTA; X-ray; 1.95 A; A=1-490. DR PDB; 3RTB; X-ray; 2.10 A; A=1-490. DR PDB; 3RTC; X-ray; 2.10 A; A=1-490. DR PDB; 3RTD; X-ray; 2.30 A; A=1-490. DR PDB; 3RTE; X-ray; 2.10 A; A=1-490. DR PDB; 3RTG; X-ray; 2.05 A; A=1-490. DR PDB; 3RU2; X-ray; 2.20 A; A=1-490. DR PDB; 3RU3; X-ray; 2.60 A; A=1-490. DR PDBsum; 2AX3; -. DR PDBsum; 3RRB; -. DR PDBsum; 3RRE; -. DR PDBsum; 3RRF; -. DR PDBsum; 3RRJ; -. DR PDBsum; 3RS8; -. DR PDBsum; 3RS9; -. DR PDBsum; 3RSF; -. DR PDBsum; 3RSG; -. DR PDBsum; 3RSQ; -. DR PDBsum; 3RSS; -. DR PDBsum; 3RT7; -. DR PDBsum; 3RT9; -. DR PDBsum; 3RTA; -. DR PDBsum; 3RTB; -. DR PDBsum; 3RTC; -. DR PDBsum; 3RTD; -. DR PDBsum; 3RTE; -. DR PDBsum; 3RTG; -. DR PDBsum; 3RU2; -. DR PDBsum; 3RU3; -. DR ProteinModelPortal; Q9X024; -. DR SMR; Q9X024; 1-489. DR DIP; DIP-59950N; -. DR STRING; 243274.TM0922; -. DR DNASU; 898596; -. DR EnsemblBacteria; AAD36003; AAD36003; TM_0922. DR GeneID; 898596; -. DR KEGG; tma:TM0922; -. DR PATRIC; 23936775; VBITheMar51294_0936. DR eggNOG; ENOG4105DR1; Bacteria. DR eggNOG; COG0062; LUCA. DR eggNOG; COG0063; LUCA. DR InParanoid; Q9X024; -. DR KO; K17758; -. DR KO; K17759; -. DR OMA; KGDHGRV; -. DR OrthoDB; EOG6C018D; -. DR BioCyc; TMAR243274:GC6P-952-MONOMER; -. DR EvolutionaryTrace; Q9X024; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.20; -; 1. DR Gene3D; 3.40.50.10260; -; 1. DR HAMAP; MF_01965; NADHX_dehydratase; 1. DR HAMAP; MF_01966; NADHX_epimerase; 1. DR InterPro; IPR017953; Carbohydrate_kinase_pred_CS. DR InterPro; IPR000631; CARKD. DR InterPro; IPR030677; Nnr. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR004443; YjeF_N_dom. DR Pfam; PF01256; Carb_kinase; 1. DR Pfam; PF03853; YjeF_N; 1. DR PIRSF; PIRSF017184; Nnr; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR SUPFAM; SSF64153; SSF64153; 1. DR TIGRFAMs; TIGR00196; yjeF_cterm; 1. DR TIGRFAMs; TIGR00197; yjeF_nterm; 1. DR PROSITE; PS01049; YJEF_C_1; 1. DR PROSITE; PS01050; YJEF_C_2; 1. DR PROSITE; PS51383; YJEF_C_3; 1. DR PROSITE; PS51385; YJEF_N; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Isomerase; Lyase; KW Metal-binding; Multifunctional enzyme; NAD; NADP; Nucleotide-binding; KW Potassium; Reference proteome. FT CHAIN 1 490 Bifunctional NAD(P)H-hydrate repair FT enzyme Nnr. FT /FTId=PRO_0000416413. FT DOMAIN 1 204 YjeF N-terminal. FT DOMAIN 212 488 YjeF C-terminal. FT NP_BIND 402 406 ADP. FT NP_BIND 421 430 ADP. FT REGION 1 204 NAD(P)H-hydrate epimerase. {ECO:0000250}. FT REGION 51 55 NAD(P)HX (for epimerase activity). FT REGION 118 124 NAD(P)HX (for epimerase activity). FT REGION 212 490 ADP-dependent (S)-NAD(P)H-hydrate FT dehydratase. {ECO:0000250}. FT REGION 366 372 NAD(P)HX (for dehydratase activity). FT METAL 52 52 Potassium. FT METAL 114 114 Potassium. FT METAL 150 150 Potassium. FT BINDING 129 129 NAD(P)HX (for epimerase activity). FT BINDING 147 147 NAD(P)HX (for epimerase activity). FT BINDING 317 317 NAD(P)HX (for dehydratase activity); via FT amide nitrogen. FT BINDING 431 431 NAD(P)HX (for dehydratase activity). FT HELIX 2 10 {ECO:0000244|PDB:3RTA}. FT HELIX 16 35 {ECO:0000244|PDB:3RTA}. FT HELIX 38 40 {ECO:0000244|PDB:3RTB}. FT STRAND 42 47 {ECO:0000244|PDB:3RTA}. FT HELIX 51 63 {ECO:0000244|PDB:3RTA}. FT TURN 64 66 {ECO:0000244|PDB:3RTA}. FT STRAND 67 74 {ECO:0000244|PDB:3RTA}. FT HELIX 81 92 {ECO:0000244|PDB:3RTA}. FT STRAND 97 100 {ECO:0000244|PDB:3RTA}. FT HELIX 103 108 {ECO:0000244|PDB:3RTA}. FT STRAND 110 116 {ECO:0000244|PDB:3RTA}. FT HELIX 127 138 {ECO:0000244|PDB:3RTA}. FT STRAND 142 148 {ECO:0000244|PDB:3RTA}. FT TURN 154 156 {ECO:0000244|PDB:3RTA}. FT STRAND 159 161 {ECO:0000244|PDB:3RTA}. FT STRAND 167 174 {ECO:0000244|PDB:3RTA}. FT HELIX 177 180 {ECO:0000244|PDB:3RTA}. FT HELIX 184 188 {ECO:0000244|PDB:3RTA}. FT STRAND 190 194 {ECO:0000244|PDB:3RTA}. FT HELIX 200 203 {ECO:0000244|PDB:3RTA}. FT STRAND 207 210 {ECO:0000244|PDB:3RTA}. FT HELIX 213 219 {ECO:0000244|PDB:3RTA}. FT HELIX 229 232 {ECO:0000244|PDB:3RTA}. FT STRAND 234 238 {ECO:0000244|PDB:3RTA}. FT HELIX 247 257 {ECO:0000244|PDB:3RTA}. FT STRAND 261 268 {ECO:0000244|PDB:3RTA}. FT TURN 269 272 {ECO:0000244|PDB:3RTA}. FT HELIX 273 278 {ECO:0000244|PDB:3RTA}. FT STRAND 282 287 {ECO:0000244|PDB:3RTA}. FT STRAND 290 293 {ECO:0000244|PDB:3RTA}. FT HELIX 296 298 {ECO:0000244|PDB:3RTA}. FT HELIX 299 306 {ECO:0000244|PDB:3RTA}. FT STRAND 310 314 {ECO:0000244|PDB:3RTA}. FT HELIX 322 334 {ECO:0000244|PDB:3RTA}. FT STRAND 339 341 {ECO:0000244|PDB:3RTA}. FT HELIX 343 347 {ECO:0000244|PDB:3RTA}. FT HELIX 351 356 {ECO:0000244|PDB:3RTA}. FT STRAND 361 363 {ECO:0000244|PDB:3RTA}. FT HELIX 367 374 {ECO:0000244|PDB:3RTA}. FT HELIX 378 381 {ECO:0000244|PDB:3RTA}. FT HELIX 385 395 {ECO:0000244|PDB:3RTA}. FT STRAND 397 401 {ECO:0000244|PDB:3RTA}. FT STRAND 403 409 {ECO:0000244|PDB:3RTA}. FT STRAND 414 417 {ECO:0000244|PDB:3RTA}. FT HELIX 422 424 {ECO:0000244|PDB:3RTA}. FT HELIX 429 442 {ECO:0000244|PDB:3RTA}. FT HELIX 447 463 {ECO:0000244|PDB:3RTA}. FT HELIX 469 471 {ECO:0000244|PDB:3RTA}. FT HELIX 474 488 {ECO:0000244|PDB:3RTA}. SQ SEQUENCE 490 AA; 53004 MW; 580917C98F8BE2FC CRC64; MKEIDELTIK EYGVDSRILM ERAGISVVLA MEEELGNLSD YRFLVLCGGG NNGGDGFVVA RNLLGVVKDV LVVFLGKKKT PDCEYNYGLY KKFGGKVVEQ FEPSILNEFD VVVDAIFGTG LRGEITGEYA EIINLVNKSG KVVVSVDVPS GIDSNTGKVL RTAVKADLTV TFGVPKIGHI LFPGRDLTGK LKVANIGHPV HLINSINRYV ITREMVRSLL PERPRDSHKG TYGKVLIIAG SRLYSGAPVL SGMGSLKVGT GLVKLAVPFP QNLIATSRFP ELISVPIDTE KGFFSLQNLQ ECLELSKDVD VVAIGPGLGN NEHVREFVNE FLKTLEKPAV IDADAINVLD TSVLKERKSP AVLTPHPGEM ARLVKKTVGD VKYNYELAEE FAKENDCVLV LKSATTIVTD GEKTLFNITG NTGLSKGGSG DVLTGMIAGF IAQGLSPLEA STVSVYLHGF AAELFEQDER GLTASELLRL IPEAIRRLKE // ID NORM_THEMA Reviewed; 464 AA. AC Q9WZS2; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Probable multidrug resistance protein NorM; DE AltName: Full=Multidrug-efflux transporter; GN Name=norM; OrderedLocusNames=TM_0815; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Multidrug efflux pump. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) CC (TC 2.A.66.1) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35897.1; -; Genomic_DNA. DR PIR; H72331; H72331. DR RefSeq; NP_228624.1; NC_000853.1. DR RefSeq; WP_010865209.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZS2; -. DR STRING; 243274.TM0815; -. DR TCDB; 2.A.66.1.28; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily. DR DNASU; 898483; -. DR EnsemblBacteria; AAD35897; AAD35897; TM_0815. DR GeneID; 898483; -. DR KEGG; tma:TM0815; -. DR KEGG; tmi:THEMA_00575; -. DR KEGG; tmw:THMA_0834; -. DR PATRIC; 23936550; VBITheMar51294_0827. DR eggNOG; ENOG4105UQX; Bacteria. DR eggNOG; COG0534; LUCA. DR InParanoid; Q9WZS2; -. DR KO; K03327; -. DR OMA; NILMNVI; -. DR OrthoDB; EOG6FV84C; -. DR BioCyc; TMAR243274:GC6P-842-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW. DR GO; GO:0015238; F:drug transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0006855; P:drug transmembrane transport; IBA:GO_Central. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR InterPro; IPR002528; MATE_fam. DR Pfam; PF01554; MatE; 2. DR PIRSF; PIRSF006603; DinF; 1. DR TIGRFAMs; TIGR00797; matE; 1. PE 3: Inferred from homology; KW Antiport; Cell membrane; Complete proteome; Ion transport; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 464 Probable multidrug resistance protein FT NorM. FT /FTId=PRO_0000164243. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TRANSMEM 64 84 Helical. {ECO:0000255}. FT TRANSMEM 104 124 Helical. {ECO:0000255}. FT TRANSMEM 142 162 Helical. {ECO:0000255}. FT TRANSMEM 172 192 Helical. {ECO:0000255}. FT TRANSMEM 204 224 Helical. {ECO:0000255}. FT TRANSMEM 258 278 Helical. {ECO:0000255}. FT TRANSMEM 288 308 Helical. {ECO:0000255}. FT TRANSMEM 326 346 Helical. {ECO:0000255}. FT TRANSMEM 358 378 Helical. {ECO:0000255}. FT TRANSMEM 384 404 Helical. {ECO:0000255}. FT TRANSMEM 410 430 Helical. {ECO:0000255}. SQ SEQUENCE 464 AA; 51054 MW; 65DA15D7DE038461 CRC64; MRYSLFKNYL PKEEVPEIRK ELIKLALPAM GENVLQMLFG MADTAFLGHY SWKAMSGVGL SNQVFWVVQV VLIAASMGAT VTIANAIGAG NRKAVRSLAW NSVFLAIFTG VILTALTPLS DVLINIFPNL EGEIESSAKE YLKVILSGSM GFSIMAVFSA MLRGAGDTRT PMIVTGLTNF LNIFLDYAMI FGKFGFPEMG VRGAAVATIL SRFVGAGILT YVIFKREEFQ LRKGLVPPKW SSQKEILRVG FPTAIENFVF STGVLMFANI LLIAGAEAYA GHRIGINVES LSFMPAFGIS VAITTLVGRY NGMGNKEHVL GVIRQGWILS LLFQVTVGII IFLFPEPLIR IFTSDPQIIE ISKLPVKIIG LFQFFLAIDS TMNGALRGTG NTLPPMIITF ISIWTARLPV AFVMVKYFQL GLLGAWIGMI ADIIFRSTLK LLFFLSGKWE KRAVLTRERV KELG // ID NRDR_THEMA Reviewed; 156 AA. AC Q9X233; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Transcriptional repressor NrdR {ECO:0000255|HAMAP-Rule:MF_00440}; GN Name=nrdR {ECO:0000255|HAMAP-Rule:MF_00440}; GN OrderedLocusNames=TM_1707; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Negatively regulates transcription of bacterial CC ribonucleotide reductase nrd genes and operons by binding to NrdR- CC boxes. {ECO:0000255|HAMAP-Rule:MF_00440}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00440}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00440}; CC -!- SIMILARITY: Belongs to the NrdR family. {ECO:0000255|HAMAP- CC Rule:MF_00440}. CC -!- SIMILARITY: Contains 1 ATP-cone domain. {ECO:0000255|HAMAP- CC Rule:MF_00440}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36774.1; -; Genomic_DNA. DR PIR; E72221; E72221. DR RefSeq; NP_229507.1; NC_000853.1. DR RefSeq; WP_010865386.1; NC_000853.1. DR STRING; 243274.TM1707; -. DR EnsemblBacteria; AAD36774; AAD36774; TM_1707. DR GeneID; 897885; -. DR KEGG; tma:TM1707; -. DR PATRIC; 23938388; VBITheMar51294_1724. DR eggNOG; ENOG4108Z11; Bacteria. DR eggNOG; COG1327; LUCA. DR InParanoid; Q9X233; -. DR KO; K07738; -. DR OMA; RFTTYET; -. DR OrthoDB; EOG6XM7J6; -. DR BioCyc; TMAR243274:GC6P-1755-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR HAMAP; MF_00440; NrdR; 1. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR003796; RNR_NrdR-like. DR Pfam; PF03477; ATP-cone; 1. DR TIGRFAMs; TIGR00244; TIGR00244; 1. DR PROSITE; PS51161; ATP_CONE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Metal-binding; KW Nucleotide-binding; Reference proteome; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 156 Transcriptional repressor NrdR. FT /FTId=PRO_0000182372. FT DOMAIN 49 139 ATP-cone. {ECO:0000255|HAMAP- FT Rule:MF_00440}. FT ZN_FING 3 34 {ECO:0000255|HAMAP-Rule:MF_00440}. SQ SEQUENCE 156 AA; 18466 MW; 117A346D81E5D2ED CRC64; MKCPFCGSMD TRVLDSRPTL DGTAIRRRRE CSSCGKRFTT YERYEEAPVL VVKKDGRREK FDREKIKNGM IKACEKRPVT YEQIEEAVNR ICLKLREEGS FEVETKRIGE LVMEELKKLD QVAYVRLASV YRDFREVDQF LEIVKELKRE KEGEEQ // ID NTPA_THEMA Reviewed; 196 AA. AC Q9WY06; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE EC=3.6.1.19 {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE Short=NTPase {ECO:0000255|HAMAP-Rule:MF_01405}; GN OrderedLocusNames=TM_0159; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine CC nucleotides such as XTP and ITP/dITP to their respective CC monophosphate derivatives. Might exclude non-canonical purines CC from DNA precursor pool, thus preventing their incorporation into CC DNA and avoiding chromosomal lesions. {ECO:0000255|HAMAP- CC Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP- CC Rule:MF_01405}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35252.1; -; Genomic_DNA. DR PIR; E72410; E72410. DR RefSeq; NP_227974.1; NC_000853.1. DR RefSeq; WP_004082779.1; NZ_CP011107.1. DR PDB; 1VP2; X-ray; 1.78 A; A/B=1-196. DR PDB; 3S86; X-ray; 2.15 A; A/B/C/D=1-196. DR PDBsum; 1VP2; -. DR PDBsum; 3S86; -. DR ProteinModelPortal; Q9WY06; -. DR SMR; Q9WY06; 3-191. DR STRING; 243274.TM0159; -. DR EnsemblBacteria; AAD35252; AAD35252; TM_0159. DR GeneID; 896997; -. DR KEGG; tma:TM0159; -. DR PATRIC; 23935164; VBITheMar51294_0159. DR eggNOG; ENOG4108V82; Bacteria. DR eggNOG; COG0127; LUCA. DR InParanoid; Q9WY06; -. DR KO; K02428; -. DR OMA; CEGLWHG; -. DR OrthoDB; EOG65QWHX; -. DR EvolutionaryTrace; Q9WY06; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro. DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR020922; NTPase. DR PANTHER; PTHR11067; PTHR11067; 1. DR Pfam; PF01725; Ham1p_like; 1. DR SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00042; TIGR00042; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Magnesium; Manganese; KW Metal-binding; Nucleotide metabolism; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 196 Non-canonical purine NTP pyrophosphatase. FT /FTId=PRO_0000178252. FT REGION 10 15 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT REGION 68 69 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT METAL 68 68 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01405}. FT BINDING 151 151 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT BINDING 176 176 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT STRAND 4 9 {ECO:0000244|PDB:1VP2}. FT HELIX 13 20 {ECO:0000244|PDB:1VP2}. FT STRAND 27 31 {ECO:0000244|PDB:1VP2}. FT HELIX 45 60 {ECO:0000244|PDB:1VP2}. FT STRAND 64 73 {ECO:0000244|PDB:1VP2}. FT HELIX 74 76 {ECO:0000244|PDB:1VP2}. FT HELIX 81 83 {ECO:0000244|PDB:1VP2}. FT TURN 84 90 {ECO:0000244|PDB:1VP2}. FT HELIX 93 103 {ECO:0000244|PDB:1VP2}. FT TURN 104 106 {ECO:0000244|PDB:1VP2}. FT STRAND 110 121 {ECO:0000244|PDB:1VP2}. FT TURN 122 125 {ECO:0000244|PDB:1VP2}. FT STRAND 126 138 {ECO:0000244|PDB:1VP2}. FT HELIX 151 153 {ECO:0000244|PDB:1VP2}. FT STRAND 154 156 {ECO:0000244|PDB:1VP2}. FT TURN 163 165 {ECO:0000244|PDB:1VP2}. FT HELIX 167 169 {ECO:0000244|PDB:1VP2}. FT HELIX 170 173 {ECO:0000244|PDB:1VP2}. FT HELIX 175 190 {ECO:0000244|PDB:1VP2}. SQ SEQUENCE 196 AA; 22338 MW; 6C6E4D11901F38A8 CRC64; MKKLTVYLAT TNPHKVEEIK MIAPEWMEIL PSPEKIEVVE DGETFLENSV KKAVVYGKKL KHPVMADDSG LVIYSLGGFP GVMSARFMEE HSYKEKMRTI LKMLEGKDRR AAFVCSATFF DPVENTLISV EDRVEGRIAN EIRGTGGFGY DPFFIPDGYD KTFGEIPHLK EKISHRSKAF RKLFSVLEKI LESENR // ID NTPTH_THEMA Reviewed; 174 AA. AC Q9WXP3; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Nucleoside-triphosphatase THEP1 {ECO:0000255|HAMAP-Rule:MF_00796}; DE Short=NTPase THEP1 {ECO:0000255|HAMAP-Rule:MF_00796}; DE EC=3.6.1.15 {ECO:0000255|HAMAP-Rule:MF_00796}; DE AltName: Full=Nucleoside triphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00796}; GN OrderedLocusNames=TM_0036; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CC CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower CC efficiency. {ECO:0000255|HAMAP-Rule:MF_00796}. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00796}. CC -!- SIMILARITY: Belongs to the THEP1 NTPase family. CC {ECO:0000255|HAMAP-Rule:MF_00796}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35130.1; -; Genomic_DNA. DR PIR; A72425; A72425. DR RefSeq; NP_227852.1; NC_000853.1. DR RefSeq; WP_004082498.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXP3; -. DR STRING; 243274.TM0036; -. DR EnsemblBacteria; AAD35130; AAD35130; TM_0036. DR GeneID; 896857; -. DR KEGG; tma:TM0036; -. DR PATRIC; 23934912; VBITheMar51294_0034. DR eggNOG; ENOG4105Q33; Bacteria. DR eggNOG; COG1618; LUCA. DR InParanoid; Q9WXP3; -. DR KO; K06928; -. DR OMA; VHKICSA; -. DR OrthoDB; EOG6N0HJM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 4. DR HAMAP; MF_00796; NTPase_1; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR004948; Nuc-triphosphatase_THEP1. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF03266; NTPase_1; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Hydrolase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 174 Nucleoside-triphosphatase THEP1. FT /FTId=PRO_0000146710. FT NP_BIND 7 14 ATP. {ECO:0000255|HAMAP-Rule:MF_00796}. FT NP_BIND 94 101 ATP. {ECO:0000255|HAMAP-Rule:MF_00796}. SQ SEQUENCE 174 AA; 20034 MW; A739CCA34DF59B52 CRC64; MKILITGRPG VGKTTLIKKL SRLLQNAGGF YTEEMREGEK RIGFKIITLD GEEGILARTD LPSPYRVGKY YVNLKDLEEI GVRSLERAFQ EKDLIIVDEI GKMELLSRKF REVVEKIFDS EKDVIATIKK SSDPFVEKIK NRNDVVIFEL NEKNRNSLLN EILSVLKFNR GEKQ // ID NUSB_THEMA Reviewed; 142 AA. AC Q9X286; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=N utilization substance protein B homolog; DE Short=Protein NusB; GN Name=nusB; OrderedLocusNames=TM_1765; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in the transcription termination process. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NusB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36829.1; -; Genomic_DNA. DR PIR; D72212; D72212. DR RefSeq; NP_229562.1; NC_000853.1. DR RefSeq; WP_004082311.1; NZ_CP011107.1. DR PDB; 1TZT; X-ray; 1.55 A; A/B=1-142. DR PDB; 1TZU; X-ray; 1.85 A; A=1-142. DR PDB; 1TZV; X-ray; 1.35 A; A=1-142. DR PDB; 1TZW; X-ray; 1.60 A; A=1-142. DR PDB; 1TZX; X-ray; 1.72 A; A/B=1-142. DR PDBsum; 1TZT; -. DR PDBsum; 1TZU; -. DR PDBsum; 1TZV; -. DR PDBsum; 1TZW; -. DR PDBsum; 1TZX; -. DR ProteinModelPortal; Q9X286; -. DR SMR; Q9X286; 1-142. DR STRING; 243274.TM1765; -. DR EnsemblBacteria; AAD36829; AAD36829; TM_1765. DR GeneID; 897855; -. DR KEGG; tma:TM1765; -. DR PATRIC; 23938510; VBITheMar51294_1784. DR eggNOG; ENOG4105M7K; Bacteria. DR eggNOG; COG0781; LUCA. DR InParanoid; Q9X286; -. DR KO; K03625; -. DR OMA; GVIQNQQ; -. DR OrthoDB; EOG6RJV9B; -. DR EvolutionaryTrace; Q9X286; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.940.10; -; 1. DR HAMAP; MF_00073; NusB; 1. DR InterPro; IPR011605; NusB_fam. DR InterPro; IPR006027; NusB_RsmB_TIM44. DR PANTHER; PTHR11078; PTHR11078; 1. DR Pfam; PF01029; NusB; 1. DR SUPFAM; SSF48013; SSF48013; 1. DR TIGRFAMs; TIGR01951; nusB; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; RNA-binding; KW Transcription; Transcription regulation; Transcription termination. FT CHAIN 1 142 N utilization substance protein B FT homolog. FT /FTId=PRO_0000176599. FT HELIX 5 19 {ECO:0000244|PDB:1TZV}. FT HELIX 27 34 {ECO:0000244|PDB:1TZV}. FT HELIX 41 56 {ECO:0000244|PDB:1TZV}. FT HELIX 58 66 {ECO:0000244|PDB:1TZV}. FT STRAND 70 72 {ECO:0000244|PDB:1TZV}. FT HELIX 74 76 {ECO:0000244|PDB:1TZV}. FT HELIX 79 94 {ECO:0000244|PDB:1TZV}. FT HELIX 100 114 {ECO:0000244|PDB:1TZV}. FT HELIX 117 134 {ECO:0000244|PDB:1TZV}. FT HELIX 137 139 {ECO:0000244|PDB:1TZV}. SQ SEQUENCE 142 AA; 16974 MW; 54C75FC72D2BEE0F CRC64; MKTPRRRMRL AVFKALFQHE FRRDEDLEQI LEEILDETYD KKAKEDARRY IRGIKENLSM IDDLISRYLE KWSLNRLSVV DRNVLRLATY ELLFEKDIPI EVTIDEAIEI AKRYGTENSG KFVNGILDRI AKEHAPKEKF EL // ID NUSG_THEMA Reviewed; 353 AA. AC P29397; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 11-MAY-2016, entry version 117. DE RecName: Full=Transcription termination/antitermination protein NusG {ECO:0000255|HAMAP-Rule:MF_00948}; GN Name=nusG {ECO:0000255|HAMAP-Rule:MF_00948}; GN OrderedLocusNames=TM_0453; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1429627; RA Liao D., Dennis P.P.; RT "The organization and expression of essential transcription RT translation component genes in the extremely thermophilic eubacterium RT Thermotoga maritima."; RL J. Biol. Chem. 267:22787-22797(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-352. RA Stegmann C.M., Mandal A., Schweimer C., Burmann B., Roesch P., RA Wahl M.C.; RT "Crystal structure of the antitermination factor Nusg from Thermotoga RT maritima."; RL Submitted (JUN-2010) to the PDB data bank. RN [4] RP STRUCTURE BY NMR, ENZYME REGULATION, AND DOMAIN. RX PubMed=23415559; DOI=10.1016/j.str.2012.12.015; RA Drogemuller J., Stegmann C.M., Mandal A., Steiner T., Burmann B.M., RA Gottesman M.E., Wohrl B.M., Rosch P., Wahl M.C., Schweimer K.; RT "An autoinhibited state in the structure of Thermotoga maritima RT NusG."; RL Structure 21:365-375(2013). CC -!- FUNCTION: Participates in transcription elongation, termination CC and antitermination. {ECO:0000255|HAMAP-Rule:MF_00948}. CC -!- ENZYME REGULATION: Regulated by autoinhibition via interaction of CC the N-terminal and the C-terminal domains. Autoinhibition may CC prevent NusG from interacting prematurely with other components of CC the transcription complex or non-specific interactions with other CC cellular components. {ECO:0000269|PubMed:23415559}. CC -!- DOMAIN: The N-terminal domain interacts with RNAP and the C- CC terminal domain binds either to Rho or to RpsJ (NusE). Contains an CC additional, species-specific domain inserted into the N-terminal CC domain. The N-terminal and C-terminal domains can interact and CC form a closed conformation. {ECO:0000269|PubMed:23415559}. CC -!- SIMILARITY: Belongs to the NusG family. {ECO:0000255|HAMAP- CC Rule:MF_00948}. CC -!- SIMILARITY: Contains 1 KOW domain. {ECO:0000255|HAMAP- CC Rule:MF_00948}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35536.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11839; CAA77858.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35536.1; ALT_INIT; Genomic_DNA. DR PIR; F72375; F72375. DR RefSeq; NP_228263.1; NC_000853.1. DR RefSeq; WP_004081513.1; NZ_CP011107.1. DR RefSeq; WP_010865124.1; NC_000853.1. DR PDB; 2LQ8; NMR; -; A=1-41, A=230-300. DR PDB; 2XHA; X-ray; 1.91 A; A/B=41-233. DR PDB; 2XHC; X-ray; 2.45 A; A=1-352. DR PDBsum; 2LQ8; -. DR PDBsum; 2XHA; -. DR PDBsum; 2XHC; -. DR ProteinModelPortal; P29397; -. DR STRING; 243274.TM0453; -. DR EnsemblBacteria; AAD35536; AAD35536; TM_0453. DR GeneID; 897482; -. DR KEGG; tma:TM0453; -. DR PATRIC; 23935801; VBITheMar51294_0459. DR eggNOG; ENOG4105E5V; Bacteria. DR eggNOG; COG0250; LUCA. DR InParanoid; P29397; -. DR KO; K02601; -. DR OMA; MIMNDEF; -. DR OrthoDB; EOG6FFS95; -. DR BioCyc; TMAR243274:GC6P-473-MONOMER; -. DR EvolutionaryTrace; P29397; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0006354; P:DNA-templated transcription, elongation; IEA:UniProtKB-HAMAP. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central. DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 3.30.70.940; -; 2. DR HAMAP; MF_00948; NusG; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR006645; NGN_dom. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR001062; Transcrpt_antiterm_NusG. DR InterPro; IPR015869; Transcrpt_antiterm_NusG_bac_CS. DR InterPro; IPR008991; Translation_prot_SH3-like. DR Pfam; PF00467; KOW; 1. DR Pfam; PF02357; NusG; 2. DR PRINTS; PR00338; NUSGTNSCPFCT. DR SMART; SM00739; KOW; 1. DR SMART; SM00738; NGN; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR SUPFAM; SSF82679; SSF82679; 2. DR TIGRFAMs; TIGR00922; nusG; 1. DR PROSITE; PS01014; NUSG; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; Transcription; KW Transcription antitermination; Transcription regulation; KW Transcription termination. FT CHAIN 1 353 Transcription termination/antitermination FT protein NusG. FT /FTId=PRO_0000113965. FT DOMAIN 301 335 KOW. {ECO:0000255|HAMAP-Rule:MF_00948}. FT STRAND 4 9 {ECO:0000244|PDB:2XHC}. FT HELIX 15 29 {ECO:0000244|PDB:2XHC}. FT STRAND 33 39 {ECO:0000244|PDB:2XHC}. FT STRAND 42 46 {ECO:0000244|PDB:2XHC}. FT STRAND 52 57 {ECO:0000244|PDB:2XHA}. FT STRAND 62 64 {ECO:0000244|PDB:2XHA}. FT STRAND 76 80 {ECO:0000244|PDB:2XHA}. FT STRAND 89 103 {ECO:0000244|PDB:2XHA}. FT STRAND 110 116 {ECO:0000244|PDB:2XHA}. FT HELIX 117 119 {ECO:0000244|PDB:2XHA}. FT STRAND 135 138 {ECO:0000244|PDB:2XHA}. FT STRAND 147 163 {ECO:0000244|PDB:2XHA}. FT STRAND 169 175 {ECO:0000244|PDB:2XHA}. FT HELIX 176 178 {ECO:0000244|PDB:2XHA}. FT TURN 181 183 {ECO:0000244|PDB:2XHA}. FT STRAND 195 197 {ECO:0000244|PDB:2XHA}. FT STRAND 200 203 {ECO:0000244|PDB:2XHA}. FT STRAND 208 214 {ECO:0000244|PDB:2XHA}. FT STRAND 219 224 {ECO:0000244|PDB:2XHA}. FT STRAND 226 232 {ECO:0000244|PDB:2XHC}. FT STRAND 235 240 {ECO:0000244|PDB:2XHC}. FT HELIX 244 251 {ECO:0000244|PDB:2XHC}. FT STRAND 262 265 {ECO:0000244|PDB:2XHC}. FT HELIX 271 280 {ECO:0000244|PDB:2XHC}. FT STRAND 304 307 {ECO:0000244|PDB:2XHC}. FT TURN 311 314 {ECO:0000244|PDB:2XHC}. FT STRAND 316 323 {ECO:0000244|PDB:2XHC}. FT TURN 324 327 {ECO:0000244|PDB:2XHC}. FT STRAND 328 335 {ECO:0000244|PDB:2XHC}. FT STRAND 338 345 {ECO:0000244|PDB:2XHC}. FT HELIX 346 348 {ECO:0000244|PDB:2XHC}. SQ SEQUENCE 353 AA; 40327 MW; 98DCB44B2E2CABB5 CRC64; MKKKWYIVLT MSGYEEKVKE NIEKKVEATG IKNLVGRIVI PEEVVLDATS PSERLILSPK AKLHVNNGKD VNKGDLIAEE PPIYARRSGV IVDVKNVRKI VVETIDRKYT KTYYIPESAG IEPGLRVGTK VKQGLPLSKN EEYICELDGK IVEIERMKKV VVQTPDGEQD VYYIPLDVFD RDRIKKGKEV KQGEMLAEAR KFFAKVSGRV EVVDYSTRKE IRIYKTKRRK LFPGYVFVEM IMNDEAYNFV RSVPYVMGFV SSGGQPVPVK DREMRPILRL AGLEEYEEKK KPVKVELGFK VGDMVKIISG PFEDFAGVIK EIDPERQELK VNVTIFGRET PVVLHVSEVE KIE // ID OBG_THEMA Reviewed; 435 AA. AC Q9WXV3; DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454}; DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454}; DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454}; GN Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=TM_0098; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: An essential GTPase which binds GTP, GDP and possibly CC (p)ppGpp with moderate affinity, with high nucleotide exchange CC rates and a fairly low GTP hydrolysis rate. Plays a role in CC control of the cell cycle, stress response, ribosome biogenesis CC and in those bacteria that undergo differentiation, in CC morphogenesis control. {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01454}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- SIMILARITY: Contains 1 OBG-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|HAMAP-Rule:MF_01454}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35192.1; -; Genomic_DNA. DR PIR; B72418; B72418. DR RefSeq; NP_227914.1; NC_000853.1. DR RefSeq; WP_004082646.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXV3; -. DR SMR; Q9WXV3; 8-338. DR STRING; 243274.TM0098; -. DR DNASU; 896925; -. DR EnsemblBacteria; AAD35192; AAD35192; TM_0098. DR GeneID; 896925; -. DR KEGG; tma:TM0098; -. DR PATRIC; 23935036; VBITheMar51294_0096. DR eggNOG; ENOG4105C9R; Bacteria. DR eggNOG; COG0536; LUCA. DR InParanoid; Q9WXV3; -. DR KO; K03979; -. DR OMA; SKNQHGR; -. DR OrthoDB; EOG6H1Q1M; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-HAMAP. DR Gene3D; 2.70.210.12; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01454; GTPase_Obg; 1. DR InterPro; IPR031167; G_OBG. DR InterPro; IPR014100; GTP-bd_Obg/CgtA. DR InterPro; IPR015349; GTP-bd_prot_GTP1/OBG_C. DR InterPro; IPR006074; GTP1-OBG_CS. DR InterPro; IPR006169; GTP1_OBG_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR11702:SF3; PTHR11702:SF3; 2. DR Pfam; PF09269; DUF1967; 1. DR Pfam; PF01018; GTP1_OBG; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF102741; SSF102741; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF82051; SSF82051; 1. DR TIGRFAMs; TIGR02729; Obg_CgtA; 1. DR TIGRFAMs; TIGR03595; Obg_CgtA_exten; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51710; G_OBG; 1. DR PROSITE; PS00905; GTP1_OBG; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 435 GTPase Obg. FT /FTId=PRO_0000386356. FT DOMAIN 165 335 OBG-type G. {ECO:0000255|HAMAP- FT Rule:MF_01454}. FT NP_BIND 171 178 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 196 200 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 217 220 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 287 290 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 316 318 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT METAL 178 178 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01454}. FT METAL 198 198 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01454}. SQ SEQUENCE 435 AA; 48595 MW; 45A496703A4F74D2 CRC64; MNIERADFVD RVKIFVKAGD GGNGCVSFRR EKYVPKGGPD GGDGGNGGFV FLRANPSVST LIEFVNKRKF MAENGKHGMG KKMKGRNGKD LFIDVPVGTV VKDAVTGEVI ADLNEPGKIV CVARGGRGGR GNAHFATSIK QAPLIAERGE KGESRWLELE LKILADVGLV GYPNVGKSSL ISRISNARPK IANYPFTTLI PNLGVVKYDD FSFVVADIPG LIEGASEGVG LGNVFLRHVE RCYLIAHVID VSGYEREDPV RDYFVIREEM KKYSPFLLEK PEIVVANKID LIGKEELEKI LKRLRDATNR EVIPVSAVTG EGIDLLVSKL ASIVREMKVE KPERKEEKFV KPSPVWRRLP EKFHLEVVKE DEGYWVVEGE NLRVWIERFD LNQRDARLML LQVLEKNGLN NKLKEAGVKE GDVVRIGDFE FEYRE // ID OTC_THEMA Reviewed; 313 AA. AC P96108; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 2. DT 13-APR-2016, entry version 130. DE RecName: Full=Ornithine carbamoyltransferase; DE Short=OTCase; DE EC=2.1.3.3; GN Name=argF; OrderedLocusNames=TM_1097; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RA van de Casteele M., Legrain C., Glansdorff N.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). RG Joint center for structural genomics (JCSG); RT "Crystal structure of ornithine carbamoyltransferase (TM1097) from RT Thermotoga maritima at 2.25 a resolution."; RL Submitted (AUG-2004) to the PDB data bank. CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group CC from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine CC (ORN) to produce L-citrulline, which is a substrate for CC argininosuccinate synthetase, the enzyme involved in the final CC step in arginine biosynthesis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate CC + L-citrulline. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 1/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ATCase/OTCase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y10661; CAA71670.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36173.1; -; Genomic_DNA. DR PIR; C72294; C72294. DR RefSeq; NP_228903.1; NC_000853.1. DR RefSeq; WP_004080343.1; NZ_CP011107.1. DR PDB; 1VLV; X-ray; 2.25 A; A=1-313. DR PDBsum; 1VLV; -. DR ProteinModelPortal; P96108; -. DR SMR; P96108; 1-313. DR STRING; 243274.TM1097; -. DR EnsemblBacteria; AAD36173; AAD36173; TM_1097. DR GeneID; 898668; -. DR KEGG; tma:TM1097; -. DR PATRIC; 23937129; VBITheMar51294_1113. DR eggNOG; ENOG4105DBV; Bacteria. DR eggNOG; COG0078; LUCA. DR InParanoid; P96108; -. DR KO; K00611; -. DR OMA; DFRIFAP; -. DR OrthoDB; EOG690MGV; -. DR UniPathway; UPA00068; UER00112. DR EvolutionaryTrace; P96108; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IBA:GO_Central. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR Gene3D; 3.40.50.1370; -; 2. DR HAMAP; MF_01109; OTCase; 1. DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd. DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase. DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd. DR InterPro; IPR002292; Orn/put_carbamltrans. DR InterPro; IPR024904; OTCase_ArgI. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00102; OTCASE. DR SUPFAM; SSF53671; SSF53671; 1. DR TIGRFAMs; TIGR00658; orni_carb_tr; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 313 Ornithine carbamoyltransferase. FT /FTId=PRO_0000113049. FT REGION 57 61 Carbamoyl phosphate binding. FT REGION 79 81 Carbamoyl phosphate binding. FT REGION 135 138 Carbamoyl phosphate binding. FT {ECO:0000250}. FT REGION 235 236 Ornithine binding. {ECO:0000250}. FT REGION 271 274 Carbamoyl phosphate binding. FT {ECO:0000250}. FT BINDING 11 11 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 74 74 Carbamoyl phosphate. FT BINDING 108 108 Carbamoyl phosphate. FT BINDING 167 167 Ornithine. {ECO:0000250}. FT BINDING 231 231 Ornithine. {ECO:0000250}. FT BINDING 282 282 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 300 300 Carbamoyl phosphate. FT SITE 32 32 Important for structural integrity. FT {ECO:0000250}. FT SITE 148 148 Important for structural integrity. FT {ECO:0000250}. FT HELIX 13 15 {ECO:0000244|PDB:1VLV}. FT HELIX 18 37 {ECO:0000244|PDB:1VLV}. FT TURN 43 46 {ECO:0000244|PDB:1VLV}. FT STRAND 48 55 {ECO:0000244|PDB:1VLV}. FT HELIX 58 70 {ECO:0000244|PDB:1VLV}. FT STRAND 74 78 {ECO:0000244|PDB:1VLV}. FT TURN 80 82 {ECO:0000244|PDB:1VLV}. FT TURN 85 87 {ECO:0000244|PDB:1VLV}. FT HELIX 91 99 {ECO:0000244|PDB:1VLV}. FT STRAND 103 110 {ECO:0000244|PDB:1VLV}. FT HELIX 112 122 {ECO:0000244|PDB:1VLV}. FT STRAND 126 129 {ECO:0000244|PDB:1VLV}. FT HELIX 136 150 {ECO:0000244|PDB:1VLV}. FT STRAND 157 162 {ECO:0000244|PDB:1VLV}. FT HELIX 167 178 {ECO:0000244|PDB:1VLV}. FT STRAND 182 187 {ECO:0000244|PDB:1VLV}. FT HELIX 189 191 {ECO:0000244|PDB:1VLV}. FT HELIX 195 208 {ECO:0000244|PDB:1VLV}. FT STRAND 211 216 {ECO:0000244|PDB:1VLV}. FT HELIX 218 222 {ECO:0000244|PDB:1VLV}. FT STRAND 226 230 {ECO:0000244|PDB:1VLV}. FT HELIX 246 249 {ECO:0000244|PDB:1VLV}. FT HELIX 250 252 {ECO:0000244|PDB:1VLV}. FT HELIX 256 260 {ECO:0000244|PDB:1VLV}. FT STRAND 268 271 {ECO:0000244|PDB:1VLV}. FT TURN 278 280 {ECO:0000244|PDB:1VLV}. FT HELIX 283 286 {ECO:0000244|PDB:1VLV}. FT HELIX 293 312 {ECO:0000244|PDB:1VLV}. SQ SEQUENCE 313 AA; 35362 MW; 0C813CAC3B8C6F8D CRC64; MSVNLKGRSL LTLLDFSPEE IRYLLDISKQ VKMENRSKLR TERFKGMTLA MIFEKRSTRT RLAFETAFAE EGGHPIFLSP NDIHLGAKES LEDTARVLGR MVDAIMFRGY KQETVEKLAE YSGVPVYNGL TDEFHPTQAL ADLMTIEENF GRLKGVKVVF MGDTRNNVAT SLMIACAKMG MNFVACGPEE LKPRSDVFKR CQEIVKETDG SVSFTSNLEE ALAGADVVYT DVWASMGEED KEKERMALLK PYQVNERVME MTGKSETIFM HCLPAVKGQE VTYEVIEGKQ SRVWDEAENR KHTIKAVMIA TLL // ID OGG1_THEMA Reviewed; 207 AA. AC Q9X2E1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Probable N-glycosylase/DNA lyase; DE Includes: DE RecName: Full=8-oxoguanine DNA glycosylase; DE EC=3.2.2.-; DE Includes: DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase; DE Short=AP lyase; DE EC=4.2.99.18; GN Name=ogg; OrderedLocusNames=TM_1821; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Responsible for removing an oxidatively damaged form of CC guanine (7,8-dihydro-8-oxoguanine = 7-oxoG) from DNA. Also nicks CC DNA at apurinic/apyrimidinic sites (AP sites) (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. CC -!- SIMILARITY: Belongs to the type-2 OGG1 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36884.1; -; Genomic_DNA. DR PIR; H72206; H72206. DR RefSeq; NP_229618.1; NC_000853.1. DR RefSeq; WP_004082367.1; NZ_CP011107.1. DR PDB; 3N0U; X-ray; 1.50 A; A/B/C=1-207. DR PDBsum; 3N0U; -. DR ProteinModelPortal; Q9X2E1; -. DR STRING; 243274.TM1821; -. DR EnsemblBacteria; AAD36884; AAD36884; TM_1821. DR GeneID; 897824; -. DR KEGG; tma:TM1821; -. DR PATRIC; 23938629; VBITheMar51294_1841. DR eggNOG; ENOG4105GRF; Bacteria. DR eggNOG; COG1059; LUCA. DR InParanoid; Q9X2E1; -. DR KO; K03653; -. DR OMA; ELCFCIL; -. DR OrthoDB; EOG68SW1J; -. DR EvolutionaryTrace; Q9X2E1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:UniProtKB-HAMAP. DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00241; Ogg; 1. DR InterPro; IPR012092; DNA_glyclase/DNA_lyase_thermo. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR003265; HhH-GPD_domain. DR PIRSF; PIRSF005954; Thrmst_ogg; 1. DR SMART; SM00478; ENDO3c; 1. DR SUPFAM; SSF48150; SSF48150; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA damage; DNA repair; Glycosidase; KW Hydrolase; Lyase; Multifunctional enzyme; Reference proteome. FT CHAIN 1 207 Probable N-glycosylase/DNA lyase. FT /FTId=PRO_0000159572. FT ACT_SITE 129 129 {ECO:0000250}. FT HELIX 1 32 {ECO:0000244|PDB:3N0U}. FT HELIX 35 47 {ECO:0000244|PDB:3N0U}. FT TURN 48 50 {ECO:0000244|PDB:3N0U}. FT HELIX 53 63 {ECO:0000244|PDB:3N0U}. FT HELIX 66 69 {ECO:0000244|PDB:3N0U}. FT HELIX 72 81 {ECO:0000244|PDB:3N0U}. FT HELIX 87 97 {ECO:0000244|PDB:3N0U}. FT HELIX 98 100 {ECO:0000244|PDB:3N0U}. FT TURN 101 103 {ECO:0000244|PDB:3N0U}. FT HELIX 104 109 {ECO:0000244|PDB:3N0U}. FT HELIX 112 122 {ECO:0000244|PDB:3N0U}. FT HELIX 128 136 {ECO:0000244|PDB:3N0U}. FT TURN 137 139 {ECO:0000244|PDB:3N0U}. FT HELIX 148 156 {ECO:0000244|PDB:3N0U}. FT HELIX 169 186 {ECO:0000244|PDB:3N0U}. FT HELIX 190 202 {ECO:0000244|PDB:3N0U}. SQ SEQUENCE 207 AA; 24210 MW; DB4F7E3EF71C6204 CRC64; MEELLKELER IREEAKPLVE QRFEEFKRLG EEGTEEDLFC ELSFCVLTAN WSAEGGIRAQ KEIGKGFVHL PLEELAEKLR EVGHRYPQKR AEFIVENRKL LGKLKNLVKG DPFQSREFLV RNAKGIGWKE ASHFLRNTGV EDLAILDKHV LRLMKRHGLI QEIPKGWSKK RYLYVEEILR KVAEAFGESP GKFDLYLWYL VKGKVDK // ID P1254_THEMA Reviewed; 216 AA. AC Q9X0Y1; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=Phosphorylated carbohydrates phosphatase TM_1254; DE EC=3.1.3.-; GN OrderedLocusNames=TM_1254; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION, COFACTOR, AND KINETIC PARAMETERS. RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006; RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.; RT "Enzyme genomics: application of general enzymatic screens to discover RT new enzymes."; RL FEMS Microbiol. Rev. 29:263-279(2005). CC -!- FUNCTION: Displays high phosphatase activity toward erythrose 4- CC phosphate, fructose 6-phosphate, 2-deoxyglucose 6-phosphate, and CC mannose 6-phosphate. May have a role in the intracellular CC metabolism of many phosphorylated carbohydrates. CC {ECO:0000269|PubMed:15808744}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:15808744}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:15808744}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:15808744}; CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000269|PubMed:15808744}; CC Note=Divalent metal cation. Highest activity with Co(2+), followed CC by Mg(2+), Mn(2+) or Ni(2+). {ECO:0000269|PubMed:15808744}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=152 uM for erythrose 4-phosphate CC {ECO:0000269|PubMed:15808744}; CC KM=0.2 mM for fructose 6-phosphate CC {ECO:0000269|PubMed:15808744}; CC Vmax=2.63 umol/min/mg enzyme with erythrose 4-phosphate as CC substrate {ECO:0000269|PubMed:15808744}; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36329.1; -; Genomic_DNA. DR PIR; H72277; H72277. DR RefSeq; NP_229059.1; NC_000853.1. DR RefSeq; WP_004080009.1; NZ_CP011107.1. DR PDB; 3KBB; X-ray; 1.74 A; A=1-216. DR PDBsum; 3KBB; -. DR ProteinModelPortal; Q9X0Y1; -. DR SMR; Q9X0Y1; 1-216. DR STRING; 243274.TM1254; -. DR DNASU; 898229; -. DR EnsemblBacteria; AAD36329; AAD36329; TM_1254. DR GeneID; 898229; -. DR KEGG; tma:TM1254; -. DR PATRIC; 23937448; VBITheMar51294_1270. DR eggNOG; ENOG4105MN5; Bacteria. DR eggNOG; COG0637; LUCA. DR InParanoid; Q9X0Y1; -. DR OMA; LPGPECQ; -. DR OrthoDB; EOG6KMBB8; -. DR BRENDA; 3.1.3.58; 6331. DR EvolutionaryTrace; Q9X0Y1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.150.240; -; 1. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR023198; PGP_dom2. DR Pfam; PF13419; HAD_2; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cobalt; Complete proteome; KW Hydrolase; Magnesium; Manganese; Metal-binding; Nickel; KW Reference proteome. FT CHAIN 1 216 Phosphorylated carbohydrates phosphatase FT TM_1254. FT /FTId=PRO_0000058124. FT ACT_SITE 7 7 Nucleophile. {ECO:0000250}. FT STRAND 3 8 {ECO:0000244|PDB:3KBB}. FT TURN 9 11 {ECO:0000244|PDB:3KBB}. FT HELIX 16 18 {ECO:0000244|PDB:3KBB}. FT HELIX 19 29 {ECO:0000244|PDB:3KBB}. FT HELIX 36 42 {ECO:0000244|PDB:3KBB}. FT HELIX 47 57 {ECO:0000244|PDB:3KBB}. FT HELIX 64 82 {ECO:0000244|PDB:3KBB}. FT HELIX 89 98 {ECO:0000244|PDB:3KBB}. FT STRAND 102 106 {ECO:0000244|PDB:3KBB}. FT HELIX 111 120 {ECO:0000244|PDB:3KBB}. FT HELIX 124 126 {ECO:0000244|PDB:3KBB}. FT STRAND 128 131 {ECO:0000244|PDB:3KBB}. FT HELIX 133 135 {ECO:0000244|PDB:3KBB}. FT STRAND 136 138 {ECO:0000244|PDB:3KBB}. FT HELIX 144 153 {ECO:0000244|PDB:3KBB}. FT HELIX 157 159 {ECO:0000244|PDB:3KBB}. FT STRAND 160 164 {ECO:0000244|PDB:3KBB}. FT HELIX 167 175 {ECO:0000244|PDB:3KBB}. FT STRAND 181 184 {ECO:0000244|PDB:3KBB}. FT STRAND 187 189 {ECO:0000244|PDB:3KBB}. FT HELIX 192 196 {ECO:0000244|PDB:3KBB}. FT STRAND 200 203 {ECO:0000244|PDB:3KBB}. FT HELIX 205 207 {ECO:0000244|PDB:3KBB}. FT HELIX 208 215 {ECO:0000244|PDB:3KBB}. SQ SEQUENCE 216 AA; 24629 MW; 20A89F394A36E9EA CRC64; MEAVIFDMDG VLMDTEPLYF EAYRRVAESY GKPYTEDLHR RIMGVPEREG LPILMEALEI KDSLENFKKR VHEEKKRVFS ELLKENPGVR EALEFVKSKR IKLALATSTP QREALERLRR LDLEKYFDVM VFGDQVKNGK PDPEIYLLVL ERLNVVPEKV VVFEDSKSGV EAAKSAGIER IYGVVHSLND GKALLEAGAV ALVKPEEILN VLKEVL // ID PANB_THEMA Reviewed; 270 AA. AC Q9X251; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00156}; DE EC=2.1.2.11 {ECO:0000255|HAMAP-Rule:MF_00156}; DE AltName: Full=Ketopantoate hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00156}; DE Short=KPHMT {ECO:0000255|HAMAP-Rule:MF_00156}; GN Name=panB {ECO:0000255|HAMAP-Rule:MF_00156}; GN OrderedLocusNames=TM_1728; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl CC group from 5,10-methylenetetrahydrofolate is tranferred onto CC alpha-ketoisovalerate to form ketopantoate. {ECO:0000255|HAMAP- CC Rule:MF_00156}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + 3-methyl-2- CC oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate. CC {ECO:0000255|HAMAP-Rule:MF_00156}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00156}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00156}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00156}. CC -!- SUBUNIT: Homodecamer; pentamer of dimers. {ECO:0000255|HAMAP- CC Rule:MF_00156}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00156}. CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000255|HAMAP- CC Rule:MF_00156}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36793.1; -; Genomic_DNA. DR PIR; G72216; G72216. DR RefSeq; NP_229526.1; NC_000853.1. DR RefSeq; WP_004082243.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X251; -. DR STRING; 243274.TM1728; -. DR EnsemblBacteria; AAD36793; AAD36793; TM_1728. DR GeneID; 897214; -. DR KEGG; tma:TM1728; -. DR PATRIC; 23938432; VBITheMar51294_1746. DR eggNOG; ENOG4105CCG; Bacteria. DR eggNOG; COG0413; LUCA. DR InParanoid; Q9X251; -. DR KO; K00606; -. DR OMA; DMLGFFD; -. DR OrthoDB; EOG63C0WN; -. DR UniPathway; UPA00028; UER00003. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.60; -; 1. DR HAMAP; MF_00156; PanB; 1. DR InterPro; IPR003700; Pantoate_hydroxy_MeTrfase. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR PANTHER; PTHR20881; PTHR20881; 1. DR Pfam; PF02548; Pantoate_transf; 1. DR PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1. DR SUPFAM; SSF51621; SSF51621; 1. DR TIGRFAMs; TIGR00222; panB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Pantothenate biosynthesis; Reference proteome; Transferase. FT CHAIN 1 270 3-methyl-2-oxobutanoate FT hydroxymethyltransferase. FT /FTId=PRO_0000184901. FT REGION 41 42 Alpha-ketoisovalerate binding. FT {ECO:0000255|HAMAP-Rule:MF_00156}. FT ACT_SITE 178 178 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00156}. FT METAL 41 41 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00156}. FT METAL 80 80 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00156}. FT METAL 111 111 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00156}. FT BINDING 80 80 Alpha-ketoisovalerate. FT {ECO:0000255|HAMAP-Rule:MF_00156}. FT BINDING 109 109 Alpha-ketoisovalerate. FT {ECO:0000255|HAMAP-Rule:MF_00156}. SQ SEQUENCE 270 AA; 29691 MW; 851D7A63A5698B5A CRC64; MNVEKLKKMK GKEKIVMVTA YDAPSARIAR DAGIDVILVG DSLGNNVLGY ENTIPVTMEE MLIHVAAVKR GAPDAFIVAD MPFLSYQTSV EKAVENAGKF LKVGANAVKI EGGEEFGELV QKLVESGIPV MGHIGLTPQF VNRFGGYRVQ GKTEKNREYL LRSARELEKR GAFAIVLELV VEEVAKEITE SVSIPTIGIG SGRFCDGQVL VWHDLLGLNP DFAPRFSKKY ANLYEVILKA LQEFRREVKK GLFPTEEHSF TDKSKGGVSS // ID OMPA_THEMA Reviewed; 400 AA. AC Q01969; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 107. DE RecName: Full=Outer membrane protein alpha; DE Flags: Precursor; GN Name=omp-alpha; OrderedLocusNames=TM_0477; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1330536; RA Engel A.M., Cejka Z., Lupas A., Lottspeich F., Baumeister W.; RT "Isolation and cloning of Omp alpha, a coiled-coil protein spanning RT the periplasmic space of the ancestral eubacterium Thermotoga RT maritima."; RL EMBO J. 11:4369-4378(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Links the outer membrane to the inner membrane. Long CC fibrous protein that could serve to separate the two membranes. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cell outer membrane. CC -!- SIMILARITY: Contains 1 SLH (S-layer homology) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00777}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X68276; CAA48337.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35562.1; -; Genomic_DNA. DR PIR; E72372; E72372. DR RefSeq; NP_228287.1; NC_000853.1. DR RefSeq; WP_004081489.1; NZ_CP011107.1. DR ProteinModelPortal; Q01969; -. DR STRING; 243274.TM0477; -. DR EnsemblBacteria; AAD35562; AAD35562; TM_0477. DR GeneID; 897510; -. DR KEGG; tma:TM0477; -. DR PATRIC; 23935853; VBITheMar51294_0484. DR eggNOG; ENOG4105QZY; Bacteria. DR eggNOG; ENOG4111ZAU; LUCA. DR InParanoid; Q01969; -. DR OMA; DYERYKE; -. DR OrthoDB; EOG6PZX78; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR001119; SLH_dom. DR Pfam; PF00395; SLH; 1. DR PROSITE; PS51272; SLH; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Coiled coil; Complete proteome; KW Direct protein sequencing; Membrane; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 20 FT CHAIN 21 400 Outer membrane protein alpha. FT /FTId=PRO_0000032645. FT TRANSMEM 380 400 Helical. {ECO:0000255}. FT DOMAIN 21 81 SLH. {ECO:0000255|PROSITE- FT ProRule:PRU00777}. FT REPEAT 208 232 1. FT REPEAT 251 275 2. FT REPEAT 326 350 3. FT REGION 208 350 3 X 25 AA approximate repeat. FT COILED 85 379 {ECO:0000255}. FT CONFLICT 179 179 V -> A (in Ref. 1; CAA48337). FT {ECO:0000305}. SQ SEQUENCE 400 AA; 45339 MW; F7C7EB0E80935583 CRC64; MKRVLLTVAM LSVFFSAMFA FFPDVPKDHW AYEYVWKLWQ RGIFIGYPDG EFKGDRYITR YEAATAVSRL LDFIEQKMLA GASGDLAQVV GNLSDKYMAL EEKVNGLTGI LDTLASQIGT TQANLTETER ELLEKIDAVK EEIEMEFDKE ISLNREVVNN IGLKLGNLSR DYERYKENVD AKISEVNEKL AALEKDLGNK IADLEGIVNL HEKDIINIYN KISSVNEELN NKIAATEEKL SRKDEEISAM VELHEKDIIN LYNKVAALNE DLNKKILDTK AELSAKIESQ EKTLNMVYTK LLDTESKLND EISALKEKDA EIQKTVDLHE QDIVNLYGKT SSLEEDLNMK YNETNEKIDQ VKAELEDKIE SVKAYNRNLS ILTGAFFGIL GLILIAISGK // ID PANC_THEMA Reviewed; 280 AA. AC Q9X0G6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=Pantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_00158}; DE Short=PS {ECO:0000255|HAMAP-Rule:MF_00158}; DE EC=6.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00158}; DE AltName: Full=Pantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00158}; DE AltName: Full=Pantoate-activating enzyme {ECO:0000255|HAMAP-Rule:MF_00158}; GN Name=panC {ECO:0000255|HAMAP-Rule:MF_00158}; GN OrderedLocusNames=TM_1077; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine CC in an ATP-dependent reaction via a pantoyl-adenylate intermediate. CC {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantoate + beta-alanine = AMP + CC diphosphate + (R)-pantothenate. {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong CC mechanism. {ECO:0000255|HAMAP-Rule:MF_00158}. CC -!- SIMILARITY: Belongs to the pantothenate synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00158}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36154.1; -; Genomic_DNA. DR PIR; E72296; E72296. DR RefSeq; NP_228883.1; NC_000853.1. DR RefSeq; WP_004080408.1; NZ_CP011107.1. DR PDB; 2EJC; X-ray; 2.40 A; A=1-280. DR PDBsum; 2EJC; -. DR ProteinModelPortal; Q9X0G6; -. DR SMR; Q9X0G6; 1-280. DR STRING; 243274.TM1077; -. DR EnsemblBacteria; AAD36154; AAD36154; TM_1077. DR GeneID; 896992; -. DR KEGG; tma:TM1077; -. DR PATRIC; 23937083; VBITheMar51294_1090. DR eggNOG; ENOG4108IAA; Bacteria. DR eggNOG; COG0414; LUCA. DR InParanoid; Q9X0G6; -. DR KO; K01918; -. DR OMA; QKDAQQF; -. DR OrthoDB; EOG6Z6FZ4; -. DR UniPathway; UPA00028; UER00005. DR EvolutionaryTrace; Q9X0G6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00158; PanC; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR003721; Pantoate_ligase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR21299:SF1; PTHR21299:SF1; 1. DR Pfam; PF02569; Pantoate_ligase; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR TIGRFAMs; TIGR00018; panC; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Ligase; KW Nucleotide-binding; Pantothenate biosynthesis; Reference proteome. FT CHAIN 1 280 Pantothenate synthetase. FT /FTId=PRO_0000128280. FT NP_BIND 30 37 ATP. {ECO:0000255|HAMAP-Rule:MF_00158}. FT NP_BIND 147 150 ATP. {ECO:0000255|HAMAP-Rule:MF_00158}. FT NP_BIND 184 187 ATP. {ECO:0000255|HAMAP-Rule:MF_00158}. FT ACT_SITE 37 37 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00158}. FT BINDING 61 61 Beta-alanine. {ECO:0000255|HAMAP- FT Rule:MF_00158}. FT BINDING 61 61 Pantoate. {ECO:0000255|HAMAP- FT Rule:MF_00158}. FT BINDING 153 153 Pantoate. {ECO:0000255|HAMAP- FT Rule:MF_00158}. FT BINDING 176 176 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00158}. FT STRAND 2 4 {ECO:0000244|PDB:2EJC}. FT HELIX 7 19 {ECO:0000244|PDB:2EJC}. FT STRAND 24 29 {ECO:0000244|PDB:2EJC}. FT HELIX 35 47 {ECO:0000244|PDB:2EJC}. FT STRAND 48 55 {ECO:0000244|PDB:2EJC}. FT HELIX 59 61 {ECO:0000244|PDB:2EJC}. FT HELIX 68 70 {ECO:0000244|PDB:2EJC}. FT HELIX 75 83 {ECO:0000244|PDB:2EJC}. FT TURN 84 86 {ECO:0000244|PDB:2EJC}. FT STRAND 88 91 {ECO:0000244|PDB:2EJC}. FT HELIX 95 98 {ECO:0000244|PDB:2EJC}. FT HELIX 112 114 {ECO:0000244|PDB:2EJC}. FT TURN 115 117 {ECO:0000244|PDB:2EJC}. FT HELIX 118 120 {ECO:0000244|PDB:2EJC}. FT HELIX 124 139 {ECO:0000244|PDB:2EJC}. FT STRAND 142 147 {ECO:0000244|PDB:2EJC}. FT HELIX 148 150 {ECO:0000244|PDB:2EJC}. FT HELIX 151 163 {ECO:0000244|PDB:2EJC}. FT STRAND 169 173 {ECO:0000244|PDB:2EJC}. FT HELIX 186 190 {ECO:0000244|PDB:2EJC}. FT HELIX 193 198 {ECO:0000244|PDB:2EJC}. FT HELIX 201 214 {ECO:0000244|PDB:2EJC}. FT HELIX 220 232 {ECO:0000244|PDB:2EJC}. FT STRAND 237 246 {ECO:0000244|PDB:2EJC}. FT TURN 247 249 {ECO:0000244|PDB:2EJC}. FT STRAND 260 268 {ECO:0000244|PDB:2EJC}. FT STRAND 271 279 {ECO:0000244|PDB:2EJC}. SQ SEQUENCE 280 AA; 32757 MW; 0BD1E4C572197163 CRC64; MRIIETIEEM KKFSEEMREK KKTIGFVPTM GYLHEGHLSL VRRARAENDV VVVSIFVNPT QFGPNEDYER YPRDFERDRK LLEKENVDCI FHPSVEEMYP PDFSTYVEET KLSKHLCGRS RPGHFRGVCT VVTKLFNIVK PHRAYFGQKD AQQFRVLRRM VRDLNMDVEM IECPIVREPD GLAMSSRNVY LSPEERQQAL SLYQSLKIAE NLYLNGERDA EKIKEEMIKH LSRFDKVKID YVEIVDEETL EPVEKIDRKV IVAVAAWVGN ARLIDNTILG // ID OXBP_THEMA Reviewed; 121 AA. AC Q9X113; DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Oxalate-binding protein {ECO:0000305|PubMed:15211523}; DE AltName: Full=Putative oxalate decarboxylase {ECO:0000303|PubMed:15211523}; GN OrderedLocusNames=TM_1287 {ECO:0000312|EMBL:AAD36361.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000312|EMBL:AAD36361.1}; RN [1] {ECO:0000312|EMBL:AAD36361.1, ECO:0000312|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000312|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000244|PDB:1O4T} RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH MANGANESE AND RP OXALATE, FUNCTION, AND SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000303|PubMed:15211523}; RX PubMed=15211523; DOI=10.1002/prot.20016; RA Schwarzenbacher R., von Delft F., Jaroszewski L., Abdubek P., RA Ambing E., Biorac T., Brinen L.S., Canaves J.M., Cambell J., RA Chiu H.J., Dai X., Deacon A.M., DiDonato M., Elsliger M.A., Eshagi S., RA Floyd R., Godzik A., Grittini C., Grzechnik S.K., Hampton E., RA Karlak C., Klock H.E., Koesema E., Kovarik J.S., Kreusch A., Kuhn P., RA Lesley S.A., Levin I., McMullan D., McPhillips T.M., Miller M.D., RA Morse A., Moy K., Ouyang J., Page R., Quijano K., Robb A., RA Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., Vincent J., RA Wang X., West B., Wolf G., Xu Q., Hodgson K.O., Wooley J., RA Wilson I.A.; RT "Crystal structure of a putative oxalate decarboxylase (TM1287) from RT Thermotoga maritima at 1.95 A resolution."; RL Proteins 56:392-395(2004). CC -!- FUNCTION: Binds oxalate. {ECO:0000269|PubMed:15211523}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15211523}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36361.1; -; Genomic_DNA. DR PIR; F72271; F72271. DR RefSeq; NP_229091.1; NC_000853.1. DR RefSeq; WP_010865298.1; NC_000853.1. DR PDB; 1O4T; X-ray; 1.95 A; A/B=1-121. DR PDBsum; 1O4T; -. DR ProteinModelPortal; Q9X113; -. DR SMR; Q9X113; 7-121. DR STRING; 243274.TM1287; -. DR EnsemblBacteria; AAD36361; AAD36361; TM_1287. DR GeneID; 898196; -. DR KEGG; tma:TM1287; -. DR PATRIC; 23937514; VBITheMar51294_1303. DR eggNOG; ENOG4105W06; Bacteria. DR eggNOG; COG0662; LUCA. DR InParanoid; Q9X113; -. DR OMA; GEVEMAH; -. DR OrthoDB; EOG69SKD9; -. DR BioCyc; TMAR243274:GC6P-1318-MONOMER; -. DR EvolutionaryTrace; Q9X113; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0046564; F:oxalate decarboxylase activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0033609; P:oxalate metabolic process; ISS:UniProtKB. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR013096; Cupin_2. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF07883; Cupin_2; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Manganese; Metal-binding; KW Reference proteome. FT CHAIN 1 121 Oxalate-binding protein. FT /FTId=PRO_0000433802. FT METAL 61 61 Manganese; via tele nitrogen. FT {ECO:0000244|PDB:1O4T, FT ECO:0000269|PubMed:15211523}. FT METAL 63 63 Manganese; via tele nitrogen. FT {ECO:0000244|PDB:1O4T, FT ECO:0000269|PubMed:15211523}. FT METAL 68 68 Manganese. {ECO:0000244|PDB:1O4T, FT ECO:0000269|PubMed:15211523}. FT METAL 102 102 Manganese; via tele nitrogen. FT {ECO:0000244|PDB:1O4T, FT ECO:0000269|PubMed:15211523}. FT BINDING 70 70 Oxalate. {ECO:0000269|PubMed:15211523}. FT STRAND 8 10 {ECO:0000244|PDB:1O4T}. FT HELIX 11 13 {ECO:0000244|PDB:1O4T}. FT STRAND 17 21 {ECO:0000244|PDB:1O4T}. FT HELIX 22 24 {ECO:0000244|PDB:1O4T}. FT STRAND 26 33 {ECO:0000244|PDB:1O4T}. FT TURN 37 42 {ECO:0000244|PDB:1O4T}. FT STRAND 43 52 {ECO:0000244|PDB:1O4T}. FT STRAND 57 62 {ECO:0000244|PDB:1O4T}. FT STRAND 65 81 {ECO:0000244|PDB:1O4T}. FT STRAND 84 89 {ECO:0000244|PDB:1O4T}. FT STRAND 92 96 {ECO:0000244|PDB:1O4T}. FT STRAND 101 105 {ECO:0000244|PDB:1O4T}. FT STRAND 108 110 {ECO:0000244|PDB:1O4T}. FT STRAND 112 120 {ECO:0000244|PDB:1O4T}. SQ SEQUENCE 121 AA; 13270 MW; A13DA3516146A62E CRC64; MKEGTGMVVR SSEITPERIS NMRGGKGEVE MAHLLSKEAM HNKARLFARM KLPPGSSVGL HKHEGEFEIY YILLGEGVFH DNGKDVPIKA GDVCFTDSGE SHSIENTGNT DLEFLAVIIL L // ID PAND_THEMA Reviewed; 114 AA. AC Q9X037; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 111. DE RecName: Full=Aspartate 1-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446}; DE EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00446}; DE AltName: Full=Aspartate alpha-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446}; DE Contains: DE RecName: Full=Aspartate 1-decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00446}; DE Contains: DE RecName: Full=Aspartate 1-decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00446}; DE Flags: Precursor; GN Name=panD {ECO:0000255|HAMAP-Rule:MF_00446}; GN OrderedLocusNames=TM_0939; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of CC aspartate to produce beta-alanine. {ECO:0000255|HAMAP- CC Rule:MF_00446}. CC -!- CATALYTIC ACTIVITY: L-aspartate = beta-alanine + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_00446}. CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00446}; CC Note=Binds 1 pyruvoyl group covalently per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00446}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC beta-alanine from L-aspartate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00446}. CC -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00446}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00446}. CC -!- PTM: Is synthesized initially as an inactive proenzyme, which is CC activated by self-cleavage at a specific serine bond to produce a CC beta-subunit with a hydroxyl group at its C-terminus and an alpha- CC subunit with a pyruvoyl group at its N-terminus. CC {ECO:0000255|HAMAP-Rule:MF_00446}. CC -!- SIMILARITY: Belongs to the PanD family. {ECO:0000255|HAMAP- CC Rule:MF_00446}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36020.1; -; Genomic_DNA. DR PIR; C72316; C72316. DR RefSeq; NP_228747.1; NC_000853.1. DR RefSeq; WP_004080623.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X037; -. DR STRING; 243274.TM0939; -. DR EnsemblBacteria; AAD36020; AAD36020; TM_0939. DR GeneID; 898613; -. DR KEGG; tma:TM0939; -. DR PATRIC; 23936809; VBITheMar51294_0953. DR eggNOG; ENOG4108Z2X; Bacteria. DR eggNOG; COG0853; LUCA. DR InParanoid; Q9X037; -. DR KO; K01579; -. DR OMA; RGSREIN; -. DR OrthoDB; EOG6P5ZMC; -. DR UniPathway; UPA00028; UER00002. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006523; P:alanine biosynthetic process; IEA:InterPro. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00446; PanD; 1. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR003190; Asp_decarbox. DR PANTHER; PTHR21012; PTHR21012; 1. DR Pfam; PF02261; Asp_decarbox; 1. DR PIRSF; PIRSF006246; Asp_decarbox; 1. DR ProDom; PD009294; Asp_decarbox; 1. DR SUPFAM; SSF50692; SSF50692; 1. DR TIGRFAMs; TIGR00223; panD; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; Cytoplasm; Decarboxylase; KW Lyase; Pantothenate biosynthesis; Pyruvate; Reference proteome; KW Schiff base; Zymogen. FT CHAIN 1 24 Aspartate 1-decarboxylase beta chain. FT {ECO:0000255|HAMAP-Rule:MF_00446}. FT /FTId=PRO_0000023179. FT CHAIN 25 114 Aspartate 1-decarboxylase alpha chain. FT {ECO:0000255|HAMAP-Rule:MF_00446}. FT /FTId=PRO_0000023180. FT REGION 73 75 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00446}. FT ACT_SITE 25 25 Schiff-base intermediate with substrate; FT via pyruvic acid. {ECO:0000255|HAMAP- FT Rule:MF_00446}. FT ACT_SITE 58 58 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00446}. FT BINDING 57 57 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00446}. FT MOD_RES 25 25 Pyruvic acid (Ser). {ECO:0000255|HAMAP- FT Rule:MF_00446}. SQ SEQUENCE 114 AA; 12838 MW; D6DBF58B4B8C679F CRC64; MLNIYLKSKI HMATITRKEV YYEGSIEIDE ELMGKAGISE GELVLVVNVN NAERFVTYVI KGKRGSREIN LYGAAARLGE EGDRVIIMAF TFSDKPVKAK TIVLNEKNEI VQEK // ID PDUL_THEMA Reviewed; 210 AA. AC Q9WYK8; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Phosphate propanoyltransferase; DE EC=2.3.1.222; DE AltName: Full=Phosphate acyltransferase PduL; DE AltName: Full=Phosphotransacylase PduL; DE Short=PTAC; DE AltName: Full=Propanediol utilization protein PduL; GN Name=pduL; OrderedLocusNames=TM_0375; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in 1,2-propanediol (1,2-PD) degradation by CC catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Propanoyl-CoA + phosphate = CoA + propanoyl CC phosphate. CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation. CC -!- SIMILARITY: Belongs to the PduL family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35462.1; -; Genomic_DNA. DR PIR; E72385; E72385. DR RefSeq; NP_228186.1; NC_000853.1. DR RefSeq; WP_010865105.1; NZ_CP011107.1. DR STRING; 243274.TM0375; -. DR EnsemblBacteria; AAD35462; AAD35462; TM_0375. DR GeneID; 897338; -. DR KEGG; tma:TM0375; -. DR KEGG; tmw:THMA_0383; -. DR PATRIC; 23935631; VBITheMar51294_0380. DR eggNOG; ENOG4108VPX; Bacteria. DR eggNOG; COG4869; LUCA. DR InParanoid; Q9WYK8; -. DR KO; K15024; -. DR OMA; RHIHFHT; -. DR OrthoDB; EOG6N94D8; -. DR BioCyc; TMAR243274:GC6P-389-MONOMER; -. DR UniPathway; UPA00621; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro. DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR008300; PTAC. DR Pfam; PF06130; PTAC; 2. DR PIRSF; PIRSF010130; PduL; 1. DR SUPFAM; SSF50692; SSF50692; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Reference proteome; Transferase. FT CHAIN 1 210 Phosphate propanoyltransferase. FT /FTId=PRO_0000407703. SQ SEQUENCE 210 AA; 23543 MW; 285CA6DA75C02B53 CRC64; MITDGIMHKV REVYQLLRKE PGIIVGVSNR HVHLSREDLE TLFGEGYELT PVKELRQPGQ YAAKETVTIV GPKGAIENVR VLGPVRKETQ VEISRTDAFR LGVRPPVRDS GDLEGTPGIV IIGPNGILVK EKGVIIAKRH IHMHPKDAEY YGVKDKDIVK VIVESGDRRL IFDDVLIRVR EDFALEFHVD TDEANAAMLN TGDLVYIVEF // ID PFKA_THEMA Reviewed; 319 AA. AC Q9WY52; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339}; DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_00339}; DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339}; DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339}; DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_00339}; GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339}; GN OrderedLocusNames=TM_0209; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF 1-39, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND ENZYME REGULATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=11976749; DOI=10.1007/s00203-002-0405-7; RA Hansen T., Musfeldt M., Schonheit P.; RT "ATP-dependent 6-phosphofructokinase from the hyperthermophilic RT bacterium Thermotoga maritima: characterization of an extremely RT thermophilic, allosterically regulated enzyme."; RL Arch. Microbiol. 177:401-409(2002). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=11133978; DOI=10.1128/JB.183.2.791-794.2001; RA Ding Y.R., Ronimus R.S., Morgan H.W.; RT "Thermotoga maritima phosphofructokinases: expression and RT characterization of two unique enzymes."; RL J. Bacteriol. 183:791-794(2001). CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate CC to fructose 1,6-bisphosphate by ATP, the first committing step of CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_00339, CC ECO:0000269|PubMed:11133978, ECO:0000269|PubMed:11976749}. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_00339, CC ECO:0000269|PubMed:11133978, ECO:0000269|PubMed:11976749}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00339, CC ECO:0000269|PubMed:11976749}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00339, CC ECO:0000269|PubMed:11976749}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00339, CC ECO:0000269|PubMed:11976749}; CC Note=Mg(2+). Mg(2+) can partially be replaced by Mn(2+) and CC Fe(2+). {ECO:0000255|HAMAP-Rule:MF_00339, CC ECO:0000269|PubMed:11976749}; CC -!- ENZYME REGULATION: Allosterically activated by ADP and other CC diphosphonucleosides, and allosterically inhibited by CC phosphoenolpyruvate. Strongly inhibited by diphosphate, CC triphosphate and polyphosphate. {ECO:0000255|HAMAP-Rule:MF_00339, CC ECO:0000269|PubMed:11976749}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.2 mM for ATP (at 75 degrees Celsius) CC {ECO:0000269|PubMed:11133978, ECO:0000269|PubMed:11976749}; CC KM=7.6 mM for fructose 1,6-bisphosphate (at 75 degrees Celsius) CC {ECO:0000269|PubMed:11133978, ECO:0000269|PubMed:11976749}; CC KM=1.4 mM for ADP (at 75 degrees Celsius) CC {ECO:0000269|PubMed:11133978, ECO:0000269|PubMed:11976749}; CC Vmax=360 umol/min/mg enzyme for the forward reaction (at 75 CC degrees Celsius) {ECO:0000269|PubMed:11133978, CC ECO:0000269|PubMed:11976749}; CC Vmax=432 umol/min/mg enzyme for the forward reaction (at 50 CC degrees Celsius) {ECO:0000269|PubMed:11133978, CC ECO:0000269|PubMed:11976749}; CC Vmax=13 umol/min/mg enzyme for the reverse reaction (at 75 CC degrees Celsius) {ECO:0000269|PubMed:11133978, CC ECO:0000269|PubMed:11976749}; CC pH dependence: CC Optimum pH is 6.7. {ECO:0000269|PubMed:11133978, CC ECO:0000269|PubMed:11976749}; CC Temperature dependence: CC Optimum temperature is 93 degrees Celsius. CC {ECO:0000269|PubMed:11133978, ECO:0000269|PubMed:11976749}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00339, CC ECO:0000269|PubMed:11133978, ECO:0000269|PubMed:11976749}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) CC family. ATP-dependent PFK group I subfamily. Prokaryotic clade CC "B1" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35301.1; -; Genomic_DNA. DR PIR; C72406; C72406. DR RefSeq; NP_228024.1; NC_000853.1. DR RefSeq; WP_004082880.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY52; -. DR SMR; Q9WY52; 1-319. DR STRING; 243274.TM0209; -. DR EnsemblBacteria; AAD35301; AAD35301; TM_0209. DR GeneID; 897081; -. DR KEGG; tma:TM0209; -. DR PATRIC; 23935290; VBITheMar51294_0211. DR eggNOG; ENOG4105CTQ; Bacteria. DR eggNOG; COG0205; LUCA. DR InParanoid; Q9WY52; -. DR KO; K00850; -. DR OMA; CGDLALH; -. DR OrthoDB; EOG644ZRM; -. DR BioCyc; MetaCyc:MONOMER-363; -. DR SABIO-RK; Q9WY52; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR HAMAP; MF_00339; Phosphofructokinase_I_B1; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR012828; PFKA_ATP_prok. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 1. DR TIGRFAMs; TIGR02482; PFKA_ATP; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 1: Evidence at protein level; KW Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm; KW Direct protein sequencing; Glycolysis; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 319 ATP-dependent 6-phosphofructokinase. FT /FTId=PRO_0000112000. FT NP_BIND 72 73 ATP. {ECO:0000255|HAMAP-Rule:MF_00339}. FT NP_BIND 102 105 ATP. {ECO:0000255|HAMAP-Rule:MF_00339}. FT REGION 21 25 Allosteric activator ADP binding; shared FT with dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT REGION 126 128 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT REGION 170 172 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT REGION 186 188 Allosteric activator ADP binding. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT REGION 214 216 Allosteric activator ADP binding. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT REGION 250 253 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT ACT_SITE 128 128 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT METAL 103 103 Magnesium; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT BINDING 11 11 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT BINDING 155 155 Allosteric activator ADP. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT BINDING 163 163 Substrate; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT BINDING 212 212 Allosteric activator ADP. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT BINDING 223 223 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT BINDING 244 244 Substrate; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT CONFLICT 2 2 K -> R (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 14 17 PGMN -> GPM (in Ref. 2; AA sequence). FT {ECO:0000305}. SQ SEQUENCE 319 AA; 34487 MW; 3809E971288D12B8 CRC64; MKKIAVLTSG GDAPGMNAAV RAVVRYGVRQ GLEVIGVRRG YSGLIDGDFV KLEYKDVAGI TEKGGTILRT SRCEEFKTEE GRELAAKQIK KHGIEGLVVI GGEGSLTGAH LLYEEHKIPV VGIPATIDND IGLTDMCIGV DTCLNTVMDA VQKLKDTASS HERAFIVEVM GRHSGYIALM AGLVTGAEAI IVPEIPVDYS QLADRILEER RRGKINSIII VAEGAASAYT VARHLEYRIG YETRITILGH VQRGGSPTAF DRRLALSMGV EAVDALLDGE VDVMIALQGN KFVRVPIMEA LSTKKTIDKK LYEIAHMLS // ID PFP_THEMA Reviewed; 419 AA. AC Q9WYC5; G4FHK3; DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01979}; DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01979}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01979}; DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01979}; DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01979}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01979}; GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01979}; OrderedLocusNames=TM_0289; GN ORFNames=THEMA_03280, Tmari_0287; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RG DOE Joint Genome Institute; RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, RP COFACTOR, AND ENZYME REGULATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=11133978; DOI=10.1128/JB.183.2.791-794.2001; RA Ding Y.R., Ronimus R.S., Morgan H.W.; RT "Thermotoga maritima phosphofructokinases: expression and RT characterization of two unique enzymes."; RL J. Bacteriol. 183:791-794(2001). CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, CC the first committing step of glycolysis. Uses inorganic phosphate CC (PPi) as phosphoryl donor instead of ATP like common ATP-dependent CC phosphofructokinases (ATP-PFKs), which renders the reaction CC reversible, and can thus function both in glycolysis and CC gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of CC both the forward (ATP-PFK) and reverse (fructose-bisphosphatase CC (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_01979, CC ECO:0000269|PubMed:11133978}. CC -!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate = CC phosphate + D-fructose 1,6-bisphosphate. {ECO:0000255|HAMAP- CC Rule:MF_01979, ECO:0000269|PubMed:11133978}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979, CC ECO:0000269|PubMed:11133978}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979, CC ECO:0000269|PubMed:11133978}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979, CC ECO:0000269|PubMed:11133978}; CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979, CC ECO:0000269|PubMed:11133978}; CC Note=Mg(2+) can be partially replaced by Co(2+), Mn(2+) and CC Ni(2+). {ECO:0000255|HAMAP-Rule:MF_01979, CC ECO:0000269|PubMed:11133978}; CC -!- ENZYME REGULATION: Non-allosteric. {ECO:0000255|HAMAP- CC Rule:MF_01979, ECO:0000269|PubMed:11133978}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.067 mM for diphosphate {ECO:0000269|PubMed:11133978}; CC KM=0.01 mM for tripolyphosphate {ECO:0000269|PubMed:11133978}; CC KM=0.0038 mM for polyphosphate {ECO:0000269|PubMed:11133978}; CC KM=0.98 mM for fructose 6-phosphate CC {ECO:0000269|PubMed:11133978}; CC Vmax=203 umol/min/mg enzyme with diphosphate as substrate CC {ECO:0000269|PubMed:11133978}; CC Vmax=249 umol/min/mg enzyme with triphosphate as substrate CC {ECO:0000269|PubMed:11133978}; CC Vmax=319 umol/min/mg enzyme with polyphosphate as substrate CC {ECO:0000269|PubMed:11133978}; CC pH dependence: CC Optimum pH is 5.6-5.8 for the forward reaction, and 5.6-6.8 for CC the reverse reaction. {ECO:0000269|PubMed:11133978}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_01979}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01979, CC ECO:0000269|PubMed:11133978}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01979}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) CC family. PPi-dependent PFK group II subfamily. Clade "Short" sub- CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01979}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35377.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49213.1; -; Genomic_DNA. DR EMBL; CP007013; AHD17947.1; -; Genomic_DNA. DR PIR; G72396; G72396. DR RefSeq; NP_228101.1; NC_000853.1. DR RefSeq; WP_004083005.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYC5; -. DR STRING; 243274.TM0289; -. DR EnsemblBacteria; AAD35377; AAD35377; TM_0289. DR EnsemblBacteria; AGL49213; AGL49213; Tmari_0287. DR EnsemblBacteria; AHD17947; AHD17947; THEMA_03280. DR GeneID; 897209; -. DR KEGG; tma:TM0289; -. DR KEGG; tmi:THEMA_03280; -. DR KEGG; tmm:Tmari_0287; -. DR KEGG; tmw:THMA_0296; -. DR PATRIC; 23935457; VBITheMar51294_0294. DR eggNOG; ENOG4107UUY; Bacteria. DR eggNOG; COG0205; LUCA. DR InParanoid; Q9WYC5; -. DR KO; K00850; -. DR OMA; RTTNRWY; -. DR OrthoDB; EOG6WDSC8; -. DR BioCyc; TMAR243274:GC6P-302-MONOMER; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR HAMAP; MF_01979; Phosphofructokinase_II_Short; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR011403; PPi-PFK_TM0289. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF036482; PPi_PFK_TM0289; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Glycolysis; Kinase; Magnesium; KW Metal-binding; Reference proteome; Transferase. FT CHAIN 1 419 Pyrophosphate--fructose 6-phosphate 1- FT phosphotransferase. FT /FTId=PRO_0000429700. FT REGION 132 134 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01979}. FT REGION 178 180 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01979}. FT REGION 300 303 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01979}. FT ACT_SITE 134 134 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01979}. FT METAL 107 107 Magnesium; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01979}. FT BINDING 12 12 Diphosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01979}. FT BINDING 238 238 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01979}. FT SITE 108 108 Important for catalytic activity and FT substrate specificity; stabilizes the FT transition state when the phosphoryl FT donor is PPi; prevents ATP from binding FT by mimicking the alpha-phosphate group of FT ATP. {ECO:0000255|HAMAP-Rule:MF_01979}. FT SITE 131 131 Important for catalytic activity; FT stabilizes the transition state when the FT phosphoryl donor is PPi. FT {ECO:0000255|HAMAP-Rule:MF_01979}. SQ SEQUENCE 419 AA; 46465 MW; 4E3FBC75A8410CEC CRC64; MAERLGILVG GGPAPGINSV ISSVTIEAIN NGLEVIGIYD GFKHLVEGKT NMVKKLSIED VSRIHIEGGS ILRTSRVNPA KSEETLEKTV QTLKKLGIKY LVTIGGDDTA FSASKVCERS KGEIKVVHVP KTIDNDLPLP ENMPTFGFET ARHVATELVY NLMQDSRTTN RWYFVAMMGR EAGHLALGVG KAASATITII PEEFKEGVTL EEVCDVLDGA ILKRKLMGRD DGVAVIGEGI AEKMDPEELA NIPGVIVEKD PHGHLRLAEI PLATILKRAI ERRYAERGER IHIVDVTIGY ELRSARPIPF DIVYTRTLGY GAVRFLLGDY SDLPGGMVCV VGGRIKILPF DAFMDPKTGR TKVRVVDVRS EDYRVARKYM IRLEKKDLED PETLEKLAKL AKMEPEEFKK KYWHTTELP // ID PHOU1_THEMA Reviewed; 232 AA. AC Q9X0Y7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 09-DEC-2015, entry version 93. DE RecName: Full=Phosphate-specific transport system accessory protein PhoU homolog 1; DE Short=Pst system accessory protein PhoU homolog 1; GN Name=phoU1; OrderedLocusNames=TM_1260; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Plays a role in the regulation of phosphate uptake. CC {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PhoU family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36334.1; -; Genomic_DNA. DR PIR; G72275; G72275. DR RefSeq; NP_229065.1; NC_000853.1. DR RefSeq; WP_004080001.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0Y7; -. DR STRING; 243274.TM1260; -. DR DNASU; 898223; -. DR EnsemblBacteria; AAD36334; AAD36334; TM_1260. DR GeneID; 898223; -. DR KEGG; tma:TM1260; -. DR KEGG; tmi:THEMA_08035; -. DR KEGG; tmw:THMA_1285; -. DR PATRIC; 23937460; VBITheMar51294_1276. DR eggNOG; ENOG4108UTW; Bacteria. DR eggNOG; COG0704; LUCA. DR InParanoid; Q9X0Y7; -. DR KO; K02039; -. DR OMA; HMVEDAL; -. DR OrthoDB; EOG6Q2SPF; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IEA:InterPro. DR GO; GO:0045936; P:negative regulation of phosphate metabolic process; ISS:UniProtKB. DR GO; GO:2000186; P:negative regulation of phosphate transmembrane transport; ISS:UniProtKB. DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW. DR InterPro; IPR028366; P_trasport_PhoU. DR InterPro; IPR026022; PhoU_dom. DR PANTHER; PTHR10010:SF14; PTHR10010:SF14; 1. DR Pfam; PF01895; PhoU; 2. DR PIRSF; PIRSF003107; PhoU; 1. DR TIGRFAMs; TIGR02135; phoU_full; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Phosphate transport; Reference proteome; KW Transport. FT CHAIN 1 232 Phosphate-specific transport system FT accessory protein PhoU homolog 1. FT /FTId=PRO_0000155182. SQ SEQUENCE 232 AA; 26937 MW; DB9F6D49363CE6C3 CRC64; MVDHVHFERE LTLLKSDVSK MLFLVSESLN DAIESLETMN ETLARKVLES DDMIDELNRE IEEKAYQIIA RYNPILKQLR YIITILKFSN DLERIGDLSC NIAEKCLFLS EEKIKFEMLK ELKDMFGSTL KVVQDAFKAF VEEDVDLAFR LWKFDDVIDE MEKKIRRIVV ERIREGNISA ELALVYILIA RDLERVGDHA NNLCEEVIYI ETGKNMKEFL RGVESGSEGA DS // ID PDXS_THEMA Reviewed; 293 AA. AC Q9WYU4; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxS {ECO:0000255|HAMAP-Rule:MF_01824}; DE Short=PLP synthase subunit PdxS {ECO:0000255|HAMAP-Rule:MF_01824}; DE EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01824}; DE AltName: Full=Pdx1 {ECO:0000255|HAMAP-Rule:MF_01824}; GN Name=pdxS {ECO:0000255|HAMAP-Rule:MF_01824}; GN Synonyms=yaaD {ECO:0000303|PubMed:17144654}; GN OrderedLocusNames=TM_0473; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH PDXT SUBUNIT; RP RIBULOSE-5-PHOSPHATE AND PHOSPHATE, SUBUNIT, ACTIVE SITE, AND REACTION RP MECHANISM. RX PubMed=17144654; DOI=10.1021/bi061464y; RA Zein F., Zhang Y., Kang Y.N., Burns K., Begley T.P., Ealick S.E.; RT "Structural insights into the mechanism of the PLP synthase holoenzyme RT from Thermotoga maritima."; RL Biochemistry 45:14609-14620(2006). CC -!- FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from CC ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and CC ammonia. The ammonia is provided by the PdxT subunit. Can also use CC ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, CC resulting from enzyme-catalyzed isomerization of RBP and G3P, CC respectively. {ECO:0000255|HAMAP-Rule:MF_01824}. CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate + D-glyceraldehyde 3- CC phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 CC H(2)O + phosphate. {ECO:0000255|HAMAP-Rule:MF_01824}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01824}. CC -!- SUBUNIT: Homohexamer and homododecamer. In the presence of PdxT, CC forms a dodecamer of heterodimers. {ECO:0000255|HAMAP- CC Rule:MF_01824, ECO:0000269|PubMed:17144654}. CC -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000255|HAMAP- CC Rule:MF_01824}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35558.1; -; Genomic_DNA. DR PIR; A72372; A72372. DR RefSeq; NP_228283.1; NC_000853.1. DR RefSeq; WP_004081493.1; NZ_CP011107.1. DR PDB; 2ISS; X-ray; 2.90 A; A/B/C=1-293. DR PDBsum; 2ISS; -. DR ProteinModelPortal; Q9WYU4; -. DR SMR; Q9WYU4; 1-280. DR STRING; 243274.TM0473; -. DR EnsemblBacteria; AAD35558; AAD35558; TM_0473. DR GeneID; 897505; -. DR KEGG; tma:TM0473; -. DR PATRIC; 23935843; VBITheMar51294_0480. DR eggNOG; ENOG4105CD9; Bacteria. DR eggNOG; COG0214; LUCA. DR InParanoid; Q9WYU4; -. DR KO; K06215; -. DR OMA; KVRIGHV; -. DR OrthoDB; EOG6W9XBJ; -. DR UniPathway; UPA00245; -. DR EvolutionaryTrace; Q9WYU4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0042819; P:vitamin B6 biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_01824; PdxS; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001852; PdxS/SNZ. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF01680; SOR_SNZ; 1. DR PIRSF; PIRSF029271; Pdx1; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00343; TIGR00343; 1. DR PROSITE; PS01235; PDXS_SNZ_1; 1. DR PROSITE; PS51129; PDXS_SNZ_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Lyase; Pyridoxal phosphate; KW Reference proteome; Schiff base. FT CHAIN 1 293 Pyridoxal 5'-phosphate synthase subunit FT PdxS. FT /FTId=PRO_0000109423. FT REGION 236 237 D-ribose 5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01824, FT ECO:0000269|PubMed:17144654}. FT ACT_SITE 82 82 Schiff-base intermediate with D-ribose 5- FT phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01824, FT ECO:0000269|PubMed:17144654}. FT BINDING 25 25 D-ribose 5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01824, FT ECO:0000269|PubMed:17144654}. FT BINDING 103 103 D-ribulose 5-phosphate. FT {ECO:0000269|PubMed:17144654}. FT BINDING 154 154 D-ribose 5-phosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01824, FT ECO:0000269|PubMed:17144654}. FT BINDING 166 166 Glyceraldehyde 3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_01824}. FT BINDING 215 215 D-ribose 5-phosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01824, FT ECO:0000269|PubMed:17144654}. FT STRAND 3 6 {ECO:0000244|PDB:2ISS}. FT HELIX 8 16 {ECO:0000244|PDB:2ISS}. FT TURN 17 20 {ECO:0000244|PDB:2ISS}. FT STRAND 22 28 {ECO:0000244|PDB:2ISS}. FT HELIX 29 38 {ECO:0000244|PDB:2ISS}. FT STRAND 41 45 {ECO:0000244|PDB:2ISS}. FT HELIX 50 56 {ECO:0000244|PDB:2ISS}. FT HELIX 65 74 {ECO:0000244|PDB:2ISS}. FT STRAND 79 84 {ECO:0000244|PDB:2ISS}. FT HELIX 88 97 {ECO:0000244|PDB:2ISS}. FT STRAND 100 105 {ECO:0000244|PDB:2ISS}. FT HELIX 119 121 {ECO:0000244|PDB:2ISS}. FT STRAND 126 132 {ECO:0000244|PDB:2ISS}. FT HELIX 133 141 {ECO:0000244|PDB:2ISS}. FT STRAND 145 149 {ECO:0000244|PDB:2ISS}. FT HELIX 159 175 {ECO:0000244|PDB:2ISS}. FT HELIX 180 190 {ECO:0000244|PDB:2ISS}. FT HELIX 194 203 {ECO:0000244|PDB:2ISS}. FT STRAND 207 214 {ECO:0000244|PDB:2ISS}. FT HELIX 219 227 {ECO:0000244|PDB:2ISS}. FT STRAND 233 236 {ECO:0000244|PDB:2ISS}. FT HELIX 237 240 {ECO:0000244|PDB:2ISS}. FT HELIX 245 257 {ECO:0000244|PDB:2ISS}. FT HELIX 262 269 {ECO:0000244|PDB:2ISS}. SQ SEQUENCE 293 AA; 32127 MW; 83092199901AF356 CRC64; MEIKKGTWII KKGFAEMFKG GVIMDVTSAE QAKIAEEAGA VAVMALERVP ADIRKEGGVA RMASIAKIRE IMEAVSIPVM AKVRIGHIAE AKILEELGVD FIDESEVLTP ADDRFHINKH EFKVPFVCGA RDLGEALRRI AEGAAMIRTK GEAGTGNVVE AVKHMRRVME QIKQVTKMED EELVAYGKEI GAPVELLREV KRLGRLPVVN FAAGGVATPA DAALMMMLGA DGVFVGSGIF KSKDPRKMAK AMVLAVTYWD NPRILLKISE DIGEPMRGLD VEELEVRMQE RGW // ID PDXT_THEMA Reviewed; 188 AA. AC Q9WYU3; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000255|HAMAP-Rule:MF_01615}; DE EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01615}; DE AltName: Full=Pdx2 {ECO:0000255|HAMAP-Rule:MF_01615}; DE AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_01615}; DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01615}; GN Name=pdxT {ECO:0000255|HAMAP-Rule:MF_01615}; GN Synonyms=yaaE {ECO:0000303|PubMed:17144654}; GN OrderedLocusNames=TM_0472; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH SUBUNIT PDXS, RP SUBUNIT, AND REACTION MECHANISM. RX PubMed=17144654; DOI=10.1021/bi061464y; RA Zein F., Zhang Y., Kang Y.N., Burns K., Begley T.P., Ealick S.E.; RT "Structural insights into the mechanism of the PLP synthase holoenzyme RT from Thermotoga maritima."; RL Biochemistry 45:14609-14620(2006). CC -!- FUNCTION: Catalyzes the hydrolysis of glutamine to glutamate and CC ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The CC resulting ammonia molecule is channeled to the active site of CC PdxS. {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate + D-glyceraldehyde 3- CC phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 CC H(2)O + phosphate. {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3). CC {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of CC heterodimers. Only shows activity in the heterodimer. CC {ECO:0000255|HAMAP-Rule:MF_01615, ECO:0000269|PubMed:17144654}. CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family. CC {ECO:0000255|HAMAP-Rule:MF_01615}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35557.1; -; Genomic_DNA. DR PIR; H72371; H72371. DR RefSeq; NP_228282.1; NC_000853.1. DR RefSeq; WP_004081494.1; NZ_CP011107.1. DR PDB; 2ISS; X-ray; 2.90 A; D/E/F=1-188. DR PDBsum; 2ISS; -. DR ProteinModelPortal; Q9WYU3; -. DR SMR; Q9WYU3; 1-187. DR STRING; 243274.TM0472; -. DR EnsemblBacteria; AAD35557; AAD35557; TM_0472. DR GeneID; 897504; -. DR KEGG; tma:TM0472; -. DR PATRIC; 23935841; VBITheMar51294_0479. DR eggNOG; ENOG4108UHX; Bacteria. DR eggNOG; COG0311; LUCA. DR InParanoid; Q9WYU3; -. DR KO; K08681; -. DR OMA; VYGTCAG; -. DR OrthoDB; EOG66F0BW; -. DR UniPathway; UPA00245; -. DR EvolutionaryTrace; Q9WYU3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:1903600; C:glutaminase complex; IBA:GO_Central. DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006543; P:glutamine catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0008614; P:pyridoxine metabolic process; IBA:GO_Central. DR GO; GO:0042819; P:vitamin B6 biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_01615; PdxT; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR002161; PdxT/SNO. DR InterPro; IPR021196; PdxT/SNO_CS. DR Pfam; PF01174; SNO; 1. DR PIRSF; PIRSF005639; Glut_amidoT_SNO; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR03800; PLP_synth_Pdx2; 1. DR PROSITE; PS01236; PDXT_SNO_1; 1. DR PROSITE; PS51130; PDXT_SNO_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Glutamine amidotransferase; KW Hydrolase; Lyase; Pyridoxal phosphate; Reference proteome. FT CHAIN 1 188 Pyridoxal 5'-phosphate synthase subunit FT PdxT. FT /FTId=PRO_0000135669. FT REGION 46 48 L-glutamine binding. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT REGION 134 135 L-glutamine binding. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT ACT_SITE 78 78 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT ACT_SITE 170 170 Charge relay system. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT ACT_SITE 172 172 Charge relay system. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT BINDING 105 105 L-glutamine. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT STRAND 2 6 {ECO:0000244|PDB:2ISS}. FT STRAND 8 10 {ECO:0000244|PDB:2ISS}. FT HELIX 12 21 {ECO:0000244|PDB:2ISS}. FT STRAND 25 29 {ECO:0000244|PDB:2ISS}. FT HELIX 32 37 {ECO:0000244|PDB:2ISS}. FT STRAND 39 43 {ECO:0000244|PDB:2ISS}. FT HELIX 48 57 {ECO:0000244|PDB:2ISS}. FT HELIX 61 69 {ECO:0000244|PDB:2ISS}. FT STRAND 74 77 {ECO:0000244|PDB:2ISS}. FT HELIX 79 84 {ECO:0000244|PDB:2ISS}. FT STRAND 85 88 {ECO:0000244|PDB:2ISS}. FT STRAND 99 104 {ECO:0000244|PDB:2ISS}. FT TURN 105 108 {ECO:0000244|PDB:2ISS}. FT HELIX 111 113 {ECO:0000244|PDB:2ISS}. FT STRAND 115 119 {ECO:0000244|PDB:2ISS}. FT HELIX 122 124 {ECO:0000244|PDB:2ISS}. FT STRAND 129 135 {ECO:0000244|PDB:2ISS}. FT STRAND 138 142 {ECO:0000244|PDB:2ISS}. FT STRAND 147 152 {ECO:0000244|PDB:2ISS}. FT STRAND 155 161 {ECO:0000244|PDB:2ISS}. FT STRAND 164 169 {ECO:0000244|PDB:2ISS}. FT HELIX 171 173 {ECO:0000244|PDB:2ISS}. FT HELIX 178 184 {ECO:0000244|PDB:2ISS}. SQ SEQUENCE 188 AA; 21178 MW; AAE2FA50E81F8348 CRC64; MKIGVLGVQG DVREHVEALH KLGVETLIVK LPEQLDMVDG LILPGGESTT MIRILKEMDM DEKLVERINN GLPVFATCAG VILLAKRIKN YSQEKLGVLD ITVERNAYGR QVESFETFVE IPAVGKDPFR AIFIRAPRIV ETGKNVEILA TYDYDPVLVK EGNILACTFH PELTDDLRLH RYFLEMVK // ID PLSX_THEMA Reviewed; 327 AA. AC Q9WXZ6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 94. DE RecName: Full=Phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019}; DE EC=2.3.1.n2 {ECO:0000255|HAMAP-Rule:MF_00019}; DE AltName: Full=Acyl-ACP phosphotransacylase {ECO:0000255|HAMAP-Rule:MF_00019}; DE AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019}; DE AltName: Full=Phosphate-acyl-ACP acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019}; GN Name=plsX {ECO:0000255|HAMAP-Rule:MF_00019}; GN OrderedLocusNames=TM_0149; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the reversible formation of acyl-phosphate CC (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This CC enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. CC {ECO:0000255|HAMAP-Rule:MF_00019}. CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + phosphate = CC acyl-phosphate + [acyl-carrier-protein]. {ECO:0000255|HAMAP- CC Rule:MF_00019}. CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. CC {ECO:0000255|HAMAP-Rule:MF_00019}. CC -!- SUBUNIT: Homodimer. Probably interacts with PlsY. CC {ECO:0000255|HAMAP-Rule:MF_00019}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00019}. CC Note=Associated with the membrane possibly through PlsY. CC {ECO:0000255|HAMAP-Rule:MF_00019}. CC -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000255|HAMAP- CC Rule:MF_00019}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35242.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35242.1; ALT_INIT; Genomic_DNA. DR PIR; C72412; C72412. DR RefSeq; NP_227964.1; NC_000853.1. DR RefSeq; WP_004082759.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXZ6; -. DR STRING; 243274.TM0149; -. DR EnsemblBacteria; AAD35242; AAD35242; TM_0149. DR GeneID; 896984; -. DR KEGG; tma:TM0149; -. DR PATRIC; 23935142; VBITheMar51294_0148. DR eggNOG; ENOG4105C6B; Bacteria. DR eggNOG; COG0416; LUCA. DR InParanoid; Q9WXZ6; -. DR KO; K03621; -. DR OMA; KFCLRTM; -. DR OrthoDB; EOG68H88P; -. DR BioCyc; TMAR243274:GC6P-150-MONOMER; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; -; 1. DR HAMAP; MF_00019; PlsX; 1. DR InterPro; IPR003664; FA_synthesis. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR InterPro; IPR012281; Phospholipid_synth_PlsX-like. DR Pfam; PF02504; FA_synthesis; 1. DR PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1. DR TIGRFAMs; TIGR00182; plsX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1 327 Phosphate acyltransferase. FT /FTId=PRO_0000189957. SQ SEQUENCE 327 AA; 34609 MW; B2D0FFCFDC5A4010 CRC64; MKIAIDVMGG DRAPDEILKG ALLASKEVEG EIVLIGPEEI VKNKGLPFVS ASEIVKMDDP PLEVLRKKNS SMHMGLKLLS EGKVDAFVSA GATGPLFLGA TSIVGKLEGI ERPALGVAVP SLKGATVLID AGANAKVRPE HLVDFAFMGI AYSKVLGAEN PRVGLLNMGS EENKGPDDIK RAYQLLKEFL GDTFFGNVEG HDINLGTVDV VVADGFSGNV ALKTMEGTAK LVTSVLKESI KDGGFLSLLG ALLMKRSFDK MKEKLDPRSY GGTFILGVKG IVVKAHGSSD AKAIKHAIKV AEKGIRVNIV QEIERGISHV RNSGDGR // ID PGKT_THEMA Reviewed; 654 AA. AC P36204; Q60031; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 4. DT 13-APR-2016, entry version 130. DE RecName: Full=Bifunctional PGK/TIM; DE Includes: DE RecName: Full=Phosphoglycerate kinase; DE EC=2.7.2.3; DE Includes: DE RecName: Full=Triosephosphate isomerase; DE Short=TIM; DE EC=5.3.1.1; DE AltName: Full=Triose-phosphate isomerase; GN Name=pgk/tpi; OrderedLocusNames=TM_0689; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=7859734; RA Schurig H., Beaucamp N., Ostendorp R., Jaenicke R., Adler E., RA Knowles J.R.; RT "Phosphoglycerate kinase and triosephosphate isomerase from the RT hyperthermophilic bacterium Thermotoga maritima form a covalent RT bifunctional enzyme complex."; RL EMBO J. 14:442-451(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-393 IN COMPLEX WITH RP SUBSTRATE AND ATP ANALOG, AND SEQUENCE REVISION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9384563; DOI=10.1016/S0969-2126(97)00297-9; RA Auerbach G., Huber R., Graettinger M., Zaiss K., Schurig H., RA Jaenicke R., Jacob U.; RT "Closed structure of phosphoglycerate kinase from Thermotoga maritima RT reveals the catalytic mechanism and determinants of thermal RT stability."; RL Structure 5:1475-1483(1997). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 400-654, AND SUBUNIT. RX PubMed=10591103; RX DOI=10.1002/(SICI)1097-0134(19991115)37:3<441::AID-PROT11>3.0.CO;2-7; RA Maes D., Zeelen J.P., Thanki N., Beaucamp N., Alvarez M., Thi M.H., RA Backmann J., Martial J.A., Wyns L., Jaenicke R., Wierenga R.K.; RT "The crystal structure of triosephosphate isomerase (TIM) from RT Thermotoga maritima: a comparative thermostability structural analysis RT of ten different TIM structures."; RL Proteins 37:441-453(1999). CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho- CC D-glyceroyl phosphate. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone CC phosphate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate from glycerone phosphate: step 1/1. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. CC -!- SUBUNIT: Monomer (PGK) and homotetramer (PGK-TIM). CC {ECO:0000269|PubMed:10591103, ECO:0000269|PubMed:7859734, CC ECO:0000269|PubMed:9384563}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC phosphoglycerate kinase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC triosephosphate isomerase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X75437; CAA53187.1; -; Genomic_DNA. DR EMBL; L27492; AAA67520.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35771.1; -; Genomic_DNA. DR PIR; G72344; G72344. DR RefSeq; NP_228498.1; NC_000853.1. DR RefSeq; WP_004081072.1; NZ_CP011107.1. DR PDB; 1B9B; X-ray; 2.85 A; A/B=400-654. DR PDB; 1VPE; X-ray; 2.00 A; A=2-398. DR PDBsum; 1B9B; -. DR PDBsum; 1VPE; -. DR ProteinModelPortal; P36204; -. DR SMR; P36204; 2-398, 400-653. DR STRING; 243274.TM0689; -. DR EnsemblBacteria; AAD35771; AAD35771; TM_0689. DR GeneID; 898356; -. DR KEGG; tma:TM0689; -. DR PATRIC; 23936296; VBITheMar51294_0701. DR eggNOG; ENOG4105BZA; Bacteria. DR eggNOG; COG0126; LUCA. DR eggNOG; COG0149; LUCA. DR InParanoid; P36204; -. DR KO; K00927; -. DR KO; K01803; -. DR OMA; HYTHLEA; -. DR OrthoDB; EOG64N9Z0; -. DR BioCyc; MetaCyc:MONOMER-382; -. DR BRENDA; 5.3.1.1; 6331. DR SABIO-RK; P36204; -. DR UniPathway; UPA00109; UER00185. DR UniPathway; UPA00109; UER00189. DR EvolutionaryTrace; P36204; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.1260; -; 1. DR Gene3D; 3.40.50.1270; -; 1. DR HAMAP; MF_00145; Phosphoglyc_kinase; 1. DR HAMAP; MF_00147_B; TIM_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001576; Phosphoglycerate_kinase. DR InterPro; IPR015901; Phosphoglycerate_kinase_C. DR InterPro; IPR015911; Phosphoglycerate_kinase_CS. DR InterPro; IPR015824; Phosphoglycerate_kinase_N. DR InterPro; IPR022896; TrioseP_Isoase_bac/euk. DR InterPro; IPR000652; Triosephosphate_isomerase. DR InterPro; IPR020861; Triosephosphate_isomerase_AS. DR PANTHER; PTHR11406; PTHR11406; 1. DR Pfam; PF00162; PGK; 1. DR Pfam; PF00121; TIM; 1. DR PRINTS; PR00477; PHGLYCKINASE. DR SUPFAM; SSF51351; SSF51351; 1. DR SUPFAM; SSF53748; SSF53748; 1. DR TIGRFAMs; TIGR00419; tim; 1. DR PROSITE; PS00111; PGLYCERATE_KINASE; 1. DR PROSITE; PS00171; TIM_1; 1. DR PROSITE; PS51440; TIM_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; KW Fatty acid biosynthesis; Fatty acid metabolism; Gluconeogenesis; KW Glycolysis; Isomerase; Kinase; Lipid biosynthesis; Lipid metabolism; KW Multifunctional enzyme; Nucleotide-binding; Pentose shunt; KW Reference proteome; Transferase. FT CHAIN 1 654 Bifunctional PGK/TIM. FT /FTId=PRO_0000146025. FT NP_BIND 353 356 ATP. FT REGION 1 399 Phosphoglycerate kinase. FT REGION 21 23 Substrate binding. FT REGION 59 62 Substrate binding. FT REGION 400 654 Triosephosphate isomerase. FT REGION 409 411 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT REGION 634 635 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 495 495 Electrophile. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 567 567 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT BINDING 36 36 Substrate. {ECO:0000269|PubMed:9384563}. FT BINDING 118 118 Substrate. {ECO:0000269|PubMed:9384563}. FT BINDING 151 151 Substrate. {ECO:0000269|PubMed:9384563}. FT BINDING 201 201 ATP. FT BINDING 293 293 ATP; via carbonyl oxygen. FT BINDING 317 317 ATP. FT BINDING 324 324 ATP. FT BINDING 572 572 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00147}. FT CONFLICT 213 213 D -> N (in Ref. 1; CAA53187). FT {ECO:0000305}. FT CONFLICT 394 396 IAD -> MRI (in Ref. 1; CAA53187). FT {ECO:0000305}. FT CONFLICT 626 626 K -> R (in Ref. 1; CAA53187). FT {ECO:0000305}. FT CONFLICT 640 640 E -> Q (in Ref. 1; CAA53187). FT {ECO:0000305}. FT HELIX 6 8 {ECO:0000244|PDB:1VPE}. FT STRAND 15 19 {ECO:0000244|PDB:1VPE}. FT STRAND 30 32 {ECO:0000244|PDB:1VPE}. FT HELIX 35 49 {ECO:0000244|PDB:1VPE}. FT STRAND 53 57 {ECO:0000244|PDB:1VPE}. FT HELIX 69 71 {ECO:0000244|PDB:1VPE}. FT HELIX 74 84 {ECO:0000244|PDB:1VPE}. FT STRAND 89 92 {ECO:0000244|PDB:1VPE}. FT STRAND 94 96 {ECO:0000244|PDB:1VPE}. FT HELIX 97 104 {ECO:0000244|PDB:1VPE}. FT STRAND 111 114 {ECO:0000244|PDB:1VPE}. FT HELIX 117 119 {ECO:0000244|PDB:1VPE}. FT HELIX 122 125 {ECO:0000244|PDB:1VPE}. FT HELIX 128 135 {ECO:0000244|PDB:1VPE}. FT STRAND 139 143 {ECO:0000244|PDB:1VPE}. FT HELIX 146 148 {ECO:0000244|PDB:1VPE}. FT TURN 154 157 {ECO:0000244|PDB:1VPE}. FT HELIX 158 161 {ECO:0000244|PDB:1VPE}. FT STRAND 165 167 {ECO:0000244|PDB:1VPE}. FT HELIX 169 183 {ECO:0000244|PDB:1VPE}. FT STRAND 187 193 {ECO:0000244|PDB:1VPE}. FT HELIX 198 208 {ECO:0000244|PDB:1VPE}. FT TURN 209 211 {ECO:0000244|PDB:1VPE}. FT STRAND 213 217 {ECO:0000244|PDB:1VPE}. FT TURN 219 221 {ECO:0000244|PDB:1VPE}. FT HELIX 222 228 {ECO:0000244|PDB:1VPE}. FT HELIX 240 242 {ECO:0000244|PDB:1VPE}. FT HELIX 243 255 {ECO:0000244|PDB:1VPE}. FT STRAND 259 261 {ECO:0000244|PDB:1VPE}. FT STRAND 264 271 {ECO:0000244|PDB:1VPE}. FT STRAND 279 282 {ECO:0000244|PDB:1VPE}. FT TURN 283 285 {ECO:0000244|PDB:1VPE}. FT STRAND 292 296 {ECO:0000244|PDB:1VPE}. FT HELIX 298 308 {ECO:0000244|PDB:1VPE}. FT STRAND 312 318 {ECO:0000244|PDB:1VPE}. FT HELIX 326 328 {ECO:0000244|PDB:1VPE}. FT HELIX 330 344 {ECO:0000244|PDB:1VPE}. FT STRAND 348 353 {ECO:0000244|PDB:1VPE}. FT HELIX 354 362 {ECO:0000244|PDB:1VPE}. FT HELIX 366 368 {ECO:0000244|PDB:1VPE}. FT STRAND 369 374 {ECO:0000244|PDB:1VPE}. FT HELIX 376 383 {ECO:0000244|PDB:1VPE}. FT HELIX 389 392 {ECO:0000244|PDB:1VPE}. FT STRAND 405 409 {ECO:0000244|PDB:1B9B}. FT HELIX 416 429 {ECO:0000244|PDB:1B9B}. FT STRAND 435 441 {ECO:0000244|PDB:1B9B}. FT HELIX 444 446 {ECO:0000244|PDB:1B9B}. FT HELIX 447 454 {ECO:0000244|PDB:1B9B}. FT STRAND 457 464 {ECO:0000244|PDB:1B9B}. FT STRAND 468 473 {ECO:0000244|PDB:1B9B}. FT HELIX 480 484 {ECO:0000244|PDB:1B9B}. FT TURN 485 487 {ECO:0000244|PDB:1B9B}. FT STRAND 490 494 {ECO:0000244|PDB:1B9B}. FT HELIX 496 500 {ECO:0000244|PDB:1B9B}. FT HELIX 506 518 {ECO:0000244|PDB:1B9B}. FT STRAND 522 527 {ECO:0000244|PDB:1B9B}. FT HELIX 531 536 {ECO:0000244|PDB:1B9B}. FT HELIX 539 551 {ECO:0000244|PDB:1B9B}. FT HELIX 556 559 {ECO:0000244|PDB:1B9B}. FT STRAND 563 566 {ECO:0000244|PDB:1B9B}. FT HELIX 569 571 {ECO:0000244|PDB:1B9B}. FT STRAND 572 575 {ECO:0000244|PDB:1B9B}. FT HELIX 580 597 {ECO:0000244|PDB:1B9B}. FT HELIX 600 605 {ECO:0000244|PDB:1B9B}. FT STRAND 606 613 {ECO:0000244|PDB:1B9B}. FT HELIX 616 619 {ECO:0000244|PDB:1B9B}. FT TURN 620 622 {ECO:0000244|PDB:1B9B}. FT STRAND 623 625 {ECO:0000244|PDB:1B9B}. FT STRAND 630 634 {ECO:0000244|PDB:1B9B}. FT HELIX 635 637 {ECO:0000244|PDB:1B9B}. FT HELIX 641 649 {ECO:0000244|PDB:1B9B}. SQ SEQUENCE 654 AA; 71585 MW; 42358A4EF0C5E481 CRC64; MEKMTIRDVD LKGKRVIMRV DFNVPVKDGV VQDDTRIRAA LPTIKYALEQ GAKVILLSHL GRPKGEPSPE FSLAPVAKRL SELLGKEVKF VPAVVGDEVK KAVEELKEGE VLLLENTRFH PGETKNDPEL AKFWASLADI HVNDAFGTAH RAHASNVGIA QFIPSVAGFL MEKEIKFLSK VTYNPEKPYV VVLGGAKVSD KIGVITNLME KADRILIGGA MMFTFLKALG KEVGSSRVEE DKIDLAKELL EKAKEKGVEI VLPVDAVIAQ KIEPGVEKKV VRIDDGIPEG WMGLDIGPET IELFKQKLSD AKTVVWNGPM GVFEIDDFAE GTKQVALAIA ALTEKGAITV VGGGDSAAAV NKFGLEDKFS HVSTGGGASL EFLEGKELPG IASIADKKKI TRKLILAGNW KMHKTISEAK KFVSLLVNEL HDVKEFEIVV CPPFTALSEV GEILSGRNIK LGAQNVFYED QGAFTGEISP LMLQEIGVEY VIVGHSERRR IFKEDDEFIN RKVKAVLEKG MTPILCVGET LEEREKGLTF CVVEKQVREG FYGLDKEEAK RVVIAYEPVW AIGTGRVATP QQAQEVHAFI RKLLSEMYDE ETAGSIRILY GGSIKPDNFL GLIVQKDIDG GLVGGASLKE SFIELARIMR GVIS // ID PHOU2_THEMA Reviewed; 235 AA. AC Q9X256; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=Phosphate-specific transport system accessory protein PhoU homolog 2; DE Short=Pst system accessory protein PhoU homolog 2; DE AltName: Full=Phosphate uptake regulator PhoU homolog 2; GN Name=phoU2; OrderedLocusNames=TM_1734; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH IRON IONS AND RP NICKEL ION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=15716271; DOI=10.1074/jbc.M414117200; RA Liu J., Lou Y., Yokota H., Adams P.D., Kim R., Kim S.H.; RT "Crystal structure of a PhoU protein homologue: a new class of RT metalloprotein containing multinuclear iron clusters."; RL J. Biol. Chem. 280:15960-15966(2005). CC -!- FUNCTION: Plays a role in the regulation of phosphate uptake. CC {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PhoU family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36799.1; -; Genomic_DNA. DR PIR; E72217; E72217. DR RefSeq; NP_229532.1; NC_000853.1. DR RefSeq; WP_004082252.1; NZ_CP011107.1. DR PDB; 1SUM; X-ray; 2.00 A; B=1-235. DR PDBsum; 1SUM; -. DR ProteinModelPortal; Q9X256; -. DR SMR; Q9X256; 2-225. DR STRING; 243274.TM1734; -. DR EnsemblBacteria; AAD36799; AAD36799; TM_1734. DR GeneID; 897173; -. DR KEGG; tma:TM1734; -. DR PATRIC; 23938444; VBITheMar51294_1752. DR eggNOG; ENOG4105QGT; Bacteria. DR eggNOG; COG0704; LUCA. DR InParanoid; Q9X256; -. DR KO; K02039; -. DR OMA; HMASIVK; -. DR OrthoDB; EOG6Q2SPF; -. DR EvolutionaryTrace; Q9X256; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IEA:InterPro. DR GO; GO:0045936; P:negative regulation of phosphate metabolic process; ISS:UniProtKB. DR GO; GO:2000186; P:negative regulation of phosphate transmembrane transport; ISS:UniProtKB. DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW. DR InterPro; IPR028366; P_trasport_PhoU. DR InterPro; IPR026022; PhoU_dom. DR PANTHER; PTHR10010:SF14; PTHR10010:SF14; 1. DR Pfam; PF01895; PhoU; 2. DR PIRSF; PIRSF003107; PhoU; 1. DR TIGRFAMs; TIGR02135; phoU_full; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Phosphate transport; KW Reference proteome; Transport. FT CHAIN 1 235 Phosphate-specific transport system FT accessory protein PhoU homolog 2. FT /FTId=PRO_0000155183. FT HELIX 5 36 {ECO:0000244|PDB:1SUM}. FT HELIX 39 70 {ECO:0000244|PDB:1SUM}. FT HELIX 75 107 {ECO:0000244|PDB:1SUM}. FT HELIX 118 138 {ECO:0000244|PDB:1SUM}. FT HELIX 142 145 {ECO:0000244|PDB:1SUM}. FT HELIX 147 172 {ECO:0000244|PDB:1SUM}. FT HELIX 174 176 {ECO:0000244|PDB:1SUM}. FT HELIX 177 209 {ECO:0000244|PDB:1SUM}. FT STRAND 213 216 {ECO:0000244|PDB:1SUM}. FT STRAND 219 222 {ECO:0000244|PDB:1SUM}. SQ SEQUENCE 235 AA; 26821 MW; 48558C71B710D831 CRC64; MNRLLNEKVE EFKKGVLKAG WFIEKMFRNS ISSLVERNES LAREVIADEE VVDQMEVEIQ EKAMEVLGLF SPIGKPLLTV TAGIRVAELI ENIADKCHDI AKNVLELMEE PPLKPLEDIP AMANQTSEML KFALRMFADV NVEKSFEVCR MDSKVDDLYE KVREELLLYM MESPKYVKRA LLLLEIAGNI EIIADYATNI VEVSVYMVQG EAYKCYHDEL LLFKKSGGVL FESSD // ID PLSY1_THEMA Reviewed; 203 AA. AC Q9X109; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Glycerol-3-phosphate acyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Acyl-PO4 G3P acyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=G3P acyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01043}; DE Short=GPAT 1 {ECO:0000255|HAMAP-Rule:MF_01043}; DE EC=2.3.1.n3 {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Lysophosphatidic acid synthase 1 {ECO:0000255|HAMAP-Rule:MF_01043}; DE Short=LPA synthase 1 {ECO:0000255|HAMAP-Rule:MF_01043}; GN Name=plsY1 {ECO:0000255|HAMAP-Rule:MF_01043}; GN OrderedLocusNames=TM_1283; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl- CC phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form CC lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate CC as fatty acyl donor, but not acyl-CoA or acyl-ACP. CC {ECO:0000255|HAMAP-Rule:MF_01043}. CC -!- CATALYTIC ACTIVITY: Acyl-phosphate + sn-glycerol 3-phosphate = 1- CC acyl-sn-glycerol 3-phosphate + phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. CC {ECO:0000255|HAMAP-Rule:MF_01043}. CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01043}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36357.1; -; Genomic_DNA. DR PIR; F72273; F72273. DR RefSeq; NP_229087.1; NC_000853.1. DR RefSeq; WP_010865296.1; NZ_CP011107.1. DR STRING; 243274.TM1283; -. DR EnsemblBacteria; AAD36357; AAD36357; TM_1283. DR GeneID; 898200; -. DR KEGG; tma:TM1283; -. DR PATRIC; 23937506; VBITheMar51294_1299. DR eggNOG; ENOG4108X8W; Bacteria. DR eggNOG; COG0344; LUCA. DR InParanoid; Q9X109; -. DR OMA; TFGVWSA; -. DR OrthoDB; EOG6M6JSX; -. DR BioCyc; TMAR243274:GC6P-1314-MONOMER; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01043; PlsY; 1. DR InterPro; IPR003811; G3P_acylTferase_PlsY. DR Pfam; PF02660; G3P_acyltransf; 1. DR SMART; SM01207; G3P_acyltransf; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Lipid biosynthesis; Lipid metabolism; Membrane; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 203 Glycerol-3-phosphate acyltransferase 1. FT /FTId=PRO_0000188479. FT TRANSMEM 2 22 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 52 72 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 82 102 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 117 137 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 150 168 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 170 190 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. SQ SEQUENCE 203 AA; 23186 MW; 5909688C51B4182B CRC64; MLNFFLITIQ FLSGAVMYSH IIAKIKGIDL RKIRDGNPGS SNLWRAAGWK YGFPALMLDY FKGTFPIAFF VWNESFHVNR YVIAFAALSG ILGHAFSPFL KFKGGKAIAT TFGAWSVLTK WEGPMVLGTV FTIFSILHRL RGKNKTTPEE DAFRVMIGFA ALLIYTMWKV FNGMPELAIL YFGNFLIVFY KHRLELRRYL KGV // ID PNP_THEMA Reviewed; 708 AA. AC Q9X166; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595}; DE EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595}; DE AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595}; DE Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595}; GN Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595}; OrderedLocusNames=TM_1345; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in mRNA degradation. Catalyzes the CC phosphorolysis of single-stranded polyribonucleotides processively CC in the 3'- to 5'-direction. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01595}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- SIMILARITY: Belongs to the polyribonucleotide CC nucleotidyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|HAMAP- CC Rule:MF_01595}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|HAMAP- CC Rule:MF_01595}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36416.1; -; Genomic_DNA. DR PIR; A72264; A72264. DR RefSeq; NP_229146.1; NC_000853.1. DR RefSeq; WP_004081541.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X166; -. DR STRING; 243274.TM1345; -. DR EnsemblBacteria; AAD36416; AAD36416; TM_1345. DR GeneID; 898135; -. DR KEGG; tma:TM1345; -. DR PATRIC; 23937628; VBITheMar51294_1357. DR eggNOG; ENOG4107QUF; Bacteria. DR eggNOG; COG1185; LUCA. DR InParanoid; Q9X166; -. DR KO; K00962; -. DR OMA; RFMFHYN; -. DR OrthoDB; EOG6WT8CC; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR Gene3D; 1.10.10.400; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.1370.10; -; 1. DR Gene3D; 3.30.230.70; -; 2. DR HAMAP; MF_01595; PNPase; 1. DR InterPro; IPR001247; ExoRNase_PH_dom1. DR InterPro; IPR015847; ExoRNase_PH_dom2. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR012162; PNPase. DR InterPro; IPR027408; PNPase/RNase_PH_dom. DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR PANTHER; PTHR11252; PTHR11252; 1. DR Pfam; PF00013; KH_1; 1. DR Pfam; PF03726; PNPase; 1. DR Pfam; PF01138; RNase_PH; 2. DR Pfam; PF03725; RNase_PH_C; 2. DR Pfam; PF00575; S1; 1. DR PIRSF; PIRSF005499; PNPase; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR SUPFAM; SSF54791; SSF54791; 1. DR SUPFAM; SSF55666; SSF55666; 2. DR TIGRFAMs; TIGR03591; polynuc_phos; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase. FT CHAIN 1 708 Polyribonucleotide FT nucleotidyltransferase. FT /FTId=PRO_0000329913. FT DOMAIN 555 615 KH. {ECO:0000255|HAMAP-Rule:MF_01595}. FT DOMAIN 625 692 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_01595}. FT METAL 488 488 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01595}. FT METAL 494 494 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01595}. SQ SEQUENCE 708 AA; 78621 MW; EC60D158C1725BC7 CRC64; MKEWRRNILG RELVVQYGKV AKQSSGSALV RFGDTVVLAT ANISDKAVEG IDFVPLTVEF QERFYAAGKI PGGFIKREGK PSESAILSAR LIDRPIRPLF PKKLRNEVQV IVTVLSVDPN VPPDVVGIFA ASLALNVSKI PFEGIVAGIR VGYRDGQFIA LPSEEDIEKG LMDITVAGTK DAVTMVEGEA KEVTEEDMVK ALRFAHSVIK ELVDFQEEIL SEFNVEKIPV VEPTPPEGLV EAFKDLLNKE ELERRILVKV KKEREVALKE YEEQLLNQIA EKLSVTDLEG IKPFVSELYE DAVKKTMRRL IVEKGIRADG RKPTEIRPIS CEVGLFPRTH GSALFTRGET QSLGIVTLGA PMDVQIIDTL LEEGVKRFML HYNFPPFCTG EVKPLRGPSR REIGHGHLAE RALKNMLPPE EEFPYTIRVV SEILESNGSS SMATVCSGSL ALMDAGVPIK KHVAGIAMGL ILEEDAEIIL TDIIGMEDHY GDMDFKVAGT RDGITAFQMD CKVSGVSDEL LMKALMQARE ARMYILDRMY ETISAPRPHL SKYAPIIKVT KVDPEKVADV IGPGGRVIKK IIKDFDVKVE IDDETGLVKV VGSSEENVDK AIELIREIAK EIEVGEVLEG KVTRIEPYGL FIEVRPGKIG LLHQSKVGED MRQFLKKVKV GDTIKVQVIN IDDLGRLQFK RVTEGENTQH GKTHSKRN // ID PLSY2_THEMA Reviewed; 196 AA. AC Q9X1F9; DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=Glycerol-3-phosphate acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Acyl-PO4 G3P acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Acyl-phosphate--glycerol-3-phosphate acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=G3P acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01043}; DE Short=GPAT 2 {ECO:0000255|HAMAP-Rule:MF_01043}; DE EC=2.3.1.n3 {ECO:0000255|HAMAP-Rule:MF_01043}; DE AltName: Full=Lysophosphatidic acid synthase 2 {ECO:0000255|HAMAP-Rule:MF_01043}; DE Short=LPA synthase 2 {ECO:0000255|HAMAP-Rule:MF_01043}; GN Name=plsY2 {ECO:0000255|HAMAP-Rule:MF_01043}; GN OrderedLocusNames=TM_1447; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl- CC phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form CC lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate CC as fatty acyl donor, but not acyl-CoA or acyl-ACP. CC {ECO:0000255|HAMAP-Rule:MF_01043}. CC -!- CATALYTIC ACTIVITY: Acyl-phosphate + sn-glycerol 3-phosphate = 1- CC acyl-sn-glycerol 3-phosphate + phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. CC {ECO:0000255|HAMAP-Rule:MF_01043}. CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01043}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36515.1; -; Genomic_DNA. DR PIR; C72253; C72253. DR RefSeq; NP_229246.1; NC_000853.1. DR RefSeq; WP_004081723.1; NZ_CP011107.1. DR STRING; 243274.TM1447; -. DR EnsemblBacteria; AAD36515; AAD36515; TM_1447. DR GeneID; 898029; -. DR KEGG; tma:TM1447; -. DR PATRIC; 23937846; VBITheMar51294_1461. DR eggNOG; ENOG4105K7Z; Bacteria. DR eggNOG; COG0344; LUCA. DR InParanoid; Q9X1F9; -. DR KO; K08591; -. DR OMA; ICRFTER; -. DR OrthoDB; EOG6M6JSX; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01043; PlsY; 1. DR InterPro; IPR003811; G3P_acylTferase_PlsY. DR PANTHER; PTHR30309:SF0; PTHR30309:SF0; 1. DR Pfam; PF02660; G3P_acyltransf; 1. DR SMART; SM01207; G3P_acyltransf; 1. DR TIGRFAMs; TIGR00023; TIGR00023; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Lipid biosynthesis; Lipid metabolism; Membrane; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 196 Glycerol-3-phosphate acyltransferase 2. FT /FTId=PRO_0000188480. FT TRANSMEM 2 22 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 52 72 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 80 100 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 112 132 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 137 156 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. SQ SEQUENCE 196 AA; 21343 MW; 5AD53DD5C502AB90 CRC64; MGWWLFPILG YFIGSIPFSY LIPKWLKGID VRKVGSGNVG ATNAIRTTGP AVGGICLLLD ALKGFFPVFI TITFSGDSKI VSLTAIATVL GHDFPIFMKF KGGKGVASTL GIIFCLSWPT GLVFTLTWLV IVMLTKYASL GSLVALYVSA LLGYLLKGYD TGMLFLILAV LSTLRHSENI QRLLNGTERK VNLFKR // ID PORC_THEMA Reviewed; 192 AA. AC O05650; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 13-APR-2016, entry version 108. DE RecName: Full=Pyruvate synthase subunit PorC; DE EC=1.2.7.1; DE AltName: Full=Pyruvate oxidoreductase gamma chain; DE Short=POR; DE AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit gamma; GN Name=porC; Synonyms=porG; OrderedLocusNames=TM_0015; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-20. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8550425; RA Kletzin A., Adams M.W.W.; RT "Molecular and phylogenetic characterization of pyruvate and 2- RT ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus RT and pyruvate ferredoxin oxidoreductase from Thermotoga maritima."; RL J. Bacteriol. 178:248-257(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: Pyruvate + CoA + 2 oxidized ferredoxin = CC acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one CC gamma chain. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35109.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA59455.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X85171; CAA59455.1; ALT_INIT; Genomic_DNA. DR EMBL; AE000512; AAD35109.1; ALT_INIT; Genomic_DNA. DR PIR; C59427; A72427. DR RefSeq; NP_227831.1; NC_000853.1. DR RefSeq; WP_004082456.1; NZ_CP011107.1. DR PDB; 2RAA; X-ray; 2.12 A; A=1-192. DR PDBsum; 2RAA; -. DR ProteinModelPortal; O05650; -. DR SMR; O05650; 5-192. DR STRING; 243274.TM0015; -. DR EnsemblBacteria; AAD35109; AAD35109; TM_0015. DR GeneID; 896829; -. DR KEGG; tma:TM0015; -. DR PATRIC; 23934870; VBITheMar51294_0013. DR eggNOG; ENOG4105EJ5; Bacteria. DR eggNOG; COG1014; LUCA. DR InParanoid; O05650; -. DR KO; K00172; -. DR OMA; FEIRWHA; -. DR OrthoDB; EOG6VMTKB; -. DR BioCyc; MetaCyc:MONOMER-425; -. DR EvolutionaryTrace; O05650; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.920.10; -; 1. DR InterPro; IPR011894; PorC_KorC. DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat. DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen. DR Pfam; PF01558; POR; 1. DR SUPFAM; SSF53323; SSF53323; 1. DR TIGRFAMs; TIGR02175; PorC_KorC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8550425}. FT CHAIN 2 192 Pyruvate synthase subunit PorC. FT /FTId=PRO_0000099917. FT CONFLICT 23 23 A -> V (in Ref. 1; CAA59455). FT {ECO:0000305}. FT STRAND 7 15 {ECO:0000244|PDB:2RAA}. FT HELIX 20 33 {ECO:0000244|PDB:2RAA}. FT STRAND 38 43 {ECO:0000244|PDB:2RAA}. FT STRAND 52 60 {ECO:0000244|PDB:2RAA}. FT STRAND 74 80 {ECO:0000244|PDB:2RAA}. FT HELIX 81 83 {ECO:0000244|PDB:2RAA}. FT HELIX 86 89 {ECO:0000244|PDB:2RAA}. FT STRAND 96 101 {ECO:0000244|PDB:2RAA}. FT HELIX 106 113 {ECO:0000244|PDB:2RAA}. FT STRAND 117 122 {ECO:0000244|PDB:2RAA}. FT HELIX 124 131 {ECO:0000244|PDB:2RAA}. FT STRAND 132 134 {ECO:0000244|PDB:2RAA}. FT HELIX 138 149 {ECO:0000244|PDB:2RAA}. FT HELIX 154 164 {ECO:0000244|PDB:2RAA}. FT HELIX 171 187 {ECO:0000244|PDB:2RAA}. SQ SEQUENCE 192 AA; 21270 MW; C58296B289254B70 CRC64; MPVAKKYFEI RWHGRAGQGA KSASQMLAEA ALEAGKYVQA FPEYGAERTG APMRAFNRIG DEYIRVRSAV ENPDVVVVID ETLLSPAIVE GLSEDGILLV NTVKDFEFVR KKTGFNGKIC VVDATDIALQ EIKRGIPNTP MLGALVRVTG IVPLEAIEKR IEKMFGKKFP QEVIDANKRA LRRGYEEVKC SE // ID PIMT_THEMA Reviewed; 317 AA. AC Q56308; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 120. DE RecName: Full=Protein-L-isoaspartate O-methyltransferase; DE EC=2.1.1.77; DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase; DE AltName: Full=Protein L-isoaspartyl methyltransferase; DE AltName: Full=Protein-beta-aspartate methyltransferase; DE Short=PIMT; GN Name=pcm; OrderedLocusNames=TM_0704; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8550470; RA Swanson R.V., Sanna M.G., Simon M.I.; RT "Thermostable chemotaxis proteins from the hyperthermophilic bacterium RT Thermotoga maritima."; RL J. Bacteriol. 178:484-489(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP CHARACTERIZATION. RX PubMed=9784234; DOI=10.1006/abbi.1998.0830; RA Ichikawa J.K., Clarke S.; RT "A highly active protein repair enzyme from an extreme thermophile: RT the L-isoaspartyl methyltransferase from Thermotoga maritima."; RL Arch. Biochem. Biophys. 358:222-231(1998). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=11080641; DOI=10.1016/S0969-2126(00)00522-0; RA Skinner M.M., Puvathingal J.M., Walter R.L., Friedman A.M.; RT "Crystal structure of protein isoaspartyl methyltransferase. A RT catalyst for protein repair."; RL Structure 8:1189-1201(2000). CC -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl CC residues in peptides and proteins that result from spontaneous CC decomposition of normal L-aspartyl and L-asparaginyl residues. It CC plays a role in the repair and/or degradation of damaged proteins. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L- CC isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate CC alpha-methyl ester. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Vmax=164 nmol/min/mg enzyme with KASA (isoD) LAKY as substrate CC at 85 degrees Celsius; CC Temperature dependence: CC Optimum temperature is 85 degrees Celsius. Highly thermostable, CC with no loss of activity after 60 min at 100 degrees Celsius. CC Enzyme activity is observed at temperatures as high as 93 CC degrees Celsius.; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L- CC isoaspartyl/D-aspartyl protein methyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U30501; AAA96385.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35786.1; -; Genomic_DNA. DR PIR; G72342; G72342. DR RefSeq; NP_228513.1; NC_000853.1. DR RefSeq; WP_004081036.1; NZ_CP011107.1. DR PDB; 1DL5; X-ray; 1.80 A; A/B=1-317. DR PDBsum; 1DL5; -. DR ProteinModelPortal; Q56308; -. DR SMR; Q56308; 1-317. DR STRING; 243274.TM0704; -. DR EnsemblBacteria; AAD35786; AAD35786; TM_0704. DR GeneID; 898371; -. DR KEGG; tma:TM0704; -. DR PATRIC; 23936326; VBITheMar51294_0716. DR eggNOG; ENOG4105E26; Bacteria. DR eggNOG; COG2518; LUCA. DR InParanoid; Q56308; -. DR KO; K00573; -. DR OMA; FARILVT; -. DR OrthoDB; EOG644ZP2; -. DR EvolutionaryTrace; Q56308; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030091; P:protein repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR Gene3D; 3.55.20.10; -; 1. DR HAMAP; MF_00090; PIMT; 1. DR InterPro; IPR000682; PCMT. DR InterPro; IPR009107; PIM_MeTrfase_C. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR11579; PTHR11579; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR SUPFAM; SSF68930; SSF68930; 1. DR PROSITE; PS01279; PCMT; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 317 Protein-L-isoaspartate O- FT methyltransferase. FT /FTId=PRO_0000111905. FT ACT_SITE 59 59 {ECO:0000250}. FT HELIX 2 11 {ECO:0000244|PDB:1DL5}. FT HELIX 16 24 {ECO:0000244|PDB:1DL5}. FT HELIX 27 30 {ECO:0000244|PDB:1DL5}. FT HELIX 37 40 {ECO:0000244|PDB:1DL5}. FT STRAND 42 44 {ECO:0000244|PDB:1DL5}. FT STRAND 46 50 {ECO:0000244|PDB:1DL5}. FT STRAND 55 58 {ECO:0000244|PDB:1DL5}. FT HELIX 61 70 {ECO:0000244|PDB:1DL5}. FT STRAND 78 82 {ECO:0000244|PDB:1DL5}. FT HELIX 88 97 {ECO:0000244|PDB:1DL5}. FT STRAND 102 108 {ECO:0000244|PDB:1DL5}. FT HELIX 110 122 {ECO:0000244|PDB:1DL5}. FT STRAND 127 133 {ECO:0000244|PDB:1DL5}. FT HELIX 135 137 {ECO:0000244|PDB:1DL5}. FT HELIX 140 142 {ECO:0000244|PDB:1DL5}. FT STRAND 145 150 {ECO:0000244|PDB:1DL5}. FT STRAND 152 155 {ECO:0000244|PDB:1DL5}. FT HELIX 159 164 {ECO:0000244|PDB:1DL5}. FT STRAND 165 175 {ECO:0000244|PDB:1DL5}. FT HELIX 178 180 {ECO:0000244|PDB:1DL5}. FT STRAND 184 191 {ECO:0000244|PDB:1DL5}. FT STRAND 194 202 {ECO:0000244|PDB:1DL5}. FT HELIX 210 212 {ECO:0000244|PDB:1DL5}. FT HELIX 215 220 {ECO:0000244|PDB:1DL5}. FT STRAND 228 233 {ECO:0000244|PDB:1DL5}. FT HELIX 237 248 {ECO:0000244|PDB:1DL5}. FT STRAND 251 254 {ECO:0000244|PDB:1DL5}. FT STRAND 257 261 {ECO:0000244|PDB:1DL5}. FT STRAND 263 270 {ECO:0000244|PDB:1DL5}. FT STRAND 273 278 {ECO:0000244|PDB:1DL5}. FT HELIX 281 292 {ECO:0000244|PDB:1DL5}. FT TURN 293 295 {ECO:0000244|PDB:1DL5}. FT HELIX 298 300 {ECO:0000244|PDB:1DL5}. FT STRAND 301 309 {ECO:0000244|PDB:1DL5}. FT STRAND 312 314 {ECO:0000244|PDB:1DL5}. SQ SEQUENCE 317 AA; 36400 MW; 2FE6019571ADDF2C CRC64; MREKLFWILK KYGVSDHIAK AFLEIPREEF LTKSYPLSYV YEDIVLVSYD DGEEYSTSSQ PSLMALFMEW VGLDKGMRVL EIGGGTGYNA AVMSRVVGEK GLVVSVEYSR KICEIAKRNV ERLGIENVIF VCGDGYYGVP EFSPYDVIFV TVGVDEVPET WFTQLKEGGR VIVPINLKLS RRQPAFLFKK KDPYLVGNYK LETRFITAGG NLGNLLERNR KLLREFPFNR EILLVRSHIF VELVDLLTRR LTEIDGTFYY AGPNGVVEFL DDRMRIYGDA PEIENLLTQW ESCGYRSFEY LMLHVGYNAF SHISCSI // ID PORA_THEMA Reviewed; 392 AA. AC O05651; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 2. DT 11-MAY-2016, entry version 103. DE RecName: Full=Pyruvate synthase subunit PorA; DE EC=1.2.7.1; DE AltName: Full=Pyruvate oxidoreductase alpha chain; DE Short=POR; DE AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit alpha; GN Name=porA; OrderedLocusNames=TM_0017; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-43. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8550425; RA Kletzin A., Adams M.W.W.; RT "Molecular and phylogenetic characterization of pyruvate and 2- RT ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus RT and pyruvate ferredoxin oxidoreductase from Thermotoga maritima."; RL J. Bacteriol. 178:248-257(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP PROTEIN SEQUENCE OF 1-43, AND CHARACTERIZATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8305426; DOI=10.1021/bi00170a019; RA Blamey J.M., Adams M.W.W.; RT "Characterization of an ancestral type of pyruvate ferredoxin RT oxidoreductase from the hyperthermophilic bacterium, Thermotoga RT maritima."; RL Biochemistry 33:1000-1007(1994). CC -!- CATALYTIC ACTIVITY: Pyruvate + CoA + 2 oxidized ferredoxin = CC acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one CC gamma chain. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35111.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA59457.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X85171; CAA59457.1; ALT_INIT; Genomic_DNA. DR EMBL; AE000512; AAD35111.1; ALT_INIT; Genomic_DNA. DR PIR; D59427; C72427. DR RefSeq; NP_227833.1; NC_000853.1. DR RefSeq; WP_004082460.1; NZ_CP011107.1. DR RefSeq; WP_010865028.1; NC_000853.1. DR ProteinModelPortal; O05651; -. DR STRING; 243274.TM0017; -. DR EnsemblBacteria; AAD35111; AAD35111; TM_0017. DR GeneID; 896831; -. DR KEGG; tma:TM0017; -. DR PATRIC; 23934874; VBITheMar51294_0015. DR eggNOG; ENOG4105D95; Bacteria. DR eggNOG; COG0674; LUCA. DR InParanoid; O05651; -. DR KO; K00169; -. DR OMA; WHFEHKA; -. DR OrthoDB; EOG68H83G; -. DR BioCyc; MetaCyc:MONOMER-423; -. DR BioCyc; TMAR243274:GC6P-17-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR033412; PFOR_II. DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR Pfam; PF17147; PFOR_II; 1. DR Pfam; PF01855; POR_N; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR SUPFAM; SSF52922; SSF52922; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Oxidoreductase; KW Reference proteome. FT CHAIN 1 392 Pyruvate synthase subunit PorA. FT /FTId=PRO_0000099902. FT COMPBIAS 72 79 Poly-Ala. SQ SEQUENCE 392 AA; 44112 MW; ACEF0E34C9EC1818 CRC64; MERVVERVAV TGAEAVANAM RQIEPDVVAA YPITPQTPIV EYFARFVADG VVRTEMIPVE SEHSAMSAVV GAAAAGARAM TATSANGLAL MHEIVYIAAS YRLPIVMPVV NRALSGPINI HCDHSDAMAE RDSGWIQLFA ETNQEAYDFT ILAVRLAEHE DVRLPVMVNL DGFILSHGVE PVEFYPDELV KKFVGELKPM YPLLDTEHPV TWGPLDLYDY YFEHKRQQIE AMENVKKVFP EIAKEFEETF GRKYWFVEPY RMEDAEHVMV ALGSTNSTIK YVVDELREEG YKVGSLKIWM FRPFPKEQLQ ELLNGRKSVV VLDRAVSFGA EAPLYEAVKS ALYEVAARPM LGSYVYGLGG RDIKPEHIRK AFEDAINGNL IADEQRYLGL RE // ID PORD_THEMA Reviewed; 99 AA. AC Q56316; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-MAY-2016, entry version 122. DE RecName: Full=Pyruvate synthase subunit PorD; DE AltName: Full=Pyruvate oxidoreductase delta chain; DE Short=POR; DE AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit delta; GN Name=porD; OrderedLocusNames=TM_0016; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8550425; RA Kletzin A., Adams M.W.W.; RT "Molecular and phylogenetic characterization of pyruvate and 2- RT ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus RT and pyruvate ferredoxin oxidoreductase from Thermotoga maritima."; RL J. Bacteriol. 178:248-257(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P94692}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:P94692}; CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one CC gamma chain. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35110.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X85171; CAA59456.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35110.1; ALT_INIT; Genomic_DNA. DR PIR; A59427; B72427. DR RefSeq; NP_227832.1; NC_000853.1. DR RefSeq; WP_004082458.1; NZ_CP011107.1. DR RefSeq; WP_010865027.1; NC_000853.1. DR ProteinModelPortal; Q56316; -. DR STRING; 243274.TM0016; -. DR EnsemblBacteria; AAD35110; AAD35110; TM_0016. DR GeneID; 896830; -. DR KEGG; tma:TM0016; -. DR PATRIC; 23934872; VBITheMar51294_0014. DR eggNOG; ENOG4105WGB; Bacteria. DR eggNOG; COG1144; LUCA. DR InParanoid; Q56316; -. DR KO; K00171; -. DR OMA; CWIFCPD; -. DR OrthoDB; EOG6R5C9P; -. DR BioCyc; MetaCyc:MONOMER-426; -. DR BioCyc; TMAR243274:GC6P-16-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR011898; PorD_KorD. DR TIGRFAMs; TIGR02179; PorD_KorD; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Direct protein sequencing; KW Electron transport; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; Repeat; Transport. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8550425}. FT CHAIN 2 99 Pyruvate synthase subunit PorD. FT /FTId=PRO_0000099924. FT DOMAIN 32 60 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 61 91 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 41 41 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 44 44 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 47 47 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 51 51 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 71 71 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 74 74 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 77 77 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 81 81 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. SQ SEQUENCE 99 AA; 11257 MW; C4253752589812F9 CRC64; MSLKSWKEIP IGGVIDKPGT AREYKTGAWR VMRPILHKEK CIDCMFCWLY CPDQAIIQEG GIMKGFNYDY CKGCGLCANV CPKQAIEMRP ETEFLSEEG // ID PPAC_THEMA Reviewed; 548 AA. AC Q9WZ56; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 111. DE RecName: Full=Probable manganese-dependent inorganic pyrophosphatase; DE EC=3.6.1.1; DE AltName: Full=Pyrophosphate phospho-hydrolase; DE Short=PPase; GN Name=ppaC; OrderedLocusNames=TM_0587; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35672.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35672.1; ALT_INIT; Genomic_DNA. DR PIR; D72359; D72359. DR RefSeq; NP_228397.1; NC_000853.1. DR RefSeq; WP_010865153.1; NC_000853.1. DR ProteinModelPortal; Q9WZ56; -. DR STRING; 243274.TM0587; -. DR PRIDE; Q9WZ56; -. DR EnsemblBacteria; AAD35672; AAD35672; TM_0587. DR GeneID; 897659; -. DR KEGG; tma:TM0587; -. DR PATRIC; 23936085; VBITheMar51294_0596. DR eggNOG; ENOG4105E2M; Bacteria. DR eggNOG; COG0517; LUCA. DR eggNOG; COG1227; LUCA. DR InParanoid; Q9WZ56; -. DR KO; K15986; -. DR OMA; TIIANMF; -. DR OrthoDB; EOG6F81QM; -. DR BioCyc; TMAR243274:GC6P-612-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central. DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006798; P:polyphosphate catabolic process; IBA:GO_Central. DR Gene3D; 3.40.1390.20; -; 1. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR004097; DHHA2. DR InterPro; IPR010766; DRTGG. DR InterPro; IPR028979; Ser_kin/Pase_Hpr_N-like. DR Pfam; PF00571; CBS; 2. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02833; DHHA2; 1. DR Pfam; PF07085; DRTGG; 1. DR SMART; SM00116; CBS; 2. DR SMART; SM01131; DHHA2; 1. DR SUPFAM; SSF75138; SSF75138; 1. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Complete proteome; Cytoplasm; Hydrolase; Manganese; KW Metal-binding; Reference proteome; Repeat. FT CHAIN 1 548 Probable manganese-dependent inorganic FT pyrophosphatase. FT /FTId=PRO_0000158597. FT DOMAIN 77 132 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 254 311 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT REGION 1 74 PPase part 1. FT REGION 306 548 PPase part 2. FT METAL 12 12 Manganese 1. {ECO:0000250}. FT METAL 16 16 Manganese 1. {ECO:0000250}. FT METAL 18 18 Manganese 2. {ECO:0000250}. FT METAL 312 312 Manganese 1. {ECO:0000250}. FT METAL 312 312 Manganese 2. {ECO:0000250}. FT METAL 334 334 Manganese 2. {ECO:0000250}. FT METAL 386 386 Manganese 2. {ECO:0000250}. SQ SEQUENCE 548 AA; 61364 MW; D1CF282F70EA56DE CRC64; MKALERVYVI GHKNPDTDSV CSAIGYAHFK NNVEKGKTFI PARSGDLTNE SLFVLKYFGM NPPLHIETLE PTVEDLELKN PIFVTPDTSA YDVAMLMESR GIKNVPVVSK EKMIGVVTES NIARVYVRRL KIEPLVIHPV PFDQLVRILK AEVVCDYMKE KTVSGKVHIA VDALHVLLGK IEIGDVVIVG DNEPAQIALL EKGAKLMIVV NNAPVSNRVL EIAKEKNAAV LRVKFDAFSA AKLINLSLPV TLVMSKKFPT VTKKDTLEEV KEIVFTSKIR AAFVEDEKGR LCGVITRTDL LKDVRKKVIL VDHNEITQAP EGVEKAEILE IIDHHRLGGL STLNPVFFYN EPVGSTSTIV AEFFLKNGVK MEREIAGILL SGIVSDTLFF KLSTTTEKDR KMANFLADVA KLDLEKFAKK LLKEGMKIPE DVDPAELLKR DVKVYEMGEE SFAVSQIMTS DFSTLLKEKE RFMNTLKTLK GEFGVKHFFV LFTNPVEEAS LLMMDGDQKL VEKAFNAEKK DGLFLLKGVM SRKKDFVPKI GEVLRRER // ID PROA_THEMA Reviewed; 415 AA. AC Q9WYC9; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 128. DE RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00412}; DE Short=GPR {ECO:0000255|HAMAP-Rule:MF_00412}; DE EC=1.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00412}; DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412}; DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412}; DE Short=GSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412}; GN Name=proA {ECO:0000255|HAMAP-Rule:MF_00412}; GN OrderedLocusNames=TM_0293; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate CC 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The CC product spontaneously undergoes cyclization to form 1-pyrroline-5- CC carboxylate. {ECO:0000255|HAMAP-Rule:MF_00412}. CC -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate + CC NADP(+) = L-glutamyl 5-phosphate + NADPH. {ECO:0000255|HAMAP- CC Rule:MF_00412}. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 5-semialdehyde from L-glutamate: step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_00412}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}. CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase CC family. {ECO:0000255|HAMAP-Rule:MF_00412}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35381.1; -; Genomic_DNA. DR PIR; E72394; E72394. DR RefSeq; NP_228105.1; NC_000853.1. DR RefSeq; WP_004083010.1; NZ_CP011107.1. DR PDB; 1O20; X-ray; 2.00 A; A=1-415. DR PDBsum; 1O20; -. DR ProteinModelPortal; Q9WYC9; -. DR SMR; Q9WYC9; 2-415. DR STRING; 243274.TM0293; -. DR PRIDE; Q9WYC9; -. DR EnsemblBacteria; AAD35381; AAD35381; TM_0293. DR GeneID; 897218; -. DR KEGG; tma:TM0293; -. DR PATRIC; 23935465; VBITheMar51294_0298. DR eggNOG; ENOG4105C2S; Bacteria. DR eggNOG; COG0014; LUCA. DR InParanoid; Q9WYC9; -. DR KO; K00147; -. DR OMA; CNAIETL; -. DR OrthoDB; EOG6FFSCX; -. DR BRENDA; 1.2.1.41; 6331. DR UniPathway; UPA00098; UER00360. DR EvolutionaryTrace; Q9WYC9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IBA:GO_Central. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006561; P:proline biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 2. DR HAMAP; MF_00412; ProA; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR020593; G-glutamylP_reductase_CS. DR InterPro; IPR012134; Glu-5-SA_DH. DR InterPro; IPR000965; GPR_dom. DR Pfam; PF00171; Aldedh; 2. DR PIRSF; PIRSF000151; GPR; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR00407; proA; 1. DR PROSITE; PS01223; PROA; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW NADP; Oxidoreductase; Proline biosynthesis; Reference proteome. FT CHAIN 1 415 Gamma-glutamyl phosphate reductase. FT /FTId=PRO_0000189802. FT HELIX 3 18 {ECO:0000244|PDB:1O20}. FT HELIX 23 39 {ECO:0000244|PDB:1O20}. FT HELIX 41 57 {ECO:0000244|PDB:1O20}. FT HELIX 62 68 {ECO:0000244|PDB:1O20}. FT HELIX 72 87 {ECO:0000244|PDB:1O20}. FT STRAND 95 100 {ECO:0000244|PDB:1O20}. FT STRAND 106 113 {ECO:0000244|PDB:1O20}. FT STRAND 117 120 {ECO:0000244|PDB:1O20}. FT HELIX 126 137 {ECO:0000244|PDB:1O20}. FT STRAND 142 145 {ECO:0000244|PDB:1O20}. FT HELIX 148 150 {ECO:0000244|PDB:1O20}. FT HELIX 151 165 {ECO:0000244|PDB:1O20}. FT STRAND 168 170 {ECO:0000244|PDB:1O20}. FT HELIX 172 174 {ECO:0000244|PDB:1O20}. FT STRAND 175 177 {ECO:0000244|PDB:1O20}. FT HELIX 184 189 {ECO:0000244|PDB:1O20}. FT TURN 193 195 {ECO:0000244|PDB:1O20}. FT STRAND 197 201 {ECO:0000244|PDB:1O20}. FT HELIX 205 214 {ECO:0000244|PDB:1O20}. FT STRAND 227 231 {ECO:0000244|PDB:1O20}. FT HELIX 237 249 {ECO:0000244|PDB:1O20}. FT STRAND 257 264 {ECO:0000244|PDB:1O20}. FT HELIX 265 281 {ECO:0000244|PDB:1O20}. FT STRAND 285 288 {ECO:0000244|PDB:1O20}. FT HELIX 290 295 {ECO:0000244|PDB:1O20}. FT STRAND 299 301 {ECO:0000244|PDB:1O20}. FT HELIX 304 306 {ECO:0000244|PDB:1O20}. FT STRAND 313 323 {ECO:0000244|PDB:1O20}. FT HELIX 324 334 {ECO:0000244|PDB:1O20}. FT STRAND 337 343 {ECO:0000244|PDB:1O20}. FT HELIX 347 356 {ECO:0000244|PDB:1O20}. FT STRAND 359 366 {ECO:0000244|PDB:1O20}. FT HELIX 368 370 {ECO:0000244|PDB:1O20}. FT TURN 373 377 {ECO:0000244|PDB:1O20}. FT STRAND 387 390 {ECO:0000244|PDB:1O20}. FT HELIX 398 400 {ECO:0000244|PDB:1O20}. FT STRAND 401 408 {ECO:0000244|PDB:1O20}. SQ SEQUENCE 415 AA; 46404 MW; 95BD703ACBE6F2AA CRC64; MDELLEKAKK VREAWDVLRN ATTREKNKAI KKIAEKLDER RKEILEANRI DVEKARERGV KESLVDRLAL NDKRIDEMIK ACETVIGLKD PVGEVIDSWV REDGLRIARV RVPIGPIGII YESRPNVTVE TTILALKSGN TILLRGGSDA LNSNKAIVSA IREALKETEI PESSVEFIEN TDRSLVLEMI RLREYLSLVI PRGGYGLISF VRDNATVPVL ETGVGNCHIF VDESADLKKA VPVIINAKTQ RPGTCNAAEK LLVHEKIAKE FLPVIVEELR KHGVEVRGCE KTREIVPDVV PATEDDWPTE YLDLIIAIKV VKNVDEAIEH IKKYSTGHSE SILTENYSNA KKFVSEIDAA AVYVNASTRF TDGGQFGFGA EIGISTQRFH ARGPVGLREL TTYKFVVLGE YHVRE // ID PROB_THEMA Reviewed; 353 AA. AC Q9WYD0; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Glutamate 5-kinase {ECO:0000255|HAMAP-Rule:MF_00456}; DE EC=2.7.2.11 {ECO:0000255|HAMAP-Rule:MF_00456}; DE AltName: Full=Gamma-glutamyl kinase {ECO:0000255|HAMAP-Rule:MF_00456}; DE Short=GK {ECO:0000255|HAMAP-Rule:MF_00456}; GN Name=proB {ECO:0000255|HAMAP-Rule:MF_00456}; GN OrderedLocusNames=TM_0294; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate CC to form L-glutamate 5-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00456}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 5-semialdehyde from L-glutamate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000255|HAMAP- CC Rule:MF_00456}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35382.1; -; Genomic_DNA. DR PIR; F72394; F72394. DR RefSeq; NP_228106.1; NC_000853.1. DR RefSeq; WP_010865089.1; NC_000853.1. DR ProteinModelPortal; Q9WYD0; -. DR STRING; 243274.TM0294; -. DR EnsemblBacteria; AAD35382; AAD35382; TM_0294. DR GeneID; 897219; -. DR KEGG; tma:TM0294; -. DR PATRIC; 23935467; VBITheMar51294_0299. DR eggNOG; ENOG4105CGT; Bacteria. DR eggNOG; COG0263; LUCA. DR InParanoid; Q9WYD0; -. DR KO; K00931; -. DR OMA; KMNKQWI; -. DR OrthoDB; EOG6PGK7G; -. DR BioCyc; TMAR243274:GC6P-307-MONOMER; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004349; F:glutamate 5-kinase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006561; P:proline biosynthetic process; IBA:GO_Central. DR Gene3D; 2.30.130.10; -; 1. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_00456; ProB; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR InterPro; IPR011529; Glu_5kinase. DR InterPro; IPR005715; Glu_5kinase/COase_Synthase. DR InterPro; IPR019797; Glutamate_5-kinase_CS. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01472; PUA; 1. DR PIRSF; PIRSF000729; GK; 1. DR PRINTS; PR00474; GLU5KINASE. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR01027; proB; 1. DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1. DR PROSITE; PS50890; PUA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Proline biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 353 Glutamate 5-kinase. FT /FTId=PRO_0000109746. FT DOMAIN 262 339 PUA. {ECO:0000255|HAMAP-Rule:MF_00456}. FT NP_BIND 198 204 ATP. {ECO:0000255|HAMAP-Rule:MF_00456}. FT BINDING 8 8 ATP. {ECO:0000255|HAMAP-Rule:MF_00456}. FT BINDING 47 47 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00456}. FT BINDING 134 134 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00456}. FT BINDING 146 146 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00456}. SQ SEQUENCE 353 AA; 38320 MW; 72E3171CBBB9F760 CRC64; MIMKVVVKVG SNLLVGSSGL RKSYIAELCR EVARLKSQGH EISIITSGAR AAGFTYLGKG KRTQDLHIKQ ALCAVGQVQL MKVYENAFDF YGIKIAQILL TRDTFSNRKR YLNLRNTLIG LSEFDVVPIV NENDTVATEE ITLGDNDTLA AMFSIAWDAD FLVLFTTVDG VIDENGKLVE RFDESVKLKD MGKSSWGTGG IRSKIESALM ASRCGVKATI CSGNDVSNLT RFVKGEPVGT VFEPQGRLKA KKAWIAFLSE PAGKIYVNKG AEEALKSGNS LLPVGVTGVE GTFDVGDVVE IVNEEGELVG RGIVNYSSSD LEKIAGHKSS DLKKILGYEG NKVVVHIDNM WVA // ID PORB_THEMA Reviewed; 324 AA. AC Q56317; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 13-APR-2016, entry version 103. DE RecName: Full=Pyruvate synthase subunit PorB; DE EC=1.2.7.1; DE AltName: Full=Pyruvate oxidoreductase beta chain; DE Short=POR; DE AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit beta; GN Name=porB; OrderedLocusNames=TM_0018; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-17 AND RP 20-44. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8550425; RA Kletzin A., Adams M.W.W.; RT "Molecular and phylogenetic characterization of pyruvate and 2- RT ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus RT and pyruvate ferredoxin oxidoreductase from Thermotoga maritima."; RL J. Bacteriol. 178:248-257(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: Pyruvate + CoA + 2 oxidized ferredoxin = CC acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P94692}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. CC {ECO:0000250|UniProtKB:P94692}; CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one CC gamma chain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X85171; CAA59458.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35112.1; -; Genomic_DNA. DR PIR; B59427; D72427. DR RefSeq; NP_227834.1; NC_000853.1. DR RefSeq; WP_004082462.1; NZ_CP011107.1. DR STRING; 243274.TM0018; -. DR EnsemblBacteria; AAD35112; AAD35112; TM_0018. DR GeneID; 896832; -. DR KEGG; tma:TM0018; -. DR PATRIC; 23934876; VBITheMar51294_0016. DR eggNOG; ENOG4105DDK; Bacteria. DR eggNOG; COG1013; LUCA. DR InParanoid; Q56317; -. DR KO; K00170; -. DR OMA; LNITYRP; -. DR OrthoDB; EOG6CS02G; -. DR BioCyc; MetaCyc:MONOMER-424; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR SUPFAM; SSF52518; SSF52518; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Direct protein sequencing; Iron; KW Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8550425}. FT CHAIN 2 324 Pyruvate synthase subunit PorB. FT /FTId=PRO_0000099909. FT METAL 26 26 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 29 29 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 57 57 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 228 228 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. SQ SEQUENCE 324 AA; 36385 MW; 2425239D778A6A0E CRC64; MPVNIKQLAQ EFDKKEIGIT QGHRLCPGCG APITVKFVMM IARHLGYEPV VGLATGCLEV STSIYPYTAW SVPYIHNAFE NVAATMSGVE TAYKALKNKG KIPEDKKYAF IAFGGDGGTY DIGLQSLSGM LERGHKVLYV LYDNEGYMNT GNQRSGSTPP GSDTTTAPVG KKLPGKVQLK KNIVEIVAAH ENVYAATASL SEPMDFFAKV EKALNFDGPS FLAVFSPCVR FWRVNDDKTV EISKLAVETK YWPLYEVERG VYRVTRKPRQ FKPVEEFLKA QGRFRKLLSR PDAKEIVDEL QEYVDRRWER LLTLEEVTKD KPIR // ID POTA_THEMA Reviewed; 368 AA. AC Q9X196; DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 119. DE RecName: Full=Spermidine/putrescine import ATP-binding protein PotA {ECO:0000255|HAMAP-Rule:MF_01726}; DE EC=3.6.3.31 {ECO:0000255|HAMAP-Rule:MF_01726}; GN Name=potA {ECO:0000255|HAMAP-Rule:MF_01726}; GN OrderedLocusNames=TM_1376; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Part of the ABC transporter complex PotABCD involved in CC spermidine/putrescine import. Responsible for energy coupling to CC the transport system. {ECO:0000255|HAMAP-Rule:MF_01726}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + polyamine(Out) = ADP + phosphate CC + polyamine(In). {ECO:0000255|HAMAP-Rule:MF_01726}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (PotA), two transmembrane proteins (PotB and PotC) and a solute- CC binding protein (PotD). {ECO:0000255|HAMAP-Rule:MF_01726}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01726}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01726}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC Spermidine/putrescine importer (TC 3.A.1.11.1) family. CC {ECO:0000255|HAMAP-Rule:MF_01726}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01726}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36446.1; -; Genomic_DNA. DR PIR; A72261; A72261. DR RefSeq; NP_229177.1; NC_000853.1. DR RefSeq; WP_004081574.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X196; -. DR STRING; 243274.TM1376; -. DR EnsemblBacteria; AAD36446; AAD36446; TM_1376. DR GeneID; 898102; -. DR KEGG; tma:TM1376; -. DR PATRIC; 23937694; VBITheMar51294_1388. DR eggNOG; ENOG4105C53; Bacteria. DR eggNOG; COG3842; LUCA. DR InParanoid; Q9X196; -. DR KO; K11072; -. DR OMA; MIQFRPH; -. DR OrthoDB; EOG6T7N3V; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0015594; F:putrescine-importing ATPase activity; IEA:InterPro. DR GO; GO:0015595; F:spermidine-importing ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR017879; ABC_Sperm/Put_ATP-bd_PotA. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005893; Sp_pt_ABC_ATP-bd. DR InterPro; IPR013611; Transp-assoc_OB_typ2. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08402; TOBE_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01187; potA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51305; POTA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; KW Transport. FT CHAIN 1 368 Spermidine/putrescine import ATP-binding FT protein PotA. FT /FTId=PRO_0000286319. FT DOMAIN 6 236 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01726}. FT NP_BIND 38 45 ATP. {ECO:0000255|HAMAP-Rule:MF_01726}. SQ SEQUENCE 368 AA; 42046 MW; 89954C183F611C9C CRC64; MIGGEVSIKN VSKFFDDFQV LKNVSLDIKK GEFFSILGPS GCGKTTLLRV IAGFEGVESG DVLLDGKSIL NLPPNKRPVN IIFQNYALFP HLTVFENIAF PLKLKKLSEN EINQRVNELL SLIRMEEHAQ KMPSQLSGGQ KQRVAIARAL ANEPRVLLLD EPLSALDAKL RQELLVELDN LHDRVGITFI YVTHDQAEAI SVSDRVALMN EGEIVQVGTP YEVYESPVNV FAATFIGETN LMKAEVVEVE DEYYVVESPG IGQFRCYRDK EAKKGDRLLI TLRPEKIRIS RKQFRSEETF NVFHGVVDEE IYMGHQTKYF VRLDEGYIMK VYKQHARYIL DEPIIKWEDE VFITWNPDDS FIVEVLEE // ID PRMC_THEMA Reviewed; 282 AA. AC Q9WYV8; DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Release factor glutamine methyltransferase; DE Short=RF MTase; DE EC=2.1.1.297; DE AltName: Full=N5-glutamine methyltransferase PrmC; DE AltName: Full=Protein-(glutamine-N5) MTase PrmC; DE AltName: Full=Protein-glutamine N-methyltransferase PrmC; GN Name=prmC; OrderedLocusNames=TM_0488; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP CRYSTALLIZATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=14651272; RA Yoon H.J., Kang K.Y., Ahn H.J., Shim S.M., Ha J.Y., Lee S.K., RA Mikami B., Suh S.W.; RT "X-ray crystallographic studies of HemK from Thermotoga maritima, an RT N5-glutamine methyltransferase."; RL Mol. Cells 16:266-269(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH RP S-ADENOSYL-L-HOMOCYSTEINE; S-ADENOSYL-L-METHIONINE AND GLUTAMINE. RX PubMed=12741815; DOI=10.1021/bi034026p; RA Schubert H.L., Phillips J.D., Hill C.P.; RT "Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine RT AdoMet-dependent methyltransferase."; RL Biochemistry 42:5592-5599(2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE AND GLUTAMINE, SUBUNIT, AND GLUTAMATE RP ANHYDRIDE CROSS-LINK. RX PubMed=18247349; DOI=10.1002/prot.21962; RA Agarwal R., Burley S.K., Swaminathan S.; RT "A novel mode of dimerization via formation of a glutamate anhydride RT crosslink in a protein crystal structure."; RL Proteins 71:1038-1041(2008). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of N5-glutamine methyltransferase, HemK(EC 2.1.1.-) RT (TM0488) from Thermotoga maritima at 2.80 A resolution."; RL Submitted (JUL-2011) to the PDB data bank. CC -!- FUNCTION: Methylates the class 1 translation termination release CC factors RF1/PrfA and RF2/PrfB on the glutamine residue of the CC universally conserved GGQ motif. {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [peptide chain CC release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + CC [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine. CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:18247349, CC ECO:0000269|Ref.5}. CC -!- MISCELLANEOUS: The crystal structure corresponding to PDB 1SG9 CC shows a glutamate anhydride cross-link formed between the Glu-97 CC side chains from two molecules, but this has not been observed in CC other PrmC structures from T.maritima. This cross-link is CC suggested being an artifact of concentration during CC crystallization (PubMed:18247349). {ECO:0000305|PubMed:18247349}. CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase CC family. PrmC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35573.1; -; Genomic_DNA. DR PIR; G72369; G72369. DR RefSeq; NP_228298.1; NC_000853.1. DR RefSeq; WP_004081478.1; NZ_CP011107.1. DR PDB; 1NV8; X-ray; 2.20 A; A/B=1-282. DR PDB; 1NV9; X-ray; 2.36 A; A=1-282. DR PDB; 1SG9; X-ray; 2.30 A; A/B/C=1-282. DR PDB; 1VQ1; X-ray; 2.80 A; A/B=1-282. DR PDBsum; 1NV8; -. DR PDBsum; 1NV9; -. DR PDBsum; 1SG9; -. DR PDBsum; 1VQ1; -. DR ProteinModelPortal; Q9WYV8; -. DR SMR; Q9WYV8; 8-281. DR STRING; 243274.TM0488; -. DR DNASU; 897528; -. DR EnsemblBacteria; AAD35573; AAD35573; TM_0488. DR GeneID; 897528; -. DR KEGG; tma:TM0488; -. DR KEGG; tmi:THEMA_02230; -. DR KEGG; tmw:THMA_0501; -. DR PATRIC; 23935881; VBITheMar51294_0495. DR eggNOG; ENOG4105EQY; Bacteria. DR eggNOG; COG2890; LUCA. DR InParanoid; Q9WYV8; -. DR KO; K02493; -. DR OMA; RVAYQNF; -. DR OrthoDB; EOG68Q0SZ; -. DR BRENDA; 2.1.1.297; 6331. DR EvolutionaryTrace; Q9WYV8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_02126; RF_methyltr_PrmC; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR004556; Modification_methylase_HemK. DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR Pfam; PF05175; MTS; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00536; hemK_fam; 1. DR TIGRFAMs; TIGR03534; RF_mod_PrmC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 282 Release factor glutamine FT methyltransferase. FT /FTId=PRO_0000414548. FT REGION 129 133 S-adenosyl-L-methionine binding. FT REGION 197 200 Substrate binding. FT BINDING 151 151 S-adenosyl-L-methionine. FT {ECO:0000269|PubMed:18247349, FT ECO:0000269|Ref.5}. FT BINDING 180 180 S-adenosyl-L-methionine. FT {ECO:0000269|PubMed:18247349, FT ECO:0000269|Ref.5}. FT BINDING 197 197 S-adenosyl-L-methionine. FT {ECO:0000269|PubMed:18247349, FT ECO:0000269|Ref.5}. FT HELIX 14 24 {ECO:0000244|PDB:1NV8}. FT TURN 25 28 {ECO:0000244|PDB:1NV8}. FT HELIX 32 44 {ECO:0000244|PDB:1NV8}. FT HELIX 48 51 {ECO:0000244|PDB:1NV8}. FT STRAND 53 55 {ECO:0000244|PDB:1NV9}. FT HELIX 60 74 {ECO:0000244|PDB:1NV8}. FT HELIX 79 83 {ECO:0000244|PDB:1NV8}. FT STRAND 85 88 {ECO:0000244|PDB:1NV8}. FT STRAND 91 94 {ECO:0000244|PDB:1NV8}. FT HELIX 106 120 {ECO:0000244|PDB:1NV8}. FT STRAND 124 129 {ECO:0000244|PDB:1NV8}. FT HELIX 134 142 {ECO:0000244|PDB:1NV8}. FT STRAND 146 152 {ECO:0000244|PDB:1NV8}. FT HELIX 154 166 {ECO:0000244|PDB:1NV8}. FT STRAND 172 179 {ECO:0000244|PDB:1NV8}. FT HELIX 182 187 {ECO:0000244|PDB:1NV8}. FT TURN 188 190 {ECO:0000244|PDB:1NV8}. FT STRAND 193 196 {ECO:0000244|PDB:1NV8}. FT HELIX 203 205 {ECO:0000244|PDB:1NV8}. FT HELIX 211 213 {ECO:0000244|PDB:1SG9}. FT HELIX 216 219 {ECO:0000244|PDB:1NV8}. FT TURN 222 224 {ECO:0000244|PDB:1NV8}. FT HELIX 227 235 {ECO:0000244|PDB:1NV8}. FT STRAND 242 246 {ECO:0000244|PDB:1NV8}. FT HELIX 249 251 {ECO:0000244|PDB:1VQ1}. FT HELIX 252 255 {ECO:0000244|PDB:1NV8}. FT TURN 256 258 {ECO:0000244|PDB:1NV8}. FT STRAND 259 261 {ECO:0000244|PDB:1SG9}. FT STRAND 263 266 {ECO:0000244|PDB:1NV8}. FT STRAND 270 278 {ECO:0000244|PDB:1NV8}. SQ SEQUENCE 282 AA; 31609 MW; 68130302E620181B CRC64; MDTRKNVSGA ERKIWSLIRD CSGKLEGVTE TSVLEVLLIV SRVLGIRKED LFLKDLGVSP TEEKRILELV EKRASGYPLH YILGEKEFMG LSFLVEEGVF VPRPETEELV ELALELIRKY GIKTVADIGT GSGAIGVSVA KFSDAIVFAT DVSSKAVEIA RKNAERHGVS DRFFVRKGEF LEPFKEKFAS IEMILSNPPY VKSSAHLPKD VLFEPPEALF GGEDGLDFYR EFFGRYDTSG KIVLMEIGED QVEELKKIVS DTVFLKDSAG KYRFLLLNRR SS // ID PSUG_THEMA Reviewed; 285 AA. AC Q9X1H5; DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=Pseudouridine-5'-phosphate glycosidase {ECO:0000255|HAMAP-Rule:MF_01876, ECO:0000303|PubMed:18591240}; DE Short=PsiMP glycosidase {ECO:0000255|HAMAP-Rule:MF_01876, ECO:0000303|PubMed:18591240}; DE EC=4.2.1.70 {ECO:0000255|HAMAP-Rule:MF_01876, ECO:0000269|PubMed:18591240}; GN Name=psuG {ECO:0000255|HAMAP-Rule:MF_01876}; GN Synonyms=indA {ECO:0000303|PubMed:18591240}; GN OrderedLocusNames=TM_1464; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=18591240; DOI=10.1074/jbc.M804122200; RA Preumont A., Snoussi K., Stroobant V., Collet J.-F., RA Van Schaftingen E.; RT "Molecular identification of pseudouridine-metabolizing enzymes."; RL J. Biol. Chem. 283:25238-25246(2008). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE, AND RP SUBUNIT. RX PubMed=15822122; DOI=10.1002/prot.20420; RA Levin I., Miller M.D., Schwarzenbacher R., McMullan D., Abdubek P., RA Ambing E., Biorac T., Cambell J., Canaves J.M., Chiu H.-J., RA Deacon A.M., DiDonato M., Elsliger M.-A., Godzik A., Grittini C., RA Grzechnik S.K., Hale J., Hampton E., Han G.W., Haugen J., Hornsby M., RA Jaroszewski L., Karlak C., Klock H.E., Koesema E., Kreusch A., RA Kuhn P., Lesley S.A., Morse A., Moy K., Nigoghossian E., Ouyang J., RA Page R., Quijano K., Reyes R., Robb A., Sims E., Spraggon G., RA Stevens R.C., van den Bedem H., Velasquez J., Vincent J., Wang X., RA West B., Wolf G., Xu Q., Zagnitko O., Hodgson K.O., Wooley J., RA Wilson I.A.; RT "Crystal structure of an indigoidine synthase A (IndA)-like protein RT (TM1464) from Thermotoga maritima at 1.90 A resolution reveals a new RT fold."; RL Proteins 59:864-868(2005). CC -!- FUNCTION: Catalyzes the hydrolysis of pseudouridine 5'-phosphate CC (PsiMP) to ribose 5-phosphate and uracil. CC {ECO:0000269|PubMed:18591240}. CC -!- FUNCTION: Catalyzes the reversible cleavage of pseudouridine 5'- CC phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions CC biologically in the cleavage direction, as part of a pseudouridine CC degradation pathway. {ECO:0000255|HAMAP-Rule:MF_01876, CC ECO:0000269|PubMed:18591240}. CC -!- CATALYTIC ACTIVITY: Uracil + D-ribose 5-phosphate = pseudouridine CC 5'-phosphate + H(2)O. {ECO:0000255|HAMAP-Rule:MF_01876, CC ECO:0000269|PubMed:18591240}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01876, CC ECO:0000269|PubMed:15822122, ECO:0000303|PubMed:18591240}; CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01876, ECO:0000269|PubMed:15822122, CC ECO:0000303|PubMed:18591240}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC No activity can be observed at or below 50 degrees Celsius. CC {ECO:0000269|PubMed:18591240}; CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01876, CC ECO:0000269|PubMed:15822122}. CC -!- SIMILARITY: Belongs to the pseudouridine-5'-phosphate glycosidase CC family. {ECO:0000255|HAMAP-Rule:MF_01876}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36532.1; -; Genomic_DNA. DR PIR; A72252; A72252. DR RefSeq; NP_229264.1; NC_000853.1. DR RefSeq; WP_004081760.1; NZ_CP011107.1. DR PDB; 1VKM; X-ray; 1.90 A; A/B/C/D/E/F=1-285. DR PDBsum; 1VKM; -. DR ProteinModelPortal; Q9X1H5; -. DR SMR; Q9X1H5; 1-284. DR STRING; 243274.TM1464; -. DR EnsemblBacteria; AAD36532; AAD36532; TM_1464. DR GeneID; 896983; -. DR KEGG; tma:TM1464; -. DR PATRIC; 23937882; VBITheMar51294_1479. DR eggNOG; ENOG4105D53; Bacteria. DR eggNOG; COG2313; LUCA. DR InParanoid; Q9X1H5; -. DR KO; K16329; -. DR OMA; IIAHGMP; -. DR OrthoDB; EOG6B09RX; -. DR EvolutionaryTrace; Q9X1H5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004730; F:pseudouridylate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046113; P:nucleobase catabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01876; PsiMP_glycosidase; 1. DR InterPro; IPR007342; PsuG. DR Pfam; PF04227; Indigoidine_A; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Glycosidase; Hydrolase; Lyase; KW Manganese; Metal-binding; Reference proteome. FT CHAIN 1 285 Pseudouridine-5'-phosphate glycosidase. FT /FTId=PRO_0000390555. FT REGION 128 130 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01876}. FT ACT_SITE 17 17 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01876}. FT ACT_SITE 147 147 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01876}. FT METAL 126 126 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01876, FT ECO:0000269|PubMed:15822122}. FT BINDING 77 77 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01876}. FT BINDING 97 97 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01876}. FT STRAND 3 5 {ECO:0000244|PDB:1VKM}. FT STRAND 13 16 {ECO:0000244|PDB:1VKM}. FT HELIX 19 22 {ECO:0000244|PDB:1VKM}. FT HELIX 27 44 {ECO:0000244|PDB:1VKM}. FT STRAND 47 54 {ECO:0000244|PDB:1VKM}. FT STRAND 57 61 {ECO:0000244|PDB:1VKM}. FT HELIX 64 73 {ECO:0000244|PDB:1VKM}. FT STRAND 76 78 {ECO:0000244|PDB:1VKM}. FT HELIX 80 82 {ECO:0000244|PDB:1VKM}. FT HELIX 83 89 {ECO:0000244|PDB:1VKM}. FT STRAND 93 95 {ECO:0000244|PDB:1VKM}. FT HELIX 97 106 {ECO:0000244|PDB:1VKM}. FT STRAND 111 113 {ECO:0000244|PDB:1VKM}. FT HELIX 129 134 {ECO:0000244|PDB:1VKM}. FT STRAND 139 146 {ECO:0000244|PDB:1VKM}. FT HELIX 152 161 {ECO:0000244|PDB:1VKM}. FT STRAND 166 170 {ECO:0000244|PDB:1VKM}. FT HELIX 192 204 {ECO:0000244|PDB:1VKM}. FT STRAND 209 214 {ECO:0000244|PDB:1VKM}. FT HELIX 219 221 {ECO:0000244|PDB:1VKM}. FT HELIX 225 233 {ECO:0000244|PDB:1VKM}. FT HELIX 241 243 {ECO:0000244|PDB:1VKM}. FT HELIX 244 255 {ECO:0000244|PDB:1VKM}. FT TURN 256 258 {ECO:0000244|PDB:1VKM}. FT HELIX 259 282 {ECO:0000244|PDB:1VKM}. SQ SEQUENCE 285 AA; 31728 MW; 9657B169EC62DB74 CRC64; MIIESRIEKG KPVVGMETTV FVHGLPRKEA IELFRRAKEI SREKGFQLAV IGILKGKIVA GMSEEELEAM MREGADKVGT REIPIVVAEG KNAATTVSAT IFLSRRIGIE VVVTGGTGGV HPGRVDVSQD LTEMSSSRAV LVSSGIKSIL DVEATFEMLE TLEIPLVGFR TNEFPLFFSR KSGRRVPRIE NVEEVLKIYE SMKEMELEKT LMVLNPVPEE YEIPHDEIER LLEKIELEVE GKEVTPFLLK KLVEMTNGRT LKANLALLEE NVKLAGEIAV KLKRS // ID PTAS_THEMA Reviewed; 294 AA. AC Q9X0L4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=Phosphate acetyltransferase; DE EC=2.3.1.8; DE AltName: Full=Phosphotransacetylase; GN Name=pta; OrderedLocusNames=TM_1130; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF 1-39, AND CHARACTERIZATION. RX PubMed=10074080; RA Bock A.-K., Glasemacher J., Schmidt R., Schoenheit P.; RT "Purification and characterization of two extremely thermostable RT enzymes, phosphate acetyltransferase and acetate kinase, from the RT hyperthermophilic eubacterium Thermotoga maritima."; RL J. Bacteriol. 181:1861-1867(1999). CC -!- FUNCTION: In addition to acetyl-CoA (100%), the enzyme accepts CC propionyl-CoA (60%) and butyryl-CoA (30%). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + phosphate = CoA + acetyl CC phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 90 degrees Celsius.; CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA CC biosynthesis; acetyl-CoA from acetate: step 2/2. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the phosphate acetyltransferase and CC butyryltransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36206.1; -; Genomic_DNA. DR PIR; G72293; G72293. DR RefSeq; NP_228936.1; NC_000853.1. DR RefSeq; WP_004080280.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0L4; -. DR DIP; DIP-2900N; -. DR STRING; 243274.TM1130; -. DR EnsemblBacteria; AAD36206; AAD36206; TM_1130. DR GeneID; 898634; -. DR KEGG; tma:TM1130; -. DR PATRIC; 23937195; VBITheMar51294_1146. DR eggNOG; ENOG4107RE7; Bacteria. DR eggNOG; COG0280; LUCA. DR InParanoid; Q9X0L4; -. DR KO; K00625; -. DR OMA; ANDDHVI; -. DR OrthoDB; EOG60GRZ3; -. DR BioCyc; MetaCyc:MONOMER-427; -. DR UniPathway; UPA00340; UER00459. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR012147; P_Ac_Bu_trans. DR InterPro; IPR002505; PTA_PTB. DR Pfam; PF01515; PTA_PTB; 2. DR PIRSF; PIRSF000428; P_Ac_trans; 1. PE 1: Evidence at protein level; KW Acyltransferase; Complete proteome; Cytoplasm; KW Direct protein sequencing; Reference proteome; Transferase. FT CHAIN 1 294 Phosphate acetyltransferase. FT /FTId=PRO_0000179149. FT CONFLICT 11 11 R -> Y (in Ref. 2; AA sequence). FT {ECO:0000305}. SQ SEQUENCE 294 AA; 32093 MW; F4B98B3CAE120AFB CRC64; MFLEKLVEMA RGKGKKLAVA AANDDHVIEA VYRAWRERVC EPVLFGPEEE ITRIIEELVP EWKNPQIIDC PPEEAGRLAV EAVSKGECDF LMKGKIKTGD LMKIYLDERY GLRTGKTMAM VSVMEIPDFP RPLIISDPGM LISPTLEQKV DMIEHCVRVA NVMGLETPKV AVVGAIEVVN PKMPITMEAA ILSKMNQRGQ IKGCIVDGPF ALDNVVSEEA AKKKGIQSPV AGKADILILP DIEAANILYK ALVFLAKAKS ASTILGGKVP VVLTSRADSE ETKFYSIALS AVFA // ID PRIA_THEMA Reviewed; 736 AA. AC Q9WY22; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 118. DE RecName: Full=Primosomal protein N' {ECO:0000255|HAMAP-Rule:MF_00983}; DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00983}; DE AltName: Full=ATP-dependent helicase PriA {ECO:0000255|HAMAP-Rule:MF_00983}; GN Name=priA {ECO:0000255|HAMAP-Rule:MF_00983}; GN OrderedLocusNames=TM_0178; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in the restart of stalled replication forks. CC Recognizes and binds the arrested nascent DNA chain at stalled CC replication forks. It can open the DNA duplex, via its helicase CC activity, and promote assembly of the primosome and loading of the CC major replicative helicase DnaB onto DNA. {ECO:0000255|HAMAP- CC Rule:MF_00983}. CC -!- SUBUNIT: Component of the primosome. {ECO:0000255|HAMAP- CC Rule:MF_00983}. CC -!- SIMILARITY: Belongs to the helicase family. PriA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00983}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00983}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_00983}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35271.1; -; Genomic_DNA. DR PIR; H72409; H72409. DR RefSeq; NP_227993.1; NC_000853.1. DR RefSeq; WP_004082813.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY22; -. DR STRING; 243274.TM0178; -. DR PRIDE; Q9WY22; -. DR EnsemblBacteria; AAD35271; AAD35271; TM_0178. DR GeneID; 897018; -. DR KEGG; tma:TM0178; -. DR PATRIC; 23935204; VBITheMar51294_0179. DR eggNOG; ENOG4105C25; Bacteria. DR eggNOG; COG1198; LUCA. DR InParanoid; Q9WY22; -. DR KO; K04066; -. DR OMA; HDDAYKS; -. DR OrthoDB; EOG6KT2K4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central. DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central. DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 3. DR HAMAP; MF_00983; PriA; 1. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005259; PriA. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00595; priA; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA replication; DNA-binding; KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Primosome; KW Reference proteome; Zinc; Zinc-finger. FT CHAIN 1 736 Primosomal protein N'. FT /FTId=PRO_0000102135. FT DOMAIN 230 396 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00983}. FT DOMAIN 487 643 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_00983}. FT NP_BIND 243 250 ATP. {ECO:0000255|HAMAP-Rule:MF_00983}. FT ZN_FING 452 464 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00983}. FT ZN_FING 479 495 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00983}. FT MOTIF 339 342 DEAH box. SQ SEQUENCE 736 AA; 84557 MW; 138ECBB3260D4C77 CRC64; MYYKVAVSGS GKVLNVFSSE ELLIGERVWL NWRNGKVKGY VLERSLSHEN EATPSERDGK SFLSEGHVEI AKWVSERFFS PLGMVFDLFF PQGIDDYKEE VVVSESPFLD FDRMTLRDFL ENFGEKALKE MVKKGLVRVE KNFYVKEPRP RVKKRLFLKK RISEIIREHL TVKQRMVVEY LQFNDGVPLE ELLEDLEVSK SVIETLQRKN IVEIVSGDVF PKKRRILRGD FKGNISKENL FFGPTGSGKT EALFELIDVY SRKGTVLFLV PEVSVLTHTL SRLKGAFPDL KIGIYHSYLS RARKNLEWYK AASGKIDVLL GTRSAVFVPV KNLSLLIVDE EHDESFYQHT RPSYDAIVVA RKISEVFDVP IILSSATPDL WTYREAKEGR IRTFNFTRRF GSLSVEVVDM RNEEKIGSFA KKTLDRIEET LEEGKRVLIY VRRKGFWGRV QCEVCGYVLK CENCDVSLVY HSDTHSLKCH QCGREYGLVE SCPRCGGRLV GRTAGTERVE RELKRYFPTR RIARVDREVV DNIMELESYI DKLIRGEIDI LVGTRLITKS LSVPEIGLVC IMDVDSLIFN PDYSSSLRTF QLVVQALGRA SRGDQGKAII QTYNPEDTII RKALEEDVNG FYAEELERRK ALGYPPYRHL IQVAVKSKNP EVGKNSLTSL KEFLKGEEVL GPVEHWVFKL RGFYRHHLIV KTEDLERVLP KLEKALRILG IDAIVRVDPP TLEVSD // ID PTH_THEMA Reviewed; 186 AA. AC Q9X1W1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083}; DE Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083}; DE EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083}; GN Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=TM_1626; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl- CC tRNAs which drop off the ribosome during protein synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00083}. CC -!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N- CC substituted amino acid + tRNA. {ECO:0000255|HAMAP-Rule:MF_00083}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}. CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP- CC Rule:MF_00083}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36693.1; -; Genomic_DNA. DR PIR; B72229; B72229. DR RefSeq; NP_229426.1; NC_000853.1. DR RefSeq; WP_004082100.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1W1; -. DR STRING; 243274.TM1626; -. DR EnsemblBacteria; AAD36693; AAD36693; TM_1626. DR GeneID; 897928; -. DR KEGG; tma:TM1626; -. DR PATRIC; 23938226; VBITheMar51294_1645. DR eggNOG; ENOG4108ZPD; Bacteria. DR eggNOG; COG0193; LUCA. DR InParanoid; Q9X1W1; -. DR KO; K01056; -. DR OMA; FEMVDAL; -. DR OrthoDB; EOG6C5RTR; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1470; -; 1. DR HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1. DR InterPro; IPR001328; Pept_tRNA_hydro. DR InterPro; IPR018171; Pept_tRNA_hydro_CS. DR PANTHER; PTHR17224; PTHR17224; 1. DR Pfam; PF01195; Pept_tRNA_hydro; 1. DR SUPFAM; SSF53178; SSF53178; 1. DR TIGRFAMs; TIGR00447; pth; 1. DR PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1. DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Reference proteome. FT CHAIN 1 186 Peptidyl-tRNA hydrolase. FT /FTId=PRO_0000187841. SQ SEQUENCE 186 AA; 20906 MW; 6C63DFED7514C1F2 CRC64; MVVVGLGNPG PRYAFTRHNV GFLFLDFLKN KDWKTEKYFA WNKINLAGNE VALVKPLTYM NLSGLAMPHV LKFFSASLDD IIVVYDDVSL KLGKIRIRKK GSDGGHNGMK SIIQALGTQE IKRIRVGIGD KPEGMDLVNF VLGEFSDEEW IILNKVFEVM KEALEVILVE GIEKAMSIYN SLEVRA // ID PRMA_THEMA Reviewed; 264 AA. AC Q9X0G8; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=Ribosomal protein L11 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00735}; DE Short=L11 Mtase {ECO:0000255|HAMAP-Rule:MF_00735}; DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00735}; GN Name=prmA {ECO:0000255|HAMAP-Rule:MF_00735}; GN OrderedLocusNames=TM_1079; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Methylates ribosomal protein L11. {ECO:0000255|HAMAP- CC Rule:MF_00735}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00735}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA CC family. {ECO:0000255|HAMAP-Rule:MF_00735}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36156.1; -; Genomic_DNA. DR PIR; G72296; G72296. DR RefSeq; NP_228885.1; NC_000853.1. DR RefSeq; WP_004080406.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0G8; -. DR STRING; 243274.TM1079; -. DR EnsemblBacteria; AAD36156; AAD36156; TM_1079. DR GeneID; 898735; -. DR KEGG; tma:TM1079; -. DR PATRIC; 23937087; VBITheMar51294_1092. DR eggNOG; ENOG4105F59; Bacteria. DR eggNOG; COG2264; LUCA. DR InParanoid; Q9X0G8; -. DR KO; K02687; -. DR OMA; WIFINIG; -. DR OrthoDB; EOG6N684G; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008276; F:protein methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00735; Methyltr_PrmA; 1. DR InterPro; IPR004498; Ribosomal_PrmA_MeTrfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 264 Ribosomal protein L11 methyltransferase. FT /FTId=PRO_0000192326. SQ SEQUENCE 264 AA; 30280 MW; E212638B2BE817AC CRC64; MRFKELILPL KIEEEELVEK FYEEGFFNFA IEEDKKGKKV LKIYLREGEP LPDFLKDWEI VDEKITTPKD WIVELEPFEI VEGIFIDPTE KINRRDAIVI KLSPGVAFGT GLHPTTRMSV FFLKKYLKEG NTVLDVGCGT GILAIAAKKL GASRVVAVDV DEQAVEVAEE NVRKNDVDVL VKWSDLLSEV EGTFDIVVSN ILAEIHVKLL EDVNRVTHRD SMLILSGIVD RKEDMVKRKA SEHGWNVLER KQEREWVTLV MKRS // ID PUR2_THEMA Reviewed; 400 AA. AC Q9X0X7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 116. DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000255|HAMAP-Rule:MF_00138}; DE EC=6.3.4.13 {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=GARS {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000255|HAMAP-Rule:MF_00138}; GN Name=purD {ECO:0000255|HAMAP-Rule:MF_00138}; GN OrderedLocusNames=TM_1250; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP CC + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. CC {ECO:0000255|HAMAP-Rule:MF_00138}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D- CC ribose 1-diphosphate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00138}. CC -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP- CC Rule:MF_00138}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_00138}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36325.1; -; Genomic_DNA. DR PIR; D72277; D72277. DR RefSeq; NP_229055.1; NC_000853.1. DR RefSeq; WP_010865290.1; NC_000853.1. DR PDB; 1VKZ; X-ray; 2.30 A; A/B=1-400. DR PDBsum; 1VKZ; -. DR ProteinModelPortal; Q9X0X7; -. DR SMR; Q9X0X7; 4-399. DR STRING; 243274.TM1250; -. DR DNASU; 898233; -. DR EnsemblBacteria; AAD36325; AAD36325; TM_1250. DR GeneID; 898233; -. DR KEGG; tma:TM1250; -. DR KEGG; tmi:THEMA_08085; -. DR PATRIC; 23937440; VBITheMar51294_1266. DR eggNOG; ENOG4107QNG; Bacteria. DR eggNOG; COG0151; LUCA. DR InParanoid; Q9X0X7; -. DR KO; K01945; -. DR OMA; DEFGPPY; -. DR OrthoDB; EOG69SKD1; -. DR BioCyc; TMAR243274:GC6P-1281-MONOMER; -. DR UniPathway; UPA00074; UER00125. DR EvolutionaryTrace; Q9X0X7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.90.600.10; -; 1. DR HAMAP; MF_00138; GARS; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp. DR InterPro; IPR000115; PRibGlycinamide_synth. DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom. DR InterPro; IPR020559; PRibGlycinamide_synth_CS. DR InterPro; IPR020562; PRibGlycinamide_synth_N. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF01071; GARS_A; 1. DR Pfam; PF02843; GARS_C; 1. DR Pfam; PF02844; GARS_N; 1. DR SMART; SM01210; GARS_C; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR00877; purD; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00184; GARS; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Ligase; Magnesium; KW Manganese; Metal-binding; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 400 Phosphoribosylamine--glycine ligase. FT /FTId=PRO_0000151495. FT DOMAIN 99 303 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_00138}. FT NP_BIND 125 186 ATP. {ECO:0000255|HAMAP-Rule:MF_00138}. FT METAL 273 273 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00138}. FT METAL 275 275 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00138}. FT STRAND 5 10 {ECO:0000244|PDB:1VKZ}. FT HELIX 13 24 {ECO:0000244|PDB:1VKZ}. FT STRAND 28 33 {ECO:0000244|PDB:1VKZ}. FT HELIX 38 40 {ECO:0000244|PDB:1VKZ}. FT STRAND 42 44 {ECO:0000244|PDB:1VKZ}. FT HELIX 50 54 {ECO:0000244|PDB:1VKZ}. FT HELIX 67 69 {ECO:0000244|PDB:1VKZ}. FT STRAND 81 83 {ECO:0000244|PDB:1VKZ}. FT HELIX 86 93 {ECO:0000244|PDB:1VKZ}. FT HELIX 95 104 {ECO:0000244|PDB:1VKZ}. FT STRAND 112 117 {ECO:0000244|PDB:1VKZ}. FT HELIX 118 125 {ECO:0000244|PDB:1VKZ}. FT STRAND 130 138 {ECO:0000244|PDB:1VKZ}. FT STRAND 145 150 {ECO:0000244|PDB:1VKZ}. FT HELIX 151 162 {ECO:0000244|PDB:1VKZ}. FT STRAND 165 167 {ECO:0000244|PDB:1VKZ}. FT STRAND 174 178 {ECO:0000244|PDB:1VKZ}. FT STRAND 182 192 {ECO:0000244|PDB:1VKZ}. FT STRAND 195 198 {ECO:0000244|PDB:1VKZ}. FT STRAND 207 209 {ECO:0000244|PDB:1VKZ}. FT TURN 210 212 {ECO:0000244|PDB:1VKZ}. FT STRAND 213 216 {ECO:0000244|PDB:1VKZ}. FT STRAND 220 224 {ECO:0000244|PDB:1VKZ}. FT HELIX 230 249 {ECO:0000244|PDB:1VKZ}. FT STRAND 255 265 {ECO:0000244|PDB:1VKZ}. FT STRAND 268 277 {ECO:0000244|PDB:1VKZ}. FT HELIX 282 289 {ECO:0000244|PDB:1VKZ}. FT HELIX 291 303 {ECO:0000244|PDB:1VKZ}. FT STRAND 314 322 {ECO:0000244|PDB:1VKZ}. FT TURN 324 328 {ECO:0000244|PDB:1VKZ}. FT STRAND 344 352 {ECO:0000244|PDB:1VKZ}. FT STRAND 355 358 {ECO:0000244|PDB:1VKZ}. FT STRAND 360 372 {ECO:0000244|PDB:1VKZ}. FT HELIX 373 386 {ECO:0000244|PDB:1VKZ}. SQ SEQUENCE 400 AA; 44326 MW; 411CE014DD7DE90F CRC64; MKAVRVHILG SGGREHAIGW AFAKQGYEVH FYPGNAGTKR DGTNHPYEGE KTLKAIPEED IVIPGSEEFL VEGVSNWRSN VFGPVKEVAR LEGSKVYAKR FMKKYGIRTA RFEVAETPEE LREKIKKFSP PYVIKADGLA RGKGVLILDS KEETIEKGSK LIIGELIKGV KGPVVIDEFL AGNELSAMAV VNGRNFVILP FVRDYKRLMD GDRGPNTGGM GSWGPVEIPS DTIKKIEELF DKTLWGVEKE GYAYRGFLYL GLMLHDGDPY ILEYNVRLGD PETEVIVTLN PEGFVNAVLE GYRGGKMEPV EPRGFAVDVV LAARGYPDAP EKGKEITLPE EGLIFFAGVA EKDGKLVTNG GRVLHCMGTG ETKEEARRKA YELAEKVHFE GKTYRRDIAL // ID PUR8_THEMA Reviewed; 431 AA. AC Q9X0I0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 128. DE RecName: Full=Adenylosuccinate lyase; DE Short=ASL; DE EC=4.3.2.2; DE AltName: Full=Adenylosuccinase; DE Short=ASase; GN Name=purB; OrderedLocusNames=TM_1095; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, AND ACTIVE SITE. RX PubMed=10673438; DOI=10.1016/S0969-2126(00)00092-7; RA Toth E.A., Yeates T.O.; RT "The structure of adenylosuccinate lyase, an enzyme with dual activity RT in the de novo purine biosynthetic pathway."; RL Structure 8:163-174(2000). CC -!- CATALYTIC ACTIVITY: N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. CC -!- CATALYTIC ACTIVITY: (S)-2-(5-amino-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1- CC (5-phospho-D-ribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; CC AMP from IMP: step 2/2. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2. CC -!- SUBUNIT: Homotetramer. Residues from neighboring subunits CC contribute catalytic and substrate-binding residues to each active CC site. {ECO:0000269|PubMed:10673438}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36171.1; -; Genomic_DNA. DR PIR; A72294; A72294. DR RefSeq; NP_228901.1; NC_000853.1. DR RefSeq; WP_004080360.1; NZ_CP011107.1. DR PDB; 1C3C; X-ray; 1.80 A; A/B=2-430. DR PDB; 1C3U; X-ray; 2.30 A; A/B=1-431. DR PDBsum; 1C3C; -. DR PDBsum; 1C3U; -. DR ProteinModelPortal; Q9X0I0; -. DR SMR; Q9X0I0; 2-430. DR STRING; 243274.TM1095; -. DR EnsemblBacteria; AAD36171; AAD36171; TM_1095. DR GeneID; 898670; -. DR KEGG; tma:TM1095; -. DR PATRIC; 23937125; VBITheMar51294_1111. DR eggNOG; ENOG4105C83; Bacteria. DR eggNOG; COG0015; LUCA. DR InParanoid; Q9X0I0; -. DR KO; K01756; -. DR OMA; VQENAMK; -. DR OrthoDB; EOG686NDB; -. DR BRENDA; 4.3.2.2; 6331. DR UniPathway; UPA00074; UER00132. DR UniPathway; UPA00075; UER00336. DR EvolutionaryTrace; Q9X0I0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; IBA:GO_Central. DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IBA:GO_Central. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0051262; P:protein tetramerization; IBA:GO_Central. DR GO; GO:0006163; P:purine nucleotide metabolic process; IBA:GO_Central. DR Gene3D; 1.10.275.10; -; 1. DR InterPro; IPR019468; AdenyloSucc_lyase_C. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR InterPro; IPR004769; Pur_lyase. DR PANTHER; PTHR11444; PTHR11444; 1. DR Pfam; PF10397; ADSL_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SMART; SM00998; ADSL_C; 1. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00928; purB; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Lyase; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 431 Adenylosuccinate lyase. FT /FTId=PRO_0000137886. FT REGION 4 5 Substrate binding. {ECO:0000250}. FT REGION 67 69 Substrate binding. {ECO:0000250}. FT REGION 68 69 Substrate binding. {ECO:0000250}. FT ACT_SITE 141 141 Proton acceptor. FT {ECO:0000269|PubMed:10673438}. FT ACT_SITE 141 141 Proton donor/acceptor. {ECO:0000250}. FT ACT_SITE 262 262 Proton donor/acceptor. {ECO:0000250}. FT BINDING 95 95 Substrate. {ECO:0000250}. FT BINDING 212 212 Substrate. {ECO:0000250}. FT BINDING 301 301 Substrate. {ECO:0000250}. FT BINDING 306 306 Substrate. {ECO:0000250}. FT BINDING 310 310 Substrate. {ECO:0000250}. FT HELIX 3 5 {ECO:0000244|PDB:1C3C}. FT HELIX 10 13 {ECO:0000244|PDB:1C3C}. FT HELIX 16 36 {ECO:0000244|PDB:1C3C}. FT HELIX 44 51 {ECO:0000244|PDB:1C3C}. FT HELIX 56 66 {ECO:0000244|PDB:1C3C}. FT HELIX 69 81 {ECO:0000244|PDB:1C3C}. FT HELIX 82 87 {ECO:0000244|PDB:1C3C}. FT TURN 88 91 {ECO:0000244|PDB:1C3C}. FT HELIX 94 130 {ECO:0000244|PDB:1C3C}. FT TURN 131 133 {ECO:0000244|PDB:1C3C}. FT STRAND 135 140 {ECO:0000244|PDB:1C3C}. FT STRAND 143 149 {ECO:0000244|PDB:1C3C}. FT HELIX 150 174 {ECO:0000244|PDB:1C3C}. FT STRAND 188 190 {ECO:0000244|PDB:1C3C}. FT HELIX 192 201 {ECO:0000244|PDB:1C3C}. FT STRAND 211 213 {ECO:0000244|PDB:1C3C}. FT HELIX 217 243 {ECO:0000244|PDB:1C3C}. FT TURN 246 248 {ECO:0000244|PDB:1C3C}. FT STRAND 250 252 {ECO:0000244|PDB:1C3C}. FT HELIX 272 286 {ECO:0000244|PDB:1C3C}. FT HELIX 288 293 {ECO:0000244|PDB:1C3C}. FT HELIX 304 333 {ECO:0000244|PDB:1C3C}. FT HELIX 338 345 {ECO:0000244|PDB:1C3C}. FT TURN 346 350 {ECO:0000244|PDB:1C3C}. FT HELIX 351 353 {ECO:0000244|PDB:1C3C}. FT HELIX 354 363 {ECO:0000244|PDB:1C3C}. FT HELIX 368 383 {ECO:0000244|PDB:1C3C}. FT STRAND 385 387 {ECO:0000244|PDB:1C3C}. FT HELIX 389 394 {ECO:0000244|PDB:1C3C}. FT HELIX 397 400 {ECO:0000244|PDB:1C3C}. FT HELIX 405 410 {ECO:0000244|PDB:1C3C}. FT HELIX 415 418 {ECO:0000244|PDB:1C3C}. FT HELIX 421 426 {ECO:0000244|PDB:1C3C}. SQ SEQUENCE 431 AA; 49873 MW; D3ACB25D87582869 CRC64; MVERYSLSPM KDLWTEEAKY RRWLEVELAV TRAYEELGMI PKGVTERIRN NAKIDVELFK KIEEKTNHDV VAFVEGIGSM IGEDSRFFHY GLTSSDVLDT ANSLALVEAG KILLESLKEF CDVLWEVANR YKHTPTIGRT HGVHAEPTSF GLKVLGWYSE MKRNVQRLER AIEEVSYGKI SGAVGNYANV PPEVEEKALS YLGLKPEPVS TQVVPRDRHA FYLSTLAIVA AGIERIAVEI RHLQRTEVLE VEEPFRKGQR GSSAMPHKKN PITCERLTGL SRMMRAYVDP SLENIALWHE RDISHSSVER YVFPDATQTL YYMIVTATNV VRNMKVNEER MKKNIDLTKG LVFSQRVLLK LIEKGLTRKE AYDIVQRNAL KTWNSEKHFL EYLLEDEEVK KLVTKEELEE LFDISYYLKH VDHIFERFEK E // ID PUR7_THEMA Reviewed; 230 AA. AC Q9X0X0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 117. DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase; DE EC=6.3.2.6; DE AltName: Full=SAICAR synthetase; GN Name=purC; OrderedLocusNames=TM_1243; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + CC (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamido)succinate. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2. CC -!- SIMILARITY: Belongs to the SAICAR synthetase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36318.1; -; Genomic_DNA. DR PIR; E72276; E72276. DR RefSeq; NP_229048.1; NC_000853.1. DR RefSeq; WP_004080029.1; NZ_CP011107.1. DR PDB; 1KUT; X-ray; 2.20 A; A/B=1-230. DR PDBsum; 1KUT; -. DR ProteinModelPortal; Q9X0X0; -. DR SMR; Q9X0X0; 2-230. DR STRING; 243274.TM1243; -. DR EnsemblBacteria; AAD36318; AAD36318; TM_1243. DR GeneID; 898240; -. DR KEGG; tma:TM1243; -. DR PATRIC; 23937426; VBITheMar51294_1259. DR eggNOG; ENOG4105C8V; Bacteria. DR eggNOG; COG0152; LUCA. DR InParanoid; Q9X0X0; -. DR KO; K01923; -. DR OMA; FNAQKRG; -. DR OrthoDB; EOG62C9HN; -. DR UniPathway; UPA00074; UER00131. DR EvolutionaryTrace; Q9X0X0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IBA:GO_Central. DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.470.20; -; 1. DR HAMAP; MF_00137; SAICAR_synth; 1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR028923; SAICAR_synt/ADE2_N. DR InterPro; IPR018236; SAICAR_synthetase_CS. DR Pfam; PF01259; SAICAR_synt; 1. DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Ligase; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1 230 Phosphoribosylaminoimidazole- FT succinocarboxamide synthase. FT /FTId=PRO_0000100891. FT STRAND 8 13 {ECO:0000244|PDB:1KUT}. FT STRAND 16 21 {ECO:0000244|PDB:1KUT}. FT HELIX 39 56 {ECO:0000244|PDB:1KUT}. FT STRAND 61 67 {ECO:0000244|PDB:1KUT}. FT TURN 68 70 {ECO:0000244|PDB:1KUT}. FT STRAND 71 74 {ECO:0000244|PDB:1KUT}. FT STRAND 81 89 {ECO:0000244|PDB:1KUT}. FT HELIX 92 98 {ECO:0000244|PDB:1KUT}. FT STRAND 105 115 {ECO:0000244|PDB:1KUT}. FT HELIX 118 120 {ECO:0000244|PDB:1KUT}. FT HELIX 127 132 {ECO:0000244|PDB:1KUT}. FT HELIX 138 160 {ECO:0000244|PDB:1KUT}. FT TURN 161 163 {ECO:0000244|PDB:1KUT}. FT STRAND 164 171 {ECO:0000244|PDB:1KUT}. FT STRAND 173 175 {ECO:0000244|PDB:1KUT}. FT STRAND 181 183 {ECO:0000244|PDB:1KUT}. FT TURN 189 191 {ECO:0000244|PDB:1KUT}. FT STRAND 192 196 {ECO:0000244|PDB:1KUT}. FT HELIX 203 208 {ECO:0000244|PDB:1KUT}. FT HELIX 209 211 {ECO:0000244|PDB:1KUT}. FT HELIX 215 227 {ECO:0000244|PDB:1KUT}. SQ SEQUENCE 230 AA; 26231 MW; 242B18AD026DB4A9 CRC64; MNYEGKTKIV KVTGDYALLE FKDDITAGDG LKHDVLTGKG SICAETTAIL MKYLSEKGIK THLVEYIPPR TLKVIPLKMF PLEVVVRLKK AGSFVRRYGG AEGEDLPVPL VEFFIKDDER HDPMVCVDHL EILGIATKKQ AEKMKEAAVK ITLALKEFFE RANFELWDIK YEFGLDKDGN VVLGDEISPD TFRLRKKGEI FDKDVYRRDL GDPLKKYREV LELCRSLNSQ // ID PUR9_THEMA Reviewed; 452 AA. AC Q9X0X6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=Bifunctional purine biosynthesis protein PurH; DE Includes: DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase; DE EC=2.1.2.3; DE AltName: Full=AICAR transformylase; DE Includes: DE RecName: Full=IMP cyclohydrolase; DE EC=3.5.4.10; DE AltName: Full=ATIC; DE AltName: Full=IMP synthase; DE AltName: Full=Inosinicase; GN Name=purH; OrderedLocusNames=TM_1249; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + 5-amino-1-(5- CC phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. CC -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl CC THF route): step 1/1. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamide: step 1/1. CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal CC region. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36324.1; -; Genomic_DNA. DR PIR; C72277; C72277. DR RefSeq; NP_229054.1; NC_000853.1. DR RefSeq; WP_004080014.1; NZ_CP011107.1. DR PDB; 1ZCZ; X-ray; 1.88 A; A/B=1-452. DR PDBsum; 1ZCZ; -. DR ProteinModelPortal; Q9X0X6; -. DR SMR; Q9X0X6; 1-452. DR STRING; 243274.TM1249; -. DR EnsemblBacteria; AAD36324; AAD36324; TM_1249. DR GeneID; 898234; -. DR KEGG; tma:TM1249; -. DR PATRIC; 23937438; VBITheMar51294_1265. DR eggNOG; ENOG4105DC1; Bacteria. DR eggNOG; COG0138; LUCA. DR InParanoid; Q9X0X6; -. DR KO; K00602; -. DR OMA; PCGVAEG; -. DR OrthoDB; EOG6QCDFF; -. DR BRENDA; 3.5.4.10; 6331. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR EvolutionaryTrace; Q9X0X6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.140.20; -; 2. DR Gene3D; 3.40.50.1380; -; 1. DR HAMAP; MF_00139; PurH; 1. DR InterPro; IPR024051; AICAR_Tfase_dom. DR InterPro; IPR002695; AICARFT_IMPCHas. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR011607; MGS-like_dom. DR PANTHER; PTHR11692; PTHR11692; 1. DR Pfam; PF01808; AICARFT_IMPCHas; 1. DR Pfam; PF02142; MGS; 1. DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1. DR SMART; SM00798; AICARFT_IMPCHas; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF52335; SSF52335; 1. DR SUPFAM; SSF53927; SSF53927; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Multifunctional enzyme; KW Purine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 452 Bifunctional purine biosynthesis protein FT PurH. FT /FTId=PRO_0000192142. FT STRAND 3 7 {ECO:0000244|PDB:1ZCZ}. FT HELIX 12 14 {ECO:0000244|PDB:1ZCZ}. FT HELIX 15 23 {ECO:0000244|PDB:1ZCZ}. FT STRAND 27 30 {ECO:0000244|PDB:1ZCZ}. FT HELIX 32 40 {ECO:0000244|PDB:1ZCZ}. FT HELIX 48 51 {ECO:0000244|PDB:1ZCZ}. FT HELIX 57 60 {ECO:0000244|PDB:1ZCZ}. FT TURN 61 64 {ECO:0000244|PDB:1ZCZ}. FT HELIX 67 74 {ECO:0000244|PDB:1ZCZ}. FT STRAND 75 77 {ECO:0000244|PDB:1ZCZ}. FT STRAND 81 85 {ECO:0000244|PDB:1ZCZ}. FT HELIX 96 106 {ECO:0000244|PDB:1ZCZ}. FT TURN 107 110 {ECO:0000244|PDB:1ZCZ}. FT STRAND 112 114 {ECO:0000244|PDB:1ZCZ}. FT HELIX 117 125 {ECO:0000244|PDB:1ZCZ}. FT HELIX 129 154 {ECO:0000244|PDB:1ZCZ}. FT STRAND 158 165 {ECO:0000244|PDB:1ZCZ}. FT STRAND 172 174 {ECO:0000244|PDB:1ZCZ}. FT STRAND 179 183 {ECO:0000244|PDB:1ZCZ}. FT STRAND 186 190 {ECO:0000244|PDB:1ZCZ}. FT STRAND 192 194 {ECO:0000244|PDB:1ZCZ}. FT HELIX 198 212 {ECO:0000244|PDB:1ZCZ}. FT STRAND 215 223 {ECO:0000244|PDB:1ZCZ}. FT STRAND 226 232 {ECO:0000244|PDB:1ZCZ}. FT HELIX 236 246 {ECO:0000244|PDB:1ZCZ}. FT TURN 247 253 {ECO:0000244|PDB:1ZCZ}. FT STRAND 254 260 {ECO:0000244|PDB:1ZCZ}. FT HELIX 264 269 {ECO:0000244|PDB:1ZCZ}. FT STRAND 274 278 {ECO:0000244|PDB:1ZCZ}. FT HELIX 284 290 {ECO:0000244|PDB:1ZCZ}. FT STRAND 296 300 {ECO:0000244|PDB:1ZCZ}. FT STRAND 306 311 {ECO:0000244|PDB:1ZCZ}. FT STRAND 314 319 {ECO:0000244|PDB:1ZCZ}. FT STRAND 328 332 {ECO:0000244|PDB:1ZCZ}. FT HELIX 337 352 {ECO:0000244|PDB:1ZCZ}. FT STRAND 358 362 {ECO:0000244|PDB:1ZCZ}. FT STRAND 365 370 {ECO:0000244|PDB:1ZCZ}. FT HELIX 376 387 {ECO:0000244|PDB:1ZCZ}. FT HELIX 388 391 {ECO:0000244|PDB:1ZCZ}. FT STRAND 395 400 {ECO:0000244|PDB:1ZCZ}. FT HELIX 405 413 {ECO:0000244|PDB:1ZCZ}. FT STRAND 418 421 {ECO:0000244|PDB:1ZCZ}. FT HELIX 428 438 {ECO:0000244|PDB:1ZCZ}. FT STRAND 441 444 {ECO:0000244|PDB:1ZCZ}. SQ SEQUENCE 452 AA; 49867 MW; E4537EF51A5C4469 CRC64; MKRILVSLYE KEKYLDILRE LHEKGWEIWA SSGTAKFLKS NGIEANDVST ITGFENLLGG LVKTLHPEIF AGILGPEPRW DVVFVDLYPP PDIDIGGVAL LRAAAKNWKK VKPAFDMETL KLAIEIDDEE TRKYLAGMTF AFTSVYDSIR ANQFVEGISL AFKREDLQLR YGENPHEKAF VYGKPAFEIL HEGKTISFNN ILDAENAWFM AKNLPRMGAV VVKHQSPCGA AIGEDKVEIV KKAIEADDES SFGGILAVNF EMDEEVAKSL KKYLEVIVAP SFTQEAIEVL SKKKVRLLKP GDYASWAGKM AFGSLVLSER KYPEGNFELV VGEPLSEKEL EDLEFAYRVV EGAKSNAVLI AKDGVTVGIG SGQPSRKRAA WIATVMAGEK AKGAVAASDA FFPFPDSLEI LAQAGVKAVV APLGSIRDEE VIEKARELGI TFYKAPSRVF RH // ID PURQ_THEMA Reviewed; 213 AA. AC Q9X0X2; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 128. DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurQ {ECO:0000255|HAMAP-Rule:MF_00421}; DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00421}; DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00421}; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit I {ECO:0000255|HAMAP-Rule:MF_00421}; DE Short=FGAR amidotransferase I {ECO:0000255|HAMAP-Rule:MF_00421}; DE Short=FGAR-AT I {ECO:0000255|HAMAP-Rule:MF_00421}; DE AltName: Full=Glutaminase PurQ {ECO:0000255|HAMAP-Rule:MF_00421}; DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00421}; DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit I {ECO:0000255|HAMAP-Rule:MF_00421}; GN Name=purQ {ECO:0000255|HAMAP-Rule:MF_00421}; GN OrderedLocusNames=TM_1245; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), FUNCTION, ACTIVE SITE, AND RP SUBUNIT. RX PubMed=18597481; DOI=10.1021/bi800329p; RA Morar M., Hoskins A.A., Stubbe J., Ealick S.E.; RT "Formylglycinamide ribonucleotide amidotransferase from Thermotoga RT maritima: structural insights into complex formation."; RL Biochemistry 47:7816-7830(2008). CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase CC complex involved in the purines biosynthetic pathway. Catalyzes CC the ATP-dependent conversion of formylglycinamide ribonucleotide CC (FGAR) and glutamine to yield formylglycinamidine ribonucleotide CC (FGAM) and glutamate. The FGAM synthase complex is composed of CC three subunits. PurQ produces an ammonia molecule by converting CC glutamine to glutamate. PurL transfers the ammonia molecule to CC FGAR to form FGAM in an ATP-dependent manner. PurS interacts with CC PurQ and PurL and is thought to assist in the transfer of the CC ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP- CC Rule:MF_00421, ECO:0000269|PubMed:18597481}. CC -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D- CC ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- CC (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00421}. CC -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3). CC {ECO:0000255|HAMAP-Rule:MF_00421}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_00421}. CC -!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1 CC PurQ and 2 PurS subunits. {ECO:0000255|HAMAP-Rule:MF_00421, CC ECO:0000269|PubMed:18597481}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00421}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_00421}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36320.1; -; Genomic_DNA. DR PIR; G72276; G72276. DR RefSeq; NP_229050.1; NC_000853.1. DR RefSeq; WP_004080023.1; NZ_CP011107.1. DR PDB; 3D54; X-ray; 3.50 A; D/H/L=1-213. DR PDBsum; 3D54; -. DR ProteinModelPortal; Q9X0X2; -. DR SMR; Q9X0X2; 1-212. DR STRING; 243274.TM1245; -. DR DNASU; 898238; -. DR EnsemblBacteria; AAD36320; AAD36320; TM_1245. DR GeneID; 898238; -. DR KEGG; tma:TM1245; -. DR PATRIC; 23937430; VBITheMar51294_1261. DR eggNOG; ENOG4105D21; Bacteria. DR eggNOG; COG0047; LUCA. DR InParanoid; Q9X0X2; -. DR KO; K01952; -. DR OMA; HAEGRFY; -. DR OrthoDB; EOG6P5ZJP; -. DR UniPathway; UPA00074; UER00128. DR EvolutionaryTrace; Q9X0X2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC. DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00421; PurQ; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ. DR PIRSF; PIRSF001586; FGAM_synth_I; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01737; FGAM_synth_I; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; KW Glutamine amidotransferase; Hydrolase; Ligase; Nucleotide-binding; KW Purine biosynthesis; Reference proteome. FT CHAIN 1 213 Phosphoribosylformylglycinamidine FT synthase subunit PurQ. FT /FTId=PRO_0000100598. FT DOMAIN 5 213 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_00421}. FT ACT_SITE 86 86 Nucleophile. FT {ECO:0000305|PubMed:18597481}. FT ACT_SITE 186 186 {ECO:0000305|PubMed:18597481}. FT ACT_SITE 188 188 {ECO:0000305|PubMed:18597481}. FT STRAND 4 8 {ECO:0000244|PDB:3D54}. FT STRAND 13 15 {ECO:0000244|PDB:3D54}. FT HELIX 16 24 {ECO:0000244|PDB:3D54}. FT TURN 25 27 {ECO:0000244|PDB:3D54}. FT STRAND 29 33 {ECO:0000244|PDB:3D54}. FT STRAND 43 47 {ECO:0000244|PDB:3D54}. FT HELIX 52 55 {ECO:0000244|PDB:3D54}. FT HELIX 61 64 {ECO:0000244|PDB:3D54}. FT HELIX 69 78 {ECO:0000244|PDB:3D54}. FT STRAND 81 84 {ECO:0000244|PDB:3D54}. FT HELIX 86 94 {ECO:0000244|PDB:3D54}. FT STRAND 100 103 {ECO:0000244|PDB:3D54}. FT STRAND 106 109 {ECO:0000244|PDB:3D54}. FT STRAND 114 119 {ECO:0000244|PDB:3D54}. FT STRAND 135 139 {ECO:0000244|PDB:3D54}. FT STRAND 142 144 {ECO:0000244|PDB:3D54}. FT STRAND 146 148 {ECO:0000244|PDB:3D54}. FT STRAND 154 161 {ECO:0000244|PDB:3D54}. FT HELIX 167 169 {ECO:0000244|PDB:3D54}. FT STRAND 170 174 {ECO:0000244|PDB:3D54}. FT STRAND 176 178 {ECO:0000244|PDB:3D54}. FT STRAND 180 183 {ECO:0000244|PDB:3D54}. FT TURN 188 191 {ECO:0000244|PDB:3D54}. FT TURN 193 196 {ECO:0000244|PDB:3D54}. FT HELIX 202 210 {ECO:0000244|PDB:3D54}. SQ SEQUENCE 213 AA; 23588 MW; A68B5A2861B0698A CRC64; MKPRACVVVY PGSNCDRDAY HALEINGFEP SYVGLDDKLD DYELIILPGG FSYGDYLRPG AVAAREKIAF EIAKAAERGK LIMGICNGFQ ILIEMGLLKG ALLQNSSGKF ICKWVDLIVE NNDTPFTNAF EKGEKIRIPI AHGFGRYVKI DDVNVVLRYV KDVNGSDERI AGVLNESGNV FGLMPHPERA VEELIGGEDG KKVFQSILNY LKR // ID PURS_THEMA Reviewed; 82 AA. AC Q9X0X1; G4FEA4; DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurS {ECO:0000255|HAMAP-Rule:MF_01926}; DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_01926}; DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_01926}; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit III {ECO:0000255|HAMAP-Rule:MF_01926}; DE Short=FGAR amidotransferase III {ECO:0000255|HAMAP-Rule:MF_01926}; DE Short=FGAR-AT III {ECO:0000255|HAMAP-Rule:MF_01926}; DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit III {ECO:0000255|HAMAP-Rule:MF_01926}; GN Name=purS {ECO:0000255|HAMAP-Rule:MF_01926}; GN OrderedLocusNames=TM_1244; ORFNames=THEMA_08115, Tmari_1249; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RG DOE Joint Genome Institute; RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [4] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT. RX PubMed=16865708; DOI=10.1002/prot.21024; RA Mathews I.I., Krishna S.S., Schwarzenbacher R., McMullan D., RA Jaroszewski L., Miller M.D., Abdubek P., Agarwalla S., Ambing E., RA Axelrod H.L., Canaves J.M., Carlton D., Chiu H.J., Clayton T., RA DiDonato M., Duan L., Elsliger M.A., Grzechnik S.K., Hale J., RA Hampton E., Haugen J., Jin K.K., Klock H.E., Koesema E., Kovarik J.S., RA Kreusch A., Kuhn P., Levin I., Morse A.T., Nigoghossian E., Okach L., RA Oommachen S., Paulsen J., Quijano K., Reyes R., Rife C.L., RA Spraggon G., Stevens R.C., van den Bedem H., White A., Wolf G., Xu Q., RA Hodgson K.O., Wooley J., Deacon A.M., Godzik A., Lesley S.A., RA Wilson I.A.; RT "Crystal structure of phosphoribosylformyl-glycinamidine synthase II, RT PurS subunit (TM1244) from Thermotoga maritima at 1.90 A resolution."; RL Proteins 65:249-254(2006). RN [5] RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, RP AND SUBUNIT. RX PubMed=18597481; DOI=10.1021/bi800329p; RA Morar M., Hoskins A.A., Stubbe J., Ealick S.E.; RT "Formylglycinamide ribonucleotide amidotransferase from Thermotoga RT maritima: structural insights into complex formation."; RL Biochemistry 47:7816-7830(2008). CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase CC complex involved in the purines biosynthetic pathway. Catalyzes CC the ATP-dependent conversion of formylglycinamide ribonucleotide CC (FGAR) and glutamine to yield formylglycinamidine ribonucleotide CC (FGAM) and glutamate. The FGAM synthase complex is composed of CC three subunits. PurQ produces an ammonia molecule by converting CC glutamine to glutamate. PurL transfers the ammonia molecule to CC FGAR to form FGAM in an ATP-dependent manner. PurS interacts with CC PurQ and PurL and is thought to assist in the transfer of the CC ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP- CC Rule:MF_01926, ECO:0000269|PubMed:18597481}. CC -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D- CC ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- CC (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_01926, ECO:0000269|PubMed:18597481}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_01926}. CC -!- SUBUNIT: Homodimer. Part of the FGAM synthase complex composed of CC 1 PurL, 1 PurQ and 2 PurS subunits. {ECO:0000269|PubMed:16865708, CC ECO:0000269|PubMed:18597481}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01926}. CC -!- SIMILARITY: Belongs to the PurS family. {ECO:0000255|HAMAP- CC Rule:MF_01926}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36319.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50173.1; -; Genomic_DNA. DR EMBL; CP007013; AHD18851.1; -; Genomic_DNA. DR PIR; F72276; F72276. DR RefSeq; NP_229049.1; NC_000853.1. DR RefSeq; WP_004080026.1; NZ_CP011107.1. DR PDB; 1VQ3; X-ray; 1.90 A; A/B/C/D=1-82. DR PDB; 3D54; X-ray; 3.50 A; B/C/F/G/J/K=1-82. DR PDBsum; 1VQ3; -. DR PDBsum; 3D54; -. DR ProteinModelPortal; Q9X0X1; -. DR SMR; Q9X0X1; 1-82. DR STRING; 243274.TM1244; -. DR EnsemblBacteria; AAD36319; AAD36319; TM_1244. DR EnsemblBacteria; AGL50173; AGL50173; Tmari_1249. DR EnsemblBacteria; AHD18851; AHD18851; THEMA_08115. DR GeneID; 898239; -. DR KEGG; tma:TM1244; -. DR KEGG; tmi:THEMA_08115; -. DR KEGG; tmm:Tmari_1249; -. DR KEGG; tmw:THMA_1269; -. DR PATRIC; 23937428; VBITheMar51294_1260. DR eggNOG; ENOG4108A1T; Bacteria. DR eggNOG; COG1828; LUCA. DR InParanoid; Q9X0X1; -. DR KO; K01952; -. DR OMA; DIQYKSN; -. DR OrthoDB; EOG6TFCXJ; -. DR BioCyc; TMAR243274:GC6P-1275-MONOMER; -. DR BRENDA; 6.3.5.3; 6331. DR UniPathway; UPA00074; UER00128. DR EvolutionaryTrace; Q9X0X1; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1280.10; -; 1. DR HAMAP; MF_01926; PurS; 1. DR InterPro; IPR003850; PurS. DR Pfam; PF02700; PurS; 1. DR ProDom; PD010362; FGAM_PurS; 1. DR TIGRFAMs; TIGR00302; TIGR00302; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Ligase; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1 82 Phosphoribosylformylglycinamidine FT synthase subunit PurS. FT /FTId=PRO_0000430099. FT STRAND 3 12 {ECO:0000244|PDB:1VQ3}. FT HELIX 19 30 {ECO:0000244|PDB:1VQ3}. FT STRAND 36 50 {ECO:0000244|PDB:1VQ3}. FT HELIX 54 67 {ECO:0000244|PDB:1VQ3}. FT TURN 72 74 {ECO:0000244|PDB:1VQ3}. FT STRAND 75 81 {ECO:0000244|PDB:1VQ3}. SQ SEQUENCE 82 AA; 9639 MW; 1B8470FFF1C78673 CRC64; MPLFKFAIDV QYRSNVRDPR GETIERVLRE EKGLPVKKLR LGKSIHLEVE AENKEKAYEI VKKACEELLV NPVVEEYEVR EL // ID PSTB_THEMA Reviewed; 251 AA. AC Q9X0Y8; DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Phosphate import ATP-binding protein PstB {ECO:0000255|HAMAP-Rule:MF_01702}; DE EC=3.6.3.27 {ECO:0000255|HAMAP-Rule:MF_01702}; DE AltName: Full=ABC phosphate transporter {ECO:0000255|HAMAP-Rule:MF_01702}; DE AltName: Full=Phosphate-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01702}; GN Name=pstB {ECO:0000255|HAMAP-Rule:MF_01702}; GN OrderedLocusNames=TM_1261; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in CC phosphate import. Responsible for energy coupling to the transport CC system. {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + phosphate(Out) = ADP + phosphate CC + phosphate(In). {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (PstB), two transmembrane proteins (PstC and PstA) and a solute- CC binding protein (PstS). {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01702}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01702}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate CC importer (TC 3.A.1.7) family. {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01702}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36335.1; -; Genomic_DNA. DR PIR; H72275; H72275. DR RefSeq; NP_229066.1; NC_000853.1. DR RefSeq; WP_004079999.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0Y8; -. DR STRING; 243274.TM1261; -. DR EnsemblBacteria; AAD36335; AAD36335; TM_1261. DR GeneID; 898222; -. DR KEGG; tma:TM1261; -. DR PATRIC; 23937462; VBITheMar51294_1277. DR eggNOG; ENOG4105BZY; Bacteria. DR eggNOG; COG1117; LUCA. DR InParanoid; Q9X0Y8; -. DR KO; K02036; -. DR OMA; LVECDNT; -. DR OrthoDB; EOG6T7N3V; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015850; ABC_transpr_PstB. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005670; Phosp_transpt1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00972; 3a0107s01c2; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51238; PSTB; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Phosphate transport; KW Reference proteome; Transport. FT CHAIN 1 251 Phosphate import ATP-binding protein FT PstB. FT /FTId=PRO_0000092918. FT DOMAIN 5 246 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01702}. FT NP_BIND 37 44 ATP. {ECO:0000255|HAMAP-Rule:MF_01702}. SQ SEQUENCE 251 AA; 28516 MW; 007229375B59A620 CRC64; MEPIIEIENF SAYYGEKIAV KNVTMKIFKN QITAIIGPSG CGKTTLLRSI NRMNDHLPGF RVEGKIYFKG QDIYDPQLDV TEYRKRVGMV FQKPTPFPMS IYDNVAFGPR IHGVKSKHIL DRIVEESLKK AALWDEVKSE LNKSGTRLSG GQQQRLCIAR ALAVEPEVIL LDEPTSALDP IATQRIEKLL EELSENYTIV IVTHNIGQAI RIADYIAFMY RGELIEYGPT REIVERPKNR LTEEYLTGKI G // ID PURA_THEMA Reviewed; 397 AA. AC Q9X0I1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 117. DE RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AdSS {ECO:0000255|HAMAP-Rule:MF_00011}; DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_00011}; DE AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00011}; GN Name=purA {ECO:0000255|HAMAP-Rule:MF_00011}; GN OrderedLocusNames=TM_1096; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Plays an important role in the de novo pathway of purine CC nucleotide biosynthesis. Catalyzes the first committed step in the CC biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate + CC N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00011}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00011}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; CC AMP from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00011}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36172.1; -; Genomic_DNA. DR PIR; B72294; B72294. DR RefSeq; NP_228902.1; NC_000853.1. DR RefSeq; WP_004080356.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0I1; -. DR STRING; 243274.TM1096; -. DR EnsemblBacteria; AAD36172; AAD36172; TM_1096. DR GeneID; 898669; -. DR KEGG; tma:TM1096; -. DR PATRIC; 23937127; VBITheMar51294_1112. DR eggNOG; ENOG4105C91; Bacteria. DR eggNOG; COG0104; LUCA. DR InParanoid; Q9X0I1; -. DR KO; K01939; -. DR OMA; YAIEISG; -. DR OrthoDB; EOG68Q0QG; -. DR UniPathway; UPA00075; UER00335. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR HAMAP; MF_00011; Adenylosucc_synth; 1. DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd. DR InterPro; IPR001114; Adenylosuccinate_synthetase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000897; SRP54_GTPase_dom. DR PANTHER; PTHR11846; PTHR11846; 1. DR Pfam; PF00709; Adenylsucc_synt; 1. DR SMART; SM00788; Adenylsucc_synt; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00184; purA; 1. DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 397 Adenylosuccinate synthetase. FT /FTId=PRO_0000095248. FT NP_BIND 11 17 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 39 41 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 318 320 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 386 388 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT REGION 12 15 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT REGION 37 40 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT REGION 286 292 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT ACT_SITE 12 12 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT ACT_SITE 40 40 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT METAL 12 12 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT METAL 39 39 Magnesium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 125 125 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 139 139 IMP; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 212 212 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 227 227 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 290 290 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 292 292 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. SQ SEQUENCE 397 AA; 44516 MW; FE49BDC5F5B393AD CRC64; MNRVVVGLQW GDEGKGKVVT YLSRYHDIVA RFSGGANAGH TVNYGDFKVI HHLLPSADFT KNRGIAIGSG VLLDPQVLTE ELRELKEKFP DYSGEIFISE SAHVVLPVHK EMDRIIDEVL KIGTTKRGIG PACADRVMRV NVRVAELGNE EKLRYFLEKN LSLKKIYGVD FDAEKMMGDL STFYETIKDF VVSPVQLKRI LEEKSVLFEG TQGVLLDLDV GTYPYVTSMN CSSSGVSAGM GFPVEVDEVL GVFKAYTTRV GEGPFPTELT GEEGEKLRKA GHEYGSTTGR PRRCGWLDLP LLRYAIEISG VDSLVMTKAD VLNGFEKIKV CVRYSDGRDL VSLRDLEKKE PVYEVFDGWK SLEDKNFERF VDFIERETGR PVRYISTGEK LEDIVEV // ID PYRC_THEMA Reviewed; 376 AA. AC Q9WYH0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Dihydroorotase; DE Short=DHOase; DE EC=3.5.2.3; GN Name=pyrC; OrderedLocusNames=TM_0335; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L- CC aspartate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 3/3. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DHOase family. Type 2 subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35422.1; -; Genomic_DNA. DR PIR; A72391; A72391. DR RefSeq; NP_228146.1; NC_000853.1. DR RefSeq; WP_004083103.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYH0; -. DR STRING; 243274.TM0335; -. DR EnsemblBacteria; AAD35422; AAD35422; TM_0335. DR GeneID; 897290; -. DR KEGG; tma:TM0335; -. DR KEGG; tmi:THEMA_03045; -. DR KEGG; tmw:THMA_0343; -. DR PATRIC; 23935551; VBITheMar51294_0340. DR eggNOG; ENOG4107VJ5; Bacteria. DR eggNOG; COG0044; LUCA. DR InParanoid; Q9WYH0; -. DR KO; K01465; -. DR OMA; PYGSSHI; -. DR OrthoDB; EOG6KHFW6; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00220_B; PyrC_type2_B; 1. DR InterPro; IPR004722; DHOase. DR InterPro; IPR002195; Dihydroorotase_CS. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR SUPFAM; SSF51338; SSF51338; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR PROSITE; PS00482; DIHYDROOROTASE_1; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 376 Dihydroorotase. FT /FTId=PRO_0000147264. FT COMPBIAS 128 132 Poly-Lys. FT METAL 35 35 Zinc 1. {ECO:0000250}. FT METAL 37 37 Zinc 1. {ECO:0000250}. FT METAL 138 138 Zinc 2. {ECO:0000250}. FT METAL 187 187 Zinc 2. {ECO:0000250}. FT METAL 257 257 Zinc 1. {ECO:0000250}. SQ SEQUENCE 376 AA; 42633 MW; C65EDF6EE0A95A81 CRC64; MRIYDPFRKK WIEEEIETPF PSKGLVATFP FVDLHVHVRL NGGEDYSSLE EASLVGGFFK VVVQPNTKPL IDSKEVLERH LDLSKNRAVE FLFAVSPFGS IEAEGERVVG FSTDGIEYDY PTLVETMKKK KKALWFDHSQ MYEVDGIFYE GAPLPFQKRP RSNEAIAIAR TVLTGLEYGF ERFHIQHVTT KYSVEVISFL KNLAKVSCEV TPHHLFFCYE DIKNTNFKIN PPLGSPEDRR ALIEAVKKDV IDVLATDHAP HHEKPDDFLT APYGSTSIEI AFPAYYTALG DLELVVKKLT KKPLEVLGVE ARLTEDTLVF IDPEAEFIVD AKKFKSKGKN SMFDGVRLKG KVVALKLKGR WVMIDGEVIA DQKEND // ID PYRDB_THEMA Reviewed; 270 AA. AC Q9WYG8; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 118. DE RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit; DE Short=DHOD B; DE Short=DHODase B; DE Short=DHOdehase B; DE EC=1.3.1.14; DE AltName: Full=Dihydroorotate oxidase B; DE AltName: Full=Orotate reductase (NADH); GN Name=pyrD; OrderedLocusNames=TM_0333; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate CC with NAD(+) as electron acceptor. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + NAD(+) = orotate + NADH. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC Note=Binds 1 FMN per subunit. {ECO:0000250}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1. CC -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. CC Type 1 subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35420.1; -; Genomic_DNA. DR PIR; G72390; G72390. DR RefSeq; NP_228144.1; NC_000853.1. DR RefSeq; WP_004083101.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYG8; -. DR STRING; 243274.TM0333; -. DR EnsemblBacteria; AAD35420; AAD35420; TM_0333. DR GeneID; 897288; -. DR KEGG; tma:TM0333; -. DR PATRIC; 23935547; VBITheMar51294_0338. DR eggNOG; ENOG4107W93; Bacteria. DR eggNOG; COG0167; LUCA. DR InParanoid; Q9WYG8; -. DR KO; K17828; -. DR OMA; EMMIAGA; -. DR OrthoDB; EOG6NPM9S; -. DR UniPathway; UPA00070; UER00945. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004589; F:orotate reductase (NADH) activity; IEA:UniProtKB-EC. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00224; DHO_dh_type1; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005720; Dihydroorotate_DH. DR InterPro; IPR024920; Dihydroorotate_DH_1. DR InterPro; IPR012135; Dihydroorotate_DH_1_2. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR Pfam; PF01180; DHO_dh; 1. DR PIRSF; PIRSF000164; DHO_oxidase; 1. DR TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1. DR PROSITE; PS00911; DHODEHASE_1; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Flavoprotein; FMN; NAD; Oxidoreductase; KW Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 270 Dihydroorotate dehydrogenase B (NAD(+)), FT catalytic subunit. FT /FTId=PRO_0000148404. FT NP_BIND 35 36 FMN. {ECO:0000250}. FT NP_BIND 226 227 FMN. {ECO:0000250}. FT NP_BIND 248 249 FMN. {ECO:0000250}. FT REGION 59 63 Substrate binding. {ECO:0000250}. FT REGION 180 181 Substrate binding. {ECO:0000250}. FT ACT_SITE 117 117 Nucleophile. FT BINDING 12 12 FMN. {ECO:0000250}. FT BINDING 35 35 Substrate. {ECO:0000250}. FT BINDING 114 114 FMN. {ECO:0000250}. FT BINDING 114 114 Substrate. {ECO:0000250}. FT BINDING 153 153 FMN. {ECO:0000250}. FT BINDING 179 179 FMN; via carbonyl oxygen. {ECO:0000250}. FT BINDING 199 199 FMN; via amide nitrogen. {ECO:0000250}. SQ SEQUENCE 270 AA; 29742 MW; E773E89BDB473C20 CRC64; MLELKPPLVL LSGPAGFGEY LKLMDHRYVG GVLLKTVTLH PKEGNPTPRM ADSDFYVINR IGLENPGIHA FVENIPELPV PMIASLGGDS FEEYLEVARV FKKVADRFYA VEFNFSCPNV KEGGLSIVKN AEEWKKLLNT LRKELPDSFL IAKVGVEGIF VEDAAEFVMK TGWDGITLVN TVRGLHFEKD TMILGGLSGP VLKPIALRAV YEVKKRFPEL FVIASGGVYS VKDAEEFLKV GADVIGVGSA LFKDPGVVEE IGKYLLEVKR // ID PTLY_THEMA Reviewed; 367 AA. AC Q9WYR4; DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Pectate trisaccharide-lyase; DE EC=4.2.2.22; DE AltName: Full=Pectate lyase A {ECO:0000303|PubMed:12443532, ECO:0000312|EMBL:AAD35518.1}; DE Short=PelA {ECO:0000303|PubMed:12443532}; DE Flags: Precursor; GN Name=pelA {ECO:0000303|PubMed:12443532}; OrderedLocusNames=TM_0433; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] {ECO:0000312|EMBL:AAD35518.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000269|PubMed:12443532}; RX PubMed=12443532; DOI=10.1042/BJ20021595; RA Kluskens L.D., van Alebeek G.J., Voragen A.G., de Vos W.M., RA van der Oost J.; RT "Molecular and biochemical characterization of the thermoactive family RT 1 pectate lyase from the hyperthermophilic bacterium Thermotoga RT maritima."; RL Biochem. J. 370:651-659(2003). CC -!- FUNCTION: Cleaves unsaturated trigalacturonate from pectin. CC Activity is highest towards polygalacturonic acid, activity on CC methylated pectins decreases with an increasing degree of CC methylation. {ECO:0000269|PubMed:12443532}. CC -!- CATALYTIC ACTIVITY: Eliminative cleavage of unsaturated CC trigalacturonate as the major product from the reducing end of CC polygalacturonic acid/pectate. {ECO:0000269|PubMed:12443532}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:12443532}; CC -!- ENZYME REGULATION: Completely inactivated by EGTA. CC {ECO:0000269|PubMed:12443532}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.6 mM for polygalacturonic acid CC {ECO:0000269|PubMed:12443532}; CC pH dependence: CC Optimum pH is 9.0. {ECO:0000269|PubMed:12443532}; CC Temperature dependence: CC Optimum temperature is 90 degrees Celsius. Half-life in the CC presence of 0.6 mM CaCl(2) is 110 minutes at 95 degrees Celsius CC and 15 minutes at 100 degrees Celsius. Half-life in the absence CC of CaCl(2) is 5 minutes at 90 degrees Celsius. CC {ECO:0000269|PubMed:12443532}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12443532}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space CC {ECO:0000269|PubMed:12443532}. CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. CC {ECO:0000255}. CC -!- SIMILARITY: Contains 2 PbH1 repeats. {ECO:0000255}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35518.1; -; Genomic_DNA. DR PIR; D72376; D72376. DR RefSeq; NP_228243.1; NC_000853.1. DR RefSeq; WP_010865117.1; NC_000853.1. DR PDB; 3ZSC; X-ray; 1.94 A; A=28-367. DR PDBsum; 3ZSC; -. DR ProteinModelPortal; Q9WYR4; -. DR STRING; 243274.TM0433; -. DR CAZy; PL1; Polysaccharide Lyase Family 1. DR EnsemblBacteria; AAD35518; AAD35518; TM_0433. DR GeneID; 897446; -. DR KEGG; tma:TM0433; -. DR PATRIC; 23935751; VBITheMar51294_0439. DR eggNOG; ENOG4105DBA; Bacteria. DR eggNOG; COG3866; LUCA. DR InParanoid; Q9WYR4; -. DR KO; K01728; -. DR OMA; NNYYENV; -. DR OrthoDB; EOG63RGPQ; -. DR BioCyc; MetaCyc:MONOMER-17962; -. DR BioCyc; TMAR243274:GC6P-448-MONOMER; -. DR BRENDA; 4.2.2.2; 6331. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.160.20.10; -; 1. DR InterPro; IPR002022; Amb_allergen_dom. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR Pfam; PF00544; Pec_lyase_C; 1. DR SMART; SM00656; Amb_all; 1. DR SUPFAM; SSF51126; SSF51126; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Carbohydrate metabolism; KW Cell wall biogenesis/degradation; Complete proteome; Lyase; KW Metal-binding; Polysaccharide degradation; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 367 Pectate trisaccharide-lyase. FT {ECO:0000255}. FT /FTId=PRO_0000405016. FT REPEAT 151 173 PbH1 1. {ECO:0000255}. FT REPEAT 263 289 PbH1 2. {ECO:0000255}. FT ACT_SITE 224 224 {ECO:0000250|UniProtKB:P39116}. FT METAL 144 144 Calcium. {ECO:0000250|UniProtKB:P39116}. FT METAL 166 166 Calcium. {ECO:0000250|UniProtKB:P39116}. FT METAL 170 170 Calcium. {ECO:0000250|UniProtKB:P39116}. FT HELIX 36 38 {ECO:0000244|PDB:3ZSC}. FT TURN 50 53 {ECO:0000244|PDB:3ZSC}. FT STRAND 54 59 {ECO:0000244|PDB:3ZSC}. FT HELIX 62 69 {ECO:0000244|PDB:3ZSC}. FT STRAND 71 73 {ECO:0000244|PDB:3ZSC}. FT STRAND 75 93 {ECO:0000244|PDB:3ZSC}. FT STRAND 95 116 {ECO:0000244|PDB:3ZSC}. FT STRAND 118 124 {ECO:0000244|PDB:3ZSC}. FT STRAND 126 128 {ECO:0000244|PDB:3ZSC}. FT STRAND 145 150 {ECO:0000244|PDB:3ZSC}. FT STRAND 152 158 {ECO:0000244|PDB:3ZSC}. FT STRAND 160 163 {ECO:0000244|PDB:3ZSC}. FT STRAND 168 172 {ECO:0000244|PDB:3ZSC}. FT STRAND 176 182 {ECO:0000244|PDB:3ZSC}. FT STRAND 184 187 {ECO:0000244|PDB:3ZSC}. FT HELIX 202 207 {ECO:0000244|PDB:3ZSC}. FT STRAND 210 215 {ECO:0000244|PDB:3ZSC}. FT STRAND 217 220 {ECO:0000244|PDB:3ZSC}. FT STRAND 227 237 {ECO:0000244|PDB:3ZSC}. FT STRAND 239 241 {ECO:0000244|PDB:3ZSC}. FT STRAND 256 261 {ECO:0000244|PDB:3ZSC}. FT STRAND 265 270 {ECO:0000244|PDB:3ZSC}. FT STRAND 272 274 {ECO:0000244|PDB:3ZSC}. FT HELIX 278 282 {ECO:0000244|PDB:3ZSC}. FT STRAND 287 292 {ECO:0000244|PDB:3ZSC}. FT TURN 294 296 {ECO:0000244|PDB:3ZSC}. FT STRAND 299 302 {ECO:0000244|PDB:3ZSC}. FT HELIX 305 307 {ECO:0000244|PDB:3ZSC}. FT STRAND 310 314 {ECO:0000244|PDB:3ZSC}. FT HELIX 331 333 {ECO:0000244|PDB:3ZSC}. FT HELIX 342 344 {ECO:0000244|PDB:3ZSC}. FT HELIX 345 352 {ECO:0000244|PDB:3ZSC}. SQ SEQUENCE 367 AA; 40607 MW; FDF57647B8476195 CRC64; MLMRFSRVVS LVLLLVFTAV LTGAVKASLN DKPVGFASVP TADLPEGTVG GLGGEIVFVR TAEELEKYTT AEGKYVIVVD GTIVFEPKRE IKVLSDKTIV GINDAKIVGG GLVIKDAQNV IIRNIHFEGF YMEDDPRGKK YDFDYINVEN SHHIWIDHCT FVNGNDGAVD IKKYSNYITV SWCKFVDHDK VSLVGSSDKE DPEQAGQAYK VTYHHNYFKN CIQRMPRIRF GMAHVFNNFY SMGLRTGVSG NVFPIYGVAS AMGAKVHVEG NYFMGYGAVM AEAGIAFLPT RIMGPVEGYL TLGEGDAKNE FYYCKEPEVR PVEEGKPALD PREYYDYTLD PVQDVPKIVV DGAGAGKLVF EELNTAQ // ID PURL_THEMA Reviewed; 603 AA. AC Q9X0X3; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 20-JAN-2016, entry version 118. DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000255|HAMAP-Rule:MF_00420}; DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00420}; DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00420}; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000255|HAMAP-Rule:MF_00420}; DE Short=FGAR amidotransferase II {ECO:0000255|HAMAP-Rule:MF_00420}; DE Short=FGAR-AT II {ECO:0000255|HAMAP-Rule:MF_00420}; DE AltName: Full=Glutamine amidotransferase PurL {ECO:0000255|HAMAP-Rule:MF_00420}; DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000255|HAMAP-Rule:MF_00420}; GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00420}; GN OrderedLocusNames=TM_1246; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-72 RP IN COMPLEX WITH SUBSTRATE ANALOGS; ATP AND MAGNESIUM, FUNCTION, RP CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-32 AND HIS-72, ACTIVE SITE, RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=17154526; DOI=10.1021/bi061591u; RA Morar M., Anand R., Hoskins A.A., Stubbe J., Ealick S.E.; RT "Complexed structures of formylglycinamide ribonucleotide RT amidotransferase from Thermotoga maritima describe a novel ATP binding RT protein superfamily."; RL Biochemistry 45:14880-14895(2006). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=16544324; DOI=10.1002/prot.20650; RA Mathews I.I., Krishna S.S., Schwarzenbacher R., McMullan D., RA Abdubek P., Ambing E., Canaves J.M., Chiu H.J., Deacon A.M., RA DiDonato M., Elsliger M.A., Godzik A., Grittini C., Grzechnik S.K., RA Hale J., Hampton E., Han G.W., Haugen J., Jaroszewski L., Klock H.E., RA Koesema E., Kreusch A., Kuhn P., Lesley S.A., Levin I., Miller M.D., RA Moy K., Nigoghossian E., Paulsen J., Quijano K., Reyes R., RA Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., White A., RA Wolf G., Xu Q., Hodgson K.O., Wooley J., Wilson I.A.; RT "Crystal structure of phosphoribosylformylglycinamidine synthase II RT (smPurL) from Thermotoga maritima at 2.15 A resolution."; RL Proteins 63:1106-1111(2006). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH ATP, FUNCTION, RP AND SUBUNIT. RX PubMed=18597481; DOI=10.1021/bi800329p; RA Morar M., Hoskins A.A., Stubbe J., Ealick S.E.; RT "Formylglycinamide ribonucleotide amidotransferase from Thermotoga RT maritima: structural insights into complex formation."; RL Biochemistry 47:7816-7830(2008). CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase CC complex involved in the purines biosynthetic pathway. Catalyzes CC the ATP-dependent conversion of formylglycinamide ribonucleotide CC (FGAR) and glutamine to yield formylglycinamidine ribonucleotide CC (FGAM) and glutamate. The FGAM synthase complex is composed of CC three subunits. PurQ produces an ammonia molecule by converting CC glutamine to glutamate. PurL transfers the ammonia molecule to CC FGAR to form FGAM in an ATP-dependent manner. PurS interacts with CC PurQ and PurL and is thought to assist in the transfer of the CC ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP- CC Rule:MF_00420, ECO:0000269|PubMed:17154526, CC ECO:0000269|PubMed:18597481}. CC -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D- CC ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- CC (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.26 mM for ATP (at pH 8 and 37 degrees Celsius) CC {ECO:0000269|PubMed:17154526}; CC KM=1.05 mM for FGAR (at pH 8 and 37 degrees Celsius) CC {ECO:0000269|PubMed:17154526}; CC KM=158 mM for NH(4)Cl (at pH 8 and 37 degrees Celsius) CC {ECO:0000269|PubMed:17154526}; CC Note=Kcat is 0.39 sec(-1) for FGAM synthase activity with CC NH(4)Cl as substrate (at pH 8 and 37 degrees Celsius). Kcat is CC 0.40 sec(-1) for FGAM synthase activity with FGAR as substrate CC (at pH 8 and 37 degrees Celsius). Kcat is 0.41 sec(-1) for FGAM CC synthase activity with ATP as substrate (at pH 8 and 37 degrees CC Celsius).; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_00420}. CC -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1 CC PurL, 1 PurQ and 2 PurS subunits. {ECO:0000255|HAMAP- CC Rule:MF_00420, ECO:0000269|PubMed:16544324, CC ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}. CC -!- MISCELLANEOUS: Purl possesses an Auxiliary ATP Binding region CC which is not catalytic, but able to bind additional ATP. The CC conformational changes associated with its binding could have a CC regulatory role in formation of the PurLSQ complex CC (PubMed:17154526). {ECO:0000305|PubMed:17154526}. CC -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000255|HAMAP- CC Rule:MF_00420}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36321.1; -; Genomic_DNA. DR PIR; H72276; H72276. DR RefSeq; NP_229051.1; NC_000853.1. DR RefSeq; WP_004080021.1; NC_000853.1. DR PDB; 1VK3; X-ray; 2.15 A; A=1-603. DR PDB; 2HRU; X-ray; 2.80 A; A=1-603. DR PDB; 2HRY; X-ray; 2.80 A; A=1-603. DR PDB; 2HS0; X-ray; 2.52 A; A=1-603. DR PDB; 2HS3; X-ray; 2.30 A; A=1-603. DR PDB; 2HS4; X-ray; 2.70 A; A=1-603. DR PDB; 3D54; X-ray; 3.50 A; A/E/I=1-603. DR PDBsum; 1VK3; -. DR PDBsum; 2HRU; -. DR PDBsum; 2HRY; -. DR PDBsum; 2HS0; -. DR PDBsum; 2HS3; -. DR PDBsum; 2HS4; -. DR PDBsum; 3D54; -. DR ProteinModelPortal; Q9X0X3; -. DR SMR; Q9X0X3; 2-603. DR STRING; 243274.TM1246; -. DR EnsemblBacteria; AAD36321; AAD36321; TM_1246. DR GeneID; 898237; -. DR KEGG; tma:TM1246; -. DR KEGG; tmw:THMA_1271; -. DR PATRIC; 23937432; VBITheMar51294_1262. DR eggNOG; ENOG4108JIU; Bacteria. DR eggNOG; COG0046; LUCA. DR InParanoid; Q9X0X3; -. DR KO; K01952; -. DR OMA; EHCGYSH; -. DR OrthoDB; EOG6FNHHR; -. DR BRENDA; 6.3.5.3; 6331. DR UniPathway; UPA00074; UER00128. DR EvolutionaryTrace; Q9X0X3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IDA:UniProtKB. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:UniProtKB. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.1330.10; -; 2. DR HAMAP; MF_00420; PurL_2; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR010074; PRibForGlyAmidine_synth_PurL. DR InterPro; IPR031652; PurL_C. DR InterPro; IPR016188; PurM-like_N. DR Pfam; PF00586; AIRS; 2. DR Pfam; PF02769; AIRS_C; 1. DR Pfam; PF16904; PurL_C; 1. DR SUPFAM; SSF56042; SSF56042; 2. DR TIGRFAMs; TIGR01736; FGAM_synth_II; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Ligase; KW Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 603 Phosphoribosylformylglycinamidine FT synthase subunit PurL. FT /FTId=PRO_0000100501. FT NP_BIND 136 139 Auxiliary ATP binding site. FT REGION 71 74 Substrate binding. FT REGION 280 282 Substrate binding. FT ACT_SITE 32 32 {ECO:0000255|HAMAP-Rule:MF_00420, FT ECO:0000269|PubMed:17154526}. FT ACT_SITE 72 72 Proton acceptor. FT {ECO:0000305|PubMed:17154526}. FT METAL 70 70 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00420, FT ECO:0000269|PubMed:17154526}. FT METAL 94 94 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00420, FT ECO:0000269|PubMed:17154526}. FT METAL 236 236 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00420, FT ECO:0000269|PubMed:17154526}. FT METAL 478 478 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00420, FT ECO:0000269|PubMed:17154526}. FT BINDING 35 35 ATP. {ECO:0000255|HAMAP-Rule:MF_00420, FT ECO:0000269|PubMed:17154526, FT ECO:0000269|PubMed:18597481}. FT BINDING 68 68 ATP. {ECO:0000255|HAMAP-Rule:MF_00420, FT ECO:0000269|PubMed:17154526, FT ECO:0000269|PubMed:18597481}. FT BINDING 93 93 Substrate. FT BINDING 107 107 ATP; auxiliary. FT {ECO:0000305|PubMed:17154526}. FT BINDING 189 189 Substrate; via carbonyl oxygen. FT BINDING 208 208 Substrate. FT BINDING 388 388 ATP; via carbonyl oxygen; auxiliary. FT {ECO:0000305|PubMed:17154526}. FT BINDING 429 429 ATP; auxiliary. FT {ECO:0000305|PubMed:17154526}. FT BINDING 442 442 ATP. {ECO:0000255|HAMAP-Rule:MF_00420, FT ECO:0000269|PubMed:17154526, FT ECO:0000269|PubMed:18597481}. FT BINDING 477 477 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP-Rule:MF_00420, FT ECO:0000269|PubMed:17154526, FT ECO:0000269|PubMed:18597481}. FT BINDING 480 480 Substrate. FT BINDING 549 549 ATP; auxiliary. FT {ECO:0000305|PubMed:17154526}. FT BINDING 556 556 ATP; auxiliary. FT {ECO:0000305|PubMed:17154526}. FT MUTAGEN 32 32 H->A: Loss of FGAM synthase activity. FT {ECO:0000269|PubMed:17154526}. FT MUTAGEN 32 32 H->Q: Loss of FGAM synthase activity. FT {ECO:0000269|PubMed:17154526}. FT MUTAGEN 72 72 H->A: Strong decrease of the binding FT affinity and 20-fold decrease of the FT catalytic efficiency for FGAR. It has no FT effect on the ATP binding site, however FT it affects binding of FGAR. FT {ECO:0000269|PubMed:17154526}. FT MUTAGEN 72 72 H->Q: 200-fold decrease of the catalytic FT efficiency for FGAR. It has no effect on FT the ATP binding site, however it affects FT binding of FGAR. FT {ECO:0000269|PubMed:17154526}. FT HELIX 3 13 {ECO:0000244|PDB:1VK3}. FT HELIX 19 28 {ECO:0000244|PDB:1VK3}. FT HELIX 31 34 {ECO:0000244|PDB:1VK3}. FT TURN 36 38 {ECO:0000244|PDB:1VK3}. FT HELIX 39 43 {ECO:0000244|PDB:1VK3}. FT STRAND 51 53 {ECO:0000244|PDB:1VK3}. FT STRAND 56 71 {ECO:0000244|PDB:1VK3}. FT HELIX 73 78 {ECO:0000244|PDB:1VK3}. FT HELIX 80 97 {ECO:0000244|PDB:1VK3}. FT STRAND 101 113 {ECO:0000244|PDB:1VK3}. FT HELIX 116 129 {ECO:0000244|PDB:1VK3}. FT STRAND 133 140 {ECO:0000244|PDB:1VK3}. FT HELIX 142 144 {ECO:0000244|PDB:1VK3}. FT STRAND 145 147 {ECO:0000244|PDB:2HS3}. FT STRAND 149 159 {ECO:0000244|PDB:1VK3}. FT HELIX 160 162 {ECO:0000244|PDB:3D54}. FT STRAND 165 167 {ECO:0000244|PDB:2HRY}. FT STRAND 170 172 {ECO:0000244|PDB:3D54}. FT STRAND 174 180 {ECO:0000244|PDB:1VK3}. FT TURN 185 188 {ECO:0000244|PDB:2HS3}. FT HELIX 189 192 {ECO:0000244|PDB:2HS3}. FT HELIX 204 206 {ECO:0000244|PDB:1VK3}. FT HELIX 212 228 {ECO:0000244|PDB:1VK3}. FT STRAND 232 236 {ECO:0000244|PDB:1VK3}. FT HELIX 241 252 {ECO:0000244|PDB:1VK3}. FT STRAND 256 260 {ECO:0000244|PDB:1VK3}. FT HELIX 261 263 {ECO:0000244|PDB:1VK3}. FT STRAND 266 268 {ECO:0000244|PDB:1VK3}. FT HELIX 273 278 {ECO:0000244|PDB:1VK3}. FT STRAND 282 289 {ECO:0000244|PDB:1VK3}. FT HELIX 291 293 {ECO:0000244|PDB:1VK3}. FT HELIX 294 303 {ECO:0000244|PDB:1VK3}. FT STRAND 307 317 {ECO:0000244|PDB:1VK3}. FT STRAND 319 324 {ECO:0000244|PDB:1VK3}. FT STRAND 327 333 {ECO:0000244|PDB:1VK3}. FT HELIX 334 338 {ECO:0000244|PDB:1VK3}. FT HELIX 366 371 {ECO:0000244|PDB:1VK3}. FT TURN 372 374 {ECO:0000244|PDB:1VK3}. FT STRAND 381 383 {ECO:0000244|PDB:1VK3}. FT HELIX 385 387 {ECO:0000244|PDB:1VK3}. FT STRAND 390 395 {ECO:0000244|PDB:1VK3}. FT STRAND 398 405 {ECO:0000244|PDB:1VK3}. FT HELIX 408 411 {ECO:0000244|PDB:1VK3}. FT HELIX 415 432 {ECO:0000244|PDB:1VK3}. FT STRAND 436 445 {ECO:0000244|PDB:1VK3}. FT TURN 449 451 {ECO:0000244|PDB:1VK3}. FT HELIX 453 470 {ECO:0000244|PDB:1VK3}. FT STRAND 474 480 {ECO:0000244|PDB:1VK3}. FT STRAND 493 502 {ECO:0000244|PDB:1VK3}. FT HELIX 504 506 {ECO:0000244|PDB:1VK3}. FT STRAND 512 522 {ECO:0000244|PDB:1VK3}. FT HELIX 525 527 {ECO:0000244|PDB:1VK3}. FT HELIX 528 540 {ECO:0000244|PDB:1VK3}. FT STRAND 544 546 {ECO:0000244|PDB:1VK3}. FT STRAND 549 552 {ECO:0000244|PDB:2HS4}. FT HELIX 554 562 {ECO:0000244|PDB:1VK3}. FT STRAND 566 569 {ECO:0000244|PDB:1VK3}. FT STRAND 579 587 {ECO:0000244|PDB:1VK3}. FT STRAND 591 593 {ECO:0000244|PDB:2HS3}. FT STRAND 595 602 {ECO:0000244|PDB:1VK3}. SQ SEQUENCE 603 AA; 65969 MW; A9F85FE258EE4914 CRC64; MKLRYLNILK EKLGREPTFV ELQAFSVMWS EHCGYSHTKK YIRRLPKTGF EGNAGVVNLD DYYSVAFKIE SHNHPSAIEP YNGAATGVGG IIRDVLAMGA RPTAIFDSLH MSRIIDGIIE GIADYGNSIG VPTVGGELRI SSLYAHNPLV NVLAAGVVRN DMLVDSKASR PGQVIVIFGG ATGRDGIHGA SFASEDLTGD KATKLSIQVG DPFAEKMLIE AFLEMVEEGL VEGAQDLGAG GVLSATSELV AKGNLGAIVH LDRVPLREPD MEPWEILISE SQERMAVVTS PQKASRILEI ARKHLLFGDV VAEVIEEPVY RVMYRNDLVM EVPVQLLANA PEEDIVEYTP GKIPEFKRVE FEEVNAREVF EQYDHMVGTD TVVPPGFGAA VMRIKRDGGY SLVTHSRADL ALQDTYWGTL IAVLESVRKT LSVGAEPLAI TNCVNYGDPD VDPVGLSAMM TALKNACEFS GVPVASGNAS LYNTYQGKPI PPTLVVGMLG KVNPQKVAKP KPSKVFAVGW NDFELEREKE LWRAIRKLSE EGAFILSSSQ LLTRTHVETF REYGLKIEVK LPEVRPAHQM VLVFSERTPV VDVPVKEIGT LSR // ID PYRK_THEMA Reviewed; 217 AA. AC Q9WYG9; DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 80. DE RecName: Full=Putative dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit; DE AltName: Full=Dihydroorotate oxidase B, electron transfer subunit; GN Name=pyrK; OrderedLocusNames=TM_0334; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Responsible for channeling the electrons from the CC oxidation of dihydroorotate from the FMN redox center in the PyrD CC type B subunit to the ultimate electron acceptor NAD(+). CC {ECO:0000250}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000250}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC Note=Binds 1 FAD per subunit. {ECO:0000250}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1. CC -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35421.1; -; Genomic_DNA. DR PIR; H72390; H72390. DR RefSeq; NP_228145.1; NC_000853.1. DR RefSeq; WP_010865096.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYG9; -. DR STRING; 243274.TM0334; -. DR EnsemblBacteria; AAD35421; AAD35421; TM_0334. DR GeneID; 897289; -. DR KEGG; tma:TM0334; -. DR KEGG; tmi:THEMA_03050; -. DR KEGG; tmw:THMA_0342; -. DR PATRIC; 23935549; VBITheMar51294_0339. DR eggNOG; ENOG4105I47; Bacteria. DR eggNOG; COG0543; LUCA. DR KO; K02823; -. DR OMA; KGCAVET; -. DR OrthoDB; EOG69WFJ4; -. DR BioCyc; TMAR243274:GC6P-348-MONOMER; -. DR UniPathway; UPA00070; UER00945. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.10.240.10; -; 1. DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu. DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF10418; DHODB_Fe-S_bind; 1. DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1. DR SUPFAM; SSF63380; SSF63380; 1. PE 3: Inferred from homology; KW 2Fe-2S; Complete proteome; Electron transport; FAD; Flavoprotein; KW Iron; Iron-sulfur; Metal-binding; Pyrimidine biosynthesis; KW Reference proteome; Transport. FT CHAIN 1 217 Putative dihydroorotate dehydrogenase B FT (NAD(+)), electron transfer subunit. FT /FTId=PRO_0000409560. FT NP_BIND 66 67 FAD. {ECO:0000250}. FT METAL 183 183 Iron-sulfur (2Fe-2S). {ECO:0000250}. FT METAL 188 188 Iron-sulfur (2Fe-2S). {ECO:0000250}. FT METAL 191 191 Iron-sulfur (2Fe-2S). {ECO:0000250}. FT METAL 203 203 Iron-sulfur (2Fe-2S). {ECO:0000250}. SQ SEQUENCE 217 AA; 24474 MW; 27A0570EA5CF6540 CRC64; MERLLLTKKK TIRVNEDTWI VLFEERIDFS PGQFVMLETP KLVRKPFVLG YWEDHTAISV QVKGKGTKWI VEEAEKIKGH GPLGNGFEKP GKGLLIISPT CLTMAEAFRK KMNVDVLVGS RTPFQIPLDH ETAVGDEEFL SKLSSTGEYD WYLVSGSRGM EKVCWEHLKG KEVYFSLEEY MGCGIGACKS CAVFTKEGVK HVCTDGPIFR GDELCWS // ID PULA_THEMA Reviewed; 843 AA. AC O33840; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-MAY-2016, entry version 131. DE RecName: Full=Pullulanase; DE EC=3.2.1.41; DE AltName: Full=Alpha-dextrin endo-1,6-alpha-glucosidase; DE AltName: Full=Pullulan 6-glucanohydrolase; DE Flags: Precursor; GN Name=pulA; OrderedLocusNames=TM_1845; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9453151; DOI=10.1111/j.1574-6968.1998.tb12793.x; RA Bibel M., Brettl C., Gosslar U., Kriegshaeuser G., Liebl W.; RT "Isolation and analysis of genes for amylolytic enzymes of the RT hyperthermophilic bacterium Thermotoga maritima."; RL FEMS Microbiol. Lett. 158:9-15(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: Hydrolysis of (1->6)-alpha-D-glucosidic CC linkages in pullulan, amylopectin and glycogen, and in the alpha- CC and beta-limit dextrins of amylopectin and glycogen. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ001087; CAA04522.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36907.1; -; Genomic_DNA. DR PIR; H72204; H72204. DR RefSeq; NP_229641.1; NC_000853.1. DR RefSeq; WP_004082389.1; NZ_CP011107.1. DR PDB; 2J71; X-ray; 1.69 A; A=18-120. DR PDB; 2J72; X-ray; 1.49 A; A/B=18-120. DR PDB; 2J73; X-ray; 1.40 A; A/B=18-120. DR PDBsum; 2J71; -. DR PDBsum; 2J72; -. DR PDBsum; 2J73; -. DR ProteinModelPortal; O33840; -. DR SMR; O33840; 18-120. DR STRING; 243274.TM1845; -. DR CAZy; CBM41; Carbohydrate-Binding Module Family 41. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblBacteria; AAD36907; AAD36907; TM_1845. DR GeneID; 897812; -. DR KEGG; tma:TM1845; -. DR PATRIC; 23938679; VBITheMar51294_1866. DR eggNOG; ENOG4108IUM; Bacteria. DR eggNOG; COG1523; LUCA. DR InParanoid; O33840; -. DR KO; K01200; -. DR OMA; WHASNSI; -. DR OrthoDB; EOG66TG1T; -. DR EvolutionaryTrace; O33840; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR013784; Carb-bd-like_fold. DR InterPro; IPR015902; Glyco_hydro_13. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR004193; Glyco_hydro_13_N. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR005323; PUD. DR InterPro; IPR011840; PulA_typeI. DR PANTHER; PTHR10357; PTHR10357; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF02922; CBM_48; 1. DR Pfam; PF03714; PUD; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF49452; SSF49452; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR SUPFAM; SSF81296; SSF81296; 1. DR TIGRFAMs; TIGR02104; pulA_typeI; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Glycosidase; Hydrolase; KW Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 843 Pullulanase. FT /FTId=PRO_0000001428. FT ACT_SITE 535 535 Nucleophile. {ECO:0000250}. FT ACT_SITE 564 564 Proton donor. {ECO:0000250}. FT SITE 652 652 Transition state stabilizer. FT {ECO:0000250}. FT STRAND 21 28 {ECO:0000244|PDB:2J73}. FT STRAND 37 47 {ECO:0000244|PDB:2J73}. FT STRAND 52 54 {ECO:0000244|PDB:2J73}. FT STRAND 58 60 {ECO:0000244|PDB:2J73}. FT STRAND 63 72 {ECO:0000244|PDB:2J73}. FT STRAND 75 83 {ECO:0000244|PDB:2J73}. FT TURN 84 87 {ECO:0000244|PDB:2J73}. FT STRAND 88 98 {ECO:0000244|PDB:2J73}. FT STRAND 103 109 {ECO:0000244|PDB:2J73}. FT STRAND 116 118 {ECO:0000244|PDB:2J73}. SQ SEQUENCE 843 AA; 96262 MW; C42DDE233D54FE77 CRC64; MKTKLWLLLV LLLSALIFSE TTIVVHYHRY DGKYDGWNLW IWPVEPVSQE GKAYQFTGED DFGKVAVVKL PMDLTKVGII VRLNEWQAKD VAKDRFIEIK DGKAEVWILQ GVEEIFYEKP DTSPRIFFAQ ARSNKVIEAF LTNPVDTKKK ELFKVTVDGK EIPVSRVEKA DPTDIDVTNY VRIVLSESLK EEDLRKDVEL IIEGYKPARV IMMEILDDYY YDGELGAVYS PEKTIFRVWS PVSKWVKVLL FKNGEDTEPY QVVNMEYKGN GVWEAVVEGD LDGVFYLYQL ENYGKIRTTV DPYSKAVYAN SKKSAVVNLA RTNPEGWEND RGPKIEGYED AIIYEIHIAD ITGLENSGVK NKGLYLGLTE ENTKGPGGVT TGLSHLVELG VTHVHILPFF DFYTGDELDK DFEKYYNWGY DPYLFMVPEG RYSTDPKNPH TRIREVKEMV KALHKHGIGV IMDMVFPHTY GIGELSAFDQ TVPYYFYRID KTGAYLNESG CGNVIASERP MMRKFIVDTV TYWVKEYHID GFRFDQMGLI DKKTMLEVER ALHKIDPTII LYGEPWGGWG APIRFGKSDV AGTHVAAFND EFRDAIRGSV FNPSVKGFVM GGYGKETKIK RGVVGSINYD GKLIKSFALD PEETINYAAC HDNHTLWDKN YLAAKADKKK EWTEEELKNA QKLAGAILLT SQGVPFLHGG QDFCRTKNFN DNSYNAPISI NGFDYERKLQ FIDVFNYHKG LIKLRKEHPA FRLKNAEEIK KHLEFLPGGR RIVAFMLKDH AGGDPWKDIV VIYNGNLEKT TYKLPEGKWN VVVNSQKAGT EVIETVEGTI ELDPLSAYVL YRE // ID PYRG_THEMA Reviewed; 524 AA. AC Q9WZR0; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=CTP synthase {ECO:0000255|HAMAP-Rule:MF_01227}; DE EC=6.3.4.2 {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=CTP synthetase {ECO:0000255|HAMAP-Rule:MF_01227}; DE AltName: Full=UTP--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_01227}; GN Name=pyrG {ECO:0000255|HAMAP-Rule:MF_01227}; GN OrderedLocusNames=TM_0803; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with CC either L-glutamine or ammonia as the source of nitrogen. CC {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine CC is the substrate. Inhibited by CTP. {ECO:0000255|HAMAP- CC Rule:MF_01227}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_01227}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Belongs to the CTP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01227}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_01227}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35885.1; -; Genomic_DNA. DR PIR; D72330; D72330. DR RefSeq; NP_228612.1; NC_000853.1. DR RefSeq; WP_004080860.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZR0; -. DR STRING; 243274.TM0803; -. DR EnsemblBacteria; AAD35885; AAD35885; TM_0803. DR GeneID; 898471; -. DR KEGG; tma:TM0803; -. DR PATRIC; 23936526; VBITheMar51294_0815. DR eggNOG; ENOG4105C8D; Bacteria. DR eggNOG; COG0504; LUCA. DR InParanoid; Q9WZR0; -. DR KO; K01937; -. DR OMA; FDHNITT; -. DR OrthoDB; EOG6RC3NR; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_01227; PyrG; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR004468; CTP_synthase. DR InterPro; IPR017456; CTP_synthase_N. DR InterPro; IPR017926; GATASE. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11550; PTHR11550; 1. DR Pfam; PF06418; CTP_synth_N; 1. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00337; PyrG; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 524 CTP synthase. FT /FTId=PRO_0000138242. FT DOMAIN 282 524 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_01227}. FT REGION 1 250 Aminator domain. FT ACT_SITE 369 369 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01227}. FT ACT_SITE 499 499 {ECO:0000255|HAMAP-Rule:MF_01227}. FT ACT_SITE 501 501 {ECO:0000255|HAMAP-Rule:MF_01227}. SQ SEQUENCE 524 AA; 59492 MW; 14DF4DC735C74610 CRC64; MKKYVIVTGG VLSGIGKGIF SASLARLMKE HGVDVNVLKI DPYLNVDAGT MNPNQHGEVF VTEDGYEADL DLGHYERFLG RDMTRQNNMT AGQVYLRVIE KERQGKYLGN TVQIVPHLTE EIKDRIRALE AELLVVEIGG TVGDIEGEVF LEAVRELQME EGKENFLFAH VTYVPYLRTT NEFKTKPTQQ SVQLLRRIGI TPDMVIVRSE FPLDVPSMNK VALFSGVPRD FVINLPDTKN VYEVPEILRD MGLHEKIASK LNVELKKSTF NWSYPKAFKP YRIALVGKYL GTDDAYKSII ESVFLTGIEK PTVVDSQMLE DMNDEEVKKV LDEYDALIIP GGFGRRGVEG KIKAIKYARE NKKPILGICL GMQLMVIEFA RNVFGYKEAN STEFDPNTPY PVVDLMEEQK RILKLGGTMR LGAQKVKIFP KTKLYEVYGG VEEVYERHRH RYEANEEAFP ELFKKPGEEG YKLVVSAKSD FIEAVELEDH PFFVGVQFHP EYKSKVGAPH PIFVYLRKVL EGSQ // ID PYRKH_THEMA Reviewed; 282 AA. AC Q9X1X4; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 109. DE RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit homolog; DE AltName: Full=Dihydroorotate oxidase B, electron transfer subunit homolog; GN OrderedLocusNames=TM_1639; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000250}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC Note=Binds 1 FAD per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00716}. CC -!- CAUTION: Lacks the first cysteine that binds the 2Fe-2S complex. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36706.1; -; Genomic_DNA. DR PIR; G72230; G72230. DR RefSeq; NP_229439.1; NC_000853.1. DR RefSeq; WP_010865374.1; NC_000853.1. DR PDB; 4YLF; X-ray; 2.30 A; A/C=1-276. DR PDB; 4YRY; X-ray; 2.40 A; A/C=1-276. DR PDBsum; 4YLF; -. DR PDBsum; 4YRY; -. DR ProteinModelPortal; Q9X1X4; -. DR STRING; 243274.TM1639; -. DR EnsemblBacteria; AAD36706; AAD36706; TM_1639. DR GeneID; 896833; -. DR KEGG; tma:TM1639; -. DR PATRIC; 23938252; VBITheMar51294_1658. DR eggNOG; ENOG4105CDJ; Bacteria. DR eggNOG; COG0543; LUCA. DR InParanoid; Q9X1X4; -. DR KO; K00528; -. DR OMA; GPIPMMK; -. DR OrthoDB; EOG6XSZQF; -. DR BioCyc; TMAR243274:GC6P-1685-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro. DR Gene3D; 2.10.240.10; -; 1. DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu. DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR008333; OxRdtase_FAD-bd_dom. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF10418; DHODB_Fe-S_bind; 1. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; Complete proteome; Electron transport; FAD; KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; Reference proteome; KW Transport. FT CHAIN 1 282 Dihydroorotate dehydrogenase B (NAD(+)), FT electron transfer subunit homolog. FT /FTId=PRO_0000148372. FT DOMAIN 2 100 FAD-binding FR-type. FT {ECO:0000255|PROSITE-ProRule:PRU00716}. FT METAL 225 225 Iron-sulfur (2Fe-2S). {ECO:0000250}. FT METAL 228 228 Iron-sulfur (2Fe-2S). {ECO:0000250}. FT METAL 240 240 Iron-sulfur (2Fe-2S). {ECO:0000250}. FT STRAND 6 14 {ECO:0000244|PDB:4YLF}. FT STRAND 16 25 {ECO:0000244|PDB:4YLF}. FT HELIX 27 32 {ECO:0000244|PDB:4YLF}. FT STRAND 38 44 {ECO:0000244|PDB:4YLF}. FT STRAND 50 58 {ECO:0000244|PDB:4YLF}. FT TURN 59 62 {ECO:0000244|PDB:4YLF}. FT STRAND 63 69 {ECO:0000244|PDB:4YLF}. FT HELIX 73 80 {ECO:0000244|PDB:4YLF}. FT STRAND 88 95 {ECO:0000244|PDB:4YLF}. FT STRAND 104 111 {ECO:0000244|PDB:4YLF}. FT HELIX 112 115 {ECO:0000244|PDB:4YLF}. FT TURN 116 118 {ECO:0000244|PDB:4YLF}. FT HELIX 119 126 {ECO:0000244|PDB:4YLF}. FT TURN 127 129 {ECO:0000244|PDB:4YLF}. FT STRAND 131 137 {ECO:0000244|PDB:4YLF}. FT STRAND 139 144 {ECO:0000244|PDB:4YLF}. FT HELIX 149 154 {ECO:0000244|PDB:4YLF}. FT STRAND 155 169 {ECO:0000244|PDB:4YLF}. FT HELIX 171 174 {ECO:0000244|PDB:4YLF}. FT TURN 175 181 {ECO:0000244|PDB:4YLF}. FT STRAND 187 192 {ECO:0000244|PDB:4YLF}. FT HELIX 193 201 {ECO:0000244|PDB:4YLF}. FT TURN 202 205 {ECO:0000244|PDB:4YLF}. FT STRAND 210 213 {ECO:0000244|PDB:4YLF}. FT STRAND 219 225 {ECO:0000244|PDB:4YLF}. FT STRAND 229 232 {ECO:0000244|PDB:4YLF}. FT STRAND 235 238 {ECO:0000244|PDB:4YLF}. FT TURN 239 241 {ECO:0000244|PDB:4YLF}. FT STRAND 244 247 {ECO:0000244|PDB:4YLF}. FT TURN 248 250 {ECO:0000244|PDB:4YLF}. FT HELIX 253 260 {ECO:0000244|PDB:4YLF}. FT HELIX 267 273 {ECO:0000244|PDB:4YLF}. SQ SEQUENCE 282 AA; 31091 MW; BEA9816C469D2AF1 CRC64; MGGTALNEIV KKVKIAEDVF DFWIHSPSVS KEARPGQFVV IRLHEKGERI PLTVADTKPE EGLFRMVVKV VGKTTHELSL KKEGDTILDV VGPLGNPSEI ENYGNVLLVG GGVGIATLYP IAKALKEAGN NITTVLGART KDYLIMVDEF KEISDVLLVT DDGSAGMKGV VTDAMDKLFR ERKFDICWAV GPTIMMKFCT LKAREFGVPI WVSLNPIMVD GTGMCGACRV TVSGQIKFAC VDGPEFRGEE VDWDELLKRL AQYREQEKIS YERFLKTAGE SE // ID PURE_THEMA Reviewed; 171 AA. AC Q9WYS7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929}; DE Short=N5-CAIR mutase {ECO:0000255|HAMAP-Rule:MF_01929}; DE EC=5.4.99.18 {ECO:0000255|HAMAP-Rule:MF_01929}; DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929}; GN Name=purE {ECO:0000255|HAMAP-Rule:MF_01929}; GN OrderedLocusNames=TM_0446; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-171, AND SUBUNIT. RX PubMed=15048837; DOI=10.1002/prot.20023; RA Schwarzenbacher R., Jaroszewski L., von Delft F., Abdubek P., RA Ambing E., Biorac T., Brinen L.S., Canaves J.M., Cambell J., RA Chiu H.-J., Dai X., Deacon A.M., DiDonato M., Elsliger M.-A., RA Eshagi S., Floyd R., Godzik A., Grittini C., Grzechnik S.K., RA Hampton E., Karlak C., Klock H.E., Koesema E., Kovarik J.S., RA Kreusch A., Kuhn P., Lesley S.A., Levin I., McMullan D., RA McPhillips T.M., Miller M.D., Morse A., Moy K., Ouyang J., Page R., RA Quijano K., Robb A., Spraggon G., Stevens R.C., van den Bedem H., RA Velasquez J., Vincent J., Wang X., West B., Wolf G., Xu Q., RA Hodgson K.O., Wooley J., Wilson I.A.; RT "Crystal structure of a phosphoribosylaminoimidazole mutase PurE RT (TM0446) from Thermotoga maritima at 1.77-A resolution."; RL Proteins 55:474-478(2004). CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole CC ribonucleotide (CAIR). {ECO:0000255|HAMAP-Rule:MF_01929}. CC -!- CATALYTIC ACTIVITY: 5-carboxyamino-1-(5-phospho-D- CC ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxylate. {ECO:0000255|HAMAP-Rule:MF_01929}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01929}. CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01929}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35541.1; -; Genomic_DNA. DR PIR; G72374; G72374. DR RefSeq; NP_228256.1; NC_000853.1. DR RefSeq; WP_004081520.1; NZ_CP011107.1. DR PDB; 1O4V; X-ray; 1.77 A; A=2-171. DR PDBsum; 1O4V; -. DR ProteinModelPortal; Q9WYS7; -. DR SMR; Q9WYS7; 2-170. DR STRING; 243274.TM0446; -. DR EnsemblBacteria; AAD35541; AAD35541; TM_0446. DR GeneID; 897464; -. DR KEGG; tma:TM0446; -. DR PATRIC; 23935777; VBITheMar51294_0452. DR eggNOG; ENOG4108UM6; Bacteria. DR eggNOG; COG0041; LUCA. DR InParanoid; Q9WYS7; -. DR KO; K01588; -. DR OMA; SDWATMR; -. DR OrthoDB; EOG6Z0QH2; -. DR UniPathway; UPA00074; UER00943. DR EvolutionaryTrace; Q9WYS7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.7700; -; 1. DR HAMAP; MF_01929; PurE_classI; 1. DR InterPro; IPR024694; N5-CAIR_mutase_PurE. DR InterPro; IPR000031; PurE_dom. DR Pfam; PF00731; AIRC; 1. DR PIRSF; PIRSF001338; AIR_carboxylase; 1. DR SMART; SM01001; AIRC; 1. DR SUPFAM; SSF52255; SSF52255; 1. DR TIGRFAMs; TIGR01162; purE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isomerase; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 171 N5-carboxyaminoimidazole ribonucleotide FT mutase. FT /FTId=PRO_0000074980. FT BINDING 10 10 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01929}. FT BINDING 13 13 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01929}. FT BINDING 40 40 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01929}. FT STRAND 3 9 {ECO:0000244|PDB:1O4V}. FT HELIX 11 13 {ECO:0000244|PDB:1O4V}. FT HELIX 14 26 {ECO:0000244|PDB:1O4V}. FT STRAND 30 35 {ECO:0000244|PDB:1O4V}. FT TURN 38 40 {ECO:0000244|PDB:1O4V}. FT HELIX 42 51 {ECO:0000244|PDB:1O4V}. FT TURN 52 56 {ECO:0000244|PDB:1O4V}. FT STRAND 59 67 {ECO:0000244|PDB:1O4V}. FT HELIX 70 77 {ECO:0000244|PDB:1O4V}. FT STRAND 82 87 {ECO:0000244|PDB:1O4V}. FT TURN 90 94 {ECO:0000244|PDB:1O4V}. FT HELIX 95 102 {ECO:0000244|PDB:1O4V}. FT HELIX 118 130 {ECO:0000244|PDB:1O4V}. FT HELIX 134 169 {ECO:0000244|PDB:1O4V}. SQ SEQUENCE 171 AA; 18618 MW; 84A995A2E29B8E5F CRC64; MPRVGIIMGS DSDLPVMKQA AEILEEFGID YEITIVSAHR TPDRMFEYAK NAEERGIEVI IAGAGGAAHL PGMVASITHL PVIGVPVKTS TLNGLDSLFS IVQMPGGVPV ATVAINNAKN AGILAASILG IKYPEIARKV KEYKERMKRE VLEKAQRLEQ IGYKEYLNQK E // ID PYRB_THEMA Reviewed; 527 AA. AC P96111; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 130. DE RecName: Full=Protein PyrBI; DE Includes: DE RecName: Full=Aspartate carbamoyltransferase; DE EC=2.1.3.2; DE AltName: Full=Aspartate transcarbamylase; DE Short=ATCase; DE Includes: DE RecName: Full=Aspartate carbamoyltransferase regulatory region; GN Name=pyrBI; OrderedLocusNames=TM_1642; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RA van de Casteele M.F.J., Chen P., van Vliet F., Legrain C., Cunin R., RA Glansdorff N.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate CC + N-carbamoyl-L-aspartate. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 2/3. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC ATCase/OTCase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PyrI family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y10300; CAA71345.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36709.1; -; Genomic_DNA. DR PIR; B72231; B72231. DR RefSeq; NP_229442.1; NC_000853.1. DR RefSeq; WP_004082131.1; NZ_CP011107.1. DR ProteinModelPortal; P96111; -. DR STRING; 243274.TM1642; -. DR EnsemblBacteria; AAD36709; AAD36709; TM_1642. DR GeneID; 897920; -. DR KEGG; tma:TM1642; -. DR PATRIC; 23938258; VBITheMar51294_1661. DR eggNOG; ENOG4105CXT; Bacteria. DR eggNOG; COG0540; LUCA. DR eggNOG; COG1781; LUCA. DR InParanoid; P96111; -. DR KO; K00608; -. DR OMA; DTFNMLT; -. DR OrthoDB; EOG6D8B62; -. DR BioCyc; MetaCyc:MONOMER-503; -. DR UniPathway; UPA00070; UER00116. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR GO; GO:0009220; P:pyrimidine ribonucleotide biosynthetic process; IBA:GO_Central. DR Gene3D; 2.30.30.20; -; 1. DR Gene3D; 3.30.70.140; -; 1. DR Gene3D; 3.40.50.1370; -; 2. DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd. DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase. DR InterPro; IPR002082; Asp_carbamoyltransf. DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd. DR InterPro; IPR020545; Asp_carbamoyltransf_reg_N. DR InterPro; IPR020542; Asp_carbamoyltrfase_reg_C. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR Pfam; PF01948; PyrI; 1. DR Pfam; PF02748; PyrI_C; 1. DR PRINTS; PR00101; ATCASE. DR ProDom; PD006194; Asp_carbamoylTrfase_reg; 1. DR SUPFAM; SSF53671; SSF53671; 1. DR SUPFAM; SSF54893; SSF54893; 1. DR SUPFAM; SSF57825; SSF57825; 1. DR TIGRFAMs; TIGR00670; asp_carb_tr; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Multifunctional enzyme; KW Pyrimidine biosynthesis; Reference proteome; Transferase; Zinc. FT CHAIN 1 527 Protein PyrBI. FT /FTId=PRO_0000113240. FT REGION 1 342 Aspartate carbamoyltransferase. FT REGION 343 357 Linker. FT REGION 368 527 Aspartate carbamoyltransferase regulatory FT region. FT METAL 483 483 Zinc. {ECO:0000250}. FT METAL 488 488 Zinc. {ECO:0000250}. FT METAL 512 512 Zinc. {ECO:0000250}. FT METAL 515 515 Zinc. {ECO:0000250}. FT CONFLICT 525 527 WSI -> T (in Ref. 1; CAA71345). FT {ECO:0000305}. SQ SEQUENCE 527 AA; 60772 MW; 24BBF883B3BFC03D CRC64; MKRDFLGRTL AVIEDLSVEE QMFLYEKTRE LKQRWYSGED VSDFRIKKRN VGIYIVFVEP STRTKESFIN AAKFHSGPNV KVNVFDSEHS SFNKQESYTD TFSMLTGYSD YSIFVVRTRL EGVCRLLERR ISEFASRNGI EVPSFINAGD GKHEHPTQEL LDEYTFLEQN GFDNSFIHVA LVGDLLHGRT VHSKVNGLKI FKNVKVDLVA PEELMMPEHY VEKMKKNGFE VRIFSSIREY LDQKDVAKIW YFTRLQLERM GEDILEKVHV LREAVTFKKE YLDALPEGVK FYHPLPRHKV YPTIPNFLDT LPLNGWETQA RNGYWVRIVL LSMFGGALEA PFDTSKKEEK PEEDFIIPAP ITHGSKGVQK EGKRGIKPIE NGTVIDHIAK GKTPEEIYST ILKIRKILRL YDVDSADGIF RSSDGSFKGY ISLPDRYLSK KEIKKLSAIS PNTTVNIIKN STVVEKYRIK LPPTIYGFEE LRCKNENCIT NPAHGENASP SFVRNEKGQF ICEYCETPHS FEEIWSI // ID PYRF_THEMA Reviewed; 201 AA. AC Q9WYG7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 118. DE RecName: Full=Orotidine 5'-phosphate decarboxylase; DE EC=4.1.1.23; DE AltName: Full=OMP decarboxylase; DE Short=OMPDCase; DE Short=OMPdecase; GN Name=pyrF; OrderedLocusNames=TM_0332; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT. RG Joint center for structural genomics (JCSG); RT "Crystal Structure of orotidine 5'-phosphate decarboxylase (TM0332) RT from Thermotoga maritima at 2.00 A resolution."; RL Submitted (JAN-2005) to the PDB data bank. CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'- CC monophosphate (OMP) to uridine 5'-monophosphate (UMP). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2). CC {ECO:0000255|PROSITE-ProRule:PRU10110}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from orotate: step 2/2. CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}. CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35419.1; -; Genomic_DNA. DR PIR; F72390; F72390. DR RefSeq; NP_228143.1; NC_000853.1. DR RefSeq; WP_004083099.1; NZ_CP011107.1. DR PDB; 1VQT; X-ray; 2.00 A; A=1-201. DR PDBsum; 1VQT; -. DR ProteinModelPortal; Q9WYG7; -. DR SMR; Q9WYG7; 1-198. DR STRING; 243274.TM0332; -. DR EnsemblBacteria; AAD35419; AAD35419; TM_0332. DR GeneID; 897284; -. DR KEGG; tma:TM0332; -. DR PATRIC; 23935545; VBITheMar51294_0337. DR eggNOG; ENOG4107YPM; Bacteria. DR eggNOG; COG0284; LUCA. DR InParanoid; Q9WYG7; -. DR KO; K01591; -. DR OMA; DYVKVGH; -. DR OrthoDB; EOG6N6815; -. DR UniPathway; UPA00070; UER00120. DR EvolutionaryTrace; Q9WYG7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR014732; OMPdecase. DR InterPro; IPR018089; OMPdecase_AS. DR InterPro; IPR001754; OMPdeCOase_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00215; OMPdecase; 1. DR SMART; SM00934; OMPdecase; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR01740; pyrF; 1. DR PROSITE; PS00156; OMPDECASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Decarboxylase; Lyase; KW Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 201 Orotidine 5'-phosphate decarboxylase. FT /FTId=PRO_0000134595. FT REGION 52 61 Substrate binding. {ECO:0000250}. FT ACT_SITE 54 54 Proton donor. {ECO:0000255|PROSITE- FT ProRule:PRU10110}. FT BINDING 8 8 Substrate. {ECO:0000250}. FT BINDING 26 26 Substrate. {ECO:0000250}. FT BINDING 106 106 Substrate. {ECO:0000250}. FT BINDING 153 153 Substrate. {ECO:0000250}. FT BINDING 161 161 Substrate. {ECO:0000250}. FT BINDING 180 180 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 181 181 Substrate. {ECO:0000250}. FT STRAND 2 6 {ECO:0000244|PDB:1VQT}. FT STRAND 9 11 {ECO:0000244|PDB:1VQT}. FT HELIX 12 19 {ECO:0000244|PDB:1VQT}. FT STRAND 23 27 {ECO:0000244|PDB:1VQT}. FT HELIX 29 32 {ECO:0000244|PDB:1VQT}. FT HELIX 37 43 {ECO:0000244|PDB:1VQT}. FT TURN 44 46 {ECO:0000244|PDB:1VQT}. FT STRAND 48 55 {ECO:0000244|PDB:1VQT}. FT HELIX 59 69 {ECO:0000244|PDB:1VQT}. FT STRAND 74 80 {ECO:0000244|PDB:1VQT}. FT HELIX 81 83 {ECO:0000244|PDB:1VQT}. FT HELIX 85 94 {ECO:0000244|PDB:1VQT}. FT STRAND 96 102 {ECO:0000244|PDB:1VQT}. FT HELIX 112 124 {ECO:0000244|PDB:1VQT}. FT STRAND 128 130 {ECO:0000244|PDB:1VQT}. FT HELIX 133 139 {ECO:0000244|PDB:1VQT}. FT TURN 140 142 {ECO:0000244|PDB:1VQT}. FT STRAND 147 149 {ECO:0000244|PDB:1VQT}. FT HELIX 167 170 {ECO:0000244|PDB:1VQT}. FT TURN 171 173 {ECO:0000244|PDB:1VQT}. FT STRAND 175 180 {ECO:0000244|PDB:1VQT}. FT HELIX 181 184 {ECO:0000244|PDB:1VQT}. FT HELIX 189 196 {ECO:0000244|PDB:1VQT}. SQ SEQUENCE 201 AA; 22809 MW; 4C2FAD77302F206D CRC64; MTPVLSLDME DPIRFIDENG SFEVVKVGHN LAIHGKKIFD ELAKRNLKII LDLKFCDIPS TVERSIKSWD HPAIIGFTVH SCAGYESVER ALSATDKHVF VVVKLTSMEG SLEDYMDRIE KLNKLGCDFV LPGPWAKALR EKIKGKILVP GIRMEVKADD QKDVVTLEEM KGIANFAVLG REIYLSENPR EKIKRIKEMR L // ID PYRH_THEMA Reviewed; 231 AA. AC Q9X1U0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=Uridylate kinase {ECO:0000255|HAMAP-Rule:MF_01220}; DE Short=UK {ECO:0000255|HAMAP-Rule:MF_01220}; DE EC=2.7.4.22 {ECO:0000255|HAMAP-Rule:MF_01220}; DE AltName: Full=Uridine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_01220}; DE Short=UMP kinase {ECO:0000255|HAMAP-Rule:MF_01220}; DE Short=UMPK {ECO:0000255|HAMAP-Rule:MF_01220}; GN Name=pyrH {ECO:0000255|HAMAP-Rule:MF_01220}; GN OrderedLocusNames=TM_1604; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. CC {ECO:0000255|HAMAP-Rule:MF_01220}. CC -!- CATALYTIC ACTIVITY: ATP + UMP = ADP + UDP. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC -!- ENZYME REGULATION: Allosterically activated by GTP. Inhibited by CC UTP. {ECO:0000255|HAMAP-Rule:MF_01220}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; UDP from UMP (UMPK route): step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01220}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01220}. CC -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36671.1; -; Genomic_DNA. DR PIR; H72234; H72234. DR RefSeq; NP_229404.1; NC_000853.1. DR RefSeq; WP_004082051.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1U0; -. DR STRING; 243274.TM1604; -. DR EnsemblBacteria; AAD36671; AAD36671; TM_1604. DR GeneID; 897939; -. DR KEGG; tma:TM1604; -. DR PATRIC; 23938182; VBITheMar51294_1623. DR eggNOG; ENOG4105C41; Bacteria. DR eggNOG; COG0528; LUCA. DR InParanoid; Q9X1U0; -. DR KO; K09903; -. DR OMA; RSRADYM; -. DR OrthoDB; EOG6M0T8S; -. DR UniPathway; UPA00159; UER00275. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0033862; F:UMP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_01220_B; PyrH_B; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR011817; Uridylate_kinase. DR InterPro; IPR015963; Uridylate_kinase_bac. DR PANTHER; PTHR21499:SF23; PTHR21499:SF23; 1. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF005650; Uridylate_kin; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR02075; pyrH_bact; 1. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm; Kinase; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 231 Uridylate kinase. FT /FTId=PRO_0000143899. FT NP_BIND 6 9 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT NP_BIND 127 134 UMP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT REGION 14 19 Involved in allosteric activation by GTP. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 49 49 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 53 53 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 66 66 UMP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 154 154 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 160 160 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01220}. FT BINDING 163 163 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. SQ SEQUENCE 231 AA; 25235 MW; 4563E9E15FA0C5ED CRC64; MRVLVKLSGE ALSGEGGRGF DPERVNYIVN EIKSAIEEGF KIGIVVGAGN LFRGVELKNL TMTRADQIGL LGTVMNSVYL KDIFERSGLK ARIYSQIVNL PDVERVNYDS IESALRENSI LIFAGGTSNP FFTTDTAAVL RAQEMRAKLV VKATKVDGVY DKDPKKFPDA KKIPHLTFSE AMKMGLKVMD AEAFALCKKL GITVKVINFF EPGTLLKALK GEDVGSTVVP D // ID QUEA_THEMA Reviewed; 335 AA. AC Q9WZ44; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 110. DE RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase; DE EC=2.4.99.17; DE AltName: Full=Queuosine biosynthesis protein QueA; GN Name=queA; OrderedLocusNames=TM_0574; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT. RX PubMed=15822125; DOI=10.1002/prot.20419; RA Mathews I., Schwarzenbacher R., McMullan D., Abdubek P., Ambing E., RA Axelrod H., Biorac T., Canaves J.M., Chiu H.-J., Deacon A.M., RA DiDonato M., Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K., RA Hale J., Hampton E., Han G.W., Haugen J., Hornsby M., Jaroszewski L., RA Klock H.E., Koesema E., Kreusch A., Kuhn P., Lesley S.A., Levin I., RA Miller M.D., Moy K., Nigoghossian E., Ouyang J., Paulsen J., RA Quijano K., Reyes R., Spraggon G., Stevens R.C., van den Bedem H., RA Velasquez J., Vincent J., White A., Wolf G., Xu Q., Hodgson K.O., RA Wooley J., Wilson I.A.; RT "Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase- RT isomerase (QueA) from Thermotoga maritima at 2.0 A resolution reveals RT a new fold."; RL Proteins 59:869-874(2005). CC -!- FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet CC to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give CC epoxyqueuosine (oQ-tRNA). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 7-aminomethyl-7- CC carbaguanosine(34) in tRNA = L-methionine + adenine + CC epoxyqueuosine(34) in tRNA. CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15822125}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the QueA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35659.1; -; Genomic_DNA. DR PIR; A72360; A72360. DR RefSeq; NP_228384.1; NC_000853.1. DR RefSeq; WP_004081288.1; NZ_CP011107.1. DR PDB; 1VKY; X-ray; 2.00 A; A/B=1-335. DR PDBsum; 1VKY; -. DR ProteinModelPortal; Q9WZ44; -. DR SMR; Q9WZ44; 4-335. DR STRING; 243274.TM0574; -. DR EnsemblBacteria; AAD35659; AAD35659; TM_0574. DR GeneID; 897639; -. DR KEGG; tma:TM0574; -. DR PATRIC; 23936057; VBITheMar51294_0583. DR eggNOG; ENOG4105E2N; Bacteria. DR eggNOG; COG0809; LUCA. DR InParanoid; Q9WZ44; -. DR KO; K07568; -. DR OMA; PYIKRDY; -. DR OrthoDB; EOG6X6RBB; -. DR BRENDA; 2.4.99.17; 6331. DR UniPathway; UPA00392; -. DR EvolutionaryTrace; Q9WZ44; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051075; F:S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity; IBA:GO_Central. DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central. DR GO; GO:0002099; P:tRNA wobble guanine modification; IBA:GO_Central. DR HAMAP; MF_00113; QueA; 1. DR InterPro; IPR003699; QueA. DR Pfam; PF02547; Queuosine_synth; 1. DR SUPFAM; SSF111337; SSF111337; 1. DR TIGRFAMs; TIGR00113; queA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Queuosine biosynthesis; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 335 S-adenosylmethionine:tRNA FT ribosyltransferase-isomerase. FT /FTId=PRO_0000165458. FT HELIX 12 14 {ECO:0000244|PDB:1VKY}. FT HELIX 23 25 {ECO:0000244|PDB:1VKY}. FT STRAND 26 32 {ECO:0000244|PDB:1VKY}. FT TURN 33 36 {ECO:0000244|PDB:1VKY}. FT STRAND 37 42 {ECO:0000244|PDB:1VKY}. FT HELIX 43 49 {ECO:0000244|PDB:1VKY}. FT STRAND 55 63 {ECO:0000244|PDB:1VKY}. FT STRAND 67 71 {ECO:0000244|PDB:1VKY}. FT STRAND 78 87 {ECO:0000244|PDB:1VKY}. FT STRAND 90 97 {ECO:0000244|PDB:1VKY}. FT STRAND 106 110 {ECO:0000244|PDB:1VKY}. FT STRAND 113 120 {ECO:0000244|PDB:1VKY}. FT STRAND 126 132 {ECO:0000244|PDB:1VKY}. FT HELIX 135 141 {ECO:0000244|PDB:1VKY}. FT HELIX 175 178 {ECO:0000244|PDB:1VKY}. FT HELIX 181 190 {ECO:0000244|PDB:1VKY}. FT STRAND 193 201 {ECO:0000244|PDB:1VKY}. FT STRAND 223 226 {ECO:0000244|PDB:1VKY}. FT HELIX 228 240 {ECO:0000244|PDB:1VKY}. FT STRAND 244 248 {ECO:0000244|PDB:1VKY}. FT HELIX 249 258 {ECO:0000244|PDB:1VKY}. FT STRAND 265 269 {ECO:0000244|PDB:1VKY}. FT STRAND 285 290 {ECO:0000244|PDB:1VKY}. FT HELIX 297 306 {ECO:0000244|PDB:1VKY}. FT HELIX 308 320 {ECO:0000244|PDB:1VKY}. FT STRAND 331 335 {ECO:0000244|PDB:1VKY}. SQ SEQUENCE 335 AA; 38662 MW; 8D634537041B13E9 CRC64; MKVSEFDYEL PPELIAQEPV EPRDASRLMV LHRKTQRIEH RIFREIIEYL EPGDLLVLNV SKVIPARLYA RKKTGASIEI LLIERLEEGI WKCLVRPGQK VKKGTELVID EDLSAVCLGR GEDGTRILKF QPQDDRLIFE KGRTPLPPYI KNEVPLERYQ TVYAKEEGSV AAPTAGLHFT PELIEKLKKK GVQFAEVVLH VGIGTFRPVK VEEVEKHKMH EEFYQVPKET VRKLRETRER GNRIVAVGTT TVRTLETIAR LPEQEEYVGK TDLFIYPPFE FKLVDALVTN FHLPRSTLLM LVAAFAGKDF VMEAYREAVK RRYRFFSFGD AMLIL // ID RBSA1_THEMA Reviewed; 520 AA. AC Q9WXX0; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 20-JAN-2016, entry version 112. DE RecName: Full=Ribose import ATP-binding protein RbsA 1 {ECO:0000255|HAMAP-Rule:MF_01716}; DE EC=3.6.3.17 {ECO:0000255|HAMAP-Rule:MF_01716}; GN Name=rbsA1 {ECO:0000255|HAMAP-Rule:MF_01716}; GN OrderedLocusNames=TM_0115; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in CC ribose import. Responsible for energy coupling to the transport CC system. {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + monosaccharide(Out) = ADP + CC phosphate + monosaccharide(In). {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA), CC two transmembrane proteins (RbsC) and a solute-binding protein CC (RbsB). {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01716}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01716}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Ribose CC importer (TC 3.A.1.2.1) family. {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|HAMAP-Rule:MF_01716}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35209.1; -; Genomic_DNA. DR PIR; B72417; B72417. DR RefSeq; NP_227931.1; NC_000853.1. DR RefSeq; WP_004082693.1; NC_000853.1. DR ProteinModelPortal; Q9WXX0; -. DR STRING; 243274.TM0115; -. DR EnsemblBacteria; AAD35209; AAD35209; TM_0115. DR GeneID; 896942; -. DR KEGG; tma:TM0115; -. DR PATRIC; 23935070; VBITheMar51294_0113. DR eggNOG; ENOG4105C2J; Bacteria. DR eggNOG; COG1129; LUCA. DR InParanoid; Q9WXX0; -. DR KO; K10441; -. DR OMA; KTPNLYE; -. DR OrthoDB; EOG6QK4RR; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0015591; F:D-ribose transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015407; F:monosaccharide-transporting ATPase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015861; ABC_transpr_RbsA. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR PROSITE; PS51254; RBSA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; Repeat; KW Sugar transport; Transport. FT CHAIN 1 520 Ribose import ATP-binding protein RbsA 1. FT /FTId=PRO_0000261113. FT DOMAIN 15 256 ABC transporter 1. {ECO:0000255|HAMAP- FT Rule:MF_01716}. FT DOMAIN 266 511 ABC transporter 2. {ECO:0000255|HAMAP- FT Rule:MF_01716}. FT NP_BIND 47 54 ATP. {ECO:0000255|HAMAP-Rule:MF_01716}. SQ SEQUENCE 520 AA; 58633 MW; 3959BE91CA9DA2EB CRC64; MFPLLAFRGD RMEILKAKGI VKRFPGVVAV DNVDFEVYEN EIVSLIGENG AGKSTLIKIL TGVLKPDAGE ILVNGERVEF HSPVDAFKKG ISVIHQELNL CDNMTVAENI FLAYEAVRGQ KRTLSSRVDE NYMYTRSKEL LDLIGAKFSP DALVRNLTTA QRQMVEICKA LVKEPRIIFM DEPTSSLTVE ETERLFEIIE MLKSRGISVV FVSHRLDEVM RISDRIVVMR DGKRIGELKK GEFDVDTIIK MMVGREVEFF PHGIETRPGE IALEVRNLKW KDKVKNVSFE VRKGEVLGFA GLVGAGRTET MLLVFGVNQK ESGDIYVNGR KVEIKNPEDA IKMGIGLIPE DRKLQGLVLR MTVKDNIVLP SLKKISRWGL VLDERKEEEI SEDYVKRLSI KTPSIYQITE NLSGGNQQKV VLAKWLATNA DILIFDEPTR GIDVGAKAEI HRMIRELAAQ GKAVIMISSE LPEILNLSDR IVVMWEGEIT AVLDNREKRV TQEEIMYYAS GQKKQNGRVA // ID PYRE_THEMA Reviewed; 187 AA. AC Q9WYG6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01208}; DE Short=OPRT {ECO:0000255|HAMAP-Rule:MF_01208}; DE Short=OPRTase {ECO:0000255|HAMAP-Rule:MF_01208}; DE EC=2.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01208}; GN Name=pyrE {ECO:0000255|HAMAP-Rule:MF_01208}; GN OrderedLocusNames=TM_0331; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from CC 5-phosphoribose 1-diphosphate to orotate, leading to the formation CC of orotidine monophosphate (OMP). {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate CC + 5-phospho-alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01208}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from orotate: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01208}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. PyrE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35418.1; -; Genomic_DNA. DR PIR; E72390; E72390. DR RefSeq; NP_228142.1; NC_000853.1. DR RefSeq; WP_004083096.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYG6; -. DR STRING; 243274.TM0331; -. DR DNASU; 897282; -. DR EnsemblBacteria; AAD35418; AAD35418; TM_0331. DR GeneID; 897282; -. DR KEGG; tma:TM0331; -. DR PATRIC; 23935543; VBITheMar51294_0336. DR eggNOG; ENOG4107QV3; Bacteria. DR eggNOG; COG0461; LUCA. DR InParanoid; Q9WYG6; -. DR KO; K00762; -. DR OMA; GHFRLTS; -. DR OrthoDB; EOG618QX7; -. DR UniPathway; UPA00070; UER00119. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01208; PyrE; 1. DR InterPro; IPR023031; OPRT. DR InterPro; IPR006273; Orotate_PRibTrfase_bac. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01367; pyrE_Therm; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Magnesium; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 187 Orotate phosphoribosyltransferase. FT /FTId=PRO_0000110759. FT REGION 110 118 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01208}. FT BINDING 114 114 Orotate. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 142 142 Orotate. {ECO:0000255|HAMAP- FT Rule:MF_01208}. SQ SEQUENCE 187 AA; 20443 MW; 43FCBAE59F51A99A CRC64; MIKEILEKTG ALMEGHFILS SGKHSSRYVQ CARLFEFPEY GDVVGEELAK LLKKYDVETV VGPAMGGVIL SYVVARYLKA RSLFAERENG VMKLRRGFFV KPGEKVAVVE DVVTTGGSVK EVIELLKEYG ANVVCVGSII DRSGGKVDFG VPFESLLKLD LPVYDPEDCP LCKQGIPAEK PGSRGLK // ID RBSA2_THEMA Reviewed; 523 AA. AC Q9X051; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=Ribose import ATP-binding protein RbsA 2 {ECO:0000255|HAMAP-Rule:MF_01716}; DE EC=3.6.3.17 {ECO:0000255|HAMAP-Rule:MF_01716}; GN Name=rbsA2 {ECO:0000255|HAMAP-Rule:MF_01716}; GN OrderedLocusNames=TM_0956; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in CC ribose import. Responsible for energy coupling to the transport CC system. {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + monosaccharide(Out) = ADP + CC phosphate + monosaccharide(In). {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA), CC two transmembrane proteins (RbsC) and a solute-binding protein CC (RbsB). {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01716}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01716}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Ribose CC importer (TC 3.A.1.2.1) family. {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|HAMAP-Rule:MF_01716}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36035.1; -; Genomic_DNA. DR PIR; E72314; E72314. DR RefSeq; NP_228764.1; NC_000853.1. DR RefSeq; WP_004080606.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X051; -. DR STRING; 243274.TM0956; -. DR TCDB; 3.A.1.2.19; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36035; AAD36035; TM_0956. DR GeneID; 898691; -. DR KEGG; tma:TM0956; -. DR PATRIC; 23936843; VBITheMar51294_0970. DR eggNOG; ENOG4105C2J; Bacteria. DR eggNOG; COG1129; LUCA. DR InParanoid; Q9X051; -. DR KO; K10441; -. DR OMA; ELAQTIC; -. DR OrthoDB; EOG6QK4RR; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0015591; F:D-ribose transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015407; F:monosaccharide-transporting ATPase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015861; ABC_transpr_RbsA. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR PROSITE; PS51254; RBSA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; Repeat; KW Sugar transport; Transport. FT CHAIN 1 523 Ribose import ATP-binding protein RbsA 2. FT /FTId=PRO_0000261114. FT DOMAIN 13 249 ABC transporter 1. {ECO:0000255|HAMAP- FT Rule:MF_01716}. FT DOMAIN 266 513 ABC transporter 2. {ECO:0000255|HAMAP- FT Rule:MF_01716}. FT NP_BIND 45 52 ATP. {ECO:0000255|HAMAP-Rule:MF_01716}. SQ SEQUENCE 523 AA; 58545 MW; 0037F39AECBC647C CRC64; MMLNTEKERE VLLEARNITK TFPGVIAVNN VTLQIYKGEV CALVGENGAG KSTLMKILAG VYPDYEGQIF LEGKEVRFRN PREAQENGIA LIPQELDLVP NLSSAENIFL SREPVNEFGV IEYQKMFEQA SKLFSKLGVN IDPKTKVEDL STSQQQMVAI AKALSLDAKI IIMDEPTSAI GKRETEQLFN IIRSLKNEGK SVIYISHRLE EIFEIADRVV VMRDGRKVGE GPIEEFDHDK LVRLMVGRSI DQFFIKERAT ITDEIFRVEG IKLWSLDRKK LLVDDVSFYV RKGEVLGIYG LVGAGRTELL EAIFGAHPGR TEGKVFIGGK EIKIHSPRDA VKNGIGLVPE DRKTAGLILQ MSVLHNITLP SVVMKLIVRK FGLIDSQLEK EIVRSFIEKL NIKTPSPYQI VENLSGGNQQ KVVLAKWLAI KPKVLLLDEP TRGIDVNAKS EIYKLISEMA VSGMGVVMVS SELPEILAMS DRILVMSEGR KTAEFLREEV TEEDLLKAAI PRSVKVETTQ REE // ID QUEF_THEMA Reviewed; 137 AA. AC Q9WZP8; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818}; DE EC=1.7.1.13 {ECO:0000255|HAMAP-Rule:MF_00818}; DE AltName: Full=7-cyano-7-carbaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818}; DE AltName: Full=NADPH-dependent nitrile oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00818}; DE AltName: Full=PreQ(0) reductase {ECO:0000255|HAMAP-Rule:MF_00818}; GN Name=queF {ECO:0000255|HAMAP-Rule:MF_00818}; GN OrderedLocusNames=TM_0791; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7- CC deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). CC {ECO:0000255|HAMAP-Rule:MF_00818}. CC -!- CATALYTIC ACTIVITY: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7- CC cyano-7-carbaguanine + 2 NADPH. {ECO:0000255|HAMAP-Rule:MF_00818}. CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00818}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00818}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type CC 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00818}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35873.1; -; Genomic_DNA. DR PIR; H72333; H72333. DR RefSeq; NP_228600.1; NC_000853.1. DR RefSeq; WP_004080885.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZP8; -. DR STRING; 243274.TM0791; -. DR EnsemblBacteria; AAD35873; AAD35873; TM_0791. DR GeneID; 898459; -. DR KEGG; tma:TM0791; -. DR PATRIC; 23936502; VBITheMar51294_0803. DR eggNOG; ENOG410816Z; Bacteria. DR eggNOG; COG0780; LUCA. DR InParanoid; Q9WZP8; -. DR KO; K09457; -. DR OMA; TSVCPMT; -. DR OrthoDB; EOG6D5G0M; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046857; F:oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0033739; F:preQ1 synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00818; QueF_type1; 1. DR InterPro; IPR029500; QueF. DR InterPro; IPR016856; QueF_type1. DR Pfam; PF14489; QueF; 1. DR PIRSF; PIRSF027377; Nitrile_oxidored_QueF; 1. DR TIGRFAMs; TIGR03139; QueF-II; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Queuosine biosynthesis; Reference proteome. FT CHAIN 1 137 NADPH-dependent 7-cyano-7-deazaguanine FT reductase. FT /FTId=PRO_0000163015. FT REGION 68 70 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00818}. FT REGION 87 88 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00818}. FT ACT_SITE 45 45 Thioimide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00818}. FT ACT_SITE 52 52 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00818}. SQ SEQUENCE 137 AA; 15675 MW; 597073A219ECF27C CRC64; MPKAEGRIFD FKGHDAIRTD FLEAIDFDGK DEYIKIETDE FSAVCPFSGL PDIGRVIIEY YPDGGKIVEL KSLKYYFVSF RNVGIYQEEA TKRIYEDLKN LLKTDRIRVT VIYNIRGGIK TTTQMGSLEG KKSGEVE // ID RAD50_THEMA Reviewed; 852 AA. AC Q9X1X1; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Probable DNA double-strand break repair Rad50 ATPase; GN Name=rad50; OrderedLocusNames=TM_1636; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in DNA double-strand break repair (DSBR). The CC Rad50/Mre11 complex possesses single-strand endonuclease activity CC and ATP-dependent double-strand-specific 3'-5' exonuclease CC activity. Rad50 provides an ATP-dependent control of Mre11 by CC unwinding and/or repositioning DNA ends into the Mre11 active site CC (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per homodimer. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. Forms a complex with Mre11 (By similarity). CC {ECO:0000250}. CC -!- INTERACTION: CC Q9X1X0:TM_1635; NbExp=3; IntAct=EBI-3954207, EBI-3954204; CC -!- DOMAIN: The two conserved Cys that bind zinc constitute the zinc- CC hook, which separates the large intramolecular coiled coil CC regions. The 2 Cys residues coordinate one molecule of zinc with CC the help of the 2 Cys residues of the zinc-hook of another Rad50 CC molecule, thereby forming a V-shaped homodimer (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 zinc-hook domain. {ECO:0000255|PROSITE- CC ProRule:PRU00471}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36703.1; -; Genomic_DNA. DR PIR; D72230; D72230. DR RefSeq; NP_229436.1; NC_000853.1. DR RefSeq; WP_004082116.1; NZ_CP011107.1. DR PDB; 3QF7; X-ray; 1.90 A; A/B=1-190, A/B=686-852. DR PDB; 3QG5; X-ray; 3.40 A; A/B=1-190, A/B=686-852. DR PDB; 3THO; X-ray; 2.61 A; A=1-190, A=686-852. DR PDB; 4W9M; X-ray; 2.70 A; C/E/I/K=1-188, C/E/I/K=687-852. DR PDBsum; 3QF7; -. DR PDBsum; 3QG5; -. DR PDBsum; 3THO; -. DR PDBsum; 4W9M; -. DR ProteinModelPortal; Q9X1X1; -. DR IntAct; Q9X1X1; 1. DR STRING; 243274.TM1636; -. DR EnsemblBacteria; AAD36703; AAD36703; TM_1636. DR GeneID; 897923; -. DR KEGG; tma:TM1636; -. DR PATRIC; 23938246; VBITheMar51294_1655. DR eggNOG; ENOG4107WZZ; Bacteria. DR eggNOG; COG0419; LUCA. DR InParanoid; Q9X1X1; -. DR KO; K03546; -. DR OMA; THIEDLM; -. DR OrthoDB; EOG6V7BNM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013134; Zn_hook_RAD50. DR SUPFAM; SSF52540; SSF52540; 5. DR PROSITE; PS51131; ZN_HOOK; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Coiled coil; Complete proteome; DNA damage; KW DNA repair; Hydrolase; Metal-binding; Nucleotide-binding; KW Reference proteome; Zinc. FT CHAIN 1 852 Probable DNA double-strand break repair FT Rad50 ATPase. FT /FTId=PRO_0000138670. FT DOMAIN 389 488 Zinc-hook. {ECO:0000255|PROSITE- FT ProRule:PRU00471}. FT NP_BIND 30 37 ATP. {ECO:0000250}. FT COILED 155 345 {ECO:0000255}. FT COILED 389 427 {ECO:0000255}. FT COILED 460 488 {ECO:0000255}. FT COILED 534 711 {ECO:0000255}. FT COMPBIAS 768 804 Ala/Asp-rich (DA-box). FT METAL 435 435 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00471}. FT METAL 438 438 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU00471}. FT STRAND 2 11 {ECO:0000244|PDB:3QF7}. FT STRAND 14 20 {ECO:0000244|PDB:3QF7}. FT STRAND 23 29 {ECO:0000244|PDB:3QF7}. FT HELIX 36 48 {ECO:0000244|PDB:3QF7}. FT HELIX 57 60 {ECO:0000244|PDB:3QF7}. FT STRAND 65 67 {ECO:0000244|PDB:3THO}. FT STRAND 69 78 {ECO:0000244|PDB:3QF7}. FT STRAND 81 90 {ECO:0000244|PDB:3QF7}. FT TURN 91 94 {ECO:0000244|PDB:3QF7}. FT STRAND 95 103 {ECO:0000244|PDB:3QF7}. FT STRAND 105 107 {ECO:0000244|PDB:3THO}. FT STRAND 109 115 {ECO:0000244|PDB:3QF7}. FT HELIX 116 127 {ECO:0000244|PDB:3QF7}. FT HELIX 131 137 {ECO:0000244|PDB:3QF7}. FT STRAND 138 141 {ECO:0000244|PDB:3QG5}. FT TURN 145 150 {ECO:0000244|PDB:3QF7}. FT HELIX 153 163 {ECO:0000244|PDB:3QF7}. FT HELIX 167 189 {ECO:0000244|PDB:3QF7}. FT HELIX 686 709 {ECO:0000244|PDB:3QF7}. FT TURN 711 713 {ECO:0000244|PDB:3QF7}. FT HELIX 714 738 {ECO:0000244|PDB:3QF7}. FT STRAND 742 747 {ECO:0000244|PDB:3QF7}. FT TURN 748 751 {ECO:0000244|PDB:3QF7}. FT STRAND 752 757 {ECO:0000244|PDB:3QF7}. FT STRAND 760 763 {ECO:0000244|PDB:3QF7}. FT HELIX 764 766 {ECO:0000244|PDB:3QF7}. FT HELIX 769 786 {ECO:0000244|PDB:3QF7}. FT TURN 787 790 {ECO:0000244|PDB:3QF7}. FT STRAND 793 798 {ECO:0000244|PDB:3QF7}. FT TURN 799 802 {ECO:0000244|PDB:3THO}. FT HELIX 805 816 {ECO:0000244|PDB:3QF7}. FT HELIX 817 820 {ECO:0000244|PDB:3QF7}. FT STRAND 821 830 {ECO:0000244|PDB:3QF7}. FT HELIX 832 835 {ECO:0000244|PDB:3QF7}. FT STRAND 841 845 {ECO:0000244|PDB:3QF7}. FT STRAND 848 850 {ECO:0000244|PDB:3QF7}. SQ SEQUENCE 852 AA; 100002 MW; 31BA9F72A4EC5CD2 CRC64; MRPERLTVRN FLGLKNVDIE FQSGITVVEG PNGAGKSSLF EAISFALFGN GIRYPNSYDY VNRNAVDGTA RLVFQFERGG KRYEIIREIN ALQRKHNAKL SEILENGKKA AIAAKPTSVK QEVEKILGIE HRTFIRTVFL PQGEIDKLLI SPPSEITEII SDVFQSKETL EKLEKLLKEK MKKLENEISS LQALYTAIWK YLEENDLEVL KSELKTVSEK KKELLKKREE LQKEEEQLKR LLEKYRELVK KKERLRVLSL RRNELQKEVI YEQKVKKAKE LEPLFREIYL RQREFERFSQ ELNSREKRYK ELESEKEAIS KEIPVHRERL SKLEEIGEKI KEELDLLEKV LKASRPLLEQ RIRLKENLTR LEEEFRRLVG EKEKREKELL SIEKTENETK NELEKLLDEL SILKKDHMKW LAYQIASSLN EGDTCPVCGG VFHGKVEAVE FNIDEFEKLD QKRSELENTL NVLKERKKSL SSLIEDLLMK IEEGKKNLKS IRNQIEKIEE ELHRLGYSED LEEKLDEKRK KLRKIEEERH SISQKITAAD VQISQIENQL KEIKGEIEAK RETLKEQREE MDQLKSDFFD RLRKIGIGFE EFRILVKEEV KDAEKELGVV ETEIRLLEES LKELESENVR DVSEDYEKVR NQLEALSQEI SDLERKEGRL NHLIEETLRR ERELKSLEKK LKEMSDEYNN LDLLRKYLFD KSNFSRYFTG RVLEAVLKRT KAYLDILTNG RFDIDFDDEK GGFIIKDWGI ERPARGLSGG ERALISISLA MSLAEVASGR LDAFFIDEGF SSLDTENKEK IASVLKELER LNKVIVFITH DREFSEAFDR KLRITGGVVV NE // ID RECA_THEMA Reviewed; 356 AA. AC P36203; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 13-APR-2016, entry version 123. DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268}; DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268}; GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268}; GN OrderedLocusNames=TM_1859; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7929298; RA Wetmur J.G., Wong D.M., Ortiz B., Tong J., Reichert F., Gelfand D.H.; RT "Cloning, sequencing, and expression of RecA proteins from three RT distantly related thermophilic eubacteria."; RL J. Biol. Chem. 269:25928-25935(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of CC single-stranded DNA, the ATP-dependent uptake of single-stranded CC DNA by duplex DNA, and the ATP-dependent hybridization of CC homologous single-stranded DNAs. It interacts with LexA causing CC its activation and leading to its autocatalytic cleavage. CC {ECO:0000255|HAMAP-Rule:MF_00268}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}. CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP- CC Rule:MF_00268}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L23425; AAA27417.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36921.1; -; Genomic_DNA. DR PIR; D55020; D55020. DR RefSeq; NP_229655.1; NC_000853.1. DR RefSeq; WP_004082410.1; NZ_CP011107.1. DR PDB; 3HR8; X-ray; 1.95 A; A=1-356. DR PDBsum; 3HR8; -. DR ProteinModelPortal; P36203; -. DR SMR; P36203; 7-336. DR STRING; 243274.TM1859; -. DR EnsemblBacteria; AAD36921; AAD36921; TM_1859. DR GeneID; 897122; -. DR KEGG; tma:TM1859; -. DR PATRIC; 23938707; VBITheMar51294_1880. DR eggNOG; ENOG4105C68; Bacteria. DR eggNOG; COG0468; LUCA. DR InParanoid; P36203; -. DR KO; K03553; -. DR OMA; TRKGAWY; -. DR OrthoDB; EOG6ZKXNZ; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central. DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central. DR GO; GO:0000150; F:recombinase activity; IBA:GO_Central. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central. DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central. DR GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR GO; GO:0042148; P:strand invasion; IBA:GO_Central. DR Gene3D; 3.30.250.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00268; RecA; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR013765; DNA_recomb/repair_RecA. DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020588; RecA_ATP-bd. DR InterPro; IPR023400; RecA_C. DR InterPro; IPR020587; RecA_monomer-monomer_interface. DR PANTHER; PTHR22942:SF1; PTHR22942:SF1; 1. DR Pfam; PF00154; RecA; 1. DR PRINTS; PR00142; RECA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54752; SSF54752; 1. DR TIGRFAMs; TIGR02012; tigrfam_recA; 1. DR PROSITE; PS00321; RECA_1; 1. DR PROSITE; PS50162; RECA_2; 1. DR PROSITE; PS50163; RECA_3; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; DNA damage; KW DNA recombination; DNA repair; DNA-binding; Nucleotide-binding; KW Reference proteome; SOS response. FT CHAIN 1 356 Protein RecA. FT /FTId=PRO_0000122878. FT NP_BIND 68 75 ATP. {ECO:0000255|HAMAP-Rule:MF_00268}. FT HELIX 5 22 {ECO:0000244|PDB:3HR8}. FT HELIX 47 52 {ECO:0000244|PDB:3HR8}. FT STRAND 54 59 {ECO:0000244|PDB:3HR8}. FT STRAND 62 69 {ECO:0000244|PDB:3HR8}. FT HELIX 74 87 {ECO:0000244|PDB:3HR8}. FT STRAND 92 98 {ECO:0000244|PDB:3HR8}. FT HELIX 103 109 {ECO:0000244|PDB:3HR8}. FT HELIX 113 115 {ECO:0000244|PDB:3HR8}. FT STRAND 117 119 {ECO:0000244|PDB:3HR8}. FT HELIX 124 136 {ECO:0000244|PDB:3HR8}. FT STRAND 141 146 {ECO:0000244|PDB:3HR8}. FT TURN 148 150 {ECO:0000244|PDB:3HR8}. FT HELIX 154 157 {ECO:0000244|PDB:3HR8}. FT HELIX 168 185 {ECO:0000244|PDB:3HR8}. FT STRAND 190 199 {ECO:0000244|PDB:3HR8}. FT STRAND 201 205 {ECO:0000244|PDB:3HR8}. FT HELIX 213 220 {ECO:0000244|PDB:3HR8}. FT STRAND 222 235 {ECO:0000244|PDB:3HR8}. FT STRAND 238 254 {ECO:0000244|PDB:3HR8}. FT STRAND 259 265 {ECO:0000244|PDB:3HR8}. FT TURN 266 268 {ECO:0000244|PDB:3HR8}. FT HELIX 272 282 {ECO:0000244|PDB:3HR8}. FT STRAND 285 289 {ECO:0000244|PDB:3HR8}. FT STRAND 292 296 {ECO:0000244|PDB:3HR8}. FT STRAND 302 307 {ECO:0000244|PDB:3HR8}. FT HELIX 308 318 {ECO:0000244|PDB:3HR8}. FT HELIX 320 333 {ECO:0000244|PDB:3HR8}. SQ SEQUENCE 356 AA; 38798 MW; A2B70853C26C95FD CRC64; MPEEKQKKSV LEKALKRIEE NFGKGSIMIL GDETQVQPVE VIPTGSLAID IATGVGGYPR GRIVEIFGQE SSGKTTLALH AIAEAQKMGG VAAFIDAEHA LDPVYAKNLG VDLKSLLISQ PDHGEQALEI VDELVRSGVV DLIVVDSVAA LVPRAEIEGA MGDMQVGLQA RLMSQALRKI AGSVNKSKAV VIFTNQIRMK IGVMFGSPET TTGGLALKFY ATMRMEVRRG EPIKEGKDVI GNVISVKIVK NKVAPPFKTA QTYIIYGKGI DREYELFNIA VNEGIVDRKG SWYYYTTLKG EEVSLGQGSS NAVQFLKDNP EIAGEIERRI REKYGLLSVE KEEQRKEKKS SGEEAS // ID RBFA_THEMA Reviewed; 131 AA. AC Q9WZV9; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003}; GN Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; GN OrderedLocusNames=TM_0855; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Associates with free 30S ribosomal subunits (but not CC with 30S subunits that are part of 70S ribosomes or polysomes). CC Essential for efficient processing of 16S rRNA. May interact with CC the 5'-terminal helix region of 16S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00003}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00003}. CC -!- SIMILARITY: Belongs to the RbfA family. {ECO:0000255|HAMAP- CC Rule:MF_00003}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35937.1; -; Genomic_DNA. DR PIR; H72324; H72324. DR RefSeq; NP_228664.1; NC_000853.1. DR RefSeq; WP_004080768.1; NZ_CP011107.1. DR PDB; 2KZF; NMR; -; A=1-105. DR PDBsum; 2KZF; -. DR ProteinModelPortal; Q9WZV9; -. DR STRING; 243274.TM0855; -. DR EnsemblBacteria; AAD35937; AAD35937; TM_0855. DR GeneID; 898527; -. DR KEGG; tma:TM0855; -. DR PATRIC; 23936638; VBITheMar51294_0868. DR eggNOG; ENOG41084NJ; Bacteria. DR eggNOG; COG0858; LUCA. DR InParanoid; Q9WZV9; -. DR KO; K02834; -. DR OMA; VDYSLHI; -. DR OrthoDB; EOG6XQ3TJ; -. DR EvolutionaryTrace; Q9WZV9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.300.20; -; 1. DR HAMAP; MF_00003; RbfA; 1. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR000238; Ribosome-bd_facA. DR InterPro; IPR023799; Ribosome-bd_facA_dom. DR InterPro; IPR020053; Ribosome-bd_factorA_CS. DR Pfam; PF02033; RBFA; 1. DR ProDom; PD007327; Rib_bd_factA; 1. DR SUPFAM; SSF89919; SSF89919; 1. DR TIGRFAMs; TIGR00082; rbfA; 1. DR PROSITE; PS01319; RBFA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Reference proteome; KW rRNA processing. FT CHAIN 1 131 Ribosome-binding factor A. FT /FTId=PRO_0000102758. FT TURN 5 7 {ECO:0000244|PDB:2KZF}. FT HELIX 8 23 {ECO:0000244|PDB:2KZF}. FT HELIX 32 34 {ECO:0000244|PDB:2KZF}. FT STRAND 37 42 {ECO:0000244|PDB:2KZF}. FT STRAND 48 53 {ECO:0000244|PDB:2KZF}. FT HELIX 59 83 {ECO:0000244|PDB:2KZF}. FT STRAND 86 88 {ECO:0000244|PDB:2KZF}. FT STRAND 91 97 {ECO:0000244|PDB:2KZF}. SQ SEQUENCE 131 AA; 15547 MW; C1C58F7E8C893763 CRC64; MNPAYRKAML ESEIQKLLME ALQQLRDPRL KKDFVTFSRV ELSKDKRYAD VYVSFLGTPE ERKETVEILN RAKGFFRTFI AKNLRLYVAP EIRFYEDKGI EASVKVHQLL VQLGYDPLKD KEKKEEDKEE E // ID RBGA_THEMA Reviewed; 262 AA. AC Q9WZM6; DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Ribosome biogenesis GTPase A {ECO:0000250|UniProtKB:O31743}; GN Name=rbgA {ECO:0000250|UniProtKB:O31743}; GN Synonyms=ylqF {ECO:0000303|PubMed:18536017}; GN OrderedLocusNames=TM_0768; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] {ECO:0000312|EMBL:AAD35850.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000305, ECO:0000312|PDB:3CNN} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH GTP; GDP AND RP GTP ANALOG. RX PubMed=18536017; DOI=10.1002/prot.22112; RA Kim D.J., Jang J.Y., Yoon H.J., Suh S.W.; RT "Crystal structure of YlqF, a circularly permuted GTPase: implications RT for its GTPase activation in 50 S ribosomal subunit assembly."; RL Proteins 72:1363-1370(2008). CC -!- FUNCTION: Required for a late step of 50S ribosomal subunit CC assembly. Has GTPase activity. Binds to the 23S rRNA (By CC similarity). {ECO:0000250|UniProtKB:O31743}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O31743, CC ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. CC MTG1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}. CC -!- SIMILARITY: Contains 1 CP-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01058}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35850.1; -; Genomic_DNA. DR PIR; F72336; F72336. DR RefSeq; NP_228577.1; NC_000853.1. DR RefSeq; WP_004080928.1; NZ_CP011107.1. DR PDB; 3CNL; X-ray; 2.00 A; A=1-262. DR PDB; 3CNN; X-ray; 2.30 A; A=1-262. DR PDB; 3CNO; X-ray; 2.30 A; A=1-262. DR PDBsum; 3CNL; -. DR PDBsum; 3CNN; -. DR PDBsum; 3CNO; -. DR ProteinModelPortal; Q9WZM6; -. DR STRING; 243274.TM0768; -. DR DNASU; 898436; -. DR EnsemblBacteria; AAD35850; AAD35850; TM_0768. DR GeneID; 898436; -. DR KEGG; tma:TM0768; -. DR PATRIC; 23936458; VBITheMar51294_0781. DR eggNOG; ENOG4105C9W; Bacteria. DR eggNOG; COG1161; LUCA. DR InParanoid; Q9WZM6; -. DR KO; K14540; -. DR OMA; ARCPISS; -. DR OrthoDB; EOG6G4VXH; -. DR EvolutionaryTrace; Q9WZM6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central. DR Gene3D; 1.10.1580.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR030378; G_CP_dom. DR InterPro; IPR023179; GTP-bd_ortho_bundle. DR InterPro; IPR019991; GTP-bd_ribosome_bgen. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016478; GTPase_MTG1. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006230; MG442; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03596; GTPase_YlqF; 1. DR PROSITE; PS51721; G_CP; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; GTP-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 262 Ribosome biogenesis GTPase A. FT /FTId=PRO_0000409886. FT DOMAIN 12 157 CP-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01058}. FT NP_BIND 54 57 GTP. {ECO:0000269|PubMed:18536017}. FT NP_BIND 109 114 GTP. {ECO:0000269|PubMed:18536017}. FT BINDING 153 153 GTP; via amide nitrogen. FT {ECO:0000269|PubMed:18536017}. FT HELIX 13 19 {ECO:0000244|PDB:3CNL}. FT STRAND 23 30 {ECO:0000244|PDB:3CNL}. FT TURN 34 37 {ECO:0000244|PDB:3CNL}. FT STRAND 47 54 {ECO:0000244|PDB:3CNL}. FT HELIX 56 58 {ECO:0000244|PDB:3CNL}. FT HELIX 61 73 {ECO:0000244|PDB:3CNL}. FT STRAND 78 80 {ECO:0000244|PDB:3CNL}. FT HELIX 87 94 {ECO:0000244|PDB:3CNL}. FT STRAND 101 107 {ECO:0000244|PDB:3CNL}. FT HELIX 112 120 {ECO:0000244|PDB:3CNL}. FT STRAND 139 141 {ECO:0000244|PDB:3CNL}. FT STRAND 147 151 {ECO:0000244|PDB:3CNL}. FT HELIX 162 170 {ECO:0000244|PDB:3CNL}. FT HELIX 176 178 {ECO:0000244|PDB:3CNL}. FT HELIX 182 196 {ECO:0000244|PDB:3CNL}. FT HELIX 202 212 {ECO:0000244|PDB:3CNL}. FT HELIX 218 220 {ECO:0000244|PDB:3CNL}. FT HELIX 224 236 {ECO:0000244|PDB:3CNL}. FT TURN 237 240 {ECO:0000244|PDB:3CNL}. SQ SEQUENCE 262 AA; 29593 MW; 9179E24C57C30CD4 CRC64; MSWYPGHIEK AKRQIKDLLR LVNTVVEVRD ARAPFATSAY GVDFSRKETI ILLNKVDIAD EKTTKKWVEF FKKQGKRVIT THKGEPRKVL LKKLSFDRLA RVLIVGVPNT GKSTIINKLK GKRASSVGAQ PGITKGIQWF SLENGVKILD TPGILYKNIF SEDLAAKLLL VGSLPVERIE DQRIFERAFE IFARSIGIES SFSEFFEDFA RKRGLLKKGG VPDIERALML FFTEVAQGKA GRVSFERPED ITPVQQEQTR GV // ID RF2_THEMA Reviewed; 369 AA. AC Q9X1R5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=Peptide chain release factor 2; DE Short=RF-2; GN Name=prfB; OrderedLocusNames=TM_1579; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Peptide chain release factor 2 directs the termination CC of translation in response to the peptide chain termination codons CC UGA and UAA. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- PTM: Methylated by PrmC. Methylation increases the termination CC efficiency of RF2 (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release CC factor family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36646.1; -; Genomic_DNA. DR PIR; D72238; D72238. DR RefSeq; NP_229379.1; NC_000853.1. DR RefSeq; WP_010865364.1; NC_000853.1. DR ProteinModelPortal; Q9X1R5; -. DR STRING; 243274.TM1579; -. DR EnsemblBacteria; AAD36646; AAD36646; TM_1579. DR GeneID; 897956; -. DR KEGG; tma:TM1579; -. DR PATRIC; 23938122; VBITheMar51294_1598. DR eggNOG; ENOG4105CG1; Bacteria. DR eggNOG; COG1186; LUCA. DR InParanoid; Q9X1R5; -. DR KO; K02836; -. DR OMA; YAYGFLK; -. DR OrthoDB; EOG6TN48J; -. DR BioCyc; TMAR243274:GC6P-1620-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR GO; GO:0016149; F:translation release factor activity, codon specific; IBA:GO_Central. DR Gene3D; 3.30.160.20; -; 1. DR HAMAP; MF_00094; Rel_fac_2; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR005139; PCRF. DR InterPro; IPR000352; Pep_chain_release_fac_I_II. DR InterPro; IPR020853; Peptide_chain_release_fac2_bac. DR InterPro; IPR004374; PrfB. DR PANTHER; PTHR11075:SF6; PTHR11075:SF6; 1. DR Pfam; PF03462; PCRF; 1. DR Pfam; PF00472; RF-1; 1. DR SMART; SM00937; PCRF; 1. DR TIGRFAMs; TIGR00020; prfB; 1. DR PROSITE; PS00745; RF_PROK_I; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methylation; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 369 Peptide chain release factor 2. FT /FTId=PRO_0000166854. FT MOD_RES 251 251 N5-methylglutamine. {ECO:0000250}. SQ SEQUENCE 369 AA; 42637 MW; BE41E95ED6A4FACB CRC64; MGMISFETKT KIEELEKKYK DVLSVVNEDE INKELEEVEK KLTDPSVWDD QKKAREYTQK LKRLKNISED LKRVRSLFED LEVAIELSDE DQEMAQHVEE IVQELEGAVK KLELEIILNG KYDPNNAYLS VHPGAGGTES QDWAQMLLRM YMRWAERKGF DVEIVEFQPG EEAGIKDATI LIKGEYAYGY LKHESGVHRL VRISPFDAAR RRHTSFASVN VIPEIDDDVD IEIRPEDLKI ETFRASGHGG QYVNKTESAV RITHLPTGIV VSCQNERSQH QNKQTALKIL KAKLYQLEME KKRREIQEIQ GELKDISWGN QIRSYIFHPY TMVKDHRTGV ETANVDAVMD GDIDMFIEAE LVYFARRSS // ID REX2_THEMA Reviewed; 204 AA. AC Q9X1E1; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Redox-sensing transcriptional repressor Rex 2; GN Name=rex2; OrderedLocusNames=TM_1427; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Modulates transcription in response to changes in CC cellular NADH/NAD(+) redox state. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the transcriptional regulatory Rex family. CC {ECO:0000305}. CC -!- CAUTION: This protein lacks the conserved Gly residues in CC positions 90 and 93 that are potentially involved in NAD(H) CC binding. They are replaced by an Asn and an Ala, respectively. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36497.1; -; Genomic_DNA. DR PIR; H72256; H72256. DR RefSeq; NP_229227.1; NC_000853.1. DR RefSeq; WP_004081679.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1E1; -. DR STRING; 243274.TM1427; -. DR EnsemblBacteria; AAD36497; AAD36497; TM_1427. DR GeneID; 898048; -. DR KEGG; tma:TM1427; -. DR PATRIC; 23937802; VBITheMar51294_1439. DR eggNOG; ENOG4105FF6; Bacteria. DR eggNOG; COG2344; LUCA. DR InParanoid; Q9X1E1; -. DR KO; K01926; -. DR OMA; GKPKVGY; -. DR OrthoDB; EOG6C01BK; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050662; F:coenzyme binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro. DR GO; GO:0051775; P:response to redox state; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01131; Rex; 1. DR InterPro; IPR003781; CoA-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR009718; Rex_DNA-bd_C_dom. DR InterPro; IPR022876; Tscrpt_rep_Rex. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02629; CoA_binding; 1. DR Pfam; PF06971; Put_DNA-bind_N; 1. DR SMART; SM00881; CoA_binding; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1 204 Redox-sensing transcriptional repressor FT Rex 2. FT /FTId=PRO_0000097927. FT DNA_BIND 17 53 H-T-H motif. {ECO:0000255}. SQ SEQUENCE 204 AA; 23187 MW; E5F3F86F97FD2D9C CRC64; MAEMIHLPRS TFERLKMYRK VLEATKKPYI SSDEIARFLE INPDLVRKDF SYLNCQGKPR VGYDVEELRK ELDDLFGVNN TTNMIIVGAN DLARALLSLD FSKAGVKVVA VFDTERENVG KFIGEFAVRE LDVLERVIRR FDAEIAALCV SKDRAQATAE FLIEKGIKAV WNFTGVHLDL PEGVIVVEED LTQSLLTIKH LLKK // ID RBSD_THEMA Reviewed; 135 AA. AC Q9X054; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=D-ribose pyranase {ECO:0000255|HAMAP-Rule:MF_01661}; DE EC=5.4.99.62 {ECO:0000255|HAMAP-Rule:MF_01661}; GN Name=rbsD {ECO:0000255|HAMAP-Rule:MF_01661}; GN OrderedLocusNames=TM_0959; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the interconversion of beta-pyran and beta- CC furan forms of D-ribose. {ECO:0000255|HAMAP-Rule:MF_01661}. CC -!- CATALYTIC ACTIVITY: Beta-D-ribopyranose = beta-D-ribofuranose. CC {ECO:0000255|HAMAP-Rule:MF_01661}. CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose CC 5-phosphate from beta-D-ribopyranose: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_01661}. CC -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_01661}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01661}. CC -!- SIMILARITY: Belongs to the RbsD / FucU family. RbsD subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01661}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36038.1; -; Genomic_DNA. DR PIR; D72311; D72311. DR RefSeq; NP_228767.1; NC_000853.1. DR RefSeq; WP_004080603.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X054; -. DR STRING; 243274.TM0959; -. DR EnsemblBacteria; AAD36038; AAD36038; TM_0959. DR GeneID; 898696; -. DR KEGG; tma:TM0959; -. DR PATRIC; 23936849; VBITheMar51294_0973. DR eggNOG; ENOG4105MRB; Bacteria. DR eggNOG; COG1869; LUCA. DR InParanoid; Q9X054; -. DR KO; K06726; -. DR OMA; IIRTGEC; -. DR OrthoDB; EOG68SW4G; -. DR UniPathway; UPA00916; UER00888. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016872; F:intramolecular lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0048029; F:monosaccharide binding; IEA:InterPro. DR GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1650.10; -; 1. DR HAMAP; MF_01661; D_rib_pyranase; 1. DR InterPro; IPR023064; D-ribose_pyranase. DR InterPro; IPR023750; RbsD-like. DR InterPro; IPR007721; RbsD_FucU. DR Pfam; PF05025; RbsD_FucU; 1. DR SUPFAM; SSF102546; SSF102546; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase; KW Reference proteome. FT CHAIN 1 135 D-ribose pyranase. FT /FTId=PRO_0000346291. FT REGION 124 126 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01661}. FT ACT_SITE 20 20 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01661}. FT BINDING 28 28 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01661}. FT BINDING 102 102 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01661}. SQ SEQUENCE 135 AA; 14974 MW; 5D2359CED5BAAC8C CRC64; MKKVGILNSE ISKIVADMGH MDTLAVVDLG FPIPQGVKKV DLVVDRGKPG LMEVIEILLR ELKVERIILA KEMDEKSIQT KQELLKLIEK MNGPVEVVTV PHKEFKEMSK NVKGIIRTGA DIPYSNVILV GGVIF // ID RIBBA_THEMA Reviewed; 388 AA. AC Q9X2E6; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 120. DE RecName: Full=Riboflavin biosynthesis protein RibBA {ECO:0000255|HAMAP-Rule:MF_01283}; DE Includes: DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01283}; DE Short=DHBP synthase {ECO:0000255|HAMAP-Rule:MF_01283}; DE EC=4.1.99.12 {ECO:0000255|HAMAP-Rule:MF_01283}; DE Includes: DE RecName: Full=GTP cyclohydrolase-2 {ECO:0000255|HAMAP-Rule:MF_01283}; DE EC=3.5.4.25 {ECO:0000255|HAMAP-Rule:MF_01283}; DE AltName: Full=GTP cyclohydrolase II {ECO:0000255|HAMAP-Rule:MF_01283}; GN Name=ribBA {ECO:0000255|HAMAP-Rule:MF_01283}; GN OrderedLocusNames=TM_1826; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to CC formate and 3,4-dihydroxy-2-butanone 4-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01283}. CC -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6- CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and CC pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_01283}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4- CC dihydroxybutan-2-one 4-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01283}. CC -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6- CC hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01283}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01283}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01283}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000255|HAMAP-Rule:MF_01283}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01283}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01283}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2- CC hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_01283}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 1/4. {ECO:0000255|HAMAP- CC Rule:MF_01283}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP CC synthase family. {ECO:0000255|HAMAP-Rule:MF_01283}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP CC cyclohydrolase II family. {ECO:0000255|HAMAP-Rule:MF_01283}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36889.1; -; Genomic_DNA. DR PIR; E72207; E72207. DR RefSeq; NP_229623.1; NC_000853.1. DR RefSeq; WP_004082372.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2E6; -. DR SMR; Q9X2E6; 192-354. DR STRING; 243274.TM1826; -. DR EnsemblBacteria; AAD36889; AAD36889; TM_1826. DR GeneID; 897563; -. DR KEGG; tma:TM1826; -. DR PATRIC; 23938639; VBITheMar51294_1846. DR eggNOG; ENOG4105C66; Bacteria. DR eggNOG; COG0108; LUCA. DR eggNOG; COG0807; LUCA. DR InParanoid; Q9X2E6; -. DR KO; K14652; -. DR OMA; SLPWDPM; -. DR OrthoDB; EOG679TK8; -. DR UniPathway; UPA00275; UER00399. DR UniPathway; UPA00275; UER00400. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.870.10; -; 1. DR HAMAP; MF_00179; RibA; 1. DR HAMAP; MF_01283; RibBA; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR000422; DHBP_synthase_RibB. DR InterPro; IPR032677; GTP_cyclohydro_II. DR InterPro; IPR000926; RibA. DR InterPro; IPR016299; Riboflavin_synth_RibBA. DR Pfam; PF00926; DHBP_synthase; 1. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR SUPFAM; SSF142695; SSF142695; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00505; ribA; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Hydrolase; Lyase; Magnesium; KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Reference proteome; Riboflavin biosynthesis; Zinc. FT CHAIN 1 388 Riboflavin biosynthesis protein RibBA. FT /FTId=PRO_0000151744. FT NP_BIND 235 239 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT NP_BIND 277 279 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT REGION 1 186 DHBP synthase. FT REGION 21 22 D-ribulose 5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT REGION 125 129 D-ribulose 5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT REGION 187 388 GTP cyclohydrolase II. FT ACT_SITE 311 311 Proton acceptor; for GTP cyclohydrolase FT activity. {ECO:0000255|HAMAP- FT Rule:MF_01283}. FT ACT_SITE 313 313 Nucleophile; for GTP cyclohydrolase FT activity. {ECO:0000255|HAMAP- FT Rule:MF_01283}. FT METAL 22 22 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT METAL 22 22 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT METAL 128 128 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT METAL 240 240 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01283}. FT METAL 251 251 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01283}. FT METAL 253 253 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01283}. FT BINDING 26 26 D-ribulose 5-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT BINDING 149 149 D-ribulose 5-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT BINDING 256 256 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT BINDING 299 299 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT BINDING 334 334 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT BINDING 339 339 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT SITE 113 113 Essential for DHBP synthase activity. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT SITE 149 149 Essential for DHBP synthase activity. FT {ECO:0000255|HAMAP-Rule:MF_01283}. SQ SEQUENCE 388 AA; 43927 MW; 65514DDDC7EDD734 CRC64; MEELREAFEE GKPVILIDRN RENEADFVFP AQLITEDVVS FFVTYGKGLF CVTADEEDLL KRGFVKLSSN YGANYFVPVD WGTGTGISAL ERAETCRKLA EGRYFHEFRY PGHVTVIGGI GFQRRKGHTE ASLEISELAG FSRHAVIVEI LDEKGNSHNL DYVLKLSEKF SLPVLEMDDV WREFVKRKLL MKKKAEATLP TDFGVFKVVS FENHLDGKEH FAIVKEPLED PVAVRIHSEC VTGDVLSSLR CDCGSQLANF LRYMSAHGGI LIYLRQEGRG IGLSNKIAAY SLQDKGLDTV EANRVLGFSE DERDYAPAAQ ILKALGIERV LLFTNNQRKT VGLEKYGIEV VETKRLYGRV TPHNRFYLST KMKKLGHELE EIFREVNS // ID RIMM_THEMA Reviewed; 176 AA. AC Q9X1Q4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Ribosome maturation factor RimM {ECO:0000255|HAMAP-Rule:MF_00014}; GN Name=rimM {ECO:0000255|HAMAP-Rule:MF_00014}; GN OrderedLocusNames=TM_1568; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: An accessory protein needed during the final step in the CC assembly of 30S ribosomal subunit, possibly for assembly of the CC head region. Probably interacts with S19. Essential for efficient CC processing of 16S rRNA. May be needed both before and after RbfA CC during the maturation of 16S rRNA. It has affinity for free CC ribosomal 30S subunits but not for 70S ribosomes. CC {ECO:0000255|HAMAP-Rule:MF_00014}. CC -!- SUBUNIT: Binds ribosomal protein S19. {ECO:0000255|HAMAP- CC Rule:MF_00014}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00014}. CC -!- DOMAIN: The PRC barrel domain binds ribosomal protein S19. CC {ECO:0000255|HAMAP-Rule:MF_00014}. CC -!- SIMILARITY: Belongs to the RimM family. {ECO:0000255|HAMAP- CC Rule:MF_00014}. CC -!- SIMILARITY: Contains 1 PRC barrel domain. {ECO:0000255|HAMAP- CC Rule:MF_00014}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36635.1; -; Genomic_DNA. DR PIR; A72237; A72237. DR RefSeq; NP_229368.1; NC_000853.1. DR RefSeq; WP_004081983.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1Q4; -. DR STRING; 243274.TM1568; -. DR EnsemblBacteria; AAD36635; AAD36635; TM_1568. DR GeneID; 897428; -. DR KEGG; tma:TM1568; -. DR PATRIC; 23938098; VBITheMar51294_1586. DR eggNOG; ENOG410836E; Bacteria. DR eggNOG; COG0806; LUCA. DR InParanoid; Q9X1Q4; -. DR KO; K02860; -. DR OMA; KTDERDI; -. DR OrthoDB; EOG6SBT2K; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IEA:InterPro. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0006364; P:rRNA processing; IEA:InterPro. DR Gene3D; 2.40.30.60; -; 1. DR HAMAP; MF_00014; Ribosome_mat_RimM; 1. DR InterPro; IPR011961; 16S_RimM. DR InterPro; IPR027275; PRC-brl_dom. DR InterPro; IPR011033; PRC_barrel-like. DR InterPro; IPR002676; RimM. DR InterPro; IPR009000; Transl_B-barrel. DR Pfam; PF05239; PRC; 1. DR Pfam; PF01782; RimM; 1. DR SUPFAM; SSF50346; SSF50346; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR TIGRFAMs; TIGR02273; 16S_RimM; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome; KW Ribosome biogenesis. FT CHAIN 1 176 Ribosome maturation factor RimM. FT /FTId=PRO_0000163378. FT DOMAIN 104 176 PRC barrel. {ECO:0000255|HAMAP- FT Rule:MF_00014}. SQ SEQUENCE 176 AA; 20419 MW; C06BB85BBB0CBDD0 CRC64; MIRTIQDLLN ERVAIGKIVN THGLKGEVKF FPYTNSEEIV KNLSSVVLYN SEKKAFYNLT VESVRRMNKL FLIRFKSIDT IEAAERIKGC EVFIKYEELP KLSEDEYYFY EILDCDVFYE SGENVGKVVD IIETGSNDVL VVRKKKKETL IPMTKDCIVE IDKGAKKIIA KEMEWI // ID RECX_THEMA Reviewed; 161 AA. AC Q9X2H3; DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 75. DE RecName: Full=Regulatory protein RecX; GN Name=recX; OrderedLocusNames=TM_1858; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Modulates RecA activity. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RecX family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36920.1; -; Genomic_DNA. DR PIR; C72201; C72201. DR RefSeq; NP_229654.1; NC_000853.1. DR RefSeq; WP_010865419.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2H3; -. DR STRING; 243274.TM1858; -. DR EnsemblBacteria; AAD36920; AAD36920; TM_1858. DR GeneID; 897805; -. DR KEGG; tma:TM1858; -. DR PATRIC; 23938705; VBITheMar51294_1879. DR eggNOG; ENOG4108489; Bacteria. DR eggNOG; COG2137; LUCA. DR InParanoid; Q9X2H3; -. DR KO; K03565; -. DR OMA; MRFNVYI; -. DR OrthoDB; EOG6VQPZ1; -. DR BioCyc; TMAR243274:GC6P-1909-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006282; P:regulation of DNA repair; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_01114; RecX; 1. DR InterPro; IPR003783; Regulatory_RecX. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02631; RecX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 161 Regulatory protein RecX. FT /FTId=PRO_0000162486. SQ SEQUENCE 161 AA; 19483 MW; F3C779622BF357DF CRC64; MDYYQWRKKN RGKKRNLQAK KPLNYALRLL KYRVRFEDEL RERLKKQGFA DEEVESTITT LKKQGYLDDE KAAYLFALDE MRLKLFGPRV VKMKLKSLGV DEEIIERAIE KALEEIDFHE ELKRLKGRFK DRWELRDYLY RRGFDSSLIE EILNKIDGGE E // ID RF1_THEMA Reviewed; 342 AA. AC Q9X183; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 117. DE RecName: Full=Peptide chain release factor 1; DE Short=RF-1; GN Name=prfA; OrderedLocusNames=TM_1363; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Peptide chain release factor 1 directs the termination CC of translation in response to the peptide chain termination codons CC UAG and UAA. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- PTM: Methylated by PrmC. Methylation increases the termination CC efficiency of RF1 (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release CC factor family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36433.1; -; Genomic_DNA. DR PIR; D72263; D72263. DR RefSeq; NP_229164.1; NC_000853.1. DR RefSeq; WP_004081559.1; NZ_CP011107.1. DR PDB; 1RQ0; X-ray; 2.65 A; A/B/C=1-342. DR PDB; 2FVO; EM; 12.80 A; A=1-333. DR PDBsum; 1RQ0; -. DR PDBsum; 2FVO; -. DR ProteinModelPortal; Q9X183; -. DR SMR; Q9X183; 1-333. DR STRING; 243274.TM1363; -. DR EnsemblBacteria; AAD36433; AAD36433; TM_1363. DR GeneID; 898117; -. DR KEGG; tma:TM1363; -. DR PATRIC; 23937664; VBITheMar51294_1375. DR eggNOG; ENOG4105C8K; Bacteria. DR eggNOG; COG0216; LUCA. DR InParanoid; Q9X183; -. DR KO; K02835; -. DR OMA; ESQGRLH; -. DR OrthoDB; EOG6TN48J; -. DR EvolutionaryTrace; Q9X183; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR GO; GO:0016149; F:translation release factor activity, codon specific; IBA:GO_Central. DR Gene3D; 3.30.160.20; -; 1. DR HAMAP; MF_00093; Rel_fac_1; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR005139; PCRF. DR InterPro; IPR000352; Pep_chain_release_fac_I_II. DR InterPro; IPR004373; PrfA. DR Pfam; PF03462; PCRF; 1. DR Pfam; PF00472; RF-1; 1. DR SMART; SM00937; PCRF; 1. DR TIGRFAMs; TIGR00019; prfA; 1. DR PROSITE; PS00745; RF_PROK_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methylation; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 342 Peptide chain release factor 1. FT /FTId=PRO_0000177761. FT MOD_RES 211 211 N5-methylglutamine. {ECO:0000250}. FT TURN 2 6 {ECO:0000244|PDB:1RQ0}. FT HELIX 7 13 {ECO:0000244|PDB:1RQ0}. FT HELIX 19 49 {ECO:0000244|PDB:1RQ0}. FT TURN 50 57 {ECO:0000244|PDB:1RQ0}. FT HELIX 62 80 {ECO:0000244|PDB:1RQ0}. FT STRAND 86 94 {ECO:0000244|PDB:1RQ0}. FT HELIX 99 119 {ECO:0000244|PDB:1RQ0}. FT STRAND 122 130 {ECO:0000244|PDB:1RQ0}. FT STRAND 136 145 {ECO:0000244|PDB:1RQ0}. FT HELIX 148 152 {ECO:0000244|PDB:1RQ0}. FT HELIX 153 155 {ECO:0000244|PDB:1RQ0}. FT STRAND 157 163 {ECO:0000244|PDB:1RQ0}. FT STRAND 174 184 {ECO:0000244|PDB:1RQ0}. FT HELIX 188 190 {ECO:0000244|PDB:1RQ0}. FT HELIX 195 197 {ECO:0000244|PDB:1RQ0}. FT STRAND 198 203 {ECO:0000244|PDB:1RQ0}. FT STRAND 214 224 {ECO:0000244|PDB:1RQ0}. FT TURN 225 227 {ECO:0000244|PDB:1RQ0}. FT STRAND 230 237 {ECO:0000244|PDB:1RQ0}. FT HELIX 239 263 {ECO:0000244|PDB:1RQ0}. FT TURN 264 266 {ECO:0000244|PDB:1RQ0}. FT STRAND 282 287 {ECO:0000244|PDB:1RQ0}. FT TURN 288 291 {ECO:0000244|PDB:1RQ0}. FT STRAND 292 295 {ECO:0000244|PDB:1RQ0}. FT TURN 296 299 {ECO:0000244|PDB:1RQ0}. FT STRAND 300 303 {ECO:0000244|PDB:1RQ0}. FT HELIX 305 309 {ECO:0000244|PDB:1RQ0}. FT HELIX 314 325 {ECO:0000244|PDB:1RQ0}. FT TURN 326 328 {ECO:0000244|PDB:1RQ0}. FT HELIX 329 332 {ECO:0000244|PDB:1RQ0}. SQ SEQUENCE 342 AA; 39657 MW; BEA59866A68F12F3 CRC64; MKEKKKEIEK LLARPDLTPE QMKNYGMEYA KIEEIENITN RIKETQEFIE LLREEGENEL EIEKYEKELD QLYQELLFLL SPEASDKAIV EIRPGTGGEE AALFARDLFR MYTRYAERKG WNLEVAEIHE TDLGGIREVV FFVKGKNAYG ILKYESGVHR VQRVPVTESG GRIHTSTATV AVLPEIEEKD IEIRPEDLKI ETFRASGHGG QYVNKTESAV RITHLPTGIV VSCQNERSQY QNKQTALRIL RARLYQLQKE QKEREISQKR KSQIGTGERS EKIRTYNFPQ NRVTDHRINY TSYRLQEILD GDLDEIISKL IEHDIENNLE EVLGIGASVE EK // ID RGYR_THEMA Reviewed; 1104 AA. AC O51934; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 13-APR-2016, entry version 124. DE RecName: Full=Reverse gyrase {ECO:0000255|HAMAP-Rule:MF_01125}; DE Includes: DE RecName: Full=Helicase {ECO:0000255|HAMAP-Rule:MF_01125}; DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01125}; DE Includes: DE RecName: Full=Topoisomerase {ECO:0000255|HAMAP-Rule:MF_01125}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_01125}; GN Name=rgy {ECO:0000255|HAMAP-Rule:MF_01125}; Synonyms=topR; GN OrderedLocusNames=TM_0173; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9440516; RA Bouthier de la Tour C., Portemer C., Kaltoum H., Duguet M.; RT "Reverse gyrase from the hyperthermophilic bacterium Thermotoga RT maritima: properties and gene structure."; RL J. Bacteriol. 180:274-281(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Modifies the topological state of DNA by introducing CC positive supercoils in an ATP-dependent process. It cleaves CC transiently a single DNA strand and remains covalently bound to CC the 5' DNA end through a tyrosine residue. May be involved in CC rewinding the DNA strands in the regions of the chromosome that CC have opened up to allow transcription or replication. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01125}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_01125}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01125}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01125}; CC -!- SUBUNIT: Monomer. CC -!- DOMAIN: Both the DNA unwinding and positive supercoiling CC activities require the cooperation of both domains. The CC cooperative action between the helicase-like and the topoisomerase CC domains is specific. The helicase-like domain probably does not CC directly unwind DNA but acts more likely by driving ATP-dependent CC conformational changes within the whole enzyme, functioning more CC like a protein motor. The "latch" region of the N-terminal domain CC plays a regulatory role in the enzyme, repressing topoisomerase CC activity in the absence of ATP and therefore preventing the enzyme CC from acting as an ATP-independent relaxing enzyme; it also helps CC to coordinate nucleotide hydrolysis by the ATPase domain with the CC supercoiling activity of the topoisomerase domain. CC {ECO:0000255|HAMAP-Rule:MF_01125}. CC -!- MISCELLANEOUS: This enzyme is the only unique feature of CC hyperthermophilic bacteria/archaea discovered so far. It appears CC to be essential for adaptation to life at high temperatures. CC -!- SIMILARITY: In the N-terminal section; belongs to the DEAD box CC helicase family. DDVD subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01125}. CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic CC type I/III topoisomerase family. {ECO:0000255|HAMAP- CC Rule:MF_01125}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_01125}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_01125}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_01125}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF013268; AAC01563.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35266.1; -; Genomic_DNA. DR PIR; C72409; C72409. DR RefSeq; NP_227988.1; NC_000853.1. DR RefSeq; WP_004082808.1; NZ_CP011107.1. DR PDB; 3P4X; X-ray; 2.41 A; A/B=59-541. DR PDB; 3P4Y; X-ray; 3.20 A; A=59-541. DR PDB; 4DDT; X-ray; 3.20 A; A=1-1104. DR PDB; 4DDU; X-ray; 3.00 A; A=1-1104. DR PDB; 4DDV; X-ray; 3.46 A; A/B=1-1104. DR PDB; 4DDW; X-ray; 3.90 A; A=1-1104. DR PDB; 4DDX; X-ray; 4.17 A; A/B=1-1104. DR PDBsum; 3P4X; -. DR PDBsum; 3P4Y; -. DR PDBsum; 4DDT; -. DR PDBsum; 4DDU; -. DR PDBsum; 4DDV; -. DR PDBsum; 4DDW; -. DR PDBsum; 4DDX; -. DR ProteinModelPortal; O51934; -. DR STRING; 243274.TM0173; -. DR EnsemblBacteria; AAD35266; AAD35266; TM_0173. DR GeneID; 897012; -. DR KEGG; tma:TM0173; -. DR PATRIC; 23935194; VBITheMar51294_0174. DR eggNOG; ENOG4106K5Q; Bacteria. DR eggNOG; COG1110; LUCA. DR InParanoid; O51934; -. DR KO; K03170; -. DR OMA; RIEMHEI; -. DR OrthoDB; EOG6S7XQ9; -. DR EvolutionaryTrace; O51934; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:InterPro. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.290.10; -; 1. DR Gene3D; 1.10.460.10; -; 2. DR Gene3D; 3.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 3. DR HAMAP; MF_01125; Reverse_gyrase; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005736; Reverse_gyrase. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. DR InterPro; IPR013826; Topo_IA_cen_sub3. DR InterPro; IPR023405; Topo_IA_core_domain. DR InterPro; IPR003602; Topo_IA_DNA-bd_dom. DR InterPro; IPR006171; Toprim_domain. DR PANTHER; PTHR11390; PTHR11390; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00382; AAA; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF56712; SSF56712; 1. DR TIGRFAMs; TIGR01054; rgy; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; DNA-binding; Helicase; KW Hydrolase; Isomerase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome; Repeat; Topoisomerase; Zinc; Zinc-finger. FT CHAIN 1 1104 Reverse gyrase. FT /FTId=PRO_0000158082. FT DOMAIN 87 242 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_01125}. FT DOMAIN 300 522 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_01125}. FT DOMAIN 542 699 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_01125}. FT ZN_FING 11 32 C4-type 1. {ECO:0000255|HAMAP- FT Rule:MF_01125}. FT NP_BIND 100 107 ATP. {ECO:0000255|HAMAP-Rule:MF_01125}. FT ZN_FING 621 638 C4-type 2. {ECO:0000255|HAMAP- FT Rule:MF_01125}. FT REGION 548 1104 Topoisomerase I. FT MOTIF 203 206 DEAD box. FT ACT_SITE 851 851 For DNA cleavage activity. FT {ECO:0000255|HAMAP-Rule:MF_01125}. FT METAL 548 548 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01125}. FT METAL 668 668 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01125}. FT METAL 668 668 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01125}. FT METAL 670 670 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01125}. FT BINDING 83 83 ATP. {ECO:0000255|HAMAP-Rule:MF_01125}. FT TURN 12 14 {ECO:0000244|PDB:4DDU}. FT HELIX 20 23 {ECO:0000244|PDB:4DDU}. FT TURN 24 26 {ECO:0000244|PDB:4DDU}. FT TURN 30 32 {ECO:0000244|PDB:4DDU}. FT HELIX 41 47 {ECO:0000244|PDB:4DDU}. FT HELIX 61 75 {ECO:0000244|PDB:3P4X}. FT HELIX 81 91 {ECO:0000244|PDB:3P4X}. FT STRAND 95 99 {ECO:0000244|PDB:3P4X}. FT HELIX 106 117 {ECO:0000244|PDB:3P4X}. FT TURN 118 121 {ECO:0000244|PDB:3P4X}. FT STRAND 124 130 {ECO:0000244|PDB:3P4X}. FT HELIX 131 144 {ECO:0000244|PDB:3P4X}. FT STRAND 151 153 {ECO:0000244|PDB:3P4X}. FT HELIX 160 172 {ECO:0000244|PDB:3P4X}. FT STRAND 176 181 {ECO:0000244|PDB:3P4X}. FT HELIX 182 187 {ECO:0000244|PDB:3P4X}. FT HELIX 189 192 {ECO:0000244|PDB:3P4X}. FT STRAND 198 203 {ECO:0000244|PDB:3P4X}. FT HELIX 205 208 {ECO:0000244|PDB:3P4X}. FT HELIX 212 221 {ECO:0000244|PDB:3P4X}. FT HELIX 226 237 {ECO:0000244|PDB:3P4X}. FT STRAND 252 259 {ECO:0000244|PDB:3P4X}. FT HELIX 265 273 {ECO:0000244|PDB:3P4X}. FT STRAND 274 276 {ECO:0000244|PDB:4DDT}. FT STRAND 288 295 {ECO:0000244|PDB:3P4X}. FT HELIX 298 308 {ECO:0000244|PDB:3P4X}. FT STRAND 310 318 {ECO:0000244|PDB:3P4X}. FT HELIX 319 331 {ECO:0000244|PDB:3P4X}. FT STRAND 336 341 {ECO:0000244|PDB:3P4X}. FT HELIX 343 352 {ECO:0000244|PDB:3P4X}. FT STRAND 356 362 {ECO:0000244|PDB:3P4X}. FT HELIX 367 370 {ECO:0000244|PDB:3P4X}. FT TURN 375 377 {ECO:0000244|PDB:3P4X}. FT STRAND 380 385 {ECO:0000244|PDB:3P4X}. FT STRAND 388 392 {ECO:0000244|PDB:4DDU}. FT STRAND 394 397 {ECO:0000244|PDB:4DDU}. FT HELIX 400 410 {ECO:0000244|PDB:4DDU}. FT HELIX 420 430 {ECO:0000244|PDB:4DDU}. FT HELIX 434 444 {ECO:0000244|PDB:4DDU}. FT STRAND 447 451 {ECO:0000244|PDB:4DDU}. FT TURN 452 455 {ECO:0000244|PDB:4DDU}. FT STRAND 456 460 {ECO:0000244|PDB:4DDU}. FT HELIX 462 470 {ECO:0000244|PDB:3P4X}. FT STRAND 475 478 {ECO:0000244|PDB:3P4Y}. FT STRAND 483 488 {ECO:0000244|PDB:3P4X}. FT HELIX 492 505 {ECO:0000244|PDB:3P4X}. FT STRAND 510 512 {ECO:0000244|PDB:3P4X}. FT HELIX 513 515 {ECO:0000244|PDB:3P4X}. FT HELIX 518 532 {ECO:0000244|PDB:3P4X}. FT STRAND 543 548 {ECO:0000244|PDB:4DDU}. FT HELIX 550 560 {ECO:0000244|PDB:4DDU}. FT STRAND 564 568 {ECO:0000244|PDB:4DDU}. FT STRAND 571 578 {ECO:0000244|PDB:4DDU}. FT STRAND 581 587 {ECO:0000244|PDB:4DDU}. FT STRAND 593 595 {ECO:0000244|PDB:4DDU}. FT STRAND 597 599 {ECO:0000244|PDB:4DDU}. FT STRAND 604 607 {ECO:0000244|PDB:4DDU}. FT STRAND 610 612 {ECO:0000244|PDB:4DDU}. FT STRAND 614 617 {ECO:0000244|PDB:4DDU}. FT STRAND 619 621 {ECO:0000244|PDB:4DDU}. FT TURN 622 624 {ECO:0000244|PDB:4DDU}. FT TURN 636 638 {ECO:0000244|PDB:4DDU}. FT STRAND 643 645 {ECO:0000244|PDB:4DDU}. FT HELIX 646 656 {ECO:0000244|PDB:4DDU}. FT TURN 657 659 {ECO:0000244|PDB:4DDU}. FT STRAND 661 665 {ECO:0000244|PDB:4DDU}. FT HELIX 671 684 {ECO:0000244|PDB:4DDU}. FT TURN 685 687 {ECO:0000244|PDB:4DDU}. FT STRAND 691 693 {ECO:0000244|PDB:4DDU}. FT STRAND 697 700 {ECO:0000244|PDB:4DDU}. FT HELIX 701 709 {ECO:0000244|PDB:4DDU}. FT HELIX 716 744 {ECO:0000244|PDB:4DDU}. FT HELIX 753 767 {ECO:0000244|PDB:4DDU}. FT TURN 768 771 {ECO:0000244|PDB:4DDU}. FT STRAND 776 781 {ECO:0000244|PDB:4DDU}. FT STRAND 786 791 {ECO:0000244|PDB:4DDU}. FT STRAND 797 810 {ECO:0000244|PDB:4DDU}. FT HELIX 818 828 {ECO:0000244|PDB:4DDU}. FT HELIX 833 845 {ECO:0000244|PDB:4DDU}. FT STRAND 848 850 {ECO:0000244|PDB:4DDU}. FT HELIX 861 874 {ECO:0000244|PDB:4DDU}. FT HELIX 877 879 {ECO:0000244|PDB:4DDU}. FT STRAND 896 899 {ECO:0000244|PDB:4DDU}. FT HELIX 902 911 {ECO:0000244|PDB:4DDU}. FT HELIX 919 936 {ECO:0000244|PDB:4DDU}. FT STRAND 940 953 {ECO:0000244|PDB:4DDU}. FT STRAND 955 966 {ECO:0000244|PDB:4DDU}. FT HELIX 969 971 {ECO:0000244|PDB:4DDU}. FT STRAND 983 994 {ECO:0000244|PDB:4DDU}. FT HELIX 1004 1014 {ECO:0000244|PDB:4DDU}. FT TURN 1019 1021 {ECO:0000244|PDB:4DDU}. FT HELIX 1022 1031 {ECO:0000244|PDB:4DDU}. FT STRAND 1034 1037 {ECO:0000244|PDB:4DDU}. FT STRAND 1043 1045 {ECO:0000244|PDB:4DDU}. FT HELIX 1047 1059 {ECO:0000244|PDB:4DDU}. FT HELIX 1061 1063 {ECO:0000244|PDB:4DDU}. FT HELIX 1066 1080 {ECO:0000244|PDB:4DDU}. FT HELIX 1086 1100 {ECO:0000244|PDB:4DDU}. SQ SEQUENCE 1104 AA; 128277 MW; C493932C2BFDAA12 CRC64; MAVNSKYHHS CINCGGLNTD ERNERGLPCE VCLPEDSPSD IYRALLERKT LKEYRFYHEF WNEYEDFRSF FKKKFGKDLT GYQRLWAKRI VQGKSFTMVA PTGVGKTTFG MMTALWLARK GKKSALVFPT VTLVKQTLER LQKLADEKVK IFGFYSSMKK EEKEKFEKSF EEDDYHILVF STQFVSKNRE KLSQKRFDFV FVDDVDAVLK ASRNIDTLLM MVGIPEEIIR KAFSTIKQGK IYERPKNLKP GILVVSSATA KPRGIRPLLF RDLLNFTVGR LVSVARNITH VRISSRSKEK LVELLEIFRD GILIFAQTEE EGKELYEYLK RFKFNVGETW SEFEKNFEDF KVGKINILIG VQAYYGKLTR GVDLPERIKY VIFWGTPSMR FSLELDKAPR FVLARVLKEM GLIKAQENPD VEELRKIAKE HLTQKEFVEK VKEMFRGVVV KDEDLELIIP DVYTYIQASG RSSRILNGVL VKGVSVIFEE DEEIFESLKT RLLLIAEEEI IEEAEANWKE LVHEVEESRR RSERELTDTS RSLLIIVESP TKAETLSRFL GRASSRKERN IIVHEAVTGE GVILFTATRG HVYDLVTKGG IHGVEEENGK FVPVYNSLKR CRDCGYQFTE DRDECPVCSS KNIDDKTETL RALREISLEA DEILVATDPD VEGEKISWDV TQYLLPSTRS LRRIEMHEIT RYGFKKARES VRFVDFNLVK AQIVRRVQDR WIGFELSGKL QKRFGRSNLS AGRVQSTVLG WIVEREEEYK KSEKDFTLLV LENGVNLEVE GKIADDVVTV VELQEAEEEK NPLPPYTTSS ALSEISQKLR LGVQEVMDIL QDLFEKGFIT YHRTDSTRIS LEGQNVARTY LRKIGKEDIF MGRSWSTEGA HEAIRPVKPI DARELEEMIE EGLIADLTKK HLRVYELIFN RFLASQSAAV KVKKQIVTVD VDGKRMGIEQ IVEILRDGWN LFVPLTVSPR FEHRTYKIKE KKFYKKHTVP LFTQASIVEE MKKRGIGRPS TYAKIVEVLF RRGYVYEDKY KRVRPTRFGV MVYSYLKERY EKYVTEETTR RLEEIMDKVE RGEEDYQATL RLLYEEIKSL MEEG // ID RHO_THEMA Reviewed; 427 AA. AC P38527; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 124. DE RecName: Full=Transcription termination factor Rho {ECO:0000255|HAMAP-Rule:MF_01884}; DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01884}; DE AltName: Full=ATP-dependent helicase Rho {ECO:0000255|HAMAP-Rule:MF_01884}; GN Name=rho {ECO:0000255|HAMAP-Rule:MF_01884}; OrderedLocusNames=TM_1470; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-427. RX PubMed=8051015; RA Opperman T., Richardson J.P.; RT "Phylogenetic analysis of sequences from diverse bacteria with RT homology to the Escherichia coli rho gene."; RL J. Bacteriol. 176:5033-5043(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), AND SUBUNIT. RX PubMed=20452362; DOI=10.1016/j.jmb.2010.05.004; RA Canals A., Uson I., Coll M.; RT "The structure of RNA-free Rho termination factor indicates a dynamic RT mechanism of transcript capture."; RL J. Mol. Biol. 400:16-23(2010). CC -!- FUNCTION: Facilitates transcription termination by a mechanism CC that involves Rho binding to the nascent RNA, activation of Rho's CC RNA-dependent ATPase activity, and release of the mRNA from the CC DNA template. {ECO:0000255|HAMAP-Rule:MF_01884}. CC -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring CC structure. {ECO:0000255|HAMAP-Rule:MF_01884, CC ECO:0000269|PubMed:20452362}. CC -!- SIMILARITY: Belongs to the Rho family. {ECO:0000255|HAMAP- CC Rule:MF_01884}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L27279; AAA59210.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36538.1; -; Genomic_DNA. DR PIR; G72246; G72246. DR RefSeq; NP_229270.1; NC_000853.1. DR RefSeq; WP_004081775.1; NZ_CP011107.1. DR PDB; 3L0O; X-ray; 2.35 A; A/B=1-427. DR PDBsum; 3L0O; -. DR ProteinModelPortal; P38527; -. DR STRING; 243274.TM1470; -. DR EnsemblBacteria; AAD36538; AAD36538; TM_1470. DR GeneID; 897108; -. DR KEGG; tma:TM1470; -. DR PATRIC; 23937896; VBITheMar51294_1486. DR eggNOG; ENOG4105C4P; Bacteria. DR eggNOG; COG1158; LUCA. DR InParanoid; P38527; -. DR KO; K03628; -. DR OMA; FLRAPDY; -. DR OrthoDB; EOG6N681W; -. DR EvolutionaryTrace; P38527; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:InterPro. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01884; Rho; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011112; Rho_N. DR InterPro; IPR011113; Rho_RNA-bd. DR InterPro; IPR004665; Term_rho. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF07498; Rho_N; 1. DR Pfam; PF07497; Rho_RNA_bind; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00357; CSP; 1. DR SMART; SM00959; Rho_N; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF68912; SSF68912; 1. DR TIGRFAMs; TIGR00767; rho; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; RNA-binding; Transcription; KW Transcription regulation; Transcription termination. FT CHAIN 1 427 Transcription termination factor Rho. FT /FTId=PRO_0000188980. FT NP_BIND 173 178 ATP. {ECO:0000255|HAMAP-Rule:MF_01884}. FT NP_BIND 185 190 ATP. {ECO:0000255|HAMAP-Rule:MF_01884}. FT BINDING 216 216 ATP. {ECO:0000255|HAMAP-Rule:MF_01884}. FT HELIX 10 15 {ECO:0000244|PDB:3L0O}. FT HELIX 18 27 {ECO:0000244|PDB:3L0O}. FT HELIX 33 35 {ECO:0000244|PDB:3L0O}. FT HELIX 38 47 {ECO:0000244|PDB:3L0O}. FT HELIX 48 50 {ECO:0000244|PDB:3L0O}. FT STRAND 51 64 {ECO:0000244|PDB:3L0O}. FT STRAND 70 73 {ECO:0000244|PDB:3L0O}. FT HELIX 75 77 {ECO:0000244|PDB:3L0O}. FT STRAND 86 88 {ECO:0000244|PDB:3L0O}. FT HELIX 90 95 {ECO:0000244|PDB:3L0O}. FT STRAND 103 109 {ECO:0000244|PDB:3L0O}. FT STRAND 113 115 {ECO:0000244|PDB:3L0O}. FT STRAND 117 126 {ECO:0000244|PDB:3L0O}. FT HELIX 140 142 {ECO:0000244|PDB:3L0O}. FT HELIX 161 169 {ECO:0000244|PDB:3L0O}. FT STRAND 177 182 {ECO:0000244|PDB:3L0O}. FT HELIX 188 202 {ECO:0000244|PDB:3L0O}. FT STRAND 206 212 {ECO:0000244|PDB:3L0O}. FT HELIX 217 220 {ECO:0000244|PDB:3L0O}. FT STRAND 221 226 {ECO:0000244|PDB:3L0O}. FT STRAND 229 233 {ECO:0000244|PDB:3L0O}. FT HELIX 240 259 {ECO:0000244|PDB:3L0O}. FT STRAND 263 269 {ECO:0000244|PDB:3L0O}. FT HELIX 271 281 {ECO:0000244|PDB:3L0O}. FT STRAND 290 292 {ECO:0000244|PDB:3L0O}. FT HELIX 299 306 {ECO:0000244|PDB:3L0O}. FT STRAND 309 314 {ECO:0000244|PDB:3L0O}. FT STRAND 316 324 {ECO:0000244|PDB:3L0O}. FT STRAND 326 328 {ECO:0000244|PDB:3L0O}. FT HELIX 331 338 {ECO:0000244|PDB:3L0O}. FT TURN 339 341 {ECO:0000244|PDB:3L0O}. FT STRAND 344 349 {ECO:0000244|PDB:3L0O}. FT HELIX 351 354 {ECO:0000244|PDB:3L0O}. FT TURN 355 357 {ECO:0000244|PDB:3L0O}. FT HELIX 372 374 {ECO:0000244|PDB:3L0O}. FT HELIX 378 391 {ECO:0000244|PDB:3L0O}. FT HELIX 396 408 {ECO:0000244|PDB:3L0O}. FT HELIX 413 419 {ECO:0000244|PDB:3L0O}. SQ SEQUENCE 427 AA; 48302 MW; 37748653910AFC95 CRC64; MSEEQKTISI SELESMNIKQ LYEIAKSLGI PRYTSMRKRD LIFAILKAQT ESTGYFFGEG VLEIHPEGFG FLRRIEDNLL PSNDDIYISP SQIRKFNLNT GDIISGVIRK PKEGEKYFAM IKIEAINYRP VEAVNDRVNF DNLTPDYPRE RFILETDPKI YSTRLIDLFA PIGKGQRGMI VAPPKAGKTT ILKEIANGIA ENHPDTIRII LLIDERPEEV TDIRESTNAI VIAAPFDMPP DKQVKVAELT LEMAKRLVEF NYDVVILLDS LTRLARVYNI VVPPSGKLLT GGVDPAALYK PKRFFGAARN TREGGSLTII ATALVETGSK MDEVIFEEFK GTGNMELVLS RQLANKRIFP AINLLLSGTR REELLLDEET LKKVWLLRRM LSAMTEEEGL TLILNKLSET SSNEEFLKLI DKEKARY // ID RIMP_THEMA Reviewed; 150 AA. AC Q9X299; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=Ribosome maturation factor RimP {ECO:0000255|HAMAP-Rule:MF_01077}; GN Name=rimP {ECO:0000255|HAMAP-Rule:MF_01077}; GN OrderedLocusNames=TM_1778; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Required for maturation of 30S ribosomal subunits. CC {ECO:0000255|HAMAP-Rule:MF_01077}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01077}. CC -!- SIMILARITY: Belongs to the RimP family. {ECO:0000255|HAMAP- CC Rule:MF_01077}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36841.1; -; Genomic_DNA. DR PIR; A72214; A72214. DR RefSeq; NP_229575.1; NC_000853.1. DR RefSeq; WP_004082324.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X299; -. DR STRING; 243274.TM1778; -. DR EnsemblBacteria; AAD36841; AAD36841; TM_1778. DR GeneID; 897846; -. DR KEGG; tma:TM1778; -. DR PATRIC; 23938538; VBITheMar51294_1798. DR eggNOG; ENOG4108396; Bacteria. DR eggNOG; COG0779; LUCA. DR InParanoid; Q9X299; -. DR KO; K09748; -. DR OMA; RPLFNLE; -. DR OrthoDB; EOG6NSGP3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.30.30.180; -; 1. DR Gene3D; 3.30.300.70; -; 1. DR HAMAP; MF_01077; RimP; 1. DR InterPro; IPR003728; Ribosome_maturation_RimP. DR InterPro; IPR028998; RimP_C. DR InterPro; IPR028989; RimP_N. DR Pfam; PF02576; DUF150; 1. DR SUPFAM; SSF74942; SSF74942; 1. DR SUPFAM; SSF75420; SSF75420; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Ribosome biogenesis. FT CHAIN 1 150 Ribosome maturation factor RimP. FT /FTId=PRO_0000181943. SQ SEQUENCE 150 AA; 17744 MW; 7E423B2EA5F6CA6F CRC64; MFEEMILEKV RKEAERIAEE QGLEIFDVQY RRESRGWVLR IIIDNPVGYV SVRDCELFSR EMERFLDRED FIEHSYTLEV SSPGLDRPLR GPRDYVRFTG KLAKIVTKDG KTFIGRIESF VDGTITISDE KRKYEINIDD VKRANLEVEF // ID REX1_THEMA Reviewed; 208 AA. AC Q9WY16; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Redox-sensing transcriptional repressor Rex 1 {ECO:0000255|HAMAP-Rule:MF_01131}; GN Name=rex1 {ECO:0000255|HAMAP-Rule:MF_01131}; GN OrderedLocusNames=TM_0169; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Modulates transcription in response to changes in CC cellular NADH/NAD(+) redox state. {ECO:0000255|HAMAP- CC Rule:MF_01131}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01131}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01131}. CC -!- SIMILARITY: Belongs to the transcriptional regulatory Rex family. CC {ECO:0000255|HAMAP-Rule:MF_01131}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35262.1; -; Genomic_DNA. DR PIR; G72408; G72408. DR RefSeq; NP_227984.1; NC_000853.1. DR RefSeq; WP_004082798.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY16; -. DR STRING; 243274.TM0169; -. DR EnsemblBacteria; AAD35262; AAD35262; TM_0169. DR GeneID; 897008; -. DR KEGG; tma:TM0169; -. DR PATRIC; 23935186; VBITheMar51294_0170. DR eggNOG; ENOG4105FF6; Bacteria. DR eggNOG; COG2344; LUCA. DR InParanoid; Q9WY16; -. DR KO; K01926; -. DR OMA; LSIELQI; -. DR OrthoDB; EOG6C01BK; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050662; F:coenzyme binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro. DR GO; GO:0051775; P:response to redox state; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01131; Rex; 1. DR InterPro; IPR003781; CoA-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR009718; Rex_DNA-bd_C_dom. DR InterPro; IPR022876; Tscrpt_rep_Rex. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02629; CoA_binding; 1. DR Pfam; PF06971; Put_DNA-bind_N; 1. DR SMART; SM00881; CoA_binding; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; NAD; Reference proteome; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1 208 Redox-sensing transcriptional repressor FT Rex 1. FT /FTId=PRO_0000097926. FT DNA_BIND 15 54 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_01131}. FT NP_BIND 89 94 NAD. {ECO:0000255|HAMAP-Rule:MF_01131}. SQ SEQUENCE 208 AA; 22954 MW; B6A2627B60D10A83 CRC64; MAEKIPKPVS KRLVSYYMCL ERLLDEGVEV VSSEELARRL DLKASQIRKD LSYFGEFGKR GVGYNVEHLY DAIGEILGVK KEWKLVVVGA GNIGRAVANY TVMKEKGFRI IGIFDSDPSK IGKEAAPGLT VSDVSELEKF VEEHGVEIGV IAVPAEHAQE IAERLEKAGI KGILNFAPVK IKVSVPVENI DITASLRVLT FEIVRRNS // ID RISB_THEMA Reviewed; 165 AA. AC Q9X2E5; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178}; DE Short=DMRL synthase {ECO:0000255|HAMAP-Rule:MF_00178}; DE Short=LS {ECO:0000255|HAMAP-Rule:MF_00178}; DE Short=Lumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178}; DE EC=2.5.1.78 {ECO:0000255|HAMAP-Rule:MF_00178}; GN Name=ribH {ECO:0000255|HAMAP-Rule:MF_00178}; GN OrderedLocusNames=TM_1825; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8- CC ribityllumazine by condensation of 5-amino-6-(D- CC ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. CC This is the penultimate step in the biosynthesis of riboflavin. CC {ECO:0000255|HAMAP-Rule:MF_00178}. CC -!- CATALYTIC ACTIVITY: 1-deoxy-L-glycero-tetrulose 4-phosphate + 5- CC amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D- CC ribityl)lumazine + 2 H(2)O + phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00178}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; CC riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D- CC ribitylamino)uracil: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00178}. CC -!- SIMILARITY: Belongs to the DMRL synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00178}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36888.1; -; Genomic_DNA. DR PIR; D72207; D72207. DR RefSeq; NP_229622.1; NC_000853.1. DR RefSeq; WP_004082371.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2E5; -. DR STRING; 243274.TM1825; -. DR EnsemblBacteria; AAD36888; AAD36888; TM_1825. DR GeneID; 897822; -. DR KEGG; tma:TM1825; -. DR PATRIC; 23938637; VBITheMar51294_1845. DR eggNOG; ENOG4108UTT; Bacteria. DR eggNOG; COG0054; LUCA. DR InParanoid; Q9X2E5; -. DR KO; K00794; -. DR OMA; CDTVDQA; -. DR OrthoDB; EOG6RC3WC; -. DR BRENDA; 2.5.1.78; 6331. DR UniPathway; UPA00275; UER00404. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro. DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IBA:GO_Central. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.960; -; 1. DR HAMAP; MF_00178; Lumazine_synth; 1. DR InterPro; IPR002180; DMRL_synthase. DR PANTHER; PTHR21058; PTHR21058; 1. DR Pfam; PF00885; DMRL_synthase; 1. DR SUPFAM; SSF52121; SSF52121; 1. DR TIGRFAMs; TIGR00114; lumazine-synth; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Riboflavin biosynthesis; KW Transferase. FT CHAIN 1 165 6,7-dimethyl-8-ribityllumazine synthase. FT /FTId=PRO_0000134822. FT REGION 56 58 5-amino-6-(D-ribitylamino)uracil binding. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT REGION 80 82 5-amino-6-(D-ribitylamino)uracil binding. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT REGION 85 86 1-deoxy-L-glycero-tetrulose 4-phosphate FT binding. {ECO:0000255|HAMAP- FT Rule:MF_00178}. FT ACT_SITE 88 88 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00178}. FT BINDING 22 22 5-amino-6-(D-ribitylamino)uracil. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT BINDING 113 113 5-amino-6-(D-ribitylamino)uracil; via FT amide nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT BINDING 127 127 1-deoxy-L-glycero-tetrulose 4-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00178}. SQ SEQUENCE 165 AA; 17967 MW; 33CE57F63679791B CRC64; MKVVQGDYRG EGLKIAVVVP RFNDLVTSKL LEGALDGLKR HGVSDENITV VRIPGSMEAI YTLKRLLDLG VHDAIIVLGA VIRGETYHFN VVANEIGKAV AQFNMTSDIP IVFGVLTTDT LEQALNRAGA KSGNKGFEAA MVAIEMANLR KRLRRDVFES DSNGR // ID RIMO_THEMA Reviewed; 430 AA. AC Q9X2H6; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Ribosomal protein S12 methylthiotransferase RimO {ECO:0000255|HAMAP-Rule:MF_01865}; DE Short=S12 MTTase {ECO:0000255|HAMAP-Rule:MF_01865}; DE Short=S12 methylthiotransferase {ECO:0000255|HAMAP-Rule:MF_01865}; DE EC=2.8.4.4 {ECO:0000255|HAMAP-Rule:MF_01865, ECO:0000269|PubMed:20007320, ECO:0000269|PubMed:23542644, ECO:0000269|PubMed:23991893}; DE AltName: Full=Ribosomal protein S12 (aspartate-C(3))-methylthiotransferase {ECO:0000255|HAMAP-Rule:MF_01865}; DE AltName: Full=Ribosome maturation factor RimO {ECO:0000255|HAMAP-Rule:MF_01865}; GN Name=rimO {ECO:0000255|HAMAP-Rule:MF_01865}; GN OrderedLocusNames=TM_1862; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM. RX PubMed=23991893; DOI=10.1021/ja4048448; RA Landgraf B.J., Arcinas A.J., Lee K.H., Booker S.J.; RT "Identification of an intermediate methyl carrier in the radical S- RT adenosylmethionine methylthiotransferases RimO and MiaB."; RL J. Am. Chem. Soc. 135:15404-15416(2013). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 135-430, CATALYTIC ACTIVITY, RP COFACTOR, SUBUNIT, AND EPR SPECTROSCOPY. RX PubMed=20007320; DOI=10.1074/jbc.M109.065516; RA Arragain S., Garcia-Serres R., Blondin G., Douki T., Clemancey M., RA Latour J.M., Forouhar F., Neely H., Montelione G.T., Hunt J.F., RA Mulliez E., Fontecave M., Atta M.; RT "Post-translational modification of ribosomal proteins: structural and RT functional characterization of RimO from Thermotoga maritima, a RT radical S-adenosylmethionine methylthiotransferase."; RL J. Biol. Chem. 285:5792-5801(2010). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR RP CLUSTERS CONNECTED VIA A PENTA-SULFIDE BRIDGE, COFACTOR, CATALYTIC RP ACTIVITY, AND EPR SPECTROSCOPY. RX PubMed=23542644; DOI=10.1038/nchembio.1229; RA Forouhar F., Arragain S., Atta M., Gambarelli S., Mouesca J.M., RA Hussain M., Xiao R., Kieffer-Jaquinod S., Seetharaman J., Acton T.B., RA Montelione G.T., Mulliez E., Hunt J.F., Fontecave M.; RT "Two Fe-S clusters catalyze sulfur insertion by radical-SAM RT methylthiotransferases."; RL Nat. Chem. Biol. 9:333-338(2013). CC -!- FUNCTION: Catalyzes the methylthiolation of an aspartic acid CC residue of ribosomal protein S12. {ECO:0000255|HAMAP- CC Rule:MF_01865, ECO:0000269|PubMed:23991893}. CC -!- CATALYTIC ACTIVITY: L-aspartate-[ribosomal protein S12] + sulfur- CC (sulfur carrier) + 2 S-adenosyl-L-methionine = 3-methylthio-L- CC aspartate-[ribosomal protein S12] + S-adenosyl-L-homocysteine + CC (sulfur carrier) + L-methionine + 5'-deoxyadenosine. CC {ECO:0000255|HAMAP-Rule:MF_01865, ECO:0000269|PubMed:20007320, CC ECO:0000269|PubMed:23542644, ECO:0000269|PubMed:23991893}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01865, CC ECO:0000269|PubMed:23542644}; CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. The two CC iron atoms in each cluster are connected via a penta-sulfide CC bridge. {ECO:0000255|HAMAP-Rule:MF_01865, CC ECO:0000269|PubMed:20007320, ECO:0000269|PubMed:23542644}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23542644}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01865}. CC -!- SIMILARITY: Belongs to the methylthiotransferase family. RimO CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01865}. CC -!- SIMILARITY: Contains 1 MTTase N-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_01865}. CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|HAMAP- CC Rule:MF_01865}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36924.1; -; Genomic_DNA. DR PIR; G72201; G72201. DR RefSeq; NP_229658.1; NC_000853.1. DR RefSeq; WP_004082413.1; NZ_CP011107.1. DR PDB; 2QGQ; X-ray; 2.00 A; A/B/C/D/E/F/G/H=135-430. DR PDB; 4JC0; X-ray; 3.30 A; A/B=1-430. DR PDBsum; 2QGQ; -. DR PDBsum; 4JC0; -. DR ProteinModelPortal; Q9X2H6; -. DR SMR; Q9X2H6; 135-430. DR STRING; 243274.TM1862; -. DR EnsemblBacteria; AAD36924; AAD36924; TM_1862. DR GeneID; 897803; -. DR KEGG; tma:TM1862; -. DR PATRIC; 23938713; VBITheMar51294_1883. DR eggNOG; ENOG4105CBM; Bacteria. DR eggNOG; COG0621; LUCA. DR InParanoid; Q9X2H6; -. DR KO; K14441; -. DR OMA; HYAYPTG; -. DR OrthoDB; EOG6P5ZD8; -. DR BRENDA; 2.8.4.4; 6331. DR EvolutionaryTrace; Q9X2H6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0035599; F:aspartic acid methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.80.30.20; -; 1. DR HAMAP; MF_01865; MTTase_RimO; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR005839; Methylthiotransferase. DR InterPro; IPR020612; Methylthiotransferase_CS. DR InterPro; IPR013848; Methylthiotransferase_N. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR005840; Ribosomal_S12_MeSTrfase_RimO. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR002792; TRAM_dom. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF00919; UPF0004; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00089; TIGR00089; 1. DR TIGRFAMs; TIGR01125; TIGR01125; 1. DR PROSITE; PS51449; MTTASE_N; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. DR PROSITE; PS50926; TRAM; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 430 Ribosomal protein S12 FT methylthiotransferase RimO. FT /FTId=PRO_0000375052. FT DOMAIN 1 116 MTTase N-terminal. {ECO:0000255|HAMAP- FT Rule:MF_01865}. FT DOMAIN 367 430 TRAM. {ECO:0000255|HAMAP-Rule:MF_01865}. FT METAL 10 10 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01865, FT ECO:0000269|PubMed:23542644}. FT METAL 46 46 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01865, FT ECO:0000269|PubMed:23542644}. FT METAL 79 79 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01865, FT ECO:0000269|PubMed:23542644}. FT METAL 148 148 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01865, FT ECO:0000269|PubMed:23542644}. FT METAL 152 152 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01865, FT ECO:0000269|PubMed:23542644}. FT METAL 155 155 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01865, FT ECO:0000269|PubMed:23542644}. FT STRAND 3 6 {ECO:0000244|PDB:4JC0}. FT HELIX 11 23 {ECO:0000244|PDB:4JC0}. FT TURN 24 26 {ECO:0000244|PDB:4JC0}. FT STRAND 34 36 {ECO:0000244|PDB:4JC0}. FT STRAND 39 45 {ECO:0000244|PDB:4JC0}. FT STRAND 48 51 {ECO:0000244|PDB:4JC0}. FT HELIX 52 55 {ECO:0000244|PDB:4JC0}. FT HELIX 57 64 {ECO:0000244|PDB:4JC0}. FT TURN 68 70 {ECO:0000244|PDB:4JC0}. FT STRAND 73 78 {ECO:0000244|PDB:4JC0}. FT HELIX 79 82 {ECO:0000244|PDB:4JC0}. FT HELIX 85 91 {ECO:0000244|PDB:4JC0}. FT STRAND 97 99 {ECO:0000244|PDB:4JC0}. FT TURN 104 107 {ECO:0000244|PDB:4JC0}. FT STRAND 138 145 {ECO:0000244|PDB:2QGQ}. FT HELIX 157 159 {ECO:0000244|PDB:4JC0}. FT HELIX 169 181 {ECO:0000244|PDB:2QGQ}. FT STRAND 186 190 {ECO:0000244|PDB:2QGQ}. FT HELIX 194 196 {ECO:0000244|PDB:2QGQ}. FT HELIX 199 202 {ECO:0000244|PDB:2QGQ}. FT HELIX 207 215 {ECO:0000244|PDB:2QGQ}. FT STRAND 217 220 {ECO:0000244|PDB:2QGQ}. FT STRAND 222 225 {ECO:0000244|PDB:2QGQ}. FT HELIX 230 232 {ECO:0000244|PDB:2QGQ}. FT HELIX 235 243 {ECO:0000244|PDB:2QGQ}. FT STRAND 250 252 {ECO:0000244|PDB:2QGQ}. FT HELIX 260 265 {ECO:0000244|PDB:2QGQ}. FT HELIX 272 285 {ECO:0000244|PDB:2QGQ}. FT STRAND 290 297 {ECO:0000244|PDB:2QGQ}. FT HELIX 304 317 {ECO:0000244|PDB:2QGQ}. FT STRAND 320 326 {ECO:0000244|PDB:2QGQ}. FT TURN 334 337 {ECO:0000244|PDB:4JC0}. FT HELIX 344 367 {ECO:0000244|PDB:2QGQ}. FT TURN 368 371 {ECO:0000244|PDB:2QGQ}. FT STRAND 373 382 {ECO:0000244|PDB:2QGQ}. FT STRAND 385 390 {ECO:0000244|PDB:2QGQ}. FT TURN 395 397 {ECO:0000244|PDB:2QGQ}. FT STRAND 401 405 {ECO:0000244|PDB:2QGQ}. FT STRAND 412 421 {ECO:0000244|PDB:2QGQ}. FT STRAND 424 429 {ECO:0000244|PDB:2QGQ}. SQ SEQUENCE 430 AA; 49222 MW; 345477B796BF3990 CRC64; MRVGIKVLGC PKNEADCEVL AGVLREGGHE IVFDVKDADV VVLDTCAFIE DAKRESIDEI FSFVDAKDQY GYKLVVKGCL VQRYYEELKK EIPEVDQWIG VADPEEIANA IENGTDLVPD QPETVYRYRK RIDLEERPYA YVKISDGCDR GCTFCSIPSF KGSLRSRSIE DITREVEDLL KEGKKEIILV AQDTTSYGID LYRKQALPDL LRRLNSLNGE FWIRVMYLHP DHLTEEIISA MLELDKVVKY FDVPVQHGSD KILKLMGRTK SSEELKKMLS SIRERFPDAV LRTSIIVGFP GETEEDFEEL KQFVEEIQFD KLGAFVYSDE EGTVAFNLKE KVDPEMAKRR QEELLLLQAE ISNSRLDRFV GKKLKFLVEG KEGKFLVGRT WTEAPEVDGV VFVRGKGKIG DFLEVVIKEH DEYDMWGSVI // ID RL10_THEMA Reviewed; 179 AA. AC P29394; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 13-APR-2016, entry version 109. DE RecName: Full=50S ribosomal protein L10; GN Name=rplJ; OrderedLocusNames=TM_0456; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1429627; RA Liao D., Dennis P.P.; RT "The organization and expression of essential transcription RT translation component genes in the extremely thermophilic eubacterium RT Thermotoga maritima."; RL J. Biol. Chem. 267:22787-22797(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 45-179. RX PubMed=8177738; DOI=10.1093/nar/21.21.4904; RA Palm P., Schleper C., Arnold-Ammer I., Holz I., Meier T., RA Lottspeich F., Zillig W.; RT "The DNA-dependent RNA-polymerase of Thermotoga maritima; RT characterisation of the enzyme and the DNA-sequence of the genes for RT the large subunits."; RL Nucleic Acids Res. 21:4904-4908(1993). RN [4] RP SUBUNIT, STOICHIOMETRY, AND MASS SPECTROMETRY. RX PubMed=15923259; DOI=10.1073/pnas.0502193102; RA Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., RA Nierhaus K.H., Robinson C.V.; RT "Heptameric (L12)6/L10 rather than canonical pentameric complexes are RT found by tandem MS of intact ribosomes from thermophilic bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), INTERACTION WITH L7/L12 (RPLL), RP AND SUBUNIT. RX PubMed=15989950; DOI=10.1016/j.cell.2005.04.015; RA Diaconu M., Kothe U., Schlunzen F., Fischer N., Harms J.M., RA Tonevitsky A.G., Stark H., Rodnina M.V., Wahl M.C.; RT "Structural basis for the function of the ribosomal L7/12 stalk in RT factor binding and GTPase activation."; RL Cell 121:991-1004(2005). CC -!- FUNCTION: Forms part of the ribosomal stalk, playing a central CC role in the interaction of the ribosome with GTP-bound translation CC factors (such as IF-2, EF-Tu, EF-G and RF3). {ECO:0000305}. CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. CC The N-terminus interacts with L11 and 23S rRNA to form the base of CC the stalk. The C-terminus forms an elongated spine to which 3 L12 CC dimers bind in a sequential fashion forming a heptameric CC L10(L12)2(L12)2(L12)2 complex. {ECO:0000269|PubMed:15923259, CC ECO:0000269|PubMed:15989950}. CC -!- MASS SPECTROMETRY: Mass=101376; Mass_error=8; Method=Electrospray; CC Range=2-128; Note=Isolated L10(L12)6.; CC Evidence={ECO:0000269|PubMed:15923259}; CC -!- MASS SPECTROMETRY: Mass=20335; Mass_error=3; Method=Electrospray; CC Range=1-179; Evidence={ECO:0000269|PubMed:15923259}; CC -!- SIMILARITY: Belongs to the ribosomal protein L10P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11839; CAA77861.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35539.1; -; Genomic_DNA. DR EMBL; X72695; CAA51244.1; -; Genomic_DNA. DR PIR; A72376; R5HG10. DR RefSeq; NP_228266.1; NC_000853.1. DR RefSeq; WP_004081510.1; NZ_CP011107.1. DR PDB; 1ZAV; X-ray; 1.90 A; A=1-179. DR PDB; 1ZAW; X-ray; 2.30 A; A=1-179. DR PDB; 1ZAX; X-ray; 2.10 A; A=1-179. DR PDBsum; 1ZAV; -. DR PDBsum; 1ZAW; -. DR PDBsum; 1ZAX; -. DR ProteinModelPortal; P29394; -. DR SMR; P29394; 1-177. DR STRING; 243274.TM0456; -. DR EnsemblBacteria; AAD35539; AAD35539; TM_0456. DR GeneID; 897486; -. DR KEGG; tma:TM0456; -. DR PATRIC; 23935809; VBITheMar51294_0463. DR eggNOG; ENOG41081WB; Bacteria. DR eggNOG; COG0244; LUCA. DR InParanoid; P29394; -. DR KO; K02864; -. DR OMA; VVVAHYS; -. DR OrthoDB; EOG6DNTDR; -. DR EvolutionaryTrace; P29394; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00362; Ribosomal_L10; 1. DR InterPro; IPR022973; Ribosomal_L10. DR InterPro; IPR002363; Ribosomal_L10_eubac_CS. DR InterPro; IPR001790; Ribosomal_L10P. DR Pfam; PF00466; Ribosomal_L10; 1. DR PROSITE; PS01109; RIBOSOMAL_L10; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 179 50S ribosomal protein L10. FT /FTId=PRO_0000154734. FT REGION 137 179 Binds L7/L12 dimers. FT HELIX 4 18 {ECO:0000244|PDB:1ZAV}. FT STRAND 22 27 {ECO:0000244|PDB:1ZAV}. FT HELIX 34 48 {ECO:0000244|PDB:1ZAV}. FT STRAND 51 57 {ECO:0000244|PDB:1ZAV}. FT HELIX 59 68 {ECO:0000244|PDB:1ZAV}. FT HELIX 75 77 {ECO:0000244|PDB:1ZAV}. FT STRAND 79 90 {ECO:0000244|PDB:1ZAV}. FT HELIX 93 105 {ECO:0000244|PDB:1ZAV}. FT HELIX 110 112 {ECO:0000244|PDB:1ZAV}. FT STRAND 113 118 {ECO:0000244|PDB:1ZAV}. FT STRAND 121 124 {ECO:0000244|PDB:1ZAV}. FT HELIX 125 132 {ECO:0000244|PDB:1ZAV}. FT HELIX 137 175 {ECO:0000244|PDB:1ZAV}. SQ SEQUENCE 179 AA; 20308 MW; 497C5764A64FC7F9 CRC64; MLTRQQKELI VKEMSEIFKK TSLILFADFL GFTVADLTEL RSRLREKYGD GARFRVVKNT LLNLALKNAE YEGYEEFLKG PTAVLYVTEG DPVEAVKIIY NFYKDKKADL SRLKGGFLEG KKFTAEEVEN IAKLPSKEEL YAMLVGRVKA PITGLVFALS GILRNLVYVL NAIKEKKSE // ID RL15_THEMA Reviewed; 147 AA. AC Q9X1J0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=50S ribosomal protein L15 {ECO:0000255|HAMAP-Rule:MF_01341}; GN Name=rplO {ECO:0000255|HAMAP-Rule:MF_01341}; GN OrderedLocusNames=TM_1481; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_01341}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01341}. CC -!- SIMILARITY: Belongs to the ribosomal protein L15P family. CC {ECO:0000255|HAMAP-Rule:MF_01341}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36547.1; -; Genomic_DNA. DR PIR; A72248; A72248. DR RefSeq; NP_229281.1; NC_000853.1. DR RefSeq; WP_004081797.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1J0; -. DR SMR; Q9X1J0; 5-147. DR STRING; 243274.TM1481; -. DR EnsemblBacteria; AAD36547; AAD36547; TM_1481. DR GeneID; 898006; -. DR KEGG; tma:TM1481; -. DR PATRIC; 23937920; VBITheMar51294_1498. DR eggNOG; ENOG4108UZ0; Bacteria. DR eggNOG; COG0200; LUCA. DR InParanoid; Q9X1J0; -. DR KO; K02876; -. DR OMA; RYQVKAG; -. DR OrthoDB; EOG6CGCM5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01341; Ribosomal_L15; 1. DR InterPro; IPR030878; Ribosomal_L15. DR InterPro; IPR005749; Ribosomal_L15_bac-type. DR InterPro; IPR001196; Ribosomal_L15_CS. DR InterPro; IPR021131; Ribosomal_L18e/L15P. DR PANTHER; PTHR12934; PTHR12934; 1. DR Pfam; PF00828; Ribosomal_L27A; 1. DR SUPFAM; SSF52080; SSF52080; 1. DR TIGRFAMs; TIGR01071; rplO_bact; 1. DR PROSITE; PS00475; RIBOSOMAL_L15; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 147 50S ribosomal protein L15. FT /FTId=PRO_0000104843. SQ SEQUENCE 147 AA; 16198 MW; 69C276AEC3BD9B9C CRC64; MRLEDLRPTP GAMKKRKRVG RGPGSGHGKT SGRGHKGQKA RGSGKVHIWF EGGQTPLQRR LPKRGFKNIN KKVYAVVNVK VLEERFEANE EVTPEKLIER KIIKDLKDGV KILGDGELTK PLVVKAHAFS KSAVEKIESA GGKAEVI // ID RL16_THEMA Reviewed; 142 AA. AC P38509; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=50S ribosomal protein L16 {ECO:0000255|HAMAP-Rule:MF_01342}; GN Name=rplP {ECO:0000255|HAMAP-Rule:MF_01342}; GN OrderedLocusNames=TM_1493; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds 23S rRNA and is also seen to make contacts with CC the A and possibly P site tRNAs. {ECO:0000255|HAMAP- CC Rule:MF_01342}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01342}. CC -!- SIMILARITY: Belongs to the ribosomal protein L16P family. CC {ECO:0000255|HAMAP-Rule:MF_01342}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79784.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36559.1; -; Genomic_DNA. DR PIR; S40195; S40195. DR RefSeq; NP_229293.1; NC_000853.1. DR RefSeq; WP_004081822.1; NZ_CP011107.1. DR ProteinModelPortal; P38509; -. DR SMR; P38509; 1-134. DR STRING; 243274.TM1493; -. DR EnsemblBacteria; AAD36559; AAD36559; TM_1493. DR GeneID; 897352; -. DR KEGG; tma:TM1493; -. DR PATRIC; 23937944; VBITheMar51294_1510. DR eggNOG; ENOG4108R70; Bacteria. DR eggNOG; COG0197; LUCA. DR InParanoid; P38509; -. DR KO; K02878; -. DR OMA; KGAVEYW; -. DR OrthoDB; EOG6WHNWS; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.1170.10; -; 1. DR HAMAP; MF_01342; Ribosomal_L16; 1. DR InterPro; IPR016180; Ribosomal_L10e/L16. DR InterPro; IPR000114; Ribosomal_L16. DR InterPro; IPR020798; Ribosomal_L16_CS. DR PANTHER; PTHR12220; PTHR12220; 1. DR Pfam; PF00252; Ribosomal_L16; 1. DR PRINTS; PR00060; RIBOSOMALL16. DR SUPFAM; SSF54686; SSF54686; 1. DR TIGRFAMs; TIGR01164; rplP_bact; 1. DR PROSITE; PS00586; RIBOSOMAL_L16_1; 1. DR PROSITE; PS00701; RIBOSOMAL_L16_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 142 50S ribosomal protein L16. FT /FTId=PRO_0000062235. SQ SEQUENCE 142 AA; 15978 MW; 958747878085F742 CRC64; MLMPRRVKYR KQQRGRMKGK AKGGTFVQFG EWGLKALEPA WITAQQIEAC RIAMLRVMKR SGKIWIRIFP DKPYTKKPPE SRMGKGKGNV EGWVAVVKPG KILFEVAGVD EETAHEALRY AASKLPIATK IVPRHHIGGE AV // ID RL19_THEMA Reviewed; 115 AA. AC Q9X1Q7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=50S ribosomal protein L19; GN Name=rplS; OrderedLocusNames=TM_1571; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: This protein is located at the 30S-50S ribosomal subunit CC interface and may play a role in the structure and function of the CC aminoacyl-tRNA binding site. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein L19P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36638.1; -; Genomic_DNA. DR PIR; D72237; D72237. DR RefSeq; NP_229371.1; NC_000853.1. DR RefSeq; WP_004081989.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1Q7; -. DR SMR; Q9X1Q7; 15-114. DR STRING; 243274.TM1571; -. DR EnsemblBacteria; AAD36638; AAD36638; TM_1571. DR GeneID; 897960; -. DR KEGG; tma:TM1571; -. DR PATRIC; 23938104; VBITheMar51294_1589. DR eggNOG; ENOG4108YY1; Bacteria. DR eggNOG; COG0335; LUCA. DR InParanoid; Q9X1Q7; -. DR KO; K02884; -. DR OMA; TFTIRKM; -. DR OrthoDB; EOG6DZF5W; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00402; Ribosomal_L19; 1. DR InterPro; IPR001857; Ribosomal_L19. DR InterPro; IPR018257; Ribosomal_L19_CS. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR15680; PTHR15680; 1. DR Pfam; PF01245; Ribosomal_L19; 1. DR PIRSF; PIRSF002191; Ribosomal_L19; 1. DR PRINTS; PR00061; RIBOSOMALL19. DR SUPFAM; SSF50104; SSF50104; 1. DR TIGRFAMs; TIGR01024; rplS_bact; 1. DR PROSITE; PS01015; RIBOSOMAL_L19; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 115 50S ribosomal protein L19. FT /FTId=PRO_0000163556. SQ SEQUENCE 115 AA; 13442 MW; 2324D12D2364D2EA CRC64; MDHLVKIIEK KYEKKEIPDF RPGDTVRVHV KVIEGDRERT QVFEGIVIAK RGSGINKTFT VRRIGSHGVG VERIFPVHSP VVEKIEVVRK GKVRRAKLYY LRNVRGKIRI KERRD // ID RIBU_THEMA Reviewed; 183 AA. AC Q9X1G6; G4FFJ0; DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=Riboflavin transporter RibU; DE AltName: Full=Riboflavin ECF transporter S component RibU; GN Name=ribU; OrderedLocusNames=TM_1455; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION, AND RP EXPRESSION IN E.COLI. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23359690; DOI=10.1073/pnas.1217361110; RA Karpowich N.K., Wang D.N.; RT "Assembly and mechanism of a group II ECF transporter."; RL Proc. Natl. Acad. Sci. U.S.A. 110:2534-2539(2013). CC -!- FUNCTION: Substrate-binding (S) component of an energy-coupling CC factor (ECF) ABC-transporter complex. Mediates riboflavin uptake, CC may also transport FMN and roseoflavin. Probably a riboflavin- CC binding protein that interacts with the energy-coupling factor CC (ECF) ABC-transporter complex. Unlike classic ABC transporters CC this ECF transporter provides the energy necessary to transport a CC number of different substrates. The substrates themselves are CC bound by transmembrane, not extracytoplasmic soluble proteins CC (Probable). Expression of the complex plus RibU in E.coli allows CC riboflavin uptake; uptake does not occur in the absence of RibU or CC the EcfA1A2T complex. {ECO:0000269|PubMed:23359690, ECO:0000305}. CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter CC complex composed of 2 membrane-embedded substrate-binding proteins CC (S component, RibU, BioY), 2 ATP-binding proteins (A component) CC and 2 transmembrane proteins (T component) upon coexpression in CC E.coli. A stable subcomplex with both A and T components are also CC isolated. This complex interacts with at least 2 substrate- CC specific components, BioY and RibU. {ECO:0000269|PubMed:23359690}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000305|PubMed:23359690}; Multi-pass membrane protein CC {ECO:0000305|PubMed:23359690}. CC -!- SIMILARITY: Belongs to the prokaryotic riboflavin transporter (P- CC RFT) (TC 2.A.87) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36523.1; -; Genomic_DNA. DR PIR; H72250; H72250. DR RefSeq; NP_229254.1; NC_000853.1. DR RefSeq; WP_004081740.1; NZ_CP011107.1. DR STRING; 243274.TM1455; -. DR TCDB; 3.A.1.25.5; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36523; AAD36523; TM_1455. DR GeneID; 898021; -. DR KEGG; tma:TM1455; -. DR PATRIC; 23937862; VBITheMar51294_1469. DR eggNOG; ENOG41081BK; Bacteria. DR eggNOG; COG3601; LUCA. DR InParanoid; Q9X1G6; -. DR OMA; FLKYDPS; -. DR OrthoDB; EOG6MM1M8; -. DR BioCyc; TMAR243274:GC6P-1493-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032217; F:riboflavin transporter activity; IGI:UniProtKB. DR GO; GO:0032218; P:riboflavin transport; IGI:UniProtKB. DR InterPro; IPR024529; ECF_trnsprt_substrate-spec. DR InterPro; IPR025720; RibU. DR Pfam; PF12822; DUF3816; 1. DR PIRSF; PIRSF037778; UCP037778_transp_RibU; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 183 Riboflavin transporter RibU. FT /FTId=PRO_0000422262. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 41 61 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. FT TRANSMEM 144 164 Helical. {ECO:0000255}. SQ SEQUENCE 183 AA; 20015 MW; BFCB532C18F64DB6 CRC64; MSSIKKISFV GIFSALATLV MFLEFPIFPQ ASFLKYDPSE IPALIVSFLL GPGVGMFVVL VKDILFFLMK SGDPVGIAMN AVLGMSFVGI AGLIYHRNKS RATAIKGMIV ATLFATAFAL GLNALIVPLY FEAPFELYLK FFPFILAFNL VKFGIDSVVT FFVYKKVSSI LKLETVEGRS NNG // ID RL17_THEMA Reviewed; 131 AA. AC Q9X1I1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=50S ribosomal protein L17 {ECO:0000255|HAMAP-Rule:MF_01368}; GN Name=rplQ {ECO:0000255|HAMAP-Rule:MF_01368}; GN OrderedLocusNames=TM_1471; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L32. CC {ECO:0000255|HAMAP-Rule:MF_01368}. CC -!- SIMILARITY: Belongs to the ribosomal protein L17P family. CC {ECO:0000255|HAMAP-Rule:MF_01368}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36539.1; -; Genomic_DNA. DR PIR; H72246; H72246. DR RefSeq; NP_229271.1; NC_000853.1. DR RefSeq; WP_004081777.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1I1; -. DR STRING; 243274.TM1471; -. DR EnsemblBacteria; AAD36539; AAD36539; TM_1471. DR GeneID; 898012; -. DR KEGG; tma:TM1471; -. DR PATRIC; 23937898; VBITheMar51294_1487. DR eggNOG; ENOG4108ZT0; Bacteria. DR eggNOG; COG0203; LUCA. DR InParanoid; Q9X1I1; -. DR KO; K02879; -. DR OMA; KYERITT; -. DR OrthoDB; EOG6GR3GR; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.1030.10; -; 1. DR HAMAP; MF_01368; Ribosomal_L17; 1. DR InterPro; IPR000456; Ribosomal_L17. DR PANTHER; PTHR14413; PTHR14413; 1. DR Pfam; PF01196; Ribosomal_L17; 1. DR SUPFAM; SSF64263; SSF64263; 1. DR TIGRFAMs; TIGR00059; L17; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 131 50S ribosomal protein L17. FT /FTId=PRO_0000175546. SQ SEQUENCE 131 AA; 14820 MW; AF169D0DA7E53CC5 CRC64; MRHRVKRHKL GRYGSHRKSL LRNLSREIVE HGSIVTTTAK AKALKTFMDK LVSKAIEAAT TDDRARSVHL RRQINAVLGD RRLTNKLVDE IAKNYVGRRG GYVRVLRIGF RRGDAAEMSL VQLVEASSQE G // ID RL20_THEMA Reviewed; 118 AA. AC Q9X1S8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=50S ribosomal protein L20; GN Name=rplT; OrderedLocusNames=TM_1592; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for CC the in vitro assembly process of the 50S ribosomal subunit. It is CC not involved in the protein synthesizing functions of that subunit CC (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein L20P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36659.1; -; Genomic_DNA. DR PIR; D72233; D72233. DR RefSeq; NP_229392.1; NC_000853.1. DR RefSeq; WP_004082031.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1S8; -. DR SMR; Q9X1S8; 1-117. DR STRING; 243274.TM1592; -. DR EnsemblBacteria; AAD36659; AAD36659; TM_1592. DR GeneID; 897945; -. DR KEGG; tma:TM1592; -. DR PATRIC; 23938158; VBITheMar51294_1611. DR eggNOG; ENOG4108YZX; Bacteria. DR eggNOG; COG0292; LUCA. DR InParanoid; Q9X1S8; -. DR KO; K02887; -. DR OMA; RKAKEQM; -. DR OrthoDB; EOG6CGCMB; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:InterPro. DR HAMAP; MF_00382; Ribosomal_L20; 1. DR InterPro; IPR005813; Ribosomal_L20. DR PANTHER; PTHR10986; PTHR10986; 1. DR Pfam; PF00453; Ribosomal_L20; 1. DR PRINTS; PR00062; RIBOSOMALL20. DR TIGRFAMs; TIGR01032; rplT_bact; 1. DR PROSITE; PS00937; RIBOSOMAL_L20; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 118 50S ribosomal protein L20. FT /FTId=PRO_0000177248. SQ SEQUENCE 118 AA; 13845 MW; DE8B62E30670A801 CRC64; MRVKRAVHAK KKRKKYLKAA KGYRGALSRR YKLAKQMYVR SKWYSYVGRK QKKRDMRKLW ITRINIAARN EGLKYSELIH GLKLAGVSIN RKMLSELAVN DPEAFKEYVK IAKEALAS // ID RL21_THEMA Reviewed; 105 AA. AC Q9X1G9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=50S ribosomal protein L21 {ECO:0000255|HAMAP-Rule:MF_01363}; GN Name=rplU {ECO:0000255|HAMAP-Rule:MF_01363}; GN OrderedLocusNames=TM_1458; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: This protein binds to 23S rRNA in the presence of CC protein L20. {ECO:0000255|HAMAP-Rule:MF_01363}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L20. CC {ECO:0000255|HAMAP-Rule:MF_01363}. CC -!- SIMILARITY: Belongs to the ribosomal protein L21P family. CC {ECO:0000255|HAMAP-Rule:MF_01363}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36526.1; -; Genomic_DNA. DR PIR; C72251; C72251. DR RefSeq; NP_229257.1; NC_000853.1. DR RefSeq; WP_010865346.1; NC_000853.1. DR ProteinModelPortal; Q9X1G9; -. DR STRING; 243274.TM1458; -. DR EnsemblBacteria; AAD36526; AAD36526; TM_1458. DR GeneID; 897166; -. DR KEGG; tma:TM1458; -. DR PATRIC; 23937868; VBITheMar51294_1472. DR eggNOG; ENOG4105KK9; Bacteria. DR eggNOG; COG0261; LUCA. DR InParanoid; Q9X1G9; -. DR KO; K02888; -. DR OMA; RQSYSYV; -. DR OrthoDB; EOG6TJ84X; -. DR BioCyc; TMAR243274:GC6P-1496-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01363; Ribosomal_L21; 1. DR InterPro; IPR028909; L21p-like. DR InterPro; IPR001787; Ribosomal_L21. DR InterPro; IPR018258; Ribosomal_L21_CS. DR Pfam; PF00829; Ribosomal_L21p; 1. DR SUPFAM; SSF141091; SSF141091; 1. DR TIGRFAMs; TIGR00061; L21; 1. DR PROSITE; PS01169; RIBOSOMAL_L21; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 105 50S ribosomal protein L21. FT /FTId=PRO_0000181017. SQ SEQUENCE 105 AA; 12210 MW; B2C58F27272F83C8 CRC64; MLYAIVETAG RQYRVEEGKI LYTEKQKDYS PGDEIVFDRV VFVRKDGEVL VGKPYVEGAK VVGKVLEHAK ARKVKTVKYR PRKNSKVEKG HRQWYTAIKI EKIEL // ID RL23_THEMA Reviewed; 100 AA. AC P38512; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369}; GN Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369}; GN OrderedLocusNames=TM_1498; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA. CC One of the proteins that surrounds the polypeptide exit tunnel on CC the outside of the ribosome. Forms the main docking site for CC trigger factor binding to the ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01369}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29, CC and trigger factor when it is bound to the ribosome. CC {ECO:0000255|HAMAP-Rule:MF_01369}. CC -!- SIMILARITY: Belongs to the ribosomal protein L23P family. CC {ECO:0000255|HAMAP-Rule:MF_01369}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79779.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36564.1; -; Genomic_DNA. DR PIR; S40190; S40190. DR RefSeq; NP_229298.1; NC_000853.1. DR RefSeq; WP_004081832.1; NZ_CP011107.1. DR ProteinModelPortal; P38512; -. DR STRING; 243274.TM1498; -. DR EnsemblBacteria; AAD36564; AAD36564; TM_1498. DR GeneID; 897997; -. DR KEGG; tma:TM1498; -. DR PATRIC; 23937954; VBITheMar51294_1515. DR eggNOG; ENOG4105KZR; Bacteria. DR eggNOG; COG0089; LUCA. DR InParanoid; P38512; -. DR KO; K02892; -. DR OMA; TAGMMND; -. DR OrthoDB; EOG6HTP4P; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.70.330; -; 1. DR HAMAP; MF_01369_B; Ribosomal_L23_B; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom. DR InterPro; IPR001014; Ribosomal_L23/L25_CS. DR InterPro; IPR013025; Ribosomal_L25/23. DR Pfam; PF00276; Ribosomal_L23; 1. DR SUPFAM; SSF54189; SSF54189; 1. DR PROSITE; PS00050; RIBOSOMAL_L23; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 100 50S ribosomal protein L23. FT /FTId=PRO_0000129426. SQ SEQUENCE 100 AA; 11738 MW; 283898D6F66B9CA7 CRC64; MKQEKLSLHD VLIRPIITEK ALILREQRKY VFEVNPLANK NLVKEAVEKL FNVKVEKVNI LNMKPKPKRR GIFEGKTRSW KKAVVTLKEG YTIKELEGEH // ID RL13_THEMA Reviewed; 149 AA. AC Q9X1G5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=50S ribosomal protein L13 {ECO:0000255|HAMAP-Rule:MF_01366}; GN Name=rplM {ECO:0000255|HAMAP-Rule:MF_01366}; GN OrderedLocusNames=TM_1454; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: This protein is one of the early assembly proteins of CC the 50S ribosomal subunit, although it is not seen to bind rRNA by CC itself. It is important during the early stages of 50S assembly. CC {ECO:0000255|HAMAP-Rule:MF_01366}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01366}. CC -!- SIMILARITY: Belongs to the ribosomal protein L13P family. CC {ECO:0000255|HAMAP-Rule:MF_01366}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36522.1; -; Genomic_DNA. DR PIR; G72250; G72250. DR RefSeq; NP_229253.1; NC_000853.1. DR RefSeq; WP_004081738.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1G5; -. DR SMR; Q9X1G5; 9-145. DR STRING; 243274.TM1454; -. DR EnsemblBacteria; AAD36522; AAD36522; TM_1454. DR GeneID; 898022; -. DR KEGG; tma:TM1454; -. DR PATRIC; 23937860; VBITheMar51294_1468. DR eggNOG; ENOG4108UM5; Bacteria. DR eggNOG; COG0102; LUCA. DR InParanoid; Q9X1G5; -. DR KO; K02871; -. DR OMA; GMLPHNR; -. DR OrthoDB; EOG628FBD; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.90.1180.10; -; 1. DR HAMAP; MF_01366; Ribosomal_L13; 1. DR InterPro; IPR005822; Ribosomal_L13. DR InterPro; IPR005823; Ribosomal_L13_bac-type. DR InterPro; IPR023563; Ribosomal_L13_CS. DR InterPro; IPR023564; Ribosomal_L13_dom. DR PANTHER; PTHR11545; PTHR11545; 1. DR Pfam; PF00572; Ribosomal_L13; 1. DR PIRSF; PIRSF002181; Ribosomal_L13; 1. DR SUPFAM; SSF52161; SSF52161; 1. DR TIGRFAMs; TIGR01066; rplM_bact; 1. DR PROSITE; PS00783; RIBOSOMAL_L13; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 149 50S ribosomal protein L13. FT /FTId=PRO_0000133753. SQ SEQUENCE 149 AA; 17284 MW; FE964C9D790BCA0F CRC64; MARYFPVQKT TMIKPEEVER KWYVVDASGK VLGRLATRIA KILMGKHKPN YTPHVDTGDY VIVVNADKVV LTGKKLDQKV YYWHSGYPGG LKSLTARQML EKHPERLIWL AVKRMLPKNR KGRKMLKRLK VYASPEHPHQ AQKPEPIEL // ID RL22_THEMA Reviewed; 159 AA. AC P38511; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 17-FEB-2016, entry version 99. DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331}; GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; GN OrderedLocusNames=TM_1495; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: This protein binds specifically to 23S rRNA; its binding CC is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. CC It is important during the early stages of 50S assembly. It makes CC multiple contacts with different domains of the 23S rRNA in the CC assembled 50S subunit and ribosome (By similarity). CC {ECO:0000255|HAMAP-Rule:MF_01331}. CC -!- FUNCTION: The globular domain of the protein is located near the CC polypeptide exit tunnel on the outside of the subunit, while an CC extended beta-hairpin is found that lines the wall of the exit CC tunnel in the center of the 70S ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01331}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01331}. CC -!- SIMILARITY: Belongs to the ribosomal protein L22P family. CC {ECO:0000255|HAMAP-Rule:MF_01331}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79782.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36561.1; -; Genomic_DNA. DR PIR; G72249; G72249. DR RefSeq; NP_229295.1; NC_000853.1. DR RefSeq; WP_004081826.1; NZ_CP011107.1. DR ProteinModelPortal; P38511; -. DR STRING; 243274.TM1495; -. DR PRIDE; P38511; -. DR EnsemblBacteria; AAD36561; AAD36561; TM_1495. DR GeneID; 898674; -. DR KEGG; tma:TM1495; -. DR KEGG; tmi:THEMA_06825; -. DR KEGG; tmw:THMA_1527; -. DR PATRIC; 23937948; VBITheMar51294_1512. DR eggNOG; ENOG4105KAP; Bacteria. DR eggNOG; COG0091; LUCA. DR InParanoid; P38511; -. DR KO; K02890; -. DR OMA; MKRIQPR; -. DR OrthoDB; EOG6V4GKB; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.470.10; -; 1. DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1. DR InterPro; IPR001063; Ribosomal_L22. DR InterPro; IPR018260; Ribosomal_L22/L17_CS. DR InterPro; IPR005727; Ribosomal_L22_bac/chlpt-type. DR PANTHER; PTHR13501; PTHR13501; 1. DR Pfam; PF00237; Ribosomal_L22; 1. DR SUPFAM; SSF54843; SSF54843; 1. DR TIGRFAMs; TIGR01044; rplV_bact; 1. DR PROSITE; PS00464; RIBOSOMAL_L22; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 159 50S ribosomal protein L22. FT /FTId=PRO_0000125247. FT CONFLICT 82 82 A -> R (in Ref. 1; CAA79782). FT {ECO:0000305}. SQ SEQUENCE 159 AA; 18333 MW; 96FADDA9A9936CC3 CRC64; MKLQVPRNGL KRSLFHKKRK ELLSSLPKIE ARAVAKYIRI SPRKARAIAN TIRGKSVEEA FQILAFSPKK AARIMEKVLK SAVANAENNF GLSVENLYVS ECYVNDGPRM KRIWPRGRGR ADIIQKRMSH ITVVVRDRSR EDEYRKALEE LQKKISSEE // ID RL25_THEMA Reviewed; 215 AA. AC Q9X1W2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=50S ribosomal protein L25 {ECO:0000255|HAMAP-Rule:MF_01334}; DE AltName: Full=General stress protein CTC {ECO:0000255|HAMAP-Rule:MF_01334}; GN Name=rplY {ECO:0000255|HAMAP-Rule:MF_01334}; GN Synonyms=ctc {ECO:0000255|HAMAP-Rule:MF_01334}; GN OrderedLocusNames=TM_1627; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: This is one of the proteins that binds to the 5S RNA in CC the ribosome where it forms part of the central protuberance. CC {ECO:0000255|HAMAP-Rule:MF_01334}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S CC rRNA independently of L5 and L18. {ECO:0000255|HAMAP- CC Rule:MF_01334}. CC -!- SIMILARITY: Belongs to the ribosomal protein L25P family. CTC CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36694.1; -; Genomic_DNA. DR PIR; C72229; C72229. DR RefSeq; NP_229427.1; NC_000853.1. DR RefSeq; WP_004082103.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1W2; -. DR STRING; 243274.TM1627; -. DR EnsemblBacteria; AAD36694; AAD36694; TM_1627. DR GeneID; 897402; -. DR KEGG; tma:TM1627; -. DR PATRIC; 23938228; VBITheMar51294_1646. DR eggNOG; ENOG4105KW6; Bacteria. DR eggNOG; COG1825; LUCA. DR InParanoid; Q9X1W2; -. DR KO; K02897; -. DR OMA; GHRMRIN; -. DR OrthoDB; EOG6SZ1PC; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0008097; F:5S rRNA binding; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.170.120.20; -; 1. DR Gene3D; 2.40.240.10; -; 1. DR HAMAP; MF_01334; Ribosomal_L25_CTC; 1. DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl. DR InterPro; IPR029751; Ribosomal_L25. DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth. DR InterPro; IPR020057; Ribosomal_L25_b-dom. DR InterPro; IPR001021; Ribosomal_L25_long. DR Pfam; PF01386; Ribosomal_L25p; 1. DR Pfam; PF14693; Ribosomal_TL5_C; 1. DR ProDom; PD012503; Ribosomal_L25; 1. DR SUPFAM; SSF50715; SSF50715; 1. DR TIGRFAMs; TIGR00731; bL25_bact_ctc; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 215 50S ribosomal protein L25. FT /FTId=PRO_0000181606. SQ SEQUENCE 215 AA; 24254 MW; 374295D664B57083 CRC64; MVSLEARVRE VKGKREARRL RRRGEVPAVV YGPATEPIPV KIKRSVLEKI FHTISEATPI QLIIKDDQGN TVAEKTVFLK MVQRDKVSET VVHLDFYEPT KGHRMRINVP LKVVGKPVGV EKGGFLEVFH EEIPVETDPD KVPQEIEVDV SSLDLGDVIH ARDLKLPEGV KCLLEEEEAV VSVLVPKEVA IEEATEEEEE AAEPEVIKRK EEEEE // ID RL14_THEMA Reviewed; 122 AA. AC P38508; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 110. DE RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367}; GN Name=rplN {ECO:0000255|HAMAP-Rule:MF_01367}; GN OrderedLocusNames=TM_1490; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit CC bridges in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and CC together make contacts with the 16S rRNA in bridges B5 and B8. CC {ECO:0000255|HAMAP-Rule:MF_01367}. CC -!- SIMILARITY: Belongs to the ribosomal protein L14P family. CC {ECO:0000255|HAMAP-Rule:MF_01367}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79787.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36556.1; -; Genomic_DNA. DR PIR; B72249; B72249. DR RefSeq; NP_229290.1; NC_000853.1. DR RefSeq; WP_004081816.1; NZ_CP011107.1. DR ProteinModelPortal; P38508; -. DR SMR; P38508; 1-121. DR STRING; 243274.TM1490; -. DR EnsemblBacteria; AAD36556; AAD36556; TM_1490. DR GeneID; 898001; -. DR KEGG; tma:TM1490; -. DR PATRIC; 23937938; VBITheMar51294_1507. DR eggNOG; ENOG4108UNN; Bacteria. DR eggNOG; COG0093; LUCA. DR InParanoid; P38508; -. DR KO; K02874; -. DR OMA; LRDKQFM; -. DR OrthoDB; EOG6GBMJ6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.150.20; -; 1. DR HAMAP; MF_01367; Ribosomal_L14; 1. DR InterPro; IPR000218; Ribosomal_L14P. DR InterPro; IPR005745; Ribosomal_L14P_bac-type. DR InterPro; IPR019972; Ribosomal_L14P_CS. DR PANTHER; PTHR11761; PTHR11761; 1. DR Pfam; PF00238; Ribosomal_L14; 1. DR SMART; SM01374; Ribosomal_L14; 1. DR SUPFAM; SSF50193; SSF50193; 1. DR TIGRFAMs; TIGR01067; rplN_bact; 1. DR PROSITE; PS00049; RIBOSOMAL_L14; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 122 50S ribosomal protein L14. FT /FTId=PRO_0000128565. FT CONFLICT 21 21 V -> I (in Ref. 1; CAA79787). FT {ECO:0000305}. SQ SEQUENCE 122 AA; 13702 MW; BD76DD918641BE11 CRC64; MIQQETYLNV ADNSGAKKLR VIRVIGGFHK KYGTVGDIVV CSVREAIPNS DVKKGDVVRA VIVRTKKEIR RNDGTYIRFD DNAAVLIDKF NAPRGTRIFG PVARELREKG FMKIVSLAPE VW // ID RL32_THEMA Reviewed; 60 AA. AC Q9WXZ7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 13-APR-2016, entry version 88. DE RecName: Full=50S ribosomal protein L32; GN Name=rpmF; OrderedLocusNames=TM_0150; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ribosomal protein L32P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35243.1; -; Genomic_DNA. DR PIR; D72412; D72412. DR RefSeq; NP_227965.1; NC_000853.1. DR RefSeq; WP_004082761.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXZ7; -. DR STRING; 243274.TM0150; -. DR EnsemblBacteria; AAD35243; AAD35243; TM_0150. DR GeneID; 896985; -. DR KEGG; tma:TM0150; -. DR PATRIC; 23935144; VBITheMar51294_0149. DR eggNOG; ENOG41085U1; Bacteria. DR eggNOG; COG0333; LUCA. DR InParanoid; Q9WXZ7; -. DR KO; K02911; -. DR OMA; CPKCGFY; -. DR OrthoDB; EOG6VMTT4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00340; Ribosomal_L32; 1. DR InterPro; IPR002677; Ribosomal_L32p. DR InterPro; IPR011332; Ribosomal_zn-bd. DR Pfam; PF01783; Ribosomal_L32p; 1. DR SUPFAM; SSF57829; SSF57829; 1. DR TIGRFAMs; TIGR01031; rpmF_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 60 50S ribosomal protein L32. FT /FTId=PRO_0000172425. SQ SEQUENCE 60 AA; 7041 MW; 35066CED4B46AD70 CRC64; MAVPKQKRSR SRTHHKRAKI YRAISVPLEK CPNCGEYKMP HRVCLHCGYY KGKQVLEISE // ID RL11_THEMA Reviewed; 141 AA. AC P29395; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-MAY-2016, entry version 131. DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736}; GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; GN OrderedLocusNames=TM_0454; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1429627; RA Liao D., Dennis P.P.; RT "The organization and expression of essential transcription RT translation component genes in the extremely thermophilic eubacterium RT Thermotoga maritima."; RL J. Biol. Chem. 267:22787-22797(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS). RX PubMed=10338213; DOI=10.1016/S0092-8674(00)80759-X; RA Wimberly B.T., Guymon R., McCutcheon J.P., White S.W., RA Ramakrishnan V.; RT "A detailed view of a ribosomal active site: the structure of the L11- RT RNA complex."; RL Cell 97:491-502(1999). CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the CC ribosome interact with GTP-bound translation factors. CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. CC Interacts with L10 and the large rRNA to form the base of the CC stalk. L10 forms an elongated spine to which 3 L12 dimers bind in CC a sequential fashion forming a heptameric L10(L12)2(L12)2(L12)2 CC complex. CC -!- PTM: One or more lysine residues are methylated. CC {ECO:0000255|HAMAP-Rule:MF_00736}. CC -!- SIMILARITY: Belongs to the ribosomal protein L11P family. CC {ECO:0000255|HAMAP-Rule:MF_00736}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11839; CAA77859.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35537.1; -; Genomic_DNA. DR PIR; B44466; R5HG11. DR RefSeq; NP_228264.1; NC_000853.1. DR RefSeq; WP_004081512.1; NZ_CP011107.1. DR PDB; 1IP8; Model; -; G=-. DR PDB; 1JQM; EM; -; A=2-140. DR PDB; 1JQS; EM; -; A=2-140. DR PDB; 1JQT; EM; -; A=2-140. DR PDB; 1MMS; X-ray; 2.57 A; A/B=2-141. DR PDB; 1MVR; EM; 12.80 A; L=2-141. DR PDB; 1OLN; NMR; -; A=2-141. DR PDB; 1PN7; EM; 10.80 A; L=8-140. DR PDB; 1PN8; EM; 10.80 A; L=8-140. DR PDB; 1R2W; EM; 9.00 A; A=2-141. DR PDB; 1R2X; EM; 9.00 A; A=2-141. DR PDB; 2BCW; EM; 11.20 A; A=8-72. DR PDB; 2GKY; Model; -; A=8-140. DR PDB; 2GKZ; Model; -; A=8-140. DR PDB; 2JQ7; NMR; -; A=1-141. DR PDB; 2K3F; NMR; -; A=1-141. DR PDBsum; 1IP8; -. DR PDBsum; 1JQM; -. DR PDBsum; 1JQS; -. DR PDBsum; 1JQT; -. DR PDBsum; 1MMS; -. DR PDBsum; 1MVR; -. DR PDBsum; 1OLN; -. DR PDBsum; 1PN7; -. DR PDBsum; 1PN8; -. DR PDBsum; 1R2W; -. DR PDBsum; 1R2X; -. DR PDBsum; 2BCW; -. DR PDBsum; 2GKY; -. DR PDBsum; 2GKZ; -. DR PDBsum; 2JQ7; -. DR PDBsum; 2K3F; -. DR ProteinModelPortal; P29395; -. DR SMR; P29395; 1-141. DR MINT; MINT-208764; -. DR STRING; 243274.TM0454; -. DR EnsemblBacteria; AAD35537; AAD35537; TM_0454. DR GeneID; 897484; -. DR KEGG; tma:TM0454; -. DR PATRIC; 23935803; VBITheMar51294_0460. DR eggNOG; ENOG4108UIK; Bacteria. DR eggNOG; COG0080; LUCA. DR InParanoid; P29395; -. DR KO; K02867; -. DR OMA; CKQFNAK; -. DR OrthoDB; EOG69PQ9D; -. DR EvolutionaryTrace; P29395; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 1.10.10.250; -; 1. DR Gene3D; 3.30.1550.10; -; 1. DR HAMAP; MF_00736; Ribosomal_L11; 1. DR InterPro; IPR000911; Ribosomal_L11/L12. DR InterPro; IPR006519; Ribosomal_L11_bac-typ. DR InterPro; IPR020783; Ribosomal_L11_C. DR InterPro; IPR020785; Ribosomal_L11_CS. DR InterPro; IPR020784; Ribosomal_L11_N. DR PANTHER; PTHR11661; PTHR11661; 1. DR Pfam; PF00298; Ribosomal_L11; 1. DR Pfam; PF03946; Ribosomal_L11_N; 1. DR SMART; SM00649; RL11; 1. DR SUPFAM; SSF46906; SSF46906; 1. DR SUPFAM; SSF54747; SSF54747; 1. DR TIGRFAMs; TIGR01632; L11_bact; 1. DR PROSITE; PS00359; RIBOSOMAL_L11; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Methylation; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 141 50S ribosomal protein L11. FT /FTId=PRO_0000104397. FT STRAND 9 14 {ECO:0000244|PDB:1MMS}. FT TURN 21 25 {ECO:0000244|PDB:1MMS}. FT HELIX 26 29 {ECO:0000244|PDB:1MMS}. FT TURN 30 32 {ECO:0000244|PDB:1MMS}. FT HELIX 35 45 {ECO:0000244|PDB:1MMS}. FT TURN 46 48 {ECO:0000244|PDB:1MMS}. FT STRAND 51 60 {ECO:0000244|PDB:1MMS}. FT STRAND 62 64 {ECO:0000244|PDB:2JQ7}. FT STRAND 66 70 {ECO:0000244|PDB:1MMS}. FT HELIX 75 83 {ECO:0000244|PDB:1MMS}. FT TURN 92 94 {ECO:0000244|PDB:1MMS}. FT STRAND 98 101 {ECO:0000244|PDB:1MMS}. FT HELIX 102 112 {ECO:0000244|PDB:1MMS}. FT HELIX 113 115 {ECO:0000244|PDB:1MMS}. FT HELIX 121 132 {ECO:0000244|PDB:1MMS}. FT TURN 133 136 {ECO:0000244|PDB:1MMS}. FT STRAND 137 140 {ECO:0000244|PDB:1MMS}. SQ SEQUENCE 141 AA; 15089 MW; 08AD83D090F651A9 CRC64; MAKKVAAQIK LQLPAGKATP APPVGPALGQ HGVNIMEFCK RFNAETADKA GMILPVVITV YEDKSFTFII KTPPASFLLK KAAGIEKGSS EPKRKIVGKV TRKQIEEIAK TKMPDLNANS LEAAMKIIEG TAKSMGIEVV D // ID RL18_THEMA Reviewed; 122 AA. AC Q9ZAE3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 100. DE RecName: Full=50S ribosomal protein L18 {ECO:0000255|HAMAP-Rule:MF_01337}; GN Name=rplR {ECO:0000255|HAMAP-Rule:MF_01337}; GN OrderedLocusNames=TM_1484; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: This is one of the proteins that binds and probably CC mediates the attachment of the 5S RNA into the large ribosomal CC subunit, where it forms part of the central protuberance. CC {ECO:0000255|HAMAP-Rule:MF_01337}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs. CC {ECO:0000255|HAMAP-Rule:MF_01337}. CC -!- SIMILARITY: Belongs to the ribosomal protein L18P family. CC {ECO:0000255|HAMAP-Rule:MF_01337}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79793.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36550.1; -; Genomic_DNA. DR PIR; D72248; D72248. DR RefSeq; NP_229284.1; NC_000853.1. DR RefSeq; WP_004081803.1; NZ_CP011107.1. DR ProteinModelPortal; Q9ZAE3; -. DR SMR; Q9ZAE3; 3-122. DR STRING; 243274.TM1484; -. DR EnsemblBacteria; AAD36550; AAD36550; TM_1484. DR GeneID; 898004; -. DR KEGG; tma:TM1484; -. DR PATRIC; 23937926; VBITheMar51294_1501. DR eggNOG; ENOG4105K4C; Bacteria. DR eggNOG; COG0256; LUCA. DR InParanoid; Q9ZAE3; -. DR KO; K02881; -. DR OMA; NQKAKRI; -. DR OrthoDB; EOG64NB48; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0008097; F:5S rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01337_B; Ribosomal_L18_B; 1. DR InterPro; IPR005484; Ribosomal_L18. DR InterPro; IPR004389; Ribosomal_L18_bac-type. DR Pfam; PF00861; Ribosomal_L18p; 1. DR TIGRFAMs; TIGR00060; L18_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 122 50S ribosomal protein L18. FT /FTId=PRO_0000131370. FT CONFLICT 60 60 D -> V (in Ref. 1; CAA79793). FT {ECO:0000305}. SQ SEQUENCE 122 AA; 14066 MW; 8A7392B57FC82D0B CRC64; MIKKESKKEQ RLRRHRRVRK KVFGTPERPR LCVFRSNKHI YAQIIDDTIG HTLVSASTLD PELREKLQKT WNVEAAKEVG LLIGKRALEK GIKKVVFDRG GYKYHGRVKA LADGAREAGL EF // ID RL2_THEMA Reviewed; 276 AA. AC P38510; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 114. DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320}; GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; GN OrderedLocusNames=TM_1497; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: One of the primary rRNA binding proteins. Required for CC association of the 30S and 50S subunits to form the 70S ribosome, CC for tRNA binding and peptide bond formation. It has been suggested CC to have peptidyltransferase activity; this is somewhat CC controversial. Makes several contacts with the 16S rRNA in the 70S CC ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the CC 30S subunit in the 70S ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01320}. CC -!- SIMILARITY: Belongs to the ribosomal protein L2P family. CC {ECO:0000255|HAMAP-Rule:MF_01320}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79780.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36563.1; -; Genomic_DNA. DR PIR; A72250; A72250. DR RefSeq; NP_229297.1; NC_000853.1. DR RefSeq; WP_004081830.1; NZ_CP011107.1. DR ProteinModelPortal; P38510; -. DR SMR; P38510; 2-272. DR STRING; 243274.TM1497; -. DR PRIDE; P38510; -. DR EnsemblBacteria; AAD36563; AAD36563; TM_1497. DR GeneID; 897341; -. DR KEGG; tma:TM1497; -. DR PATRIC; 23937952; VBITheMar51294_1514. DR eggNOG; ENOG4105CFD; Bacteria. DR eggNOG; COG0090; LUCA. DR InParanoid; P38510; -. DR KO; K02886; -. DR OMA; NKRTTSM; -. DR OrthoDB; EOG6TR0J1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 4.10.950.10; -; 1. DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR002171; Ribosomal_L2. DR InterPro; IPR005880; Ribosomal_L2_bac/org-type. DR InterPro; IPR022669; Ribosomal_L2_C. DR InterPro; IPR022671; Ribosomal_L2_CS. DR InterPro; IPR014726; Ribosomal_L2_dom3. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR13691; PTHR13691; 1. DR PANTHER; PTHR13691:SF5; PTHR13691:SF5; 1. DR Pfam; PF00181; Ribosomal_L2; 1. DR Pfam; PF03947; Ribosomal_L2_C; 1. DR PIRSF; PIRSF002158; Ribosomal_L2; 1. DR SMART; SM01383; Ribosomal_L2; 1. DR SMART; SM01382; Ribosomal_L2_C; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR01171; rplB_bact; 1. DR PROSITE; PS00467; RIBOSOMAL_L2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 276 50S ribosomal protein L2. FT /FTId=PRO_0000129640. FT CONFLICT 168 168 K -> N (in Ref. 1; CAA79780). FT {ECO:0000305}. FT CONFLICT 203 203 N -> K (in Ref. 1; CAA79780). FT {ECO:0000305}. SQ SEQUENCE 276 AA; 30611 MW; 1ED4DFCE4348E20E CRC64; MGLKRFKPVT PGRRFMVISD FSDITKTEPE KSLLAPLKKT GGRNHHGRVT VRHRGGGHKR RYRIIDFKRY DKAGIPAKVL AIEYDPNRSA RIALLLYADG EKRYILAPKG VNVGDTLMSG PDAEIRPGNA LPLEKIPVGT LVHNVEFTPG KGGQIARAAG TYCQIMAKEG NYALLRMPSG ELRKVHIKCY ATVGVVGNED HKNEVHGKAG RVRWLGRRPH VRGVAMNPVD HPHGGGEGRG KGHHPTSPWG LPTKGYKTRR GKRPSDKFIV RRRNEV // ID RL1_THEMA Reviewed; 233 AA. AC P29393; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 13-APR-2016, entry version 111. DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318}; GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; GN OrderedLocusNames=TM_0455; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1429627; RA Liao D., Dennis P.P.; RT "The organization and expression of essential transcription RT translation component genes in the extremely thermophilic eubacterium RT Thermotoga maritima."; RL J. Biol. Chem. 267:22787-22797(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile CC in the ribosome, and is involved in E site tRNA release. CC {ECO:0000255|HAMAP-Rule:MF_01318}. CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it CC controls the translation of the L11 operon by binding to its mRNA. CC {ECO:0000255|HAMAP-Rule:MF_01318}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01318}. CC -!- SIMILARITY: Belongs to the ribosomal protein L1P family. CC {ECO:0000255|HAMAP-Rule:MF_01318}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11839; CAA77860.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35538.1; -; Genomic_DNA. DR PIR; C44466; R5HG1T. DR RefSeq; NP_228265.1; NC_000853.1. DR RefSeq; WP_004081511.1; NZ_CP011107.1. DR ProteinModelPortal; P29393; -. DR SMR; P29393; 6-229. DR STRING; 243274.TM0455; -. DR EnsemblBacteria; AAD35538; AAD35538; TM_0455. DR GeneID; 897485; -. DR KEGG; tma:TM0455; -. DR PATRIC; 23935805; VBITheMar51294_0461. DR eggNOG; ENOG4105C64; Bacteria. DR eggNOG; COG0081; LUCA. DR InParanoid; P29393; -. DR KO; K02863; -. DR OMA; NEGWTDF; -. DR OrthoDB; EOG6FBX2G; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.190.20; -; 2. DR Gene3D; 3.40.50.790; -; 1. DR HAMAP; MF_01318_B; Ribosomal_L1_B; 1. DR InterPro; IPR005878; Ribosom_L1_bac-type. DR InterPro; IPR002143; Ribosomal_L1. DR InterPro; IPR023674; Ribosomal_L1-like. DR InterPro; IPR028364; Ribosomal_L1/biogenesis. DR InterPro; IPR016094; Ribosomal_L1_2-a/b-sand. DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand. DR InterPro; IPR023673; Ribosomal_L1_CS. DR Pfam; PF00687; Ribosomal_L1; 1. DR PIRSF; PIRSF002155; Ribosomal_L1; 1. DR SUPFAM; SSF56808; SSF56808; 1. DR TIGRFAMs; TIGR01169; rplA_bact; 1. DR PROSITE; PS01199; RIBOSOMAL_L1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repressor; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; Translation regulation; KW tRNA-binding. FT CHAIN 1 233 50S ribosomal protein L1. FT /FTId=PRO_0000125762. SQ SEQUENCE 233 AA; 25932 MW; F115A70F5C193108 CRC64; MPKHSKRYLE ARKLVDRTKY YDLDEAIELV KKTATAKFDE TIELHIQTGI DYRKPEQHIR GTIVLPHGTG KEVKVLVFAK GEKAKEALEA GADYVGAEDL VEKIEKEGFL DFDVAIATPD MMRIIGRLGK ILGPRGLMPS PKSGTVTQEV AEAVKEFKKG RIEVRTDKTG NIHIPVGKRS FDNEKLKENI IAAIKQIMQM KPAGVKGQFI KKVVLASTMG PGIKLNLQSL LKE // ID RL34_THEMA Reviewed; 44 AA. AC P58288; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 1. DT 13-APR-2016, entry version 76. DE RecName: Full=50S ribosomal protein L34; GN Name=rpmH; OrderedLocusNames=TM_1463.1; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Jovanovic M., Gopalan V.; RT "Ribosomal protein L34."; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ribosomal protein L34P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF411294; AAL05866.1; -; Genomic_DNA. DR EMBL; AE000512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_229263.1; NC_000853.1. DR RefSeq; WP_004081758.1; NZ_CP011107.1. DR ProteinModelPortal; P58288; -. DR SMR; P58288; 1-44. DR STRING; 243274.TM1463a; -. DR GeneID; 897518; -. DR KEGG; tma:TM1463a; -. DR eggNOG; ENOG41085QA; Bacteria. DR eggNOG; COG0230; LUCA. DR InParanoid; P58288; -. DR KO; K02914; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00391; Ribosomal_L34; 1. DR InterPro; IPR000271; Ribosomal_L34. DR InterPro; IPR020939; Ribosomal_L34_CS. DR PANTHER; PTHR14503; PTHR14503; 1. DR Pfam; PF00468; Ribosomal_L34; 1. DR ProDom; PD003101; Ribosomal_L34; 1. DR TIGRFAMs; TIGR01030; rpmH_bact; 1. DR PROSITE; PS00784; RIBOSOMAL_L34; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 44 50S ribosomal protein L34. FT /FTId=PRO_0000187490. SQ SEQUENCE 44 AA; 5504 MW; 5521877292526C51 CRC64; MKRTYQPSRR KRKRTHGFLA RKRTPGGRRV LKNRRRKGRW RLTV // ID RL35_THEMA Reviewed; 65 AA. AC Q9X1S7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=50S ribosomal protein L35 {ECO:0000255|HAMAP-Rule:MF_00514}; GN Name=rpmI {ECO:0000255|HAMAP-Rule:MF_00514}; GN OrderedLocusNames=TM_1591; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ribosomal protein L35P family. CC {ECO:0000255|HAMAP-Rule:MF_00514}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36658.1; -; Genomic_DNA. DR PIR; C72233; C72233. DR RefSeq; NP_229391.1; NC_000853.1. DR RefSeq; WP_004082029.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1S7; -. DR STRING; 243274.TM1591; -. DR EnsemblBacteria; AAD36658; AAD36658; TM_1591. DR GeneID; 897526; -. DR KEGG; tma:TM1591; -. DR PATRIC; 23938156; VBITheMar51294_1610. DR eggNOG; ENOG41085B1; Bacteria. DR eggNOG; COG0291; LUCA. DR InParanoid; Q9X1S7; -. DR KO; K02916; -. DR OMA; AWHKTGK; -. DR OrthoDB; EOG651T3B; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00514; Ribosomal_L35; 1. DR InterPro; IPR021137; Ribosomal_L35. DR InterPro; IPR018265; Ribosomal_L35_CS. DR InterPro; IPR001706; Ribosomal_L35_non-mt. DR Pfam; PF01632; Ribosomal_L35p; 1. DR PRINTS; PR00064; RIBOSOMALL35. DR TIGRFAMs; TIGR00001; rpmI_bact; 1. DR PROSITE; PS00936; RIBOSOMAL_L35; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 65 50S ribosomal protein L35. FT /FTId=PRO_0000177441. SQ SEQUENCE 65 AA; 7585 MW; E94E3B9F22FAF44C CRC64; MPKVKTNRSA AKRFRITKNG KIMRNHAYRS HKTGKKRRNA LRALRKKDVV SSADKNRVLR LLGKK // ID RL3_THEMA Reviewed; 207 AA. AC P38515; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325}; GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; GN OrderedLocusNames=TM_1500; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly near the 3'-end of the 23S rRNA, where it nucleates CC assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01325}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L14 and L19. {ECO:0000255|HAMAP-Rule:MF_01325}. CC -!- SIMILARITY: Belongs to the ribosomal protein L3P family. CC {ECO:0000255|HAMAP-Rule:MF_01325}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79777.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36566.1; -; Genomic_DNA. DR PIR; S40188; S40188. DR RefSeq; NP_229300.1; NC_000853.1. DR RefSeq; WP_004081835.1; NZ_CP011107.1. DR ProteinModelPortal; P38515; -. DR SMR; P38515; 1-203. DR STRING; 243274.TM1500; -. DR PRIDE; P38515; -. DR EnsemblBacteria; AAD36566; AAD36566; TM_1500. DR GeneID; 897996; -. DR KEGG; tma:TM1500; -. DR PATRIC; 23937958; VBITheMar51294_1517. DR eggNOG; ENOG4105EEE; Bacteria. DR eggNOG; COG0087; LUCA. DR InParanoid; P38515; -. DR KO; K02906; -. DR OMA; QVWDENN; -. DR OrthoDB; EOG6WDSMH; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01325_B; Ribosomal_L3_B; 1. DR InterPro; IPR000597; Ribosomal_L3. DR InterPro; IPR019927; Ribosomal_L3_bac/org-type. DR InterPro; IPR019926; Ribosomal_L3_CS. DR InterPro; IPR009000; Transl_B-barrel. DR PANTHER; PTHR11229; PTHR11229; 1. DR Pfam; PF00297; Ribosomal_L3; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR TIGRFAMs; TIGR03625; L3_bact; 1. DR PROSITE; PS00474; RIBOSOMAL_L3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 207 50S ribosomal protein L3. FT /FTId=PRO_0000077178. SQ SEQUENCE 207 AA; 22784 MW; 67972CFB6D7AFA9E CRC64; MKMIIGRKIG MTRVFVGNDS VPVTVIKAGP CVVVQKKTVE KDGYNAVQLG FEKAKKVNKP LAGHFKKFGV EPMKILREFR VENPDEYEPG QVIKVDVFEK GEYVDVTGWT KGRGFAGAMK RWGFSGGPKS HGSKFHRELG SVGQHTEPAK IWKGKKMPGR YGNERVTVRN LQVVDIDPEN DLLVVKGGVP GARGGLVLIR SAKAPKK // ID RL24_THEMA Reviewed; 105 AA. AC P38513; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 11-MAY-2016, entry version 105. DE RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326}; GN Name=rplX {ECO:0000255|HAMAP-Rule:MF_01326}; GN OrderedLocusNames=TM_1489; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: One of two assembly initiator proteins, it binds CC directly to the 5'-end of the 23S rRNA, where it nucleates CC assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. CC -!- FUNCTION: One of the proteins that surrounds the polypeptide exit CC tunnel on the outside of the subunit. {ECO:0000255|HAMAP- CC Rule:MF_01326}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01326}. CC -!- SIMILARITY: Belongs to the ribosomal protein L24P family. CC {ECO:0000255|HAMAP-Rule:MF_01326}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79788.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36555.1; -; Genomic_DNA. DR PIR; S40199; S40199. DR RefSeq; NP_229289.1; NC_000853.1. DR RefSeq; WP_004081814.1; NZ_CP011107.1. DR ProteinModelPortal; P38513; -. DR STRING; 243274.TM1489; -. DR EnsemblBacteria; AAD36555; AAD36555; TM_1489. DR GeneID; 897353; -. DR KEGG; tma:TM1489; -. DR PATRIC; 23937936; VBITheMar51294_1506. DR eggNOG; ENOG4105KAR; Bacteria. DR eggNOG; COG0198; LUCA. DR InParanoid; P38513; -. DR KO; K02895; -. DR OMA; VRVGQTQ; -. DR OrthoDB; EOG6FFSDM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.30.30.30; -; 1. DR HAMAP; MF_01326_B; Ribosomal_L24_B; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR003256; Ribosomal_L24. DR InterPro; IPR005825; Ribosomal_L24/26_CS. DR InterPro; IPR008991; Translation_prot_SH3-like. DR Pfam; PF00467; KOW; 1. DR Pfam; PF17136; ribosomal_L24; 1. DR SMART; SM00739; KOW; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR TIGRFAMs; TIGR01079; rplX_bact; 1. DR PROSITE; PS01108; RIBOSOMAL_L24; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 105 50S ribosomal protein L24. FT /FTId=PRO_0000130740. SQ SEQUENCE 105 AA; 12023 MW; E7BCCF1B553C43D8 CRC64; MRIKKGDLVE VISGKDKGKR GKVLRVIPKE NKVIVENVNM VKRHQRPVPQ LREGGIIERE APIYASKVMV VCPACDKRTR VGYRFTEDGK KVRYCKKCGE IIDKD // ID RL28_THEMA Reviewed; 70 AA. AC Q9WY96; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 11-NOV-2015, entry version 79. DE RecName: Full=50S ribosomal protein L28; GN Name=rpmB; OrderedLocusNames=TM_0255; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ribosomal protein L28P family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35344.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35344.1; ALT_INIT; Genomic_DNA. DR PIR; G72399; G72399. DR RefSeq; NP_228069.1; NC_000853.1. DR PDB; 2JZ6; NMR; -; A=1-70. DR PDBsum; 2JZ6; -. DR ProteinModelPortal; Q9WY96; -. DR SMR; Q9WY96; 1-70. DR STRING; 243274.TM0255; -. DR EnsemblBacteria; AAD35344; AAD35344; TM_0255. DR GeneID; 897163; -. DR KEGG; tma:TM0255; -. DR PATRIC; 23935385; VBITheMar51294_0258. DR eggNOG; ENOG4105VB9; Bacteria. DR eggNOG; COG0227; LUCA. DR InParanoid; Q9WY96; -. DR KO; K02902; -. DR OMA; ISHAHNV; -. DR OrthoDB; EOG6W727M; -. DR BioCyc; TMAR243274:GC6P-268-MONOMER; -. DR EvolutionaryTrace; Q9WY96; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 4.10.1160.10; -; 1. DR HAMAP; MF_00373; Ribosomal_L28; 1. DR InterPro; IPR026569; Ribo_L28/L24. DR InterPro; IPR001383; Ribosomal_L28. DR Pfam; PF00830; Ribosomal_L28; 1. DR TIGRFAMs; TIGR00009; L28; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein. FT CHAIN 1 70 50S ribosomal protein L28. FT /FTId=PRO_0000178576. FT TURN 6 8 {ECO:0000244|PDB:2JZ6}. FT STRAND 26 28 {ECO:0000244|PDB:2JZ6}. FT STRAND 33 40 {ECO:0000244|PDB:2JZ6}. FT TURN 41 43 {ECO:0000244|PDB:2JZ6}. FT STRAND 44 51 {ECO:0000244|PDB:2JZ6}. FT HELIX 52 57 {ECO:0000244|PDB:2JZ6}. SQ SEQUENCE 70 AA; 7807 MW; 4AE821FBC0F70B7F CRC64; MAKRCEVCGK APRSGNTVSH SDKKSGRWFR PNLQKVRVVL PDGTIKRMRV CTSCLKSGKV KKYVGQVSEV // ID RL29_THEMA Reviewed; 66 AA. AC P38514; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=50S ribosomal protein L29; GN Name=rpmC; OrderedLocusNames=TM_1492; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ribosomal protein L29P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79785.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36558.1; -; Genomic_DNA. DR PIR; S40196; S40196. DR RefSeq; NP_229292.1; NC_000853.1. DR RefSeq; WP_004081820.1; NZ_CP011107.1. DR PDB; 1R73; NMR; -; A=1-66. DR PDBsum; 1R73; -. DR ProteinModelPortal; P38514; -. DR SMR; P38514; 1-66. DR STRING; 243274.TM1492; -. DR EnsemblBacteria; AAD36558; AAD36558; TM_1492. DR GeneID; 898000; -. DR KEGG; tma:TM1492; -. DR PATRIC; 23937942; VBITheMar51294_1509. DR eggNOG; ENOG41084ME; Bacteria. DR eggNOG; COG0255; LUCA. DR InParanoid; P38514; -. DR KO; K02904; -. DR OMA; LFHLRFQ; -. DR OrthoDB; EOG6VTK8Z; -. DR EvolutionaryTrace; P38514; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.310; -; 1. DR HAMAP; MF_00374; Ribosomal_L29; 1. DR InterPro; IPR001854; Ribosomal_L29. DR InterPro; IPR018254; Ribosomal_L29_CS. DR Pfam; PF00831; Ribosomal_L29; 1. DR SUPFAM; SSF46561; SSF46561; 1. DR TIGRFAMs; TIGR00012; L29; 1. DR PROSITE; PS00579; RIBOSOMAL_L29; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein. FT CHAIN 1 66 50S ribosomal protein L29. FT /FTId=PRO_0000130481. FT HELIX 5 8 {ECO:0000244|PDB:1R73}. FT HELIX 11 34 {ECO:0000244|PDB:1R73}. FT HELIX 40 62 {ECO:0000244|PDB:1R73}. FT TURN 63 65 {ECO:0000244|PDB:1R73}. SQ SEQUENCE 66 AA; 7972 MW; 83488556251ED647 CRC64; MKASELRNYT DEELKNLLEE KKRQLMELRF QLAMGQLKNT SLIKLTKRDI ARIKTILRER ELGIRR // ID RL30_THEMA Reviewed; 67 AA. AC Q9X1J1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=50S ribosomal protein L30 {ECO:0000255|HAMAP-Rule:MF_01371}; GN Name=rpmD {ECO:0000255|HAMAP-Rule:MF_01371}; GN OrderedLocusNames=TM_1482; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01371}. CC -!- SIMILARITY: Belongs to the ribosomal protein L30P family. CC {ECO:0000255|HAMAP-Rule:MF_01371}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36548.1; -; Genomic_DNA. DR PIR; B72248; B72248. DR RefSeq; NP_229282.1; NC_000853.1. DR RefSeq; WP_004081798.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1J1; -. DR STRING; 243274.TM1482; -. DR EnsemblBacteria; AAD36548; AAD36548; TM_1482. DR GeneID; 898648; -. DR KEGG; tma:TM1482; -. DR PATRIC; 23937922; VBITheMar51294_1499. DR eggNOG; ENOG4105VPB; Bacteria. DR eggNOG; COG1841; LUCA. DR InParanoid; Q9X1J1; -. DR KO; K02907; -. DR OMA; MVFKVKH; -. DR OrthoDB; EOG6BGP7P; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1390.20; -; 1. DR HAMAP; MF_01371_B; Ribosomal_L30_B; 1. DR InterPro; IPR005996; Ribosomal_L30_bac-type. DR InterPro; IPR018038; Ribosomal_L30_CS. DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like. DR Pfam; PF00327; Ribosomal_L30; 1. DR PIRSF; PIRSF002211; Ribosomal_L30_bac-type; 1. DR SUPFAM; SSF55129; SSF55129; 1. DR TIGRFAMs; TIGR01308; rpmD_bact; 1. DR PROSITE; PS00634; RIBOSOMAL_L30; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 67 50S ribosomal protein L30. FT /FTId=PRO_0000104615. SQ SEQUENCE 67 AA; 7667 MW; B5B43F2CE43C54BC CRC64; MPKKLKIKLV KSPIGYSWDQ KDTVKRLGLK KLNQVVIKDD LPQIRGMIRK VKHLVEVEEI EEGGSNA // ID RL31_THEMA Reviewed; 71 AA. AC O54311; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 100. DE RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501}; GN Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501}; GN OrderedLocusNames=TM_1684; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10048332; DOI=10.1110/ps.8.2.394; RA Welker C., Bohm G., Schurig H., Jaenicke R.; RT "Cloning, overexpression, purification, and physicochemical RT characterization of a cold shock protein homolog from the RT hyperthermophilic bacterium Thermotoga maritima."; RL Protein Sci. 8:394-403(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00501}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00501}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00501}; CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_00501}. CC -!- SIMILARITY: Belongs to the ribosomal protein L31P family. Type A CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00501}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA72106.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y11219; CAA72106.1; ALT_INIT; mRNA. DR EMBL; AE000512; AAD36751.1; -; Genomic_DNA. DR PIR; F72222; F72222. DR RefSeq; NP_229484.1; NC_000853.1. DR RefSeq; WP_004082200.1; NZ_CP011107.1. DR ProteinModelPortal; O54311; -. DR SMR; O54311; 1-71. DR STRING; 243274.TM1684; -. DR EnsemblBacteria; AAD36751; AAD36751; TM_1684. DR GeneID; 897211; -. DR KEGG; tma:TM1684; -. DR PATRIC; 23938342; VBITheMar51294_1701. DR eggNOG; ENOG41084K4; Bacteria. DR eggNOG; COG0254; LUCA. DR InParanoid; O54311; -. DR KO; K02909; -. DR OMA; YTGQQKA; -. DR OrthoDB; EOG6DVJZM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00501; Ribosomal_L31_1; 1. DR InterPro; IPR002150; Ribosomal_L31. DR InterPro; IPR027491; Ribosomal_L31_A. DR Pfam; PF01197; Ribosomal_L31; 1. DR PRINTS; PR01249; RIBOSOMALL31. DR TIGRFAMs; TIGR00105; L31; 1. DR PROSITE; PS01143; RIBOSOMAL_L31; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc. FT CHAIN 1 71 50S ribosomal protein L31. FT /FTId=PRO_0000173169. FT METAL 16 16 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. FT METAL 18 18 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. FT METAL 36 36 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. FT METAL 39 39 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. SQ SEQUENCE 71 AA; 7986 MW; 39505125D6A61256 CRC64; MKKGIHPEMK LVTVKCACGA EHTFYTTVDN IRIDVCSNCH PFYTSGGKGG VLIVDTEGRV EKFRRKYGDN Y // ID RL4_THEMA Reviewed; 235 AA. AC P38516; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 116. DE RecName: Full=50S ribosomal protein L4; DE AltName: Full=TmaL4; GN Name=rplD; OrderedLocusNames=TM_1499; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP MUTAGENESIS OF LOOPS SPECIFIC TO T.MARITIMA AND NUCLEIC ACID-BINDING RP RESIDUES, AND REPLACEMENT STUDIES IN E.COLI. RX PubMed=12457561; DOI=10.1016/S0300-9084(02)01410-4; RA Worbs M., Wahl M.C., Lindahl L., Zengel J.M.; RT "Comparative anatomy of a regulatory ribosomal protein."; RL Biochimie 84:731-743(2002). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-226. RX PubMed=10698923; DOI=10.1093/emboj/19.5.807; RA Worbs M., Huber R., Wahl M.C.; RT "Crystal structure of ribosomal protein L4 shows RNA-binding sites for RT ribosome incorporation and feedback control of the S10 operon."; RL EMBO J. 19:807-818(2000). CC -!- FUNCTION: One of the primary rRNA binding proteins, this protein CC initially binds near the 5'-end of the 23S rRNA. It is important CC during the early stages of 50S assembly. It makes multiple CC contacts with different domains of the 23S rRNA in the assembled CC 50S subunit and ribosome (By similarity). {ECO:0000250}. CC -!- FUNCTION: This protein only weakly controls expression of the CC E.coli S10 operon. It is incorporated into E.coli ribosomes, CC however it is not as firmly associated as the endogenous protein. CC -!- FUNCTION: Forms part of the polypeptide exit tunnel. CC {ECO:0000250}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. CC -!- DOMAIN: The structure indicates that the N-terminal domain may CC bind to the 23S rRNA, while the C-terminal domain may bind to the CC mRNA, which could then be implicated in transcriptional and CC translational control of the S10 operon. However, it is not known CC if the S10 operon is controlled in this fashion in this organism. CC -!- MISCELLANEOUS: A protein containing 11 mutations, chosen as amino CC acids which probably interact with nucleic acids (K140A, E141Q, CC Q144K, Q147A, S149E, K151delta, K152delta, I155M, P158G, W159E and CC K160L), gained the ability to regulate the E.coli S10 operon, CC suggesting it is now able to mediate contacts of L4 with the S10 CC mRNA leader in E.coli. This mutant protein did not associate any CC better with E.coli ribosomes however, indicating a separation of CC residues interacting with rRNA and mRNA. CC -!- SIMILARITY: Belongs to the ribosomal protein L4P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79778.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36565.1; -; Genomic_DNA. DR PIR; C72250; C72250. DR RefSeq; NP_229299.1; NC_000853.1. DR RefSeq; WP_004081834.1; NZ_CP011107.1. DR PDB; 1DMG; X-ray; 1.70 A; A=2-226. DR PDBsum; 1DMG; -. DR ProteinModelPortal; P38516; -. DR SMR; P38516; 2-226. DR STRING; 243274.TM1499; -. DR EnsemblBacteria; AAD36565; AAD36565; TM_1499. DR GeneID; 897335; -. DR KEGG; tma:TM1499; -. DR PATRIC; 23937956; VBITheMar51294_1516. DR eggNOG; ENOG4106U5A; Bacteria. DR eggNOG; COG0088; LUCA. DR InParanoid; P38516; -. DR KO; K02926; -. DR OMA; VVRSHEH; -. DR OrthoDB; EOG6M0T9G; -. DR EvolutionaryTrace; P38516; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1370.10; -; 1. DR HAMAP; MF_01328_B; Ribosomal_L4_B; 1. DR InterPro; IPR002136; Ribosomal_L4/L1e. DR InterPro; IPR023574; Ribosomal_L4_dom. DR InterPro; IPR013005; Ribosomal_uL4/L1e. DR PANTHER; PTHR10746; PTHR10746; 2. DR Pfam; PF00573; Ribosomal_L4; 1. DR SUPFAM; SSF52166; SSF52166; 1. DR TIGRFAMs; TIGR03953; rplD_bact; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 235 50S ribosomal protein L4. FT /FTId=PRO_0000129301. FT MUTAGEN 140 140 K->A: Able to regulate the E.coli S10 FT operon, but does not improve association FT with E.coli ribosome; when associated FT with E141Q, Q144K, Q147A, S149E, FT K151delta, K152delta, I155M, P158G, W159E FT and K160L. {ECO:0000269|PubMed:12457561}. FT MUTAGEN 163 165 Missing: Little change in either FT regulation of the E.coli S10 operon or FT ribosome assembly. FT {ECO:0000269|PubMed:12457561}. FT MUTAGEN 184 198 Missing: Considerably improves stable FT incorporation into E.coli ribosomes, FT however no change in regulation of the FT E.coli S10 operon. FT {ECO:0000269|PubMed:12457561}. FT CONFLICT 74 74 R -> S (in Ref. 1; CAA79778). FT {ECO:0000305}. FT CONFLICT 128 128 D -> H (in Ref. 1; CAA79778). FT {ECO:0000305}. FT CONFLICT 155 155 I -> M (in Ref. 1; CAA79778). FT {ECO:0000305}. FT STRAND 3 7 {ECO:0000244|PDB:1DMG}. FT STRAND 13 18 {ECO:0000244|PDB:1DMG}. FT HELIX 21 24 {ECO:0000244|PDB:1DMG}. FT HELIX 30 41 {ECO:0000244|PDB:1DMG}. FT HELIX 97 119 {ECO:0000244|PDB:1DMG}. FT STRAND 123 127 {ECO:0000244|PDB:1DMG}. FT HELIX 136 145 {ECO:0000244|PDB:1DMG}. FT STRAND 153 157 {ECO:0000244|PDB:1DMG}. FT HELIX 162 171 {ECO:0000244|PDB:1DMG}. FT STRAND 177 181 {ECO:0000244|PDB:1DMG}. FT HELIX 202 207 {ECO:0000244|PDB:1DMG}. FT STRAND 208 214 {ECO:0000244|PDB:1DMG}. FT HELIX 215 225 {ECO:0000244|PDB:1DMG}. SQ SEQUENCE 235 AA; 26631 MW; 40BC63279019B74E CRC64; MAQVDLLNVK GEKVGTLEIS DFVFNIDPNY DVMWRYVDMQ LSNRRAGTAS TKTRGEVSGG GRKPWPQKHT GRARHGSIRS PIWRHGGVVH GPKPRDWSKK LNKKMKKLAL RSALSVKYRE NKLLVLDDLK LERPKTKSLK EILQNLQLSD KKTLIVLPWK EEGYMNVKLS GRNLPDVKVI IADNPNNSKN GEKAVRIDGL NVFDMLKYDY LVLTRDMVSK IEEVLGNEAG KALTA // ID RL27_THEMA Reviewed; 83 AA. AC Q9X1G7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=50S ribosomal protein L27; GN Name=rpmA; OrderedLocusNames=TM_1456; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ribosomal protein L27P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36524.1; -; Genomic_DNA. DR PIR; A72251; A72251. DR RefSeq; NP_229255.1; NC_000853.1. DR RefSeq; WP_004081742.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1G7; -. DR SMR; Q9X1G7; 1-72. DR STRING; 243274.TM1456; -. DR EnsemblBacteria; AAD36524; AAD36524; TM_1456. DR GeneID; 898020; -. DR KEGG; tma:TM1456; -. DR PATRIC; 23937864; VBITheMar51294_1470. DR eggNOG; ENOG4105K46; Bacteria. DR eggNOG; COG0211; LUCA. DR InParanoid; Q9X1G7; -. DR KO; K02899; -. DR OMA; SYVSVIP; -. DR OrthoDB; EOG6N94H6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00539; Ribosomal_L27; 1. DR InterPro; IPR001684; Ribosomal_L27. DR InterPro; IPR018261; Ribosomal_L27_CS. DR PANTHER; PTHR15893; PTHR15893; 1. DR Pfam; PF01016; Ribosomal_L27; 1. DR PRINTS; PR00063; RIBOSOMALL27. DR ProDom; PD003114; Ribosomal_L27; 1. DR TIGRFAMs; TIGR00062; L27; 1. DR PROSITE; PS00831; RIBOSOMAL_L27; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 83 50S ribosomal protein L27. FT /FTId=PRO_0000181192. SQ SEQUENCE 83 AA; 9221 MW; 4A34E93ECE0463C1 CRC64; MAHKKSGGVA KNGRDSLPKY LGVKVGDGQI VKAGNILVRQ RGTRFYPGKN VGMGRDFTLF ALKDGRVKFE TKNNKKYVSV YEE // ID RLMH_THEMA Reviewed; 151 AA. AC Q9WZU8; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Ribosomal RNA large subunit methyltransferase H {ECO:0000255|HAMAP-Rule:MF_00658}; DE EC=2.1.1.177 {ECO:0000255|HAMAP-Rule:MF_00658}; DE AltName: Full=23S rRNA (pseudouridine1915-N3)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00658}; DE AltName: Full=23S rRNA m3Psi1915 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00658}; DE AltName: Full=rRNA (pseudouridine-N3-)-methyltransferase RlmH {ECO:0000255|HAMAP-Rule:MF_00658}; GN Name=rlmH {ECO:0000255|HAMAP-Rule:MF_00658}; GN OrderedLocusNames=TM_0844; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 2-151. RX PubMed=16460560; DOI=10.1186/1471-2105-7-53; RA von Grotthuss M., Plewczynski D., Ginalski K., Rychlewski L., RA Shakhnovich E.I.; RT "PDB-UF: database of predicted enzymatic functions for unannotated RT protein structures from structural genomics."; RL BMC Bioinformatics 7:53-53(2006). CC -!- FUNCTION: Specifically methylates the pseudouridine at position CC 1915 (m3Psi1915) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00658}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + pseudouridine(1915) CC in 23S rRNA = S-adenosyl-L-homocysteine + N(3)- CC methylpseudouridine(1915) in 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00658}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00658}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00658}. CC -!- SIMILARITY: Belongs to the RNA methyltransferase RlmH family. CC {ECO:0000255|HAMAP-Rule:MF_00658}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35926.1; -; Genomic_DNA. DR PIR; E72326; E72326. DR RefSeq; NP_228653.1; NC_000853.1. DR RefSeq; WP_004080783.1; NZ_CP011107.1. DR PDB; 1O6D; X-ray; 1.66 A; A=2-151. DR PDBsum; 1O6D; -. DR ProteinModelPortal; Q9WZU8; -. DR SMR; Q9WZU8; 1-147. DR STRING; 243274.TM0844; -. DR EnsemblBacteria; AAD35926; AAD35926; TM_0844. DR GeneID; 898515; -. DR KEGG; tma:TM0844; -. DR PATRIC; 23936614; VBITheMar51294_0857. DR eggNOG; ENOG41082VF; Bacteria. DR eggNOG; COG1576; LUCA. DR InParanoid; Q9WZU8; -. DR KO; K00783; -. DR OMA; YRAFMIL; -. DR OrthoDB; EOG6S26HR; -. DR EvolutionaryTrace; Q9WZU8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070038; F:rRNA (pseudouridine-N3-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_00658; 23SrRNA_methyltr_H; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR003742; SPOUT_MeTrfase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF02590; SPOUT_MTase; 1. DR PIRSF; PIRSF004505; MT_bac; 1. DR SUPFAM; SSF75217; SSF75217; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW Reference proteome; rRNA processing; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 151 Ribosomal RNA large subunit FT methyltransferase H. FT /FTId=PRO_0000198200. FT STRAND 2 9 {ECO:0000244|PDB:1O6D}. FT HELIX 13 26 {ECO:0000244|PDB:1O6D}. FT TURN 27 29 {ECO:0000244|PDB:1O6D}. FT STRAND 31 37 {ECO:0000244|PDB:1O6D}. FT HELIX 45 57 {ECO:0000244|PDB:1O6D}. FT STRAND 65 69 {ECO:0000244|PDB:1O6D}. FT STRAND 73 75 {ECO:0000244|PDB:1O6D}. FT HELIX 78 91 {ECO:0000244|PDB:1O6D}. FT STRAND 95 99 {ECO:0000244|PDB:1O6D}. FT HELIX 107 112 {ECO:0000244|PDB:1O6D}. FT STRAND 114 118 {ECO:0000244|PDB:1O6D}. FT HELIX 126 144 {ECO:0000244|PDB:1O6D}. SQ SEQUENCE 151 AA; 17591 MW; 1A08C07987AC5DE4 CRC64; MRVRIAVIGK LDGFIKEGIK HYEKFLRRFC KPEVLEIKRV HRGSIEEIVR KETEDLTNRI LPGSFVMVMD KRGEEVSSEE FADFLKDLEM KGKDITILIG GPYGLNEEIF AKAHRVFSLS KMTFTHGMTV LIVLEQIFRA FKIIHGENYH Y // ID RLMN_THEMA Reviewed; 343 AA. AC Q9X240; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Probable dual-specificity RNA methyltransferase RlmN {ECO:0000255|HAMAP-Rule:MF_01849}; DE EC=2.1.1.192 {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA m2A37 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; GN Name=rlmN {ECO:0000255|HAMAP-Rule:MF_01849}; GN OrderedLocusNames=TM_1715; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in CC 23S rRNA and position 2 of adenine 37 in tRNAs. CC {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(2503) in CC 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L- CC homocysteine + L-methionine + 5'-deoxyadenosine + 2- CC methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin. CC {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(37) in CC tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + CC L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2 CC oxidized [2Fe-2S] ferredoxin. {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01849}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01849}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism CC involving intermediate methylation of a conserved cysteine CC residue. {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. CC {ECO:0000255|HAMAP-Rule:MF_01849}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36781.1; -; Genomic_DNA. DR PIR; G72218; G72218. DR RefSeq; NP_229514.1; NC_000853.1. DR RefSeq; WP_004082231.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X240; -. DR STRING; 243274.TM1715; -. DR EnsemblBacteria; AAD36781; AAD36781; TM_1715. DR GeneID; 897881; -. DR KEGG; tma:TM1715; -. DR PATRIC; 23938406; VBITheMar51294_1733. DR eggNOG; ENOG4105C55; Bacteria. DR eggNOG; COG0820; LUCA. DR InParanoid; Q9X240; -. DR KO; K06941; -. DR OMA; VNNRWSV; -. DR OrthoDB; EOG6DJZ2N; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central. DR GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central. DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01849; RNA_methyltr_RlmN; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR027492; RNA_MTrfase_RlmN. DR InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr. DR InterPro; IPR007197; rSAM. DR PANTHER; PTHR30544; PTHR30544; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF006004; CHP00048; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Disulfide bond; Iron; KW Iron-sulfur; Metal-binding; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1 343 Probable dual-specificity RNA FT methyltransferase RlmN. FT /FTId=PRO_0000350500. FT REGION 158 159 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT REGION 213 215 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT ACT_SITE 91 91 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01849}. FT ACT_SITE 331 331 S-methylcysteine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 111 111 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 115 115 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 118 118 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT BINDING 190 190 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT BINDING 289 289 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT DISULFID 104 331 (transient). {ECO:0000255|HAMAP- FT Rule:MF_01849}. SQ SEQUENCE 343 AA; 39257 MW; 2BECF2EAB9EE986C CRC64; MKNLLDLSYE ELVTEITNLG LERYRADQIL DWVFDKKVNN FDEMTNLSKK HRALLKEHFS ISFLKLLDKK VSRIDGTTKF LWELEDGNTI ESVMLFHPDR ITACISTQVG CPVKCIFCAT GMSGFVRNLT TGEIVAQILS MEKEEKKKIG NVVYMGMGEP LLNYENTIKS IRILNHKKMG NIGIRRITIS TVGIPDRIIQ LAEEGLDVKL ALSLHAPTNF KRDQLVPLNK KYSIEEILNA VKIYQRKTGN RVTIEYVLIR GINDEISDAK KLAEILRNMK VFVNLIPVNP TVEGLRRPSR ERLLTFKRIL LENGIEAEIR REKGTDIEAA CGQLRLKRIK SRS // ID RL33_THEMA Reviewed; 49 AA. AC P35873; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=50S ribosomal protein L33; GN Name=rpmG; OrderedLocusNames=TM_0451; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1429627; RA Liao D., Dennis P.P.; RT "The organization and expression of essential transcription RT translation component genes in the extremely thermophilic eubacterium RT Thermotoga maritima."; RL J. Biol. Chem. 267:22787-22797(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP IDENTIFICATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8112583; DOI=10.1016/0378-1119(94)90537-1; RA Sharp P.M.; RT "Identification of genes encoding ribosomal protein L33 from Bacillus RT licheniformis, Thermus thermophilus and Thermotoga maritima."; RL Gene 139:135-136(1994). CC -!- SIMILARITY: Belongs to the ribosomal protein L33P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11839; CAA77864.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35534.1; -; Genomic_DNA. DR PIR; D72375; D72375. DR RefSeq; NP_228261.1; NC_000853.1. DR RefSeq; WP_004081515.1; NZ_CP011107.1. DR ProteinModelPortal; P35873; -. DR SMR; P35873; 2-49. DR STRING; 243274.TM0451; -. DR EnsemblBacteria; AAD35534; AAD35534; TM_0451. DR GeneID; 897475; -. DR KEGG; tma:TM0451; -. DR PATRIC; 23935795; VBITheMar51294_0457. DR eggNOG; ENOG41086IP; Bacteria. DR eggNOG; COG0267; LUCA. DR InParanoid; P35873; -. DR KO; K02913; -. DR OrthoDB; EOG60KNBM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00294; Ribosomal_L33; 1. DR InterPro; IPR001705; Ribosomal_L33. DR InterPro; IPR018264; Ribosomal_L33_CS. DR InterPro; IPR011332; Ribosomal_zn-bd. DR Pfam; PF00471; Ribosomal_L33; 1. DR SUPFAM; SSF57829; SSF57829; 1. DR TIGRFAMs; TIGR01023; rpmG_bact; 1. DR PROSITE; PS00582; RIBOSOMAL_L33; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 49 50S ribosomal protein L33. FT /FTId=PRO_0000170256. SQ SEQUENCE 49 AA; 5744 MW; 0074804C6FF3ABE2 CRC64; MRVKVALKCS QCGNKNYYTT RNKDKRAKLE LRKYCPKCNA HTIHTETKA // ID RL7_THEMA Reviewed; 128 AA. AC P29396; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 13-APR-2016, entry version 123. DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368}; GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; GN OrderedLocusNames=TM_0457; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1429627; RA Liao D., Dennis P.P.; RT "The organization and expression of essential transcription RT translation component genes in the extremely thermophilic eubacterium RT Thermotoga maritima."; RL J. Biol. Chem. 267:22787-22797(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8177738; DOI=10.1093/nar/21.21.4904; RA Palm P., Schleper C., Arnold-Ammer I., Holz I., Meier T., RA Lottspeich F., Zillig W.; RT "The DNA-dependent RNA-polymerase of Thermotoga maritima; RT characterisation of the enzyme and the DNA-sequence of the genes for RT the large subunits."; RL Nucleic Acids Res. 21:4904-4908(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [4] RP SUBUNIT, STOICHIOMETRY, AND MASS SPECTROMETRY. RX PubMed=15923259; DOI=10.1073/pnas.0502193102; RA Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., RA Nierhaus K.H., Robinson C.V.; RT "Heptameric (L12)6/L10 rather than canonical pentameric complexes are RT found by tandem MS of intact ribosomes from thermophilic bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10637222; DOI=10.1093/emboj/19.2.174; RA Wahl M.C., Bourenkov G.P., Bartunik H.D., Huber R.; RT "Flexibility, conformational diversity and two dimerization modes in RT complexes of ribosomal protein L12."; RL EMBO J. 19:174-186(2000). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-30, INTERACTION WITH L10 RP (RPLJ), AND SUBUNIT. RX PubMed=15989950; DOI=10.1016/j.cell.2005.04.015; RA Diaconu M., Kothe U., Schlunzen F., Fischer N., Harms J.M., RA Tonevitsky A.G., Stark H., Rodnina M.V., Wahl M.C.; RT "Structural basis for the function of the ribosomal L7/12 stalk in RT factor binding and GTPase activation."; RL Cell 121:991-1004(2005). CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the CC ribosome interact with GTP-bound translation factors. Is thus CC essential for accurate translation. CC -!- SUBUNIT: Homodimer. Part of the 50S ribosomal subunit; present in CC 6 copies per ribosome. Forms part of the ribosomal stalk which CC helps the ribosome interact with GTP-bound translation factors. CC Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms CC an elongated spine to which 3 L12 dimers bind in a sequential CC fashion. {ECO:0000269|PubMed:15923259, CC ECO:0000269|PubMed:15989950}. CC -!- MASS SPECTROMETRY: Mass=101376; Mass_error=8; Method=Electrospray; CC Range=2-128; Note=Isolated L10(L12)6.; CC Evidence={ECO:0000269|PubMed:15923259}; CC -!- MASS SPECTROMETRY: Mass=13477; Mass_error=2; Method=Electrospray; CC Range=2-128; Evidence={ECO:0000269|PubMed:15923259}; CC -!- SIMILARITY: Belongs to the ribosomal protein L7/L12P family. CC {ECO:0000255|HAMAP-Rule:MF_00368}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35540.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11839; CAA77862.1; -; Genomic_DNA. DR EMBL; X72695; CAA51245.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35540.1; ALT_INIT; Genomic_DNA. DR PIR; E44466; R7HG12. DR RefSeq; NP_228267.1; NC_000853.1. DR RefSeq; WP_004081509.1; NZ_CP011107.1. DR PDB; 1DD3; X-ray; 2.00 A; A/B=1-128, C/D=1-32. DR PDB; 1DD4; X-ray; 2.40 A; A/B=1-128, C/D=1-40. DR PDB; 1L1U; Model; -; 3/4=1-128. DR PDB; 1ZAV; X-ray; 1.90 A; U/V/W/X/Y/Z=1-30. DR PDB; 1ZAW; X-ray; 2.30 A; U/V/W/X/Y/Z=1-30. DR PDB; 1ZAX; X-ray; 2.10 A; U/V/W/X/Y/Z=1-30. DR PDBsum; 1DD3; -. DR PDBsum; 1DD4; -. DR PDBsum; 1L1U; -. DR PDBsum; 1ZAV; -. DR PDBsum; 1ZAW; -. DR PDBsum; 1ZAX; -. DR ProteinModelPortal; P29396; -. DR SMR; P29396; 1-128. DR STRING; 243274.TM0457; -. DR EnsemblBacteria; AAD35540; AAD35540; TM_0457. DR GeneID; 897487; -. DR KEGG; tma:TM0457; -. DR PATRIC; 23935811; VBITheMar51294_0464. DR eggNOG; ENOG4105KBC; Bacteria. DR eggNOG; COG0222; LUCA. DR InParanoid; P29396; -. DR KO; K02935; -. DR OMA; LEDKWGV; -. DR OrthoDB; EOG6WMJ69; -. DR BioCyc; TMAR243274:GC6P-477-MONOMER; -. DR EvolutionaryTrace; P29396; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.1390.10; -; 1. DR HAMAP; MF_00368; Ribosomal_L7_L12; 1. DR InterPro; IPR000206; Ribosomal_L7/12. DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like. DR InterPro; IPR013823; Ribosomal_L7/L12_C. DR InterPro; IPR008932; Ribosomal_L7/L12_oligo. DR Pfam; PF00542; Ribosomal_L12; 1. DR Pfam; PF16320; Ribosomal_L12_N; 1. DR ProDom; PD001326; Ribosomal_L7/L12_C; 1. DR SUPFAM; SSF48300; SSF48300; 1. DR SUPFAM; SSF54736; SSF54736; 1. DR TIGRFAMs; TIGR00855; L12; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein. FT CHAIN 1 128 50S ribosomal protein L7/L12. FT /FTId=PRO_0000157596. FT HELIX 3 12 {ECO:0000244|PDB:1ZAV}. FT HELIX 15 28 {ECO:0000244|PDB:1ZAV}. FT HELIX 31 54 {ECO:0000244|PDB:1DD3}. FT STRAND 57 65 {ECO:0000244|PDB:1DD3}. FT HELIX 70 81 {ECO:0000244|PDB:1DD3}. FT HELIX 85 92 {ECO:0000244|PDB:1DD3}. FT TURN 93 96 {ECO:0000244|PDB:1DD3}. FT STRAND 101 106 {ECO:0000244|PDB:1DD3}. FT HELIX 108 120 {ECO:0000244|PDB:1DD3}. FT STRAND 124 128 {ECO:0000244|PDB:1DD3}. SQ SEQUENCE 128 AA; 13458 MW; FCA849CFE85906BE CRC64; MTIDEIIEAI EKLTVSELAE LVKKLEDKFG VTAAAPVAVA AAPVAGAAAG AAQEEKTEFD VVLKSFGQNK IQVIKVVREI TGLGLKEAKD LVEKAGSPDA VIKSGVSKEE AEEIKKKLEE AGAEVELK // ID RL36_THEMA Reviewed; 38 AA. AC Q9X1I6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=50S ribosomal protein L36 {ECO:0000255|HAMAP-Rule:MF_00251}; GN Name=rpmJ {ECO:0000255|HAMAP-Rule:MF_00251}; GN OrderedLocusNames=TM_1476; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ribosomal protein L36P family. CC {ECO:0000255|HAMAP-Rule:MF_00251}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36568.1; -; Genomic_DNA. DR PIR; E72247; E72247. DR RefSeq; NP_229276.1; NC_000853.1. DR RefSeq; WP_004081787.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1I6; -. DR SMR; Q9X1I6; 1-38. DR STRING; 243274.TM1476; -. DR EnsemblBacteria; AAD36568; AAD36568; TM_1476. DR GeneID; 898009; -. DR KEGG; tma:TM1476; -. DR PATRIC; 23937908; VBITheMar51294_1492. DR eggNOG; ENOG41086MH; Bacteria. DR eggNOG; ENOG410ZYFH; LUCA. DR InParanoid; Q9X1I6; -. DR KO; K02919; -. DR OrthoDB; EOG676ZC2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00251; Ribosomal_L36; 1. DR InterPro; IPR000473; Ribosomal_L36. DR PANTHER; PTHR18804; PTHR18804; 1. DR Pfam; PF00444; Ribosomal_L36; 1. DR SUPFAM; SSF57840; SSF57840; 1. DR TIGRFAMs; TIGR01022; rpmJ_bact; 1. DR PROSITE; PS00828; RIBOSOMAL_L36; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 38 50S ribosomal protein L36. FT /FTId=PRO_0000126282. SQ SEQUENCE 38 AA; 4564 MW; 263FD7D59798800B CRC64; MKVQASVKKR CEHCKIIRRK KRVYVICKVN PKHNQKQG // ID RNC_THEMA Reviewed; 240 AA. AC Q9X0I6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 119. DE RecName: Full=Ribonuclease 3; DE EC=3.1.26.3; DE AltName: Full=Ribonuclease III; DE Short=RNase III; GN Name=rnc; OrderedLocusNames=TM_1102; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION AS AN RNASE, FUNCTION AS AN ENDONUCLEASE, BIOPHYSICOCHEMICAL RP PROPERTIES, COFACTOR, AND RRNA-BINDING. RX PubMed=20677811; DOI=10.1021/bi100930u; RA Nathania L., Nicholson A.W.; RT "Thermotoga maritima ribonuclease III. Characterization of RT thermostable biochemical behavior and analysis of conserved base pairs RT that function as reactivity epitopes for the Thermotoga 23S rRNA RT precursor."; RL Biochemistry 49:7164-7178(2010). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT. RG Joint center for structural genomics (JCSG); RT "Crystal structure of ribonuclease III (TM1102) from Thermotoga RT maritima at 2.0 A resolution."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Digests double-stranded RNA. Involved in the processing CC of primary rRNA transcript to yield the immediate precursors to CC the large and small rRNAs (23S and 16S). Also processes some CC mRNAs, and tRNAs when they are encoded in the rRNA operon. CC Probably processes pre-crRNA and tracrRNA of type II CRISPR loci CC if present in the organism. {ECO:0000269|PubMed:20677811}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:20677811}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.0. {ECO:0000269|PubMed:20677811}; CC Temperature dependence: CC Optimum temperature is 40-70 degrees Celsius. CC {ECO:0000269|PubMed:20677811}; CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.3}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 RNase III domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36178.1; -; Genomic_DNA. DR PIR; H72294; H72294. DR RefSeq; NP_228908.1; NC_000853.1. DR RefSeq; WP_004080335.1; NZ_CP011107.1. DR PDB; 1O0W; X-ray; 2.00 A; A/B=1-240. DR PDBsum; 1O0W; -. DR ProteinModelPortal; Q9X0I6; -. DR SMR; Q9X0I6; 1-237. DR STRING; 243274.TM1102; -. DR EnsemblBacteria; AAD36178; AAD36178; TM_1102. DR GeneID; 898663; -. DR KEGG; tma:TM1102; -. DR PATRIC; 23937137; VBITheMar51294_1117. DR eggNOG; ENOG4108ZBM; Bacteria. DR eggNOG; COG0571; LUCA. DR InParanoid; Q9X0I6; -. DR KO; K03685; -. DR OMA; NSYANER; -. DR OrthoDB; EOG6T1WVS; -. DR BRENDA; 3.1.26.3; 6331. DR EvolutionaryTrace; Q9X0I6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-HAMAP. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central. DR GO; GO:0006396; P:RNA processing; IBA:GO_Central. DR GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR Gene3D; 1.10.1520.10; -; 1. DR Gene3D; 3.30.160.20; -; 1. DR HAMAP; MF_00104; RNase_III; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR011907; RNase_III. DR InterPro; IPR000999; RNase_III_dom. DR Pfam; PF00035; dsrm; 1. DR Pfam; PF14622; Ribonucleas_3_3; 1. DR SMART; SM00358; DSRM; 1. DR SMART; SM00535; RIBOc; 1. DR SUPFAM; SSF69065; SSF69065; 1. DR TIGRFAMs; TIGR02191; RNaseIII; 1. DR PROSITE; PS50137; DS_RBD; 1. DR PROSITE; PS00517; RNASE_3_1; 1. DR PROSITE; PS50142; RNASE_3_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Endonuclease; Hydrolase; KW Magnesium; Metal-binding; mRNA processing; Nuclease; KW Reference proteome; RNA-binding; rRNA processing; rRNA-binding; KW tRNA processing. FT CHAIN 1 240 Ribonuclease 3. FT /FTId=PRO_0000180448. FT DOMAIN 9 141 RNase III. FT DOMAIN 168 237 DRBM. FT ACT_SITE 58 58 {ECO:0000255}. FT ACT_SITE 130 130 {ECO:0000250}. FT METAL 54 54 Magnesium. {ECO:0000250}. FT METAL 127 127 Magnesium. {ECO:0000250}. FT METAL 130 130 Magnesium. {ECO:0000250}. FT HELIX 3 16 {ECO:0000244|PDB:1O0W}. FT HELIX 23 30 {ECO:0000244|PDB:1O0W}. FT HELIX 33 41 {ECO:0000244|PDB:1O0W}. FT HELIX 51 72 {ECO:0000244|PDB:1O0W}. FT HELIX 78 88 {ECO:0000244|PDB:1O0W}. FT HELIX 91 100 {ECO:0000244|PDB:1O0W}. FT HELIX 103 106 {ECO:0000244|PDB:1O0W}. FT HELIX 111 115 {ECO:0000244|PDB:1O0W}. FT HELIX 118 120 {ECO:0000244|PDB:1O0W}. FT HELIX 122 140 {ECO:0000244|PDB:1O0W}. FT HELIX 142 161 {ECO:0000244|PDB:1O0W}. FT HELIX 169 181 {ECO:0000244|PDB:1O0W}. FT STRAND 186 193 {ECO:0000244|PDB:1O0W}. FT STRAND 200 207 {ECO:0000244|PDB:1O0W}. FT STRAND 210 219 {ECO:0000244|PDB:1O0W}. FT HELIX 220 235 {ECO:0000244|PDB:1O0W}. SQ SEQUENCE 240 AA; 27530 MW; 94330E8898D48A0D CRC64; MNESERKIVE EFQKETGINF KNEELLFRAL CHSSYANEQN QAGRKDVESN EKLEFLGDAV LELFVCEILY KKYPEAEVGD LARVKSAAAS EEVLAMVSRK MNLGKFLFLG KGEEKTGGRD RDSILADAFE ALLAAIYLDQ GYEKIKELFE QEFEFYIEKI MKGEMLFDYK TALQEIVQSE HKVPPEYILV RTEKNDGDRI FVVEVRVNGK TIATGKGRTK KEAEKEAARI AYEKLLKERS // ID RL5_THEMA Reviewed; 184 AA. AC P38517; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 106. DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333}; GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; GN OrderedLocusNames=TM_1488; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP SEQUENCE REVISION TO 158. RA Sanangelantoni A.M.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: This is 1 of the proteins that binds and probably CC mediates the attachment of the 5S RNA into the large ribosomal CC subunit, where it forms part of the central protuberance. In the CC 70S ribosome it contacts protein S13 of the 30S subunit (bridge CC B1b), connecting the 2 subunits; this bridge is implicated in CC subunit movement. Contacts the P site tRNA; the 5S rRNA and some CC of its associated proteins might help stabilize positioning of CC ribosome-bound tRNAs. {ECO:0000255|HAMAP-Rule:MF_01333}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site CC tRNA. Forms a bridge to the 30S subunit in the 70S ribosome. CC {ECO:0000255|HAMAP-Rule:MF_01333}. CC -!- SIMILARITY: Belongs to the ribosomal protein L5P family. CC {ECO:0000255|HAMAP-Rule:MF_01333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79789.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36554.1; -; Genomic_DNA. DR PIR; H72248; H72248. DR RefSeq; NP_229288.1; NC_000853.1. DR RefSeq; WP_004081811.1; NZ_CP011107.1. DR ProteinModelPortal; P38517; -. DR SMR; P38517; 6-183. DR STRING; 243274.TM1488; -. DR EnsemblBacteria; AAD36554; AAD36554; TM_1488. DR GeneID; 898002; -. DR KEGG; tma:TM1488; -. DR PATRIC; 23937934; VBITheMar51294_1505. DR eggNOG; ENOG4105CW6; Bacteria. DR eggNOG; COG0094; LUCA. DR InParanoid; P38517; -. DR KO; K02931; -. DR OMA; EQVMFHE; -. DR OrthoDB; EOG6M9F1R; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.1440.10; -; 1. DR HAMAP; MF_01333_B; Ribosomal_L5_B; 1. DR InterPro; IPR002132; Ribosomal_L5. DR InterPro; IPR020930; Ribosomal_L5_bac-type. DR InterPro; IPR031309; Ribosomal_L5_C. DR InterPro; IPR020929; Ribosomal_L5_CS. DR InterPro; IPR022803; Ribosomal_L5_domain. DR InterPro; IPR031310; Ribosomal_L5_N. DR Pfam; PF00281; Ribosomal_L5; 1. DR Pfam; PF00673; Ribosomal_L5_C; 1. DR PIRSF; PIRSF002161; Ribosomal_L5; 1. DR SUPFAM; SSF55282; SSF55282; 1. DR PROSITE; PS00358; RIBOSOMAL_L5; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 184 50S ribosomal protein L5. FT /FTId=PRO_0000125012. FT CONFLICT 24 24 F -> L (in Ref. 1; CAA79789). FT {ECO:0000305}. FT CONFLICT 102 102 N -> S (in Ref. 1; CAA79789). FT {ECO:0000305}. FT CONFLICT 146 146 N -> D (in Ref. 1; CAA79789). FT {ECO:0000305}. FT CONFLICT 170 170 A -> V (in Ref. 1; CAA79789). FT {ECO:0000305}. SQ SEQUENCE 184 AA; 21306 MW; 52702CB5A4513989 CRC64; MRYEYVPLKD QYEKEIVPAL MKEFNYKNIH QVPKLVKIVI NMGIGEGSRN YDLIERHANE LAKITGQKPI VTRARKSISN FKIRKGMPIG LKVTLRGARM YNFLYKLINI VLPKVRDFRG LDPNSFDGRG NYSFGLSEQL VFPELNPDEV RRIQGMDITI VTTAKTDQEA RRLLELFGMP FKRG // ID RL6_THEMA Reviewed; 184 AA. AC Q9ZAE4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 102. DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365}; GN Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; GN OrderedLocusNames=TM_1485; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: This protein binds to the 23S rRNA, and is important in CC its secondary structure. It is located near the subunit interface CC in the base of the L7/L12 stalk, and near the tRNA binding site of CC the peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01365}. CC -!- SIMILARITY: Belongs to the ribosomal protein L6P family. CC {ECO:0000255|HAMAP-Rule:MF_01365}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79792.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36551.1; -; Genomic_DNA. DR PIR; E72248; E72248. DR RefSeq; NP_229285.1; NC_000853.1. DR RefSeq; WP_004081804.1; NZ_CP011107.1. DR ProteinModelPortal; Q9ZAE4; -. DR SMR; Q9ZAE4; 8-177. DR STRING; 243274.TM1485; -. DR EnsemblBacteria; AAD36551; AAD36551; TM_1485. DR GeneID; 897340; -. DR KEGG; tma:TM1485; -. DR PATRIC; 23937928; VBITheMar51294_1502. DR eggNOG; ENOG4108R5J; Bacteria. DR eggNOG; COG0097; LUCA. DR InParanoid; Q9ZAE4; -. DR KO; K02933; -. DR OMA; TIGYSHP; -. DR OrthoDB; EOG67DPRD; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR Gene3D; 3.90.930.12; -; 2. DR HAMAP; MF_01365_B; Ribosomal_L6_B; 1. DR InterPro; IPR000702; Ribosomal_L6. DR InterPro; IPR020040; Ribosomal_L6_a/b-dom. DR InterPro; IPR019906; Ribosomal_L6_bac-type. DR PANTHER; PTHR11655; PTHR11655; 1. DR Pfam; PF00347; Ribosomal_L6; 2. DR PIRSF; PIRSF002162; Ribosomal_L6; 1. DR PRINTS; PR00059; RIBOSOMALL6. DR SUPFAM; SSF56053; SSF56053; 2. DR TIGRFAMs; TIGR03654; L6_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 184 50S ribosomal protein L6. FT /FTId=PRO_0000131071. FT CONFLICT 50 50 V -> G (in Ref. 1; CAA79792). FT {ECO:0000305}. SQ SEQUENCE 184 AA; 20786 MW; C4BCA1ED9F4CF865 CRC64; MSRLAKKPIV LPQGVTVEIK DNVVKVKGPK GELSQEFLPY VKIEVEGNEV WVRPNEEQII RKSDWRKVKM FQGTYWSLIR NMVVGVTEGY KKELEIVGIG YRAQLQGNTL VMNLGYAHPV VYEIPSDVKI EVPAPNRIIV SGIDKQRVGQ VAAEIRAFRP PNVYTGKGIR YVGEVVRQKE GKKA // ID RNY_THEMA Reviewed; 508 AA. AC Q9X2H2; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Ribonuclease Y {ECO:0000255|HAMAP-Rule:MF_00335}; DE Short=RNase Y {ECO:0000255|HAMAP-Rule:MF_00335}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00335}; GN Name=rny {ECO:0000255|HAMAP-Rule:MF_00335}; OrderedLocusNames=TM_1857; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Endoribonuclease that initiates mRNA decay. CC {ECO:0000255|HAMAP-Rule:MF_00335}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00335}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00335}. CC -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000255|HAMAP- CC Rule:MF_00335}. CC -!- SIMILARITY: Contains 1 HD domain. {ECO:0000255|HAMAP- CC Rule:MF_00335}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|HAMAP- CC Rule:MF_00335}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36919.1; -; Genomic_DNA. DR PIR; B72201; B72201. DR RefSeq; NP_229653.1; NC_000853.1. DR RefSeq; WP_004082408.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2H2; -. DR STRING; 243274.TM1857; -. DR EnsemblBacteria; AAD36919; AAD36919; TM_1857. DR GeneID; 897145; -. DR KEGG; tma:TM1857; -. DR KEGG; tmi:THEMA_04885; -. DR KEGG; tmw:THMA_1907; -. DR PATRIC; 23938703; VBITheMar51294_1878. DR eggNOG; ENOG4105E4Y; Bacteria. DR eggNOG; COG1418; LUCA. DR InParanoid; Q9X2H2; -. DR KO; K18682; -. DR OMA; YYARGQA; -. DR OrthoDB; EOG6QCD98; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3210.10; -; 1. DR Gene3D; 3.30.1370.10; -; 1. DR HAMAP; MF_00335; RNase_Y; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR006675; HDIG_dom. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR017705; Ribonuclease_Y. DR InterPro; IPR022711; RNase_Y_N. DR Pfam; PF12072; DUF3552; 1. DR Pfam; PF01966; HD; 1. DR Pfam; PF00013; KH_1; 1. DR SMART; SM00471; HDc; 1. DR SMART; SM00322; KH; 1. DR SUPFAM; SSF54791; SSF54791; 1. DR TIGRFAMs; TIGR00277; HDIG; 1. DR TIGRFAMs; TIGR03319; RNase_Y; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Endonuclease; Hydrolase; Membrane; KW Nuclease; Reference proteome; RNA-binding; Transmembrane; KW Transmembrane helix. FT CHAIN 1 508 Ribonuclease Y. FT /FTId=PRO_0000163803. FT TRANSMEM 1 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00335}. FT DOMAIN 198 283 KH. {ECO:0000255|HAMAP-Rule:MF_00335}. FT DOMAIN 324 416 HD. {ECO:0000255|HAMAP-Rule:MF_00335}. SQ SEQUENCE 508 AA; 58171 MW; 0C093F96E13B9E4B CRC64; MMLWYIVAGA GGLLIGYLIA NYQINQKLRK AKEDAQTIIE KAEKEANEIK KKAIIEGREE VHRLREEFEK ERSRREEELR ALEERLLKRE ELLTRKEENL EKREQQVEEL KANLEEKMRE VEEKEKRIDE ELKRLAGMTV EEARELILEE ARQRYEHDLA KLYKEMKEQV EEEAEKEAKK VIAFAVQRYA PDYVGEITVS TVSLPSDDMK GRIIGREGRN IRTFEKITGV DLIIDDTPEV VVLSCFNPLR REIARITLEK LVADGRIHPA RIEEMYEKAK QEVEKAIKEA GQEATFKAGV MGLHPELVKL LGKLKYRTSY GQNVLNHSIE VALLAGYMAS ELGLNADKAR RGGLLHDIGK AVDQELEGSH TTIGAELARR YGEKEDIINM ILSHHGEEEP MTPEAVLVAA ADALSAARPG ARRESLENYI KRLMKLEEIA KSFKYVEKAY AIQAGREIRV IVEPDKVDDA LAEKLAYDIS KKIEEELEYP GVLKVVVIRE KRSVAYAK // ID RL9_THEMA Reviewed; 149 AA. AC Q9WZW7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503}; GN Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; GN OrderedLocusNames=TM_0863; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00503}. CC -!- SIMILARITY: Belongs to the ribosomal protein L9P family. CC {ECO:0000255|HAMAP-Rule:MF_00503}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35945.1; -; Genomic_DNA. DR PIR; B72322; B72322. DR RefSeq; NP_228672.1; NC_000853.1. DR RefSeq; WP_004080743.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZW7; -. DR STRING; 243274.TM0863; -. DR EnsemblBacteria; AAD35945; AAD35945; TM_0863. DR GeneID; 898536; -. DR KEGG; tma:TM0863; -. DR PATRIC; 23936654; VBITheMar51294_0876. DR eggNOG; ENOG4105K9Q; Bacteria. DR eggNOG; COG0359; LUCA. DR InParanoid; Q9WZW7; -. DR KO; K02939; -. DR OMA; GSINNQE; -. DR OrthoDB; EOG6D8BH0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.10.430.100; -; 1. DR Gene3D; 3.40.5.10; -; 1. DR HAMAP; MF_00503; Ribosomal_L9; 1. DR InterPro; IPR000244; Ribosomal_L9. DR InterPro; IPR009027; Ribosomal_L9/RNase_H1_N. DR InterPro; IPR020594; Ribosomal_L9_bac/chp. DR InterPro; IPR020069; Ribosomal_L9_C. DR InterPro; IPR020070; Ribosomal_L9_N. DR PANTHER; PTHR21368; PTHR21368; 1. DR Pfam; PF03948; Ribosomal_L9_C; 1. DR Pfam; PF01281; Ribosomal_L9_N; 1. DR SUPFAM; SSF55653; SSF55653; 1. DR SUPFAM; SSF55658; SSF55658; 1. DR TIGRFAMs; TIGR00158; L9; 1. DR PROSITE; PS00651; RIBOSOMAL_L9; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 149 50S ribosomal protein L9. FT /FTId=PRO_0000176695. SQ SEQUENCE 149 AA; 17062 MW; EA24E1613B81FFC1 CRC64; MKVILLRDVP KIGKKGEIKE VSDGYARNYL IPRGFAKEYT EGLERAIKHE KEIEKRKKER EREESEKILK ELKKRTHVVK VKAGEGGKIF GAVTAATVAE EISKTTGLKL DKRWFKLDKP IKELGEYSLE VSLPGGVKDT IKIRVEREE // ID RNH2_THEMA Reviewed; 238 AA. AC Q9X017; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Ribonuclease HII; DE Short=RNase HII; DE EC=3.1.26.4; GN Name=rnhB; OrderedLocusNames=TM_0915; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA- CC DNA hybrids. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Manganese or magnesium. Binds 1 divalent metal ion per CC monomer in the absence of substrate. May bind a second metal ion CC after substrate binding. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35996.1; -; Genomic_DNA. DR PIR; B72320; B72320. DR RefSeq; NP_228723.1; NC_000853.1. DR RefSeq; WP_004080647.1; NZ_CP011107.1. DR PDB; 2ETJ; X-ray; 1.74 A; A=1-238. DR PDB; 3O3F; X-ray; 2.00 A; A=2-223. DR PDB; 3O3G; X-ray; 2.10 A; A=2-223. DR PDB; 3O3H; X-ray; 2.80 A; A=2-223. DR PDB; 4HHT; X-ray; 3.10 A; A=2-238. DR PDBsum; 2ETJ; -. DR PDBsum; 3O3F; -. DR PDBsum; 3O3G; -. DR PDBsum; 3O3H; -. DR PDBsum; 4HHT; -. DR ProteinModelPortal; Q9X017; -. DR SMR; Q9X017; 1-221. DR STRING; 243274.TM0915; -. DR EnsemblBacteria; AAD35996; AAD35996; TM_0915. DR GeneID; 898589; -. DR KEGG; tma:TM0915; -. DR PATRIC; 23936761; VBITheMar51294_0929. DR eggNOG; ENOG4108UH2; Bacteria. DR eggNOG; COG0164; LUCA. DR InParanoid; Q9X017; -. DR KO; K03470; -. DR OMA; GFASHKG; -. DR OrthoDB; EOG6BKJC8; -. DR BRENDA; 3.1.26.4; 6331. DR EvolutionaryTrace; Q9X017; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IBA:GO_Central. DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central. DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GOC. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00052_B; RNase_HII_B; 1. DR InterPro; IPR022898; RNase_HII. DR InterPro; IPR001352; RNase_HII/HIII. DR InterPro; IPR024567; RNase_HII/HIII_dom. DR InterPro; IPR012337; RNaseH-like_dom. DR PANTHER; PTHR10954; PTHR10954; 1. DR Pfam; PF01351; RNase_HII; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Endonuclease; Hydrolase; KW Manganese; Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 238 Ribonuclease HII. FT /FTId=PRO_0000111643. FT METAL 18 18 Divalent metal cation. {ECO:0000250}. FT METAL 19 19 Divalent metal cation. {ECO:0000250}. FT METAL 107 107 Divalent metal cation. {ECO:0000250}. FT HELIX 3 7 {ECO:0000244|PDB:2ETJ}. FT TURN 8 10 {ECO:0000244|PDB:2ETJ}. FT STRAND 11 20 {ECO:0000244|PDB:2ETJ}. FT STRAND 25 27 {ECO:0000244|PDB:2ETJ}. FT STRAND 29 36 {ECO:0000244|PDB:2ETJ}. FT TURN 41 44 {ECO:0000244|PDB:4HHT}. FT HELIX 46 48 {ECO:0000244|PDB:3O3F}. FT HELIX 53 64 {ECO:0000244|PDB:2ETJ}. FT STRAND 65 72 {ECO:0000244|PDB:2ETJ}. FT HELIX 74 80 {ECO:0000244|PDB:2ETJ}. FT HELIX 82 96 {ECO:0000244|PDB:2ETJ}. FT STRAND 97 99 {ECO:0000244|PDB:2ETJ}. FT STRAND 102 110 {ECO:0000244|PDB:2ETJ}. FT STRAND 117 120 {ECO:0000244|PDB:2ETJ}. FT HELIX 123 126 {ECO:0000244|PDB:2ETJ}. FT HELIX 128 151 {ECO:0000244|PDB:2ETJ}. FT HELIX 157 160 {ECO:0000244|PDB:2ETJ}. FT HELIX 166 175 {ECO:0000244|PDB:2ETJ}. FT HELIX 186 189 {ECO:0000244|PDB:2ETJ}. FT HELIX 194 202 {ECO:0000244|PDB:2ETJ}. FT HELIX 208 219 {ECO:0000244|PDB:2ETJ}. FT TURN 220 222 {ECO:0000244|PDB:3O3F}. SQ SEQUENCE 238 AA; 26630 MW; 2A0C0156954AE923 CRC64; MGIDELYKKE FGIVAGVDEA GRGCLAGPVV AAAVVLEKEI EGINDSKQLS PAKRERLLDE IMEKAAVGIG IASPEEIDLY NIFNATKLAM NRALENLSVK PSFVLVDGKG IELSVPGTCL VKGDQKSKLI GAASIVAKVF RDRLMSEFHR MYPQFSFHKH KGYATKEHLN EIRKNGVLPI HRLSFEPVLE LLTDDLLREF FEKGLISENR FERILNLLGA RKSVVFRKER TNHNLPLF // ID RPOB_THEMA Reviewed; 1263 AA. AC P29398; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 17-FEB-2016, entry version 113. DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321}; DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; GN OrderedLocusNames=TM_0458; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8177738; DOI=10.1093/nar/21.21.4904; RA Palm P., Schleper C., Arnold-Ammer I., Holz I., Meier T., RA Lottspeich F., Zillig W.; RT "The DNA-dependent RNA-polymerase of Thermotoga maritima; RT characterisation of the enzyme and the DNA-sequence of the genes for RT the large subunits."; RL Nucleic Acids Res. 21:4904-4908(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-404. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1429627; RA Liao D., Dennis P.P.; RT "The organization and expression of essential transcription RT translation component genes in the extremely thermophilic eubacterium RT Thermotoga maritima."; RL J. Biol. Chem. 267:22787-22797(1992). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000255|HAMAP-Rule:MF_01321}. CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 CC beta' and 1 omega subunit. When a sigma factor is associated with CC the core the holoenzyme is formed, which can initiate CC transcription. {ECO:0000255|HAMAP-Rule:MF_01321}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000255|HAMAP-Rule:MF_01321}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X72695; CAA51246.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35543.1; -; Genomic_DNA. DR EMBL; Z11839; CAA77863.1; -; Genomic_DNA. DR PIR; S41466; F44466. DR RefSeq; NP_228268.1; NC_000853.1. DR RefSeq; WP_004081508.1; NZ_CP011107.1. DR ProteinModelPortal; P29398; -. DR STRING; 243274.TM0458; -. DR EnsemblBacteria; AAD35543; AAD35543; TM_0458. DR GeneID; 897488; -. DR KEGG; tma:TM0458; -. DR KEGG; tmi:THEMA_02400; -. DR KEGG; tmw:THMA_0468; -. DR PATRIC; 23935813; VBITheMar51294_0465. DR eggNOG; ENOG4108IIJ; Bacteria. DR eggNOG; COG0085; LUCA. DR InParanoid; P29398; -. DR KO; K03043; -. DR OMA; AKIDEYG; -. DR OrthoDB; EOG6M9DS6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.150.10; -; 1. DR Gene3D; 2.40.270.10; -; 2. DR Gene3D; 2.40.50.150; -; 1. DR Gene3D; 3.90.1110.10; -; 2. DR HAMAP; MF_01321; RNApol_bact_RpoB; 1. DR InterPro; IPR010243; DNA-dir_RNA_pol_bsu. DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNA_pol_su2_6. DR InterPro; IPR007121; RNA_pol_bsu_CS. DR InterPro; IPR007644; RNA_pol_bsu_protrusion. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold. DR PANTHER; PTHR20856; PTHR20856; 5. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF10385; RNA_pol_Rpb2_45; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR TIGRFAMs; TIGR02013; rpoB; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 1263 DNA-directed RNA polymerase subunit beta. FT /FTId=PRO_0000047984. SQ SEQUENCE 1263 AA; 143138 MW; 04B79368567C8237 CRC64; MKEISCGRRT RVSFGKSREP LPIPDLVEIQ KSSYRRFLEE GLLEVLKKFS PIYSQATRSD LRKSDRGFAL EFVSTRTGEP AIDPLECKAK GLTYSVPIYA TARLTDMKSG EMKEEEVFLG YIPYMTDRGT FIINGAERVV VNQIVVSPGL YFSSEYIDRE EYGGYFLPSR GAWLEVILDP YDGVLYAGLD GKKVNLFLFL KTIGYEKDED ILSLYPTYLD ADDEDSLLLH VGSILLEDIY DGGRKIAEKW DILTKDLAER ILMIDDINQI KIVHPIAQNT FEKMLEVVSS SSEEGEEEEE KTKIYGLNEV TVVDAYLEIF RRLRPEELPR INAAKRYLHD LFFNPERYDL SEVGRYKVNE RLRNAYIRYL IEVEGEDPEE ARKKVYNETS LVLKPLDIVL ASRILFDYFE RRYVNDFEID SYELKNLIRI FKEEYLEKRK TAPYDLRKLV SVFRRNYGVT SDLGVFAAIR YVSNINKELP SIPFDTKDHL GNKRVRTVGE LVQREFERLF ARAQKAIQER LTLINSLSKV SIQSLINIKS IISTVNQFFA MNQLSQFMDQ VNPLSELTHK RRVSAVGPGG LRRESKVFEA RNVHYSQYGR LCPIETPEGA NIGFITSLAI YAKIDEYGFL MTPYRKVVNG KVTDEVVYLR ANEEEEYKII PATTPVDEEG NIIPERVVAR MGEDIRLVPK EEVDFMDVST KQPFSVSASL IPFLEHDDAS RALMGSNMQR QAVPLLKTEA PLVGTGMEWE AAKNSGYVIL AEHDGIVKEV DAARVVVHRT DENGNLMYDD KGNPVVDEYR LLKFVRSNQD TMINQKPIVN EGDFVKKGDP IADGPATDMG ELALGRNILV AFMPWEGYNY EDAILVSQEL LEEDVFTSIH IEVYETQARE TRLGPEEITA DIPNVSKELL KNLDENGIIR VGAYVVSDYG VGSQAILVGK VTPKGEGDTT PEEKIIRSVF GERGRDVKDT SLRLPHGVEG RVIRVDVYDQ NDIAELGAGV LKLVRVYVAS RKTLDIGDKL AGRHGNKGVV SNILPKEDMP FLPDGTPVQM VLNPLGIPSR MNVGQILETH LGWLAKLTGK WFATPVFEGA KEDEILRPLY EERKKRGLHL GDDENNPNGK VVLRDGRTGE PFDNPVVVGY MYMLKLIHIA KEKIHARSTG PYSLIHQQPL GGKSHFGGQR LGEMEVWALE AYGAAHTLAE MLTIKSDDIK GRNEAYKAIL KNMNIPEPGV PESFRVLIKE LRGLALDVRL YDENGNEIDI DKY // ID RNPA_THEMA Reviewed; 117 AA. AC Q9X1H4; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 111. DE RecName: Full=Ribonuclease P protein component {ECO:0000255|HAMAP-Rule:MF_00227}; DE Short=RNase P protein {ECO:0000255|HAMAP-Rule:MF_00227}; DE Short=RNaseP protein {ECO:0000255|HAMAP-Rule:MF_00227}; DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00227}; DE AltName: Full=Protein C5 {ECO:0000255|HAMAP-Rule:MF_00227}; GN Name=rnpA {ECO:0000255|HAMAP-Rule:MF_00227}; GN OrderedLocusNames=TM_1463; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS). RX PubMed=12799461; DOI=10.1073/pnas.0932597100; RA Kazantsev A.V., Krivenko A.A., Harrington D.J., Carter R.J., RA Holbrook S.R., Adams P.D., Pace N.R.; RT "High-resolution structure of RNase P protein from Thermotoga RT maritima."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7497-7502(2003). CC -!- FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence CC from pre-tRNA to produce the mature 5'-terminus. It can also CC cleave other RNA substrates such as 4.5S RNA. The protein CC component plays an auxiliary but essential role in vivo by binding CC to the 5'-leader sequence and broadening the substrate specificity CC of the ribozyme. {ECO:0000255|HAMAP-Rule:MF_00227}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 5'- CC extranucleotides from tRNA precursor. {ECO:0000255|HAMAP- CC Rule:MF_00227}. CC -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a CC protein subunit. {ECO:0000255|HAMAP-Rule:MF_00227}. CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP- CC Rule:MF_00227}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36531.1; -; Genomic_DNA. DR PIR; H72251; H72251. DR RefSeq; NP_229262.1; NC_000853.1. DR RefSeq; WP_004081756.1; NZ_CP011107.1. DR PDB; 1NZ0; X-ray; 1.20 A; A/B/C/D=1-117. DR PDB; 3Q1Q; X-ray; 3.80 A; A=3-117. DR PDB; 3Q1R; X-ray; 4.21 A; A=3-117. DR PDBsum; 1NZ0; -. DR PDBsum; 3Q1Q; -. DR PDBsum; 3Q1R; -. DR ProteinModelPortal; Q9X1H4; -. DR SMR; Q9X1H4; 11-117. DR STRING; 243274.TM1463; -. DR EnsemblBacteria; AAD36531; AAD36531; TM_1463. DR GeneID; 898016; -. DR KEGG; tma:TM1463; -. DR PATRIC; 23937878; VBITheMar51294_1477. DR eggNOG; ENOG41084AH; Bacteria. DR eggNOG; COG0594; LUCA. DR InParanoid; Q9X1H4; -. DR KO; K03536; -. DR OMA; REFLEVQ; -. DR OrthoDB; EOG6C01C6; -. DR EvolutionaryTrace; Q9X1H4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_00227; RNase_P; 1. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR000100; RNase_P. DR InterPro; IPR020539; RNase_P_CS. DR Pfam; PF00825; Ribonuclease_P; 1. DR ProDom; PD003629; Ribonuclease_P; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR00188; rnpA; 1. DR PROSITE; PS00648; RIBONUCLEASE_P; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; RNA-binding; tRNA processing. FT CHAIN 1 117 Ribonuclease P protein component. FT /FTId=PRO_0000198555. FT HELIX 13 23 {ECO:0000244|PDB:1NZ0}. FT STRAND 24 28 {ECO:0000244|PDB:1NZ0}. FT STRAND 30 38 {ECO:0000244|PDB:1NZ0}. FT STRAND 40 43 {ECO:0000244|PDB:1NZ0}. FT STRAND 45 48 {ECO:0000244|PDB:1NZ0}. FT HELIX 52 54 {ECO:0000244|PDB:1NZ0}. FT HELIX 57 74 {ECO:0000244|PDB:1NZ0}. FT TURN 75 77 {ECO:0000244|PDB:1NZ0}. FT STRAND 80 88 {ECO:0000244|PDB:1NZ0}. FT HELIX 90 95 {ECO:0000244|PDB:1NZ0}. FT HELIX 96 98 {ECO:0000244|PDB:1NZ0}. FT HELIX 101 112 {ECO:0000244|PDB:1NZ0}. SQ SEQUENCE 117 AA; 14317 MW; 0E68A9B25D023C64 CRC64; MTESFTRRER LRLRRDFLLI FKEGKSLQNE YFVVLFRKNG LDYSRLGIVV KRKFGKATRR NKLKRWVREI FRRNKGVIPK GFDIVVIPRK KLSEEFERVD FWTVREKLLN LLKRIEG // ID RNR_THEMA Reviewed; 710 AA. AC Q9WZI1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Ribonuclease R {ECO:0000255|HAMAP-Rule:MF_01895}; DE Short=RNase R {ECO:0000255|HAMAP-Rule:MF_01895}; DE EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01895}; DE AltName: Full=VacB protein homolog; GN Name=rnr {ECO:0000255|HAMAP-Rule:MF_01895}; Synonyms=vacB; GN OrderedLocusNames=TM_0722; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside CC monophosphates and is involved in maturation of structured RNAs. CC {ECO:0000255|HAMAP-Rule:MF_01895}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'- CC direction to yield nucleoside 5'-phosphates. {ECO:0000255|HAMAP- CC Rule:MF_01895}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01895}. CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01895}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|HAMAP- CC Rule:MF_01895}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35804.1; -; Genomic_DNA. DR PIR; H72341; H72341. DR RefSeq; NP_228531.1; NC_000853.1. DR RefSeq; WP_004081010.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZI1; -. DR STRING; 243274.TM0722; -. DR EnsemblBacteria; AAD35804; AAD35804; TM_0722. DR GeneID; 898389; -. DR KEGG; tma:TM0722; -. DR PATRIC; 23936364; VBITheMar51294_0735. DR eggNOG; ENOG4105C40; Bacteria. DR eggNOG; COG0557; LUCA. DR InParanoid; Q9WZI1; -. DR KO; K12573; -. DR OMA; YRVHEGP; -. DR OrthoDB; EOG6Q5NRD; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central. DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central. DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IBA:GOC. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_01895; RNase_R; 1. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR013223; RNase_B_OB_dom. DR InterPro; IPR022966; RNase_II/R_CS. DR InterPro; IPR004476; RNase_II/RNase_R. DR InterPro; IPR011805; RNase_R. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF08206; OB_RNB; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00357; CSP; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 4. DR TIGRFAMs; TIGR00358; 3_prime_RNase; 1. DR TIGRFAMs; TIGR02063; RNase_R; 1. DR PROSITE; PS01175; RIBONUCLEASE_II; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease; KW Reference proteome; RNA-binding. FT CHAIN 1 710 Ribonuclease R. FT /FTId=PRO_0000166412. FT DOMAIN 625 705 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_01895}. SQ SEQUENCE 710 AA; 81783 MW; 5EC09EBAE3B81912 CRC64; MSSIRKKDVE RFILSDDYKP MVLKELYKKF RAKTREQRKK VREVVKKLEK EGRIFRDSRG RYRKLGEDLK VGTIEFTRSG YVAFVITDDF EEIAVPVEDT KYAMHKDRVV VEITGTWRGL PRGRVVRVLE RGLKRVVGVF DHKGTFGFVV PDDPKIAYDF YVAPENIDGA KPNQKVIAEI LKYPSPGKNP EAKVVKVLGD LDDPSIDLPS VIVKHDLPEP GEFPEEVIRE ANAIPARVRK KDLVGRKDLR DKVIVTIDGE DAKDFDDAIS VEKLPNGNYL LGVHIADVSH YVKEGSALDQ EAFKRGTSVY LIDTVIPMLP FRLSNGICSL VEGKDRLTMS VEMEIDRDGR VVRYDVYPSV IKSKKRMIYE RVNEFLEDPS SMKEYEPFKD LIYNAVELAE ILREARRKRG AILDIESDEV KVILDENGQV VDIVPRKRGI AEKLIEEFMI RANETVAEIF DHAGLPFMYR VHEEPDPETI FQLKNYLEAM GIRAKFSHKI HPGMLQKLLE KVKDHPLRSS VERLLVRSMK RAMYSAVNIG HFGLASYAYT HFTSPIRRYP DLVVHRLLKL YLEQNGYFTP EQIEKFSKVL PKIAKHCSRR ERVADEAEWD LVAMKKVEYI ARHIGEVFNV VVTNITKFGL FVEIPEKSIS GLVHISTLDD YYYYDETRNM LIGKRKGKVF RLGDVLKAKV VRADKIRGEI DFVLVEEDEE // ID RPOA_THEMA Reviewed; 336 AA. AC Q9X1I2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE Short=RNAP subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059}; DE AltName: Full=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE AltName: Full=Transcriptase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; GN Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059}; GN OrderedLocusNames=TM_1472; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {ECO:0000255|HAMAP-Rule:MF_00059}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000255|HAMAP-Rule:MF_00059}. CC -!- SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1 CC beta, 1 beta' and 1 omega subunit. When a sigma factor is CC associated with the core the holoenzyme is formed, which can CC initiate transcription. {ECO:0000255|HAMAP-Rule:MF_00059}. CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and CC basal transcription, whereas the C-terminal domain is involved in CC interaction with transcriptional regulators and with upstream CC promoter elements. {ECO:0000255|HAMAP-Rule:MF_00059}. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC {ECO:0000255|HAMAP-Rule:MF_00059}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36540.1; -; Genomic_DNA. DR PIR; A72247; A72247. DR RefSeq; NP_229272.1; NC_000853.1. DR RefSeq; WP_004081779.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1I2; -. DR SMR; Q9X1I2; 269-333. DR STRING; 243274.TM1472; -. DR PRIDE; Q9X1I2; -. DR EnsemblBacteria; AAD36540; AAD36540; TM_1472. DR GeneID; 897063; -. DR KEGG; tma:TM1472; -. DR PATRIC; 23937900; VBITheMar51294_1488. DR eggNOG; ENOG4105CTF; Bacteria. DR eggNOG; COG0202; LUCA. DR InParanoid; Q9X1I2; -. DR KO; K03040; -. DR OMA; LMKFRNF; -. DR OrthoDB; EOG68WR84; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 2.170.120.12; -; 1. DR HAMAP; MF_00059; RNApol_bact_RpoA; 1. DR InterPro; IPR011262; DNA-dir_RNA_pol_insert. DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3. DR InterPro; IPR011773; DNA-dir_RpoA. DR InterPro; IPR009025; RBP11-like_dimer. DR InterPro; IPR011260; RNAP_asu_C. DR Pfam; PF01000; RNA_pol_A_bac; 1. DR Pfam; PF03118; RNA_pol_A_CTD; 1. DR Pfam; PF01193; RNA_pol_L; 1. DR ProDom; PD001179; RNAP_asu_C; 1. DR SMART; SM00662; RPOLD; 1. DR SUPFAM; SSF55257; SSF55257; 2. DR SUPFAM; SSF56553; SSF56553; 1. DR TIGRFAMs; TIGR02027; rpoA; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 336 DNA-directed RNA polymerase subunit FT alpha. FT /FTId=PRO_0000175406. FT REGION 1 235 Alpha N-terminal domain (alpha-NTD). FT {ECO:0000255|HAMAP-Rule:MF_00059}. FT REGION 264 336 Alpha C-terminal domain (alpha-CTD). FT {ECO:0000255|HAMAP-Rule:MF_00059}. SQ SEQUENCE 336 AA; 38600 MW; E361EED8D4408CF2 CRC64; MIEFVIPKKL KVEEEREERD YYYSRFSLSP LERGYAITIG NALRRVLLSS IPSLAIVGVR FIKPEKYHEY DYIEGVKEDI LDIILNLKKV QFRINVTVKG TIKMEVEKKG PGELVAGDIK TPAGIEVVNP DLHIATLNSK ADLFFEVYAE VGKGFVPVSE REERPDVGWI PIDGVFSPVI KVNFLTENVR VGKRTDYDKL ILEIWTKKSI RPEEALRKAA DILINHFKIV TEGLPELKIS EEYIITSEEE EAEVPASEHE EEHRENSDVY NRKIDELELS VRSLNCLKRA KIETIGDLLS KTEEELLKIK NFGQKSLDEV KEKLKEKFGL ELRKGE // ID RPOC_THEMA Reviewed; 1690 AA. AC P36252; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 11-NOV-2015, entry version 111. DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322}; DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; GN OrderedLocusNames=TM_0459; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8177738; DOI=10.1093/nar/21.21.4904; RA Palm P., Schleper C., Arnold-Ammer I., Holz I., Meier T., RA Lottspeich F., Zillig W.; RT "The DNA-dependent RNA-polymerase of Thermotoga maritima; RT characterisation of the enzyme and the DNA-sequence of the genes for RT the large subunits."; RL Nucleic Acids Res. 21:4904-4908(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000255|HAMAP-Rule:MF_01322}. CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 CC beta' and 1 omega subunit. When a sigma factor is associated with CC the core the holoenzyme is formed, which can initiate CC transcription. {ECO:0000255|HAMAP-Rule:MF_01322}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. CC {ECO:0000255|HAMAP-Rule:MF_01322}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X72695; CAA51247.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35544.1; -; Genomic_DNA. DR PIR; S41467; S41467. DR RefSeq; NP_228269.1; NC_000853.1. DR RefSeq; WP_004081507.1; NZ_CP011107.1. DR ProteinModelPortal; P36252; -. DR STRING; 243274.TM0459; -. DR PRIDE; P36252; -. DR EnsemblBacteria; AAD35544; AAD35544; TM_0459. DR GeneID; 897490; -. DR KEGG; tma:TM0459; -. DR KEGG; tmi:THEMA_02395; -. DR KEGG; tmw:THMA_0469; -. DR PATRIC; 23935815; VBITheMar51294_0466. DR eggNOG; ENOG4107QR0; Bacteria. DR eggNOG; COG0086; LUCA. DR InParanoid; P36252; -. DR KO; K03046; -. DR OMA; YFAAYMI; -. DR OrthoDB; EOG6M9DS6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01322; RNApol_bact_RpoC; 1. DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime. DR InterPro; IPR000722; RNA_pol_asu. DR InterPro; IPR006592; RNA_pol_N. DR InterPro; IPR007080; RNA_pol_Rpb1_1. DR InterPro; IPR007066; RNA_pol_Rpb1_3. DR InterPro; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR Pfam; PF04997; RNA_pol_Rpb1_1; 2. DR Pfam; PF00623; RNA_pol_Rpb1_2; 2. DR Pfam; PF04983; RNA_pol_Rpb1_3; 1. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 1. DR SMART; SM00663; RPOLA_N; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 1690 DNA-directed RNA polymerase subunit FT beta'. FT /FTId=PRO_0000067818. SQ SEQUENCE 1690 AA; 190521 MW; 9ED23FD2E9512CE6 CRC64; MPMSSFKRKI KAIQIKIASP EVIRSWSGGE VKKPETINYR TFKPERDGLF CERIFGPVKD YECACGKYKG KKYEGTVCER CGVRVESREA RRKRMGHIEL AAPAVHIWYL ESIPSVLGTL LNMSTSDLEN IIYYGSRRVI ERAFIVTDPK DTPFSQGDVI YETEYRIYRK KWDFDVEQAF VVKNPKSPVL SDIDGEVTLK TEKSITGREI TWIIVKNITR ATHTVLPGMI LVVKDGQEVE KGQDLTKEMT IDPVYAPFDG HVEIDELSNT ITLKPLTTSK DQPVVFTIPY GAKILVSNGQ KVKKGDQITT STSLPAVKAS ISGTVRFGSN LNIRALEDGN FEVLSTGEVY VEQVIEERKY PVFEGALVYV NNGDQVKKGD HLADRFLFEE EYLSATEYKI FESHYPTMFD VEERTENDRP IVVITDIDPE VSKETGLKVG DIVTENEYEA YLQIYPEKIV ADAGAQAIKK LLQNLDLEAL QAEIEAELKK LPSSSSKAIK LRRRLKMVKD FLKSGNKPEW MVLEVVPVIP PDLRPMIQIE GGRFATTDLN ELYRRLINRN NRLKKLLELG APEIILRNEK RMLQEAVDAL IHNGSDSEGK RSRRAVLKDR NGRPLKSLTD LLKGKKGRFR RNLLGKRVDY SGRAVIVVGP NLKIHQCGIP KKMAMELFKP FVLAKLLGEG SSSKTMRKVK KAIIEKEMPE AWEVLEEVIK GSVVLLNRAP TLHRMSIQAF EPKLVEGNAI QLHPVVCPPF NADFDGDQMA VHVPLSAAAQ AEARFLMLSR YNIISPAHGK PISLPTQDII IGSYYLTTVG KEFDSLKEED VKWKFSSPEE AMLAYHLGFI KLHTPILIKV AVNGEEKRIK TTLGRVIFNG ILPEDLRDYN RIFDKKQINA LVYETFKRHG IDRAADLLDD IKDIGFHYAT VSGLTLSLKD LKIPPERDEI LRKTWEKVRI IEENYEKGFL TEEQRKSEII RLWMSVTEEI TKLTSKTLAE DPFNPIYMMV NSGARGNIDQ VKQLAGIRGL MIKAYDPRSR EIKSKIFKGQ AIHEALTFDY PVDKNLREGV DILQFFISTY GARKGQVDTA MNTSFAGYLT RRLVDVAQSV TVAEPDCGTH EGIRAMDLIK EGTVVEKMNE FLFGRVLARD VLDPETKEVL KNPETGKEYT RNTMLTDDDA NFLASYKKMV DVVRYEEIDI TELSLPNMYA EIAEPVGEYE EGTELTWDVI KAAKNEGKYR IKVKVYPVVG TVYAEEEPLY DKKGERQLLV YQEVINEIVA KMLEENGIEK VSVRPDIIVR SPLTCESEYG VCAACYGMDL SNHKIVNVGE AVGVVAAQSI GEPGTQLTMR TFHVGGVMGA SDIVSGLTTV EKTFEPYAFL REEKSGGKKE IRKYYGSEAI LCEVDGFVKD IATDESGRTV IYIEDYAGNI HAYKVPKRAK VRVEKGQKVL RGETLTSGAI VWWKLLELES EKGVMTAMNL LKIIKNAYVQ QGVSIHDKHF EIIFKQMLSM ATIVDPGDSD YLPDQLVPLV DIKRFNREIL EGNAKVEENR KWVIGKTLAK RIITETEEGE LVELAQKGDE VTEELLKKII EAGIKEIDVF EKDKVVTYQI LPKEPIKYKR RLLSLKKAAL NYPGWLSAAA FEETAWVLTA AAIEGKVDPL IGLKENVIVG QLIPAGTGLD VFAGIQVEET PRAAVEEELA // ID RRF_THEMA Reviewed; 185 AA. AC Q9X1B9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Ribosome-recycling factor {ECO:0000255|HAMAP-Rule:MF_00040}; DE Short=RRF {ECO:0000255|HAMAP-Rule:MF_00040}; DE AltName: Full=Ribosome-releasing factor {ECO:0000255|HAMAP-Rule:MF_00040}; GN Name=frr {ECO:0000255|HAMAP-Rule:MF_00040}; OrderedLocusNames=TM_1399; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS). RX PubMed=10600747; DOI=10.1126/science.286.5448.2349; RA Selmer M., Al-Karadaghi S., Hirokawa G., Kaji A., Liljas A.; RT "Crystal structure of Thermotoga maritima ribosome recycling factor: a RT tRNA mimic."; RL Science 286:2349-2352(1999). CC -!- FUNCTION: Responsible for the release of ribosomes from messenger CC RNA at the termination of protein biosynthesis. May increase the CC efficiency of translation by recycling ribosomes from one round of CC translation to another. {ECO:0000255|HAMAP-Rule:MF_00040}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00040}. CC -!- SIMILARITY: Belongs to the RRF family. {ECO:0000255|HAMAP- CC Rule:MF_00040}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36470.1; -; Genomic_DNA. DR PIR; H72259; H72259. DR RefSeq; NP_229200.1; NC_000853.1. DR RefSeq; WP_004081616.1; NZ_CP011107.1. DR PDB; 1DD5; X-ray; 2.55 A; A=1-185. DR PDBsum; 1DD5; -. DR ProteinModelPortal; Q9X1B9; -. DR SMR; Q9X1B9; 2-185. DR STRING; 243274.TM1399; -. DR EnsemblBacteria; AAD36470; AAD36470; TM_1399. DR GeneID; 898077; -. DR KEGG; tma:TM1399; -. DR PATRIC; 23937744; VBITheMar51294_1411. DR eggNOG; ENOG4108VCV; Bacteria. DR eggNOG; COG0233; LUCA. DR InParanoid; Q9X1B9; -. DR KO; K02838; -. DR OMA; MLSVQVW; -. DR OrthoDB; EOG6SV5F9; -. DR EvolutionaryTrace; Q9X1B9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IBA:GOC. DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central. DR GO; GO:0002184; P:cytoplasmic translational termination; IBA:GO_Central. DR Gene3D; 1.10.132.20; -; 1. DR HAMAP; MF_00040; RRF; 1. DR InterPro; IPR002661; Ribosome_recyc_fac. DR InterPro; IPR023584; Ribosome_recyc_fac_dom. DR PANTHER; PTHR20982; PTHR20982; 1. DR Pfam; PF01765; RRF; 1. DR SUPFAM; SSF55194; SSF55194; 1. DR TIGRFAMs; TIGR00496; frr; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 185 Ribosome-recycling factor. FT /FTId=PRO_0000167565. FT HELIX 4 26 {ECO:0000244|PDB:1DD5}. FT HELIX 34 37 {ECO:0000244|PDB:1DD5}. FT STRAND 41 44 {ECO:0000244|PDB:1DD5}. FT STRAND 47 50 {ECO:0000244|PDB:1DD5}. FT HELIX 51 53 {ECO:0000244|PDB:1DD5}. FT STRAND 54 59 {ECO:0000244|PDB:1DD5}. FT STRAND 64 71 {ECO:0000244|PDB:1DD5}. FT HELIX 74 84 {ECO:0000244|PDB:1DD5}. FT STRAND 85 87 {ECO:0000244|PDB:1DD5}. FT STRAND 98 101 {ECO:0000244|PDB:1DD5}. FT HELIX 107 144 {ECO:0000244|PDB:1DD5}. FT HELIX 150 183 {ECO:0000244|PDB:1DD5}. SQ SEQUENCE 185 AA; 21513 MW; 626E349B97495852 CRC64; MVNPFIKEAK EKMKRTLEKI EDELRKMRTG KPSPAILEEI KVDYYGVPTP VNQLATISIS EERTLVIKPW DKSVLSLIEK AINASDLGLN PINDGNVIRL VFPSPTTEQR EKWVKKAKEI VEEGKIAIRN IRREILKKIK EDQKEGLIPE DDAKRLENEI QKLTDEFIEK LDEVFEIKKE EIMEF // ID RPOZ_THEMA Reviewed; 79 AA. AC Q9X214; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 103. DE RecName: Full=DNA-directed RNA polymerase subunit omega; DE Short=RNAP omega subunit; DE EC=2.7.7.6; DE AltName: Full=RNA polymerase omega subunit; DE AltName: Full=Transcriptase subunit omega; GN Name=rpoZ; OrderedLocusNames=TM_1688; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C- CC terminal regions of the beta' subunit thereby facilitating its CC interaction with the beta and alpha subunits (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 CC beta' and 1 omega subunit. When a sigma factor is associated with CC the core the holoenzyme is formed, which can initiate CC transcription (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36755.1; -; Genomic_DNA. DR PIR; B72223; B72223. DR RefSeq; NP_229488.1; NC_000853.1. DR RefSeq; WP_004082204.1; NZ_CP011107.1. DR STRING; 243274.TM1688; -. DR EnsemblBacteria; AAD36755; AAD36755; TM_1688. DR GeneID; 897237; -. DR KEGG; tma:TM1688; -. DR PATRIC; 23938350; VBITheMar51294_1705. DR eggNOG; ENOG41065EC; Bacteria. DR eggNOG; COG1758; LUCA. DR KO; K03060; -. DR OMA; YKFAIPI; -. DR OrthoDB; EOG6Q5NV5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.940.10; -; 1. DR HAMAP; MF_00366; RNApol_bact_RpoZ; 1. DR InterPro; IPR003716; DNA-dir_RNA_pol_omega. DR InterPro; IPR006110; Pol_omega/K/RPB6. DR InterPro; IPR012293; RNAP_RPB6_omega. DR Pfam; PF01192; RNA_pol_Rpb6; 1. DR SMART; SM01409; RNA_pol_Rpb6; 1. DR SUPFAM; SSF63562; SSF63562; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 79 DNA-directed RNA polymerase subunit FT omega. FT /FTId=PRO_0000129003. SQ SEQUENCE 79 AA; 9350 MW; CEFF0D30676249D9 CRC64; MEKIVKFDLK YDELLKKIPY KYAIPVVVAK RAEAIREYAR PFVITDDENY VSIAFMELSL NYIRIKNEEI LKALIPKVK // ID RS12_THEMA Reviewed; 127 AA. AC Q9X1J3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 2. DT 13-APR-2016, entry version 105. DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403}; GN Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; GN OrderedLocusNames=TM_1505; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: With S4 and S5 plays an important role in translational CC accuracy. {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that CC are involved in tRNA selection in the A site and with the mRNA CC backbone. Located at the interface of the 30S and 50S subunits, it CC traverses the body of the 30S subunit contacting proteins on the CC other side and probably holding the rRNA structure together. The CC combined cluster of proteins S8, S12 and S17 appears to hold CC together the shoulder and platform of the 30S subunit. CC {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8 CC and S17. May interact with IF1 in the 30S initiation complex. CC {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- SIMILARITY: Belongs to the ribosomal protein S12P family. CC {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD36572.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36572.1; ALT_INIT; Genomic_DNA. DR PIR; B72244; B72244. DR RefSeq; NP_229305.2; NC_000853.1. DR RefSeq; WP_004081846.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1J3; -. DR SMR; Q9X1J3; 1-123. DR STRING; 243274.TM1505; -. DR EnsemblBacteria; AAD36572; AAD36572; TM_1505. DR GeneID; 898713; -. DR KEGG; tma:TM1505; -. DR PATRIC; 23937968; VBITheMar51294_1522. DR eggNOG; ENOG4108UKE; Bacteria. DR eggNOG; COG0048; LUCA. DR InParanoid; Q9X1J3; -. DR KO; K02950; -. DR OMA; LKSCPER; -. DR OrthoDB; EOG61ZTNF; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IBA:GO_Central. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00403_B; Ribosomal_S12_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR006032; Ribosomal_S12/S23. DR InterPro; IPR005679; Ribosomal_S12_bac. DR PANTHER; PTHR11652; PTHR11652; 1. DR Pfam; PF00164; Ribosom_S12_S23; 1. DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1. DR PRINTS; PR01034; RIBOSOMALS12. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00981; rpsL_bact; 1. DR PROSITE; PS00055; RIBOSOMAL_S12; 1. PE 3: Inferred from homology; KW Complete proteome; Methylation; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 127 30S ribosomal protein S12. FT /FTId=PRO_0000146339. FT MOD_RES 89 89 3-methylthioaspartic acid. {ECO:0000250}. SQ SEQUENCE 127 AA; 14061 MW; 71399C5CF10BCA80 CRC64; MPTINQLIRY GRKPKKKKSK APALQGNPQK RGVCIKVSTM TPKKPNSALR KIARVRLSNG IEVTAYIPGI GHNLQEHSVV LVRGGRVKDL PGVRYKIIRG ALDAAGVEGR RQSRSKYGAK RPKDQKK // ID RS15_THEMA Reviewed; 90 AA. AC Q9X165; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343}; GN Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; GN OrderedLocusNames=TM_1344; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA where it helps nucleate assembly of the CC platform of the 30S subunit by binding and bridging several RNA CC helices of the 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01343}. CC -!- FUNCTION: Forms an intersubunit bridge (bridge B4) with the 23S CC rRNA of the 50S subunit in the ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01343}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a bridge to the CC 50S subunit in the 70S ribosome, contacting the 23S rRNA. CC {ECO:0000255|HAMAP-Rule:MF_01343}. CC -!- SIMILARITY: Belongs to the ribosomal protein S15P family. CC {ECO:0000255|HAMAP-Rule:MF_01343}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36415.1; -; Genomic_DNA. DR PIR; G72266; G72266. DR RefSeq; NP_229145.1; NC_000853.1. DR RefSeq; WP_004081540.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X165; -. DR SMR; Q9X165; 4-88. DR STRING; 243274.TM1344; -. DR EnsemblBacteria; AAD36415; AAD36415; TM_1344. DR GeneID; 898136; -. DR KEGG; tma:TM1344; -. DR PATRIC; 23937626; VBITheMar51294_1356. DR eggNOG; ENOG4105K77; Bacteria. DR eggNOG; COG0184; LUCA. DR InParanoid; Q9X165; -. DR KO; K02956; -. DR OMA; TEHFKSH; -. DR OrthoDB; EOG6B368J; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.10; -; 1. DR HAMAP; MF_01343_B; Ribosomal_S15_B; 1. DR InterPro; IPR000589; Ribosomal_S15. DR InterPro; IPR005290; Ribosomal_S15_bac-type. DR InterPro; IPR009068; S15_NS1_RNA-bd. DR Pfam; PF00312; Ribosomal_S15; 1. DR SMART; SM01387; Ribosomal_S15; 1. DR SUPFAM; SSF47060; SSF47060; 1. DR TIGRFAMs; TIGR00952; S15_bact; 1. DR PROSITE; PS00362; RIBOSOMAL_S15; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 90 30S ribosomal protein S15. FT /FTId=PRO_0000115571. SQ SEQUENCE 90 AA; 10808 MW; A695955A002BCA94 CRC64; MVSLDPEKKN EIIKEFQIHE NDTGSVEVQI ALLTARIKHL TEHLRKHPKD FHSRRGLMKM IGRRRKMLKY LRHKKPEVYR ELIAKLGIRK // ID RS13_THEMA Reviewed; 125 AA. AC Q9X1I5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315}; GN Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; GN OrderedLocusNames=TM_1475; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Located at the top of the head of the 30S subunit, it CC contacts several helices of the 16S rRNA. In the 70S ribosome it CC contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S CC subunit (bridge B1b), connecting the 2 subunits; these bridges are CC implicated in subunit movement. Contacts the tRNAs in the A and P- CC sites. {ECO:0000255|HAMAP-Rule:MF_01315}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a loose CC heterodimer with protein S19. Forms two bridges to the 50S subunit CC in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01315}. CC -!- SIMILARITY: Belongs to the ribosomal protein S13P family. CC {ECO:0000255|HAMAP-Rule:MF_01315}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36543.1; -; Genomic_DNA. DR PIR; D72247; D72247. DR RefSeq; NP_229275.1; NC_000853.1. DR RefSeq; WP_004081785.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1I5; -. DR SMR; Q9X1I5; 2-116. DR STRING; 243274.TM1475; -. DR EnsemblBacteria; AAD36543; AAD36543; TM_1475. DR GeneID; 897029; -. DR KEGG; tma:TM1475; -. DR PATRIC; 23937906; VBITheMar51294_1491. DR eggNOG; ENOG4108Z04; Bacteria. DR eggNOG; COG0099; LUCA. DR InParanoid; Q9X1I5; -. DR KO; K02952; -. DR OMA; RTKNNSR; -. DR OrthoDB; EOG618R01; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 4.10.910.10; -; 1. DR HAMAP; MF_01315; Ribosomal_S13_S18; 1. DR InterPro; IPR027437; 30s_Rbsml_prot_S13_C. DR InterPro; IPR001892; Ribosomal_S13. DR InterPro; IPR010979; Ribosomal_S13-like_H2TH. DR InterPro; IPR019980; Ribosomal_S13_bac-type. DR InterPro; IPR018269; Ribosomal_S13_CS. DR Pfam; PF00416; Ribosomal_S13; 1. DR PIRSF; PIRSF002134; Ribosomal_S13; 1. DR SUPFAM; SSF46946; SSF46946; 1. DR TIGRFAMs; TIGR03631; uS13_bact; 1. DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1. DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 125 30S ribosomal protein S13. FT /FTId=PRO_0000132158. SQ SEQUENCE 125 AA; 14432 MW; 55E66FDF6FA16097 CRC64; MARIVGVELP NNKKVWVALT YIYGIGRSRS FEILKNTGID PEKRVGDLTD EEISKITKYI QDHFKVEGEL RSEVERNIRR LIEIGCYRGI RHKLGLPVRG QKTRSNARTR KGPRPSRIKT KKKSS // ID RS10_THEMA Reviewed; 102 AA. AC P38518; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 11-MAY-2016, entry version 105. DE RecName: Full=30S ribosomal protein S10 {ECO:0000255|HAMAP-Rule:MF_00508}; GN Name=rpsJ {ECO:0000255|HAMAP-Rule:MF_00508}; GN OrderedLocusNames=TM_1501; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in the binding of tRNA to the ribosomes. CC {ECO:0000255|HAMAP-Rule:MF_00508}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_00508}. CC -!- SIMILARITY: Belongs to the ribosomal protein S10P family. CC {ECO:0000255|HAMAP-Rule:MF_00508}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79776.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36567.1; -; Genomic_DNA. DR PIR; S40187; S40187. DR RefSeq; NP_229301.1; NC_000853.1. DR RefSeq; WP_004081837.1; NZ_CP011107.1. DR ProteinModelPortal; P38518; -. DR SMR; P38518; 5-101. DR STRING; 243274.TM1501; -. DR EnsemblBacteria; AAD36567; AAD36567; TM_1501. DR GeneID; 897440; -. DR KEGG; tma:TM1501; -. DR PATRIC; 23937960; VBITheMar51294_1518. DR eggNOG; ENOG4108Z10; Bacteria. DR eggNOG; COG0051; LUCA. DR InParanoid; P38518; -. DR KO; K02946; -. DR OMA; LANMDIP; -. DR OrthoDB; EOG6VXFHB; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.600; -; 1. DR HAMAP; MF_00508; Ribosomal_S10; 1. DR InterPro; IPR001848; Ribosomal_S10. DR InterPro; IPR018268; Ribosomal_S10_CS. DR InterPro; IPR027486; Ribosomal_S10_dom. DR PANTHER; PTHR11700; PTHR11700; 1. DR Pfam; PF00338; Ribosomal_S10; 1. DR PRINTS; PR00971; RIBOSOMALS10. DR SMART; SM01403; Ribosomal_S10; 1. DR SUPFAM; SSF54999; SSF54999; 1. DR TIGRFAMs; TIGR01049; rpsJ_bact; 1. DR PROSITE; PS00361; RIBOSOMAL_S10; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 102 30S ribosomal protein S10. FT /FTId=PRO_0000146618. SQ SEQUENCE 102 AA; 11637 MW; 4CB4D266F7D7C7F7 CRC64; MPGQKIRIKL KAYDHELLDE SAKKIVEVAK STNSKVSGPI PLPTERTLYC VLRSPMKHKD SREHFEKRVH KRLIDIIDPS PKTIDALMRI NLPAGVDVEI KL // ID RS16_THEMA Reviewed; 95 AA. AC Q9X1Q2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=30S ribosomal protein S16 {ECO:0000255|HAMAP-Rule:MF_00385}; GN Name=rpsP {ECO:0000255|HAMAP-Rule:MF_00385}; GN OrderedLocusNames=TM_1566; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ribosomal protein S16P family. CC {ECO:0000255|HAMAP-Rule:MF_00385}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36633.1; -; Genomic_DNA. DR PIR; G72236; G72236. DR RefSeq; NP_229366.1; NC_000853.1. DR RefSeq; WP_004081979.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1Q2; -. DR STRING; 243274.TM1566; -. DR EnsemblBacteria; AAD36633; AAD36633; TM_1566. DR GeneID; 897459; -. DR KEGG; tma:TM1566; -. DR PATRIC; 23938094; VBITheMar51294_1584. DR eggNOG; ENOG4105K5M; Bacteria. DR eggNOG; COG0228; LUCA. DR InParanoid; Q9X1Q2; -. DR KO; K02959; -. DR OMA; HEAKFSK; -. DR OrthoDB; EOG6CVVKH; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1320.10; -; 1. DR HAMAP; MF_00385; Ribosomal_S16; 1. DR InterPro; IPR000307; Ribosomal_S16. DR InterPro; IPR020592; Ribosomal_S16_CS. DR InterPro; IPR023803; Ribosomal_S16_dom. DR PANTHER; PTHR12919; PTHR12919; 1. DR Pfam; PF00886; Ribosomal_S16; 1. DR SUPFAM; SSF54565; SSF54565; 1. DR TIGRFAMs; TIGR00002; S16; 1. DR PROSITE; PS00732; RIBOSOMAL_S16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 95 30S ribosomal protein S16. FT /FTId=PRO_0000167267. SQ SEQUENCE 95 AA; 11254 MW; 7260BB14A40F8B84 CRC64; MVRIRLTRMG KRHQPFYRIV VVDSRKRRDG AYIESLGYYN PLKEGEIKID VERAVEWILK GAQPSDTVRD IFRKFGVMKR VHEIKYGKKE EATAE // ID RS18_THEMA Reviewed; 75 AA. AC Q9WZ74; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=30S ribosomal protein S18 {ECO:0000255|HAMAP-Rule:MF_00270}; GN Name=rpsR {ECO:0000255|HAMAP-Rule:MF_00270}; GN OrderedLocusNames=TM_0605; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds as a heterodimer with protein S6 to the central CC domain of the 16S rRNA, where it helps stabilize the platform of CC the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_00270}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight CC heterodimer with protein S6. {ECO:0000255|HAMAP-Rule:MF_00270}. CC -!- SIMILARITY: Belongs to the ribosomal protein S18P family. CC {ECO:0000255|HAMAP-Rule:MF_00270}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35690.1; -; Genomic_DNA. DR PIR; A72355; A72355. DR RefSeq; NP_228415.1; NC_000853.1. DR RefSeq; WP_004081224.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ74; -. DR STRING; 243274.TM0605; -. DR EnsemblBacteria; AAD35690; AAD35690; TM_0605. DR GeneID; 897686; -. DR KEGG; tma:TM0605; -. DR PATRIC; 23936125; VBITheMar51294_0616. DR eggNOG; ENOG4105VH8; Bacteria. DR eggNOG; COG0238; LUCA. DR InParanoid; Q9WZ74; -. DR KO; K02963; -. DR OMA; NFMNDKG; -. DR OrthoDB; EOG6PCQ4R; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 4.10.640.10; -; 1. DR HAMAP; MF_00270; Ribosomal_S18; 1. DR InterPro; IPR001648; Ribosomal_S18. DR InterPro; IPR018275; Ribosomal_S18_CS. DR Pfam; PF01084; Ribosomal_S18; 1. DR PRINTS; PR00974; RIBOSOMALS18. DR ProDom; PD002239; Ribosomal_S18; 1. DR SUPFAM; SSF46911; SSF46911; 1. DR TIGRFAMs; TIGR00165; S18; 1. DR PROSITE; PS00057; RIBOSOMAL_S18; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 75 30S ribosomal protein S18. FT /FTId=PRO_0000111248. SQ SEQUENCE 75 AA; 9016 MW; C496FE7E86DBDA76 CRC64; MAYRRRKKKI KKCRLCEMKL DYVDYKDTRL LSEFLTDKGK IIPKRLTGNC SKHQRMVKVA IKRARQMGLL PYLKI // ID RS11_THEMA Reviewed; 130 AA. AC Q9X1I4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310}; GN Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; GN OrderedLocusNames=TM_1474; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Located on the platform of the 30S subunit, it bridges CC several disparate RNA helices of the 16S rRNA. Forms part of the CC Shine-Dalgarno cleft in the 70S ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01310}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Interacts with CC proteins S7 and S18. Binds to IF-3. {ECO:0000255|HAMAP- CC Rule:MF_01310}. CC -!- SIMILARITY: Belongs to the ribosomal protein S11P family. CC {ECO:0000255|HAMAP-Rule:MF_01310}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36542.1; -; Genomic_DNA. DR PIR; C72247; C72247. DR RefSeq; NP_229274.1; NC_000853.1. DR RefSeq; WP_004081783.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1I4; -. DR SMR; Q9X1I4; 17-130. DR STRING; 243274.TM1474; -. DR EnsemblBacteria; AAD36542; AAD36542; TM_1474. DR GeneID; 898010; -. DR KEGG; tma:TM1474; -. DR PATRIC; 23937904; VBITheMar51294_1490. DR eggNOG; ENOG4108UHH; Bacteria. DR eggNOG; COG0100; LUCA. DR InParanoid; Q9X1I4; -. DR KO; K02948; -. DR OMA; NTPYASQ; -. DR OrthoDB; EOG6ZSPF3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central. DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.420.80; -; 1. DR HAMAP; MF_01310; Ribosomal_S11; 1. DR InterPro; IPR001971; Ribosomal_S11. DR InterPro; IPR019981; Ribosomal_S11_bac-type. DR InterPro; IPR018102; Ribosomal_S11_CS. DR PANTHER; PTHR11759; PTHR11759; 1. DR Pfam; PF00411; Ribosomal_S11; 1. DR PIRSF; PIRSF002131; Ribosomal_S11; 1. DR TIGRFAMs; TIGR03632; uS11_bact; 1. DR PROSITE; PS00054; RIBOSOMAL_S11; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 130 30S ribosomal protein S11. FT /FTId=PRO_0000123244. SQ SEQUENCE 130 AA; 14092 MW; E2D826640FE037CA CRC64; MARKRGGSSK KQKKVSFDYG VVHIKSTFNN TIITLTDKDG NTLTWASGGT VGFEGTRKGT PYAAQLAADK VAREALRMGI KKVDVLVKGP GPGREPAIRT LQGAGLEINQ IKDVTPIPFN GCRPKKRRRV // ID RS14Z_THEMA Reviewed; 61 AA. AC Q9ZAE6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=30S ribosomal protein S14 type Z {ECO:0000255|HAMAP-Rule:MF_01364}; GN Name=rpsZ {ECO:0000255|HAMAP-Rule:MF_01364}; GN Synonyms=rpsN {ECO:0000255|HAMAP-Rule:MF_01364}; GN OrderedLocusNames=TM_1487; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RA Sanangelantoni A.M.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds 16S rRNA, required for the assembly of 30S CC particles and may also be responsible for determining the CC conformation of the 16S rRNA at the A site. {ECO:0000255|HAMAP- CC Rule:MF_01364}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01364}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01364}; CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S3 CC and S10. {ECO:0000255|HAMAP-Rule:MF_01364}. CC -!- SIMILARITY: Belongs to the ribosomal protein S14P family. Zinc- CC binding S14P subfamily. {ECO:0000255|HAMAP-Rule:MF_01364}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79790.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36553.1; -; Genomic_DNA. DR PIR; G72248; G72248. DR RefSeq; NP_229287.1; NC_000853.1. DR RefSeq; WP_004081809.1; NZ_CP011107.1. DR ProteinModelPortal; Q9ZAE6; -. DR SMR; Q9ZAE6; 2-61. DR STRING; 243274.TM1487; -. DR EnsemblBacteria; AAD36553; AAD36553; TM_1487. DR GeneID; 897342; -. DR KEGG; tma:TM1487; -. DR PATRIC; 23937932; VBITheMar51294_1504. DR eggNOG; ENOG41082QR; Bacteria. DR eggNOG; COG0199; LUCA. DR InParanoid; Q9ZAE6; -. DR KO; K02954; -. DR OMA; RAYTRCN; -. DR OrthoDB; EOG6BCT0K; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR HAMAP; MF_01364_B; Ribosomal_S14_2_B; 1. DR InterPro; IPR001209; Ribosomal_S14. DR InterPro; IPR018271; Ribosomal_S14_CS. DR InterPro; IPR023053; Ribosomal_S14_Z. DR PANTHER; PTHR19836; PTHR19836; 1. DR Pfam; PF00253; Ribosomal_S14; 1. DR PROSITE; PS00527; RIBOSOMAL_S14; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc. FT CHAIN 1 61 30S ribosomal protein S14 type Z. FT /FTId=PRO_0000130953. FT METAL 24 24 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. FT METAL 27 27 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. FT METAL 40 40 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. FT METAL 43 43 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. SQ SEQUENCE 61 AA; 7343 MW; EA3609561FC3CC69 CRC64; MAKKAMIERW KKPKKYKVRE YTRCHICGRP RAVYREFGLC RICFRKLALE GKLPGVRKAS W // ID RS8_THEMA Reviewed; 134 AA. AC Q9ZAE5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 101. DE RecName: Full=30S ribosomal protein S8 {ECO:0000255|HAMAP-Rule:MF_01302}; GN Name=rpsH {ECO:0000255|HAMAP-Rule:MF_01302}; GN OrderedLocusNames=TM_1486; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA central domain where it helps coordinate CC assembly of the platform of the 30S subunit. {ECO:0000255|HAMAP- CC Rule:MF_01302}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S5 CC and S12. {ECO:0000255|HAMAP-Rule:MF_01302}. CC -!- SIMILARITY: Belongs to the ribosomal protein S8P family. CC {ECO:0000255|HAMAP-Rule:MF_01302}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA79791.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79791.1; ALT_INIT; Genomic_DNA. DR EMBL; AE000512; AAD36552.1; -; Genomic_DNA. DR PIR; F72248; F72248. DR RefSeq; NP_229286.1; NC_000853.1. DR RefSeq; WP_004081806.1; NZ_CP011107.1. DR ProteinModelPortal; Q9ZAE5; -. DR SMR; Q9ZAE5; 3-133. DR STRING; 243274.TM1486; -. DR DNASU; 898003; -. DR EnsemblBacteria; AAD36552; AAD36552; TM_1486. DR GeneID; 898003; -. DR KEGG; tma:TM1486; -. DR PATRIC; 23937930; VBITheMar51294_1503. DR eggNOG; ENOG4108UJY; Bacteria. DR eggNOG; COG0096; LUCA. DR InParanoid; Q9ZAE5; -. DR KO; K02994; -. DR OMA; RIYKNTR; -. DR OrthoDB; EOG6Z0QH1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01302_B; Ribosomal_S8_B; 1. DR InterPro; IPR000630; Ribosomal_S8. DR PANTHER; PTHR11758; PTHR11758; 1. DR Pfam; PF00410; Ribosomal_S8; 1. DR SUPFAM; SSF56047; SSF56047; 1. DR PROSITE; PS00053; RIBOSOMAL_S8; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 134 30S ribosomal protein S8. FT /FTId=PRO_0000126509. FT CONFLICT 122 123 QL -> PV (in Ref. 1; CAA79791). FT {ECO:0000305}. SQ SEQUENCE 134 AA; 15289 MW; DABF913F5FF67B78 CRC64; MWSDPIADML TRIRNANMVF KEYTDIPASN LKKKICEILK REGFIADYKY IEDGKQGILR VYLKYKGGRK NRERVIHGIV RVSHAGRRIY VDKDHIPKVK NGLGIAILTT SKGVLTDKEA RQLGVGGEVI AYVW // ID RS17_THEMA Reviewed; 107 AA. AC P38519; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 104. DE RecName: Full=30S ribosomal protein S17 {ECO:0000255|HAMAP-Rule:MF_01345}; GN Name=rpsQ {ECO:0000255|HAMAP-Rule:MF_01345}; GN OrderedLocusNames=TM_1491; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC specifically to the 5'-end of 16S ribosomal RNA. CC {ECO:0000255|HAMAP-Rule:MF_01345}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01345}. CC -!- SIMILARITY: Belongs to the ribosomal protein S17P family. CC {ECO:0000255|HAMAP-Rule:MF_01345}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79786.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36557.1; -; Genomic_DNA. DR PIR; C72249; C72249. DR RefSeq; NP_229291.1; NC_000853.1. DR RefSeq; WP_004081818.1; NZ_CP011107.1. DR ProteinModelPortal; P38519; -. DR SMR; P38519; 4-79. DR STRING; 243274.TM1491; -. DR EnsemblBacteria; AAD36557; AAD36557; TM_1491. DR GeneID; 897479; -. DR KEGG; tma:TM1491; -. DR PATRIC; 23937940; VBITheMar51294_1508. DR eggNOG; ENOG4105K87; Bacteria. DR eggNOG; COG0186; LUCA. DR InParanoid; P38519; -. DR KO; K02961; -. DR OMA; LKAHDEQ; -. DR OrthoDB; EOG63JRH2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_01345_B; Ribosomal_S17_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000266; Ribosomal_S17/S11. DR InterPro; IPR019984; Ribosomal_S17_bac-type. DR InterPro; IPR019979; Ribosomal_S17_CS. DR PANTHER; PTHR10744; PTHR10744; 1. DR Pfam; PF00366; Ribosomal_S17; 1. DR PRINTS; PR00973; RIBOSOMALS17. DR ProDom; PD001295; Ribosomal_S17; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR03635; uS17_bact; 1. DR PROSITE; PS00056; RIBOSOMAL_S17; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 107 30S ribosomal protein S17. FT /FTId=PRO_0000128490. FT CONFLICT 68 68 T -> A (in Ref. 1; CAA79786). FT {ECO:0000305}. SQ SEQUENCE 107 AA; 12598 MW; 58C7216698E6D138 CRC64; MPRKRLTGIV VSDKMDKTVV VAVEKLVQHP LYKKYVKRTK KYHAHDERNE CKIGDVVEIE ETRPLSKTKR WRVVRIIQRF EPERVVKEKE DIQEEIEAVE GKGGVES // ID RS4_THEMA Reviewed; 209 AA. AC Q9X1I3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=30S ribosomal protein S4; GN Name=rpsD; OrderedLocusNames=TM_1473; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA where it nucleates assembly of the body of CC the 30S subunit. {ECO:0000250}. CC -!- FUNCTION: With S5 and S12 plays an important role in translational CC accuracy. {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. CC The interaction surface between S4 and S5 is involved in control CC of translational fidelity (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S4P family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36541.1; -; Genomic_DNA. DR PIR; B72247; B72247. DR RefSeq; NP_229273.1; NC_000853.1. DR RefSeq; WP_004081780.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1I3; -. DR SMR; Q9X1I3; 2-209. DR STRING; 243274.TM1473; -. DR PRIDE; Q9X1I3; -. DR EnsemblBacteria; AAD36541; AAD36541; TM_1473. DR GeneID; 898011; -. DR KEGG; tma:TM1473; -. DR PATRIC; 23937902; VBITheMar51294_1489. DR eggNOG; ENOG4105G6W; Bacteria. DR eggNOG; COG0522; LUCA. DR InParanoid; Q9X1I3; -. DR KO; K02986; -. DR OMA; VYEWITW; -. DR OrthoDB; EOG6N3CXM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1050.10; -; 1. DR Gene3D; 3.10.290.10; -; 1. DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1. DR InterPro; IPR022801; Ribosomal_S4/S9. DR InterPro; IPR001912; Ribosomal_S4/S9_N. DR InterPro; IPR005709; Ribosomal_S4_bac-type. DR InterPro; IPR002942; S4_RNA-bd. DR PANTHER; PTHR11831; PTHR11831; 1. DR Pfam; PF00163; Ribosomal_S4; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM01390; Ribosomal_S4; 1. DR SMART; SM00363; S4; 1. DR TIGRFAMs; TIGR01017; rpsD_bact; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc; KW Zinc-finger. FT CHAIN 1 209 30S ribosomal protein S4. FT /FTId=PRO_0000132481. FT DOMAIN 98 161 S4 RNA-binding. FT ZN_FING 9 31 C4-type. {ECO:0000250}. FT METAL 9 9 Zinc. {ECO:0000250}. FT METAL 12 12 Zinc. {ECO:0000250}. FT METAL 26 26 Zinc. {ECO:0000250}. FT METAL 31 31 Zinc. {ECO:0000250}. SQ SEQUENCE 209 AA; 24721 MW; 441E442403A56721 CRC64; MARYTGPLCK LCRREGMKLY LKGERCYTDK CAFDRRPYAP GQHGQRRTKL TQYGIQLRAK QTVKRIYGIL ERQFERYVEK AMQKAGDTRE NLIQILEARL DNVVYRMGFA INRRQARQLV NHGHFLVNGK KVNIPSYLLR PNDVVEVREK SRDLEVIKKA IEANKERSIV PWIEVDYDNY RGTFLRYPSL EEVTDLPVDL QTVIEFYSR // ID RS19_THEMA Reviewed; 95 AA. AC P38520; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 111. DE RecName: Full=30S ribosomal protein S19; GN Name=rpsS; OrderedLocusNames=TM_1496; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Protein S19 forms a complex with S13 that binds strongly CC to the 16S ribosomal RNA. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S19P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79781.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36562.1; -; Genomic_DNA. DR PIR; H72249; H72249. DR RefSeq; NP_229296.1; NC_000853.1. DR RefSeq; WP_004081828.1; NZ_CP011107.1. DR ProteinModelPortal; P38520; -. DR SMR; P38520; 3-84. DR STRING; 243274.TM1496; -. DR EnsemblBacteria; AAD36562; AAD36562; TM_1496. DR GeneID; 897998; -. DR KEGG; tma:TM1496; -. DR PATRIC; 23937950; VBITheMar51294_1513. DR eggNOG; ENOG4105K7S; Bacteria. DR eggNOG; COG0185; LUCA. DR InParanoid; P38520; -. DR KO; K02965; -. DR OMA; VHNGRQF; -. DR OrthoDB; EOG61S365; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.860.10; -; 1. DR HAMAP; MF_00531; Ribosomal_S19; 1. DR InterPro; IPR002222; Ribosomal_S19. DR InterPro; IPR005732; Ribosomal_S19_bac-type. DR InterPro; IPR020934; Ribosomal_S19_CS. DR InterPro; IPR023575; Ribosomal_S19_SF. DR PANTHER; PTHR11880; PTHR11880; 1. DR Pfam; PF00203; Ribosomal_S19; 1. DR PIRSF; PIRSF002144; Ribosomal_S19; 1. DR PRINTS; PR00975; RIBOSOMALS19. DR SUPFAM; SSF54570; SSF54570; 1. DR TIGRFAMs; TIGR01050; rpsS_bact; 1. DR PROSITE; PS00323; RIBOSOMAL_S19; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 95 30S ribosomal protein S19. FT /FTId=PRO_0000129925. FT CONFLICT 43 44 EM -> KW (in Ref. 1; CAA79781). FT {ECO:0000305}. FT CONFLICT 48 48 T -> G (in Ref. 1; CAA79781). FT {ECO:0000305}. SQ SEQUENCE 95 AA; 10889 MW; 18FD96DB6A64B252 CRC64; MGRSRKKGPY VDRKLLEKIR KLNETGEKKV IKTWSRASMI IPEMVGHTIA VYNGMKHIPV YITENMIGHR LGEFAPTRRF GGHADKKAKK GELKK // ID RS20_THEMA Reviewed; 96 AA. AC Q9X1Y7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=30S ribosomal protein S20 {ECO:0000255|HAMAP-Rule:MF_00500}; GN Name=rpsT {ECO:0000255|HAMAP-Rule:MF_00500}; GN OrderedLocusNames=TM_1657; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds directly to 16S ribosomal RNA. {ECO:0000255|HAMAP- CC Rule:MF_00500}. CC -!- SIMILARITY: Belongs to the ribosomal protein S20P family. CC {ECO:0000255|HAMAP-Rule:MF_00500}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36724.1; -; Genomic_DNA. DR PIR; F72228; F72228. DR RefSeq; NP_229457.1; NC_000853.1. DR RefSeq; WP_004082168.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1Y7; -. DR STRING; 243274.TM1657; -. DR EnsemblBacteria; AAD36724; AAD36724; TM_1657. DR GeneID; 896901; -. DR KEGG; tma:TM1657; -. DR PATRIC; 23938288; VBITheMar51294_1676. DR eggNOG; ENOG410857I; Bacteria. DR eggNOG; COG0268; LUCA. DR InParanoid; Q9X1Y7; -. DR KO; K02968; -. DR OMA; PNIKSAM; -. DR OrthoDB; EOG6HMXNQ; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.58.110; -; 1. DR HAMAP; MF_00500; Ribosomal_S20; 1. DR InterPro; IPR002583; Ribosomal_S20. DR Pfam; PF01649; Ribosomal_S20p; 1. DR ProDom; PD004231; Ribosomal_S20; 1. DR SUPFAM; SSF46992; SSF46992; 1. DR TIGRFAMs; TIGR00029; S20; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 96 30S ribosomal protein S20. FT /FTId=PRO_0000168048. SQ SEQUENCE 96 AA; 11292 MW; D5D9758D69D21A42 CRC64; MPNIKSAKKR VRVSEKRRLR NKAYKTFFKN RIKEVLKAIE NKEPKEVVLE LTRKAQAAID KAVSKGVIHK NQGARRKARL FEKVNEYLRT LETTQE // ID RS7_THEMA Reviewed; 155 AA. AC P38526; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 112. DE RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480}; GN Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480}; GN OrderedLocusNames=TM_1504; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-155. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1920450; DOI=10.1007/BF02193628; RA Tiboni O., Cantoni R., Creti R., Cammarano P., Sanangelantoni A.M.; RT "Phylogenetic depth of Thermotoga maritima inferred from analysis of RT the fus gene: amino acid sequence of elongation factor G and RT organization of the Thermotoga str operon."; RL J. Mol. Evol. 33:142-151(1991). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA where it nucleates assembly of the head CC domain of the 30S subunit. Is located at the subunit interface CC close to the decoding center, probably blocks exit of the E-site CC tRNA. {ECO:0000255|HAMAP-Rule:MF_00480}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S9 CC and S11. {ECO:0000255|HAMAP-Rule:MF_00480}. CC -!- INTERACTION: CC Q9WZF8:tig; NbExp=5; IntAct=EBI-2463521, EBI-2463534; CC -!- SIMILARITY: Belongs to the ribosomal protein S7P family. CC {ECO:0000255|HAMAP-Rule:MF_00480}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36571.1; -; Genomic_DNA. DR EMBL; S57688; AAB19928.1; -; Genomic_DNA. DR PIR; A72244; A72244. DR RefSeq; NP_229304.1; NC_000853.1. DR RefSeq; WP_004081843.1; NZ_CP011107.1. DR PDB; 3GTY; X-ray; 3.40 A; S=9-155. DR PDBsum; 3GTY; -. DR ProteinModelPortal; P38526; -. DR SMR; P38526; 9-147. DR IntAct; P38526; 1. DR STRING; 243274.TM1504; -. DR DNASU; 897994; -. DR EnsemblBacteria; AAD36571; AAD36571; TM_1504. DR GeneID; 897994; -. DR KEGG; tma:TM1504; -. DR PATRIC; 23937966; VBITheMar51294_1521. DR eggNOG; ENOG4108UHY; Bacteria. DR eggNOG; COG0049; LUCA. DR InParanoid; P38526; -. DR KO; K02992; -. DR OMA; TKFVNHL; -. DR OrthoDB; EOG6P5ZKW; -. DR EvolutionaryTrace; P38526; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 1.10.455.10; -; 1. DR HAMAP; MF_00480_B; Ribosomal_S7_B; 1. DR InterPro; IPR000235; Ribosomal_S5/S7. DR InterPro; IPR005717; Ribosomal_S7_bac/org-type. DR InterPro; IPR020606; Ribosomal_S7_CS. DR InterPro; IPR023798; Ribosomal_S7_dom. DR PANTHER; PTHR11205; PTHR11205; 1. DR Pfam; PF00177; Ribosomal_S7; 1. DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1. DR SUPFAM; SSF47973; SSF47973; 1. DR TIGRFAMs; TIGR01029; rpsG_bact; 1. DR PROSITE; PS00052; RIBOSOMAL_S7; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; KW tRNA-binding. FT CHAIN 1 155 30S ribosomal protein S7. FT /FTId=PRO_0000124367. FT CONFLICT 105 105 E -> Q (in Ref. 2; AAB19928). FT {ECO:0000305}. FT STRAND 15 17 {ECO:0000244|PDB:3GTY}. FT HELIX 20 29 {ECO:0000244|PDB:3GTY}. FT TURN 35 37 {ECO:0000244|PDB:3GTY}. FT HELIX 38 51 {ECO:0000244|PDB:3GTY}. FT HELIX 57 68 {ECO:0000244|PDB:3GTY}. FT STRAND 71 77 {ECO:0000244|PDB:3GTY}. FT STRAND 79 82 {ECO:0000244|PDB:3GTY}. FT STRAND 84 89 {ECO:0000244|PDB:3GTY}. FT HELIX 93 108 {ECO:0000244|PDB:3GTY}. FT STRAND 111 113 {ECO:0000244|PDB:3GTY}. FT HELIX 115 127 {ECO:0000244|PDB:3GTY}. FT HELIX 132 144 {ECO:0000244|PDB:3GTY}. FT HELIX 148 150 {ECO:0000244|PDB:3GTY}. SQ SEQUENCE 155 AA; 17988 MW; DB52CB3AF8F942E1 CRC64; MRRRRAEKRQ IPPDPVFGDV LVAKLINRVM WDGKKTIAQK IVYGAFDIIR EKTKKDPLEV FRQAVENVKP VLEVRPRRVG GATYQVPIEV QEPRRTSLAL RWIVEAARAK KGRPMKEKLA EEIIAAYNNT GTAIKKKEDT HRMAEANRAF AHYRW // ID RSGA_THEMA Reviewed; 295 AA. AC Q9X242; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 105. DE RecName: Full=Putative ribosome biogenesis GTPase RsgA {ECO:0000255|HAMAP-Rule:MF_01820}; DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01820}; GN Name=rsgA {ECO:0000255|HAMAP-Rule:MF_01820}; Synonyms=yjeQ; GN OrderedLocusNames=TM_1717; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GDP AND ZINC RP IONS, AND PROBABLE SUBUNIT. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=15331784; DOI=10.1073/pnas.0405202101; RA Shin D.H., Lou Y., Jancarik J., Yokota H., Kim R., Kim S.-H.; RT "Crystal structure of YjeQ from Thermotoga maritima contains a RT circularly permuted GTPase domain."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13198-13203(2004). CC -!- FUNCTION: May play a role in 30S ribosomal subunit biogenesis. CC Unusual circulary permuted GTPase that catalyzes rapid hydrolysis CC of GTP with a slow catalytic turnover. {ECO:0000255|HAMAP- CC Rule:MF_01820}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:15331784}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:15331784}; CC -!- SUBUNIT: Monomer. Associates with ribosomes. {ECO:0000255|HAMAP- CC Rule:MF_01820, ECO:0000305|PubMed:15331784}. CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. CC RsgA subfamily. {ECO:0000255|HAMAP-Rule:MF_01820}. CC -!- SIMILARITY: Contains 1 CP-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01058}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36783.1; -; Genomic_DNA. DR PIR; A72219; A72219. DR RefSeq; NP_229516.1; NC_000853.1. DR RefSeq; WP_010865389.1; NC_000853.1. DR PDB; 1U0L; X-ray; 2.80 A; A/B/C=1-295. DR PDBsum; 1U0L; -. DR ProteinModelPortal; Q9X242; -. DR SMR; Q9X242; 3-293. DR STRING; 243274.TM1717; -. DR EnsemblBacteria; AAD36783; AAD36783; TM_1717. DR GeneID; 897880; -. DR KEGG; tma:TM1717; -. DR KEGG; tmi:THEMA_05655; -. DR PATRIC; 23938410; VBITheMar51294_1735. DR eggNOG; ENOG4105E06; Bacteria. DR eggNOG; COG1162; LUCA. DR InParanoid; Q9X242; -. DR KO; K06949; -. DR OMA; PIICITK; -. DR OrthoDB; EOG69SKDD; -. DR BioCyc; TMAR243274:GC6P-1765-MONOMER; -. DR EvolutionaryTrace; Q9X242; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01820; GTPase_RsgA; 1. DR InterPro; IPR030378; G_CP_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA. DR InterPro; IPR010914; RsgA_GTPase_dom. DR InterPro; IPR031944; RsgA_N. DR Pfam; PF03193; DUF258; 1. DR Pfam; PF16745; RsgA_N; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00157; TIGR00157; 1. DR PROSITE; PS50936; ENGC_GTPASE; 1. DR PROSITE; PS51721; G_CP; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; GTP-binding; Hydrolase; KW Metal-binding; Nucleotide-binding; Reference proteome; Zinc. FT CHAIN 1 295 Putative ribosome biogenesis GTPase RsgA. FT /FTId=PRO_0000171536. FT DOMAIN 68 228 CP-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01058}. FT NP_BIND 117 120 GTP. {ECO:0000255|HAMAP-Rule:MF_01820, FT ECO:0000305|PubMed:15331784}. FT NP_BIND 170 178 GTP. {ECO:0000255|HAMAP-Rule:MF_01820, FT ECO:0000305|PubMed:15331784}. FT MOTIF 250 263 Knuckle-like cysteine cluster. FT {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 250 250 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820, FT ECO:0000269|PubMed:15331784}. FT METAL 255 255 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820, FT ECO:0000269|PubMed:15331784}. FT METAL 257 257 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820, FT ECO:0000269|PubMed:15331784}. FT METAL 263 263 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820, FT ECO:0000269|PubMed:15331784}. FT STRAND 5 13 {ECO:0000244|PDB:1U0L}. FT STRAND 16 21 {ECO:0000244|PDB:1U0L}. FT TURN 22 24 {ECO:0000244|PDB:1U0L}. FT STRAND 27 32 {ECO:0000244|PDB:1U0L}. FT HELIX 34 36 {ECO:0000244|PDB:1U0L}. FT TURN 37 40 {ECO:0000244|PDB:1U0L}. FT STRAND 48 52 {ECO:0000244|PDB:1U0L}. FT STRAND 56 64 {ECO:0000244|PDB:1U0L}. FT TURN 72 75 {ECO:0000244|PDB:1U0L}. FT STRAND 76 78 {ECO:0000244|PDB:1U0L}. FT STRAND 81 86 {ECO:0000244|PDB:1U0L}. FT HELIX 95 107 {ECO:0000244|PDB:1U0L}. FT STRAND 111 116 {ECO:0000244|PDB:1U0L}. FT HELIX 119 121 {ECO:0000244|PDB:1U0L}. FT HELIX 124 137 {ECO:0000244|PDB:1U0L}. FT TURN 138 140 {ECO:0000244|PDB:1U0L}. FT STRAND 143 145 {ECO:0000244|PDB:1U0L}. FT TURN 148 150 {ECO:0000244|PDB:1U0L}. FT HELIX 154 161 {ECO:0000244|PDB:1U0L}. FT STRAND 162 169 {ECO:0000244|PDB:1U0L}. FT HELIX 176 183 {ECO:0000244|PDB:1U0L}. FT STRAND 210 212 {ECO:0000244|PDB:1U0L}. FT STRAND 218 222 {ECO:0000244|PDB:1U0L}. FT HELIX 235 238 {ECO:0000244|PDB:1U0L}. FT HELIX 239 241 {ECO:0000244|PDB:1U0L}. FT STRAND 245 247 {ECO:0000244|PDB:1U0L}. FT STRAND 257 259 {ECO:0000244|PDB:1U0L}. FT HELIX 264 271 {ECO:0000244|PDB:1U0L}. FT HELIX 276 290 {ECO:0000244|PDB:1U0L}. SQ SEQUENCE 295 AA; 33642 MW; E8A9E7396C855848 CRC64; MNLRRRGIVV SFHSNMVTVE DEETGERILC KLRGKFRLQN LKIYVGDRVE YTPDETGSGV IENVLHRKNL LTKPHVANVD QVILVVTVKM PETSTYIIDK FLVLAEKNEL ETVMVINKMD LYDEDDLRKV RELEEIYSGL YPIVKTSAKT GMGIEELKEY LKGKISTMAG LSGVGKSSLL NAINPGLKLR VSEVSEKLQR GRHTTTTAQL LKFDFGGYVV DTPGFANLEI NDIEPEELKH YFKEFGDKQC FFSDCNHVDE PECGVKEAVE NGEIAESRYE NYVKMFYELL GRRKK // ID RSMG_THEMA Reviewed; 238 AA. AC Q9WZG6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074}; DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00074}; DE AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074}; DE Short=16S rRNA m7G methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074}; GN Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; GN OrderedLocusNames=TM_0707; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Specifically methylates the N7 position of a guanine in CC 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00074}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA CC methyltransferase RsmG family. {ECO:0000255|HAMAP-Rule:MF_00074}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35789.1; -; Genomic_DNA. DR PIR; B72343; B72343. DR RefSeq; NP_228516.1; NC_000853.1. DR RefSeq; WP_010865189.1; NC_000853.1. DR ProteinModelPortal; Q9WZG6; -. DR STRING; 243274.TM0707; -. DR EnsemblBacteria; AAD35789; AAD35789; TM_0707. DR GeneID; 898374; -. DR KEGG; tma:TM0707; -. DR KEGG; tmi:THEMA_01130; -. DR PATRIC; 23936332; VBITheMar51294_0719. DR eggNOG; ENOG4107YBR; Bacteria. DR eggNOG; COG0357; LUCA. DR InParanoid; Q9WZG6; -. DR KO; K03501; -. DR OMA; DSAVHKN; -. DR OrthoDB; EOG6HF639; -. DR BioCyc; TMAR243274:GC6P-733-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00074; 16SrRNA_methyltr_G; 1. DR InterPro; IPR003682; rRNA_ssu_MeTfrase_G. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02527; GidB; 1. DR PIRSF; PIRSF003078; GidB; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00138; rsmG_gidB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 238 Ribosomal RNA small subunit FT methyltransferase G. FT /FTId=PRO_0000184356. FT REGION 131 132 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00074}. FT BINDING 80 80 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00074}. FT BINDING 148 148 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00074}. SQ SEQUENCE 238 AA; 27235 MW; 5362759372B953D6 CRC64; MLEFSSEVSL LDSVKNILLE YGLRFQEPQI EKVDKYIEEL LGVPYNLTAH RDLDSAVHKN VVEILLPLKE ELKGTLLDVG SGNGVPGLIL AIFFSKLKVV LLDSREKSVN FLRGVIEKLD LENVSVVKER AENFSKERRE EFDYVTARAV ARLNVLVEIC TPALKTGGKL LFYKGPSYIE ELKEAQRAMK ELKVELEKVR EYSLKTGERR ALLILRKYES SPEKYPRRVG VPFKRPLL // ID RS2_THEMA Reviewed; 262 AA. AC Q9WZM1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=30S ribosomal protein S2; GN Name=rpsB; OrderedLocusNames=TM_0762; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ribosomal protein S2P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35844.1; -; Genomic_DNA. DR PIR; H72335; H72335. DR RefSeq; NP_228571.1; NC_000853.1. DR RefSeq; WP_004080936.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZM1; -. DR SMR; Q9WZM1; 6-230. DR STRING; 243274.TM0762; -. DR EnsemblBacteria; AAD35844; AAD35844; TM_0762. DR GeneID; 898430; -. DR KEGG; tma:TM0762; -. DR PATRIC; 23936446; VBITheMar51294_0775. DR eggNOG; ENOG4105CE9; Bacteria. DR eggNOG; COG0052; LUCA. DR InParanoid; Q9WZM1; -. DR KO; K02967; -. DR OMA; RIPDILY; -. DR OrthoDB; EOG6XWV6P; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR HAMAP; MF_00291_B; Ribosomal_S2_B; 1. DR InterPro; IPR001865; Ribosomal_S2. DR InterPro; IPR005706; Ribosomal_S2_bac/mit/plastid. DR InterPro; IPR018130; Ribosomal_S2_CS. DR InterPro; IPR023591; Ribosomal_S2_flav_dom. DR PANTHER; PTHR12534; PTHR12534; 1. DR Pfam; PF00318; Ribosomal_S2; 1. DR PRINTS; PR00395; RIBOSOMALS2. DR SUPFAM; SSF52313; SSF52313; 1. DR TIGRFAMs; TIGR01011; rpsB_bact; 1. DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 262 30S ribosomal protein S2. FT /FTId=PRO_0000134262. SQ SEQUENCE 262 AA; 29906 MW; D06514E3804E0734 CRC64; MPVVTMKQLL EAGVHFGHRT RRWNPKMAPY IYTERKGIYI IDLQKTQQLL EEAYYFVREK ASEGATILFV GTKKQAQGVI KAEAERCGAF YVNNRWLGGL LTNFKTIRSR IDKLIELEEM EQSGKLEELP KKEQSRIRRV LEKLRKNLGG LKEMRRLPDI IYIVDPRKEK IAVAEANKLG IPIVAIVDTN CDPDPIDYVI PGNDDAIRSI KLITSVIADA YLEGREGAPL TAEKEETESA EETSEEVTED INLEELEEEE EV // ID RS3_THEMA Reviewed; 209 AA. AC P46772; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 117. DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309}; GN Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; GN OrderedLocusNames=TM_1494; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8002596; RA Sanangelantoni A.M., Bocchetta M., Cammarano P., Tiboni O.; RT "Phylogenetic depth of S10 and spc operons: cloning and sequencing of RT a ribosomal protein gene cluster from the extremely thermophilic RT bacterium Thermotoga maritima."; RL J. Bacteriol. 176:7703-7710(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA CC in the 70S ribosome, positioning it for translation. CC {ECO:0000255|HAMAP-Rule:MF_01309}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight complex CC with proteins S10 and S14. {ECO:0000255|HAMAP-Rule:MF_01309}. CC -!- SIMILARITY: Belongs to the ribosomal protein S3P family. CC {ECO:0000255|HAMAP-Rule:MF_01309}. CC -!- SIMILARITY: Contains 1 KH type-2 domain. {ECO:0000255|HAMAP- CC Rule:MF_01309}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21677; CAA79783.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36560.1; -; Genomic_DNA. DR PIR; S40194; S40194. DR RefSeq; NP_229294.1; NC_000853.1. DR RefSeq; WP_010865350.1; NZ_CP011107.1. DR ProteinModelPortal; P46772; -. DR SMR; P46772; 2-206. DR STRING; 243274.TM1494; -. DR PRIDE; P46772; -. DR EnsemblBacteria; AAD36560; AAD36560; TM_1494. DR GeneID; 897999; -. DR KEGG; tma:TM1494; -. DR PATRIC; 23937946; VBITheMar51294_1511. DR eggNOG; ENOG4105CKE; Bacteria. DR eggNOG; COG0092; LUCA. DR InParanoid; P46772; -. DR KO; K02982; -. DR OMA; KTNPIGN; -. DR OrthoDB; EOG6K13X3; -. DR BioCyc; TMAR243274:GC6P-1534-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1140.32; -; 1. DR Gene3D; 3.30.300.20; -; 1. DR HAMAP; MF_01309_B; Ribosomal_S3_B; 1. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR004044; KH_dom_type_2. DR InterPro; IPR009019; KH_prok-type. DR InterPro; IPR005704; Ribosomal_S3_bac. DR InterPro; IPR001351; Ribosomal_S3_C. DR InterPro; IPR018280; Ribosomal_S3_CS. DR Pfam; PF07650; KH_2; 1. DR SMART; SM00322; KH; 1. DR SUPFAM; SSF54814; SSF54814; 1. DR SUPFAM; SSF54821; SSF54821; 1. DR TIGRFAMs; TIGR01009; rpsC_bact; 1. DR PROSITE; PS50823; KH_TYPE_2; 1. DR PROSITE; PS00548; RIBOSOMAL_S3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 209 30S ribosomal protein S3. FT /FTId=PRO_0000130221. FT DOMAIN 38 107 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_01309}. SQ SEQUENCE 209 AA; 24076 MW; C6CB9DFC28305493 CRC64; MGQKVHPRGF RLGLSADWQA KWFNEKNYKE WLLEDEEIRK IIKNKYYHAG ISEIYVERPD AERINITVKT ARPGIIIGRK GSEITSLREE LERKFNRRVV INIEEIKTPE LDAQLVAESI ASRIEKRASY KVAMKRAIMN AMRKGAQGIK VMVAGRLGGA EIARREWYLR GRLPLQKIKA IIDYGTATAW TKYGTIGIKV WIYKGDADI // ID RS5_THEMA Reviewed; 178 AA. AC Q9X1J2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307}; GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; GN OrderedLocusNames=TM_1483; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: With S4 and S12 plays an important role in translational CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}. CC -!- FUNCTION: Located at the back of the 30S subunit body where it CC stabilizes the conformation of the head with respect to the body. CC {ECO:0000255|HAMAP-Rule:MF_01307}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S4 CC and S8. {ECO:0000255|HAMAP-Rule:MF_01307}. CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S CC subunit; the C-terminal domain interacts with the body and CC contacts protein S4. The interaction surface between S4 and S5 is CC involved in control of translational fidelity. CC -!- SIMILARITY: Belongs to the ribosomal protein S5P family. CC {ECO:0000255|HAMAP-Rule:MF_01307}. CC -!- SIMILARITY: Contains 1 S5 DRBM domain. {ECO:0000255|HAMAP- CC Rule:MF_01307}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36549.1; -; Genomic_DNA. DR PIR; C72248; C72248. DR RefSeq; NP_229283.1; NC_000853.1. DR RefSeq; WP_004081800.1; NC_000853.1. DR ProteinModelPortal; Q9X1J2; -. DR SMR; Q9X1J2; 14-162. DR STRING; 243274.TM1483; -. DR EnsemblBacteria; AAD36549; AAD36549; TM_1483. DR GeneID; 898005; -. DR KEGG; tma:TM1483; -. DR PATRIC; 23937924; VBITheMar51294_1500. DR eggNOG; ENOG4108RA9; Bacteria. DR eggNOG; COG0098; LUCA. DR InParanoid; Q9X1J2; -. DR KO; K02988; -. DR OMA; PHEQKGK; -. DR OrthoDB; EOG6FJNM5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.160.20; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_01307_B; Ribosomal_S5_B; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR000851; Ribosomal_S5. DR InterPro; IPR005712; Ribosomal_S5_bac-type. DR InterPro; IPR005324; Ribosomal_S5_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR013810; Ribosomal_S5_N. DR InterPro; IPR018192; Ribosomal_S5_N_CS. DR PANTHER; PTHR13718; PTHR13718; 1. DR Pfam; PF00333; Ribosomal_S5; 1. DR Pfam; PF03719; Ribosomal_S5_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR01021; rpsE_bact; 1. DR PROSITE; PS00585; RIBOSOMAL_S5; 1. DR PROSITE; PS50881; S5_DSRBD; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 178 30S ribosomal protein S5. FT /FTId=PRO_0000131619. FT DOMAIN 15 78 S5 DRBM. {ECO:0000255|HAMAP- FT Rule:MF_01307}. SQ SEQUENCE 178 AA; 19125 MW; E7153790C3DAE18F CRC64; METQGVMKEI QYEEFEEKII EIRRTSKVTK GGKNLSFRVV AIVGNKNGKV GLGIGKAREV PEAIRKAISA AKRNIVEVPV INGTIPHEVI GRQDASKVLL KPAAPGTGII AGGTVRAVVE LAGIQNILTK SLGSTNPLNL ALATMNGLKN LLDPRKVAKL RDISVEEVFK GVRRENNA // ID RS6_THEMA Reviewed; 128 AA. AC Q9WZ72; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=30S ribosomal protein S6; GN Name=rpsF; OrderedLocusNames=TM_0603; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds together with S18 to 16S ribosomal RNA. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S6P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35688.1; -; Genomic_DNA. DR PIR; G72354; G72354. DR RefSeq; NP_228413.1; NC_000853.1. DR RefSeq; WP_004081227.1; NZ_CP011107.1. DR PDB; 1VMB; X-ray; 1.70 A; A=1-128. DR PDBsum; 1VMB; -. DR ProteinModelPortal; Q9WZ72; -. DR SMR; Q9WZ72; 5-111. DR STRING; 243274.TM0603; -. DR EnsemblBacteria; AAD35688; AAD35688; TM_0603. DR GeneID; 897684; -. DR KEGG; tma:TM0603; -. DR PATRIC; 23936121; VBITheMar51294_0614. DR eggNOG; ENOG41083EQ; Bacteria. DR eggNOG; COG0360; LUCA. DR InParanoid; Q9WZ72; -. DR KO; K02990; -. DR OMA; IDKVERM; -. DR OrthoDB; EOG6P33DH; -. DR EvolutionaryTrace; Q9WZ72; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.60; -; 1. DR HAMAP; MF_00360; Ribosomal_S6; 1. DR InterPro; IPR000529; Ribosomal_S6. DR InterPro; IPR020814; Ribosomal_S6_plastid/chlpt. DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6. DR Pfam; PF01250; Ribosomal_S6; 1. DR SUPFAM; SSF54995; SSF54995; 1. DR TIGRFAMs; TIGR00166; S6; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 128 30S ribosomal protein S6. FT /FTId=PRO_0000176861. FT STRAND 7 15 {ECO:0000244|PDB:1VMB}. FT HELIX 21 37 {ECO:0000244|PDB:1VMB}. FT STRAND 42 58 {ECO:0000244|PDB:1VMB}. FT STRAND 61 73 {ECO:0000244|PDB:1VMB}. FT STRAND 75 77 {ECO:0000244|PDB:1VMB}. FT HELIX 79 86 {ECO:0000244|PDB:1VMB}. FT STRAND 91 98 {ECO:0000244|PDB:1VMB}. FT HELIX 100 110 {ECO:0000244|PDB:1VMB}. SQ SEQUENCE 128 AA; 15369 MW; A151E99D8BFF7A48 CRC64; MAYVKERIYE SMFIIAPNVP EEERENLVER VKKIIEERVK GKIDKVERMG MRKFAYEIKK FNEGDYTVIY FRCDGQNLQE LENFYRVTPE IIRWQTFRRF DLEKKERKAQ REKAAAEATE SSEGGSED // ID RSMA_THEMA Reviewed; 279 AA. AC Q9X1F1; DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000255|HAMAP-Rule:MF_00607}; DE EC=2.1.1.182 {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethylase {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607}; GN Name=rsmA {ECO:0000255|HAMAP-Rule:MF_00607}; GN Synonyms=ksgA {ECO:0000255|HAMAP-Rule:MF_00607}; GN OrderedLocusNames=TM_1437; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 CC and A1519) in the loop of a conserved hairpin near the 3'-end of CC 16S rRNA in the 30S particle. May play a critical role in CC biogenesis of 30S subunits. {ECO:0000255|HAMAP-Rule:MF_00607}. CC -!- CATALYTIC ACTIVITY: 4 S-adenosyl-L-methionine + CC adenine(1518)/adenine(1519) in 16S rRNA = 4 S-adenosyl-L- CC homocysteine + N(6)-dimethyladenine(1518)/N(6)- CC dimethyladenine(1519) in 16S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00607}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00607}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. rRNA adenine N(6)-methyltransferase CC family. RsmA subfamily. {ECO:0000255|HAMAP-Rule:MF_00607}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36507.1; -; Genomic_DNA. DR PIR; B72255; B72255. DR RefSeq; NP_229237.1; NC_000853.1. DR RefSeq; WP_010865342.1; NC_000853.1. DR ProteinModelPortal; Q9X1F1; -. DR STRING; 243274.TM1437; -. DR DNASU; 898038; -. DR EnsemblBacteria; AAD36507; AAD36507; TM_1437. DR GeneID; 898038; -. DR KEGG; tma:TM1437; -. DR PATRIC; 23937822; VBITheMar51294_1449. DR eggNOG; ENOG4105D1X; Bacteria. DR eggNOG; COG0030; LUCA. DR InParanoid; Q9X1F1; -. DR KO; K02528; -. DR OMA; HYPGRLE; -. DR OrthoDB; EOG66F08Z; -. DR BioCyc; TMAR243274:GC6P-1475-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052908; F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:InterPro. DR Gene3D; 1.10.8.100; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1. DR InterPro; IPR001737; KsgA/Erm. DR InterPro; IPR023165; rRNA_Ade_diMease-like. DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS. DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N. DR InterPro; IPR011530; rRNA_adenine_dimethylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR11727; PTHR11727; 1. DR Pfam; PF00398; RrnaAD; 1. DR SMART; SM00650; rADc; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00755; ksgA; 1. DR PROSITE; PS01131; RRNA_A_DIMETH; 1. DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 279 Ribosomal RNA small subunit FT methyltransferase A. FT /FTId=PRO_0000101629. FT BINDING 42 42 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 67 67 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 88 88 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. FT BINDING 113 113 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. FT BINDING 129 129 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. SQ SEQUENCE 279 AA; 31814 MW; D321CCAE0D0BC6E4 CRC64; MDGCHLSRDK LQGDGEGCDL KTSDYLKKYG VRLKKHLGQV FLSDDRIAKR IVKAAELTPE DVVVEIGAGA GTLTEELAKT GARVIAYEID ESLAPILQER LSKYPNVELR FEDFLKAKNV PEGAICVSNI PYNITGPLME KIIEWKFKRA IVMIQKEVGE RILAKPGKKT YGYLSVVVQT FYEVKKLFDV SRSCFVPNPE VDSTVVDLKR KPVDLDFEKF KKFVSMIFAK KRKTLKNNLR PFLSIFEGVD LSRRAEQLTV EEIVELYEKW RRALECSRG // ID RS9_THEMA Reviewed; 134 AA. AC Q9X1G4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=30S ribosomal protein S9; GN Name=rpsI; OrderedLocusNames=TM_1453; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ribosomal protein S9P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36521.1; -; Genomic_DNA. DR PIR; F72250; F72250. DR RefSeq; NP_229252.1; NC_000853.1. DR RefSeq; WP_004081735.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1G4; -. DR SMR; Q9X1G4; 7-134. DR STRING; 243274.TM1453; -. DR EnsemblBacteria; AAD36521; AAD36521; TM_1453. DR GeneID; 898023; -. DR KEGG; tma:TM1453; -. DR PATRIC; 23937858; VBITheMar51294_1467. DR eggNOG; ENOG4108UJD; Bacteria. DR eggNOG; COG0103; LUCA. DR InParanoid; Q9X1G4; -. DR KO; K02996; -. DR OMA; IKQGAAR; -. DR OrthoDB; EOG6MWNH0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_00532_B; Ribosomal_S9_B; 1. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR000754; Ribosomal_S9. DR InterPro; IPR023035; Ribosomal_S9_bac/plastid. DR InterPro; IPR020574; Ribosomal_S9_CS. DR PANTHER; PTHR21569; PTHR21569; 1. DR Pfam; PF00380; Ribosomal_S9; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR PROSITE; PS00360; RIBOSOMAL_S9; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 134 30S ribosomal protein S9. FT /FTId=PRO_0000111429. SQ SEQUENCE 134 AA; 15198 MW; 698FB55B73E0A539 CRC64; MAEVVGYYGT GRRKTAVARV YLRPGEGKVK VNGKEYESLN DYFKNPAWTK HAIEPLEVTN TLGKFDLVIR VNGGGLSGQS GAVRLGIARA LLQYDQNLRP VLKKYKMLTR DPREVERKKY GLKKARRAPQ FSKR // ID RSMH_THEMA Reviewed; 299 AA. AC Q9WZX6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 118. DE RecName: Full=Ribosomal RNA small subunit methyltransferase H {ECO:0000255|HAMAP-Rule:MF_01007}; DE EC=2.1.1.199 {ECO:0000255|HAMAP-Rule:MF_01007}; DE AltName: Full=16S rRNA m(4)C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01007}; DE AltName: Full=rRNA (cytosine-N(4)-)-methyltransferase RsmH {ECO:0000255|HAMAP-Rule:MF_01007}; GN Name=rsmH {ECO:0000255|HAMAP-Rule:MF_01007}; Synonyms=mraW; GN OrderedLocusNames=TM_0872; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH RP S-ADENOSYL-L-METHIONINE AND S-ADENOSYL-L-HOMOCYSTEINE. RX PubMed=12824489; DOI=10.1110/ps.0302403; RA Miller D.J., Ouellette N., Evdokimova E., Savchenko A., Edwards A., RA Anderson W.F.; RT "Crystal complexes of a predicted S-adenosylmethionine-dependent RT methyltransferase reveal a typical AdoMet binding domain and a RT substrate recognition domain."; RL Protein Sci. 12:1432-1442(2003). CC -!- FUNCTION: Specifically methylates the N4 position of cytidine in CC position 1402 (C1402) of 16S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_01007}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(1402) in CC 16S rRNA = S-adenosyl-L-homocysteine + N(4)-methylcytosine(1402) CC in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01007}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01007}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH CC family. {ECO:0000255|HAMAP-Rule:MF_01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35954.1; -; Genomic_DNA. DR PIR; C72323; C72323. DR RefSeq; NP_228681.1; NC_000853.1. DR RefSeq; WP_004080729.1; NZ_CP011107.1. DR PDB; 1M6Y; X-ray; 1.90 A; A/B=1-299. DR PDB; 1N2X; X-ray; 1.90 A; A/B=1-299. DR PDBsum; 1M6Y; -. DR PDBsum; 1N2X; -. DR ProteinModelPortal; Q9WZX6; -. DR SMR; Q9WZX6; 2-294. DR STRING; 243274.TM0872; -. DR EnsemblBacteria; AAD35954; AAD35954; TM_0872. DR GeneID; 898545; -. DR KEGG; tma:TM0872; -. DR PATRIC; 23936672; VBITheMar51294_0885. DR eggNOG; ENOG4105CGJ; Bacteria. DR eggNOG; COG0275; LUCA. DR InParanoid; Q9WZX6; -. DR KO; K03438; -. DR OMA; HVPVMLQ; -. DR OrthoDB; EOG6X9MQ1; -. DR EvolutionaryTrace; Q9WZX6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central. DR Gene3D; 1.10.150.170; -; 1. DR Gene3D; 3.40.50.150; -; 2. DR HAMAP; MF_01007; 16SrRNA_methyltr_H; 1. DR InterPro; IPR002903; RsmH. DR InterPro; IPR023397; SAM-dep_MeTrfase_MraW_recog. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR11265; PTHR11265; 1. DR Pfam; PF01795; Methyltransf_5; 1. DR PIRSF; PIRSF004486; MraW; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR SUPFAM; SSF81799; SSF81799; 1. DR TIGRFAMs; TIGR00006; TIGR00006; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW Reference proteome; rRNA processing; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 299 Ribosomal RNA small subunit FT methyltransferase H. FT /FTId=PRO_0000108732. FT REGION 36 38 S-adenosyl-L-methionine binding. FT {ECO:0000269|PubMed:12824489}. FT BINDING 55 55 S-adenosyl-L-methionine. FT {ECO:0000269|PubMed:12824489}. FT BINDING 82 82 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000269|PubMed:12824489}. FT BINDING 103 103 S-adenosyl-L-methionine. FT {ECO:0000269|PubMed:12824489}. FT BINDING 110 110 S-adenosyl-L-methionine. FT {ECO:0000269|PubMed:12824489}. FT HELIX 13 20 {ECO:0000244|PDB:1M6Y}. FT STRAND 27 30 {ECO:0000244|PDB:1M6Y}. FT HELIX 37 45 {ECO:0000244|PDB:1M6Y}. FT STRAND 50 56 {ECO:0000244|PDB:1M6Y}. FT HELIX 58 67 {ECO:0000244|PDB:1M6Y}. FT HELIX 69 71 {ECO:0000244|PDB:1M6Y}. FT TURN 72 74 {ECO:0000244|PDB:1M6Y}. FT STRAND 75 79 {ECO:0000244|PDB:1M6Y}. FT HELIX 82 84 {ECO:0000244|PDB:1M6Y}. FT HELIX 85 91 {ECO:0000244|PDB:1M6Y}. FT STRAND 97 103 {ECO:0000244|PDB:1M6Y}. FT HELIX 108 112 {ECO:0000244|PDB:1M6Y}. FT STRAND 118 122 {ECO:0000244|PDB:1M6Y}. FT HELIX 138 144 {ECO:0000244|PDB:1M6Y}. FT HELIX 147 156 {ECO:0000244|PDB:1M6Y}. FT TURN 161 163 {ECO:0000244|PDB:1M6Y}. FT HELIX 164 173 {ECO:0000244|PDB:1M6Y}. FT HELIX 180 190 {ECO:0000244|PDB:1M6Y}. FT HELIX 193 198 {ECO:0000244|PDB:1M6Y}. FT HELIX 205 216 {ECO:0000244|PDB:1M6Y}. FT HELIX 218 228 {ECO:0000244|PDB:1M6Y}. FT HELIX 229 232 {ECO:0000244|PDB:1M6Y}. FT STRAND 233 245 {ECO:0000244|PDB:1M6Y}. FT HELIX 246 258 {ECO:0000244|PDB:1M6Y}. FT STRAND 260 265 {ECO:0000244|PDB:1M6Y}. FT HELIX 274 279 {ECO:0000244|PDB:1M6Y}. FT HELIX 281 283 {ECO:0000244|PDB:1M6Y}. FT STRAND 287 293 {ECO:0000244|PDB:1M6Y}. SQ SEQUENCE 299 AA; 34893 MW; 790BBC2F3BB271F7 CRC64; MRKYSQRHIP VMVREVIEFL KPEDEKIILD CTVGEGGHSR AILEHCPGCR IIGIDVDSEV LRIAEEKLKE FSDRVSLFKV SYREADFLLK TLGIEKVDGI LMDLGVSTYQ LKGENRGFTF EREEPLDMRM DLESEVTAQK VLNELPEEEL ARIIFEYGEE KRFARRIARK IVENRPLNTT LDLVKAVREA LPSYEIRRRK RHFATKTFQA IRIYVNRELE NLKEFLKKAE DLLNPGGRIV VISFHSLEDR IVKETFRNSK KLRILTEKPV RPSEEEIREN PRARSGRLRA AERIEEGGD // ID SAHH_THEMA Reviewed; 404 AA. AC O51933; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 125. DE RecName: Full=Adenosylhomocysteinase {ECO:0000255|HAMAP-Rule:MF_00563}; DE EC=3.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00563}; DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000255|HAMAP-Rule:MF_00563}; DE Short=AdoHcyase {ECO:0000255|HAMAP-Rule:MF_00563}; GN Name=ahcY {ECO:0000255|HAMAP-Rule:MF_00563}; GN OrderedLocusNames=TM_0172; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9440516; RA Bouthier de la Tour C., Portemer C., Kaltoum H., Duguet M.; RT "Reverse gyrase from the hyperthermophilic bacterium Thermotoga RT maritima: properties and gene structure."; RL J. Bacteriol. 180:274-281(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: May play a key role in the regulation of the CC intracellular concentration of adenosylhomocysteine. CC {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L- CC homocysteine + adenosine. {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00563}; CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00563}; CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L- CC homocysteine from S-adenosyl-L-homocysteine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family. CC {ECO:0000255|HAMAP-Rule:MF_00563}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF013268; AAC01562.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35265.1; -; Genomic_DNA. DR PIR; B72409; B72409. DR RefSeq; NP_227987.1; NC_000853.1. DR RefSeq; WP_004082805.1; NZ_CP011107.1. DR PDB; 3X2E; X-ray; 2.85 A; A/B/C/D=2-404. DR PDB; 3X2F; X-ray; 2.04 A; A/B=2-404. DR PDBsum; 3X2E; -. DR PDBsum; 3X2F; -. DR ProteinModelPortal; O51933; -. DR STRING; 243274.TM0172; -. DR ChEMBL; CHEMBL1075032; -. DR EnsemblBacteria; AAD35265; AAD35265; TM_0172. DR GeneID; 897011; -. DR KEGG; tma:TM0172; -. DR PATRIC; 23935192; VBITheMar51294_0173. DR eggNOG; ENOG4105C3E; Bacteria. DR eggNOG; COG0499; LUCA. DR InParanoid; O51933; -. DR KO; K01251; -. DR OMA; VHDKYPQ; -. DR OrthoDB; EOG6F296M; -. DR UniPathway; UPA00314; UER00076. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004013; F:adenosylhomocysteinase activity; IBA:GO_Central. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00563; AdoHcyase; 1. DR InterPro; IPR000043; Adenosylhomocysteinase. DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS. DR PANTHER; PTHR23420; PTHR23420; 1. DR Pfam; PF05221; AdoHcyase; 2. DR Pfam; PF00670; AdoHcyase_NAD; 1. DR PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1. DR SMART; SM00996; AdoHcyase; 1. DR SMART; SM00997; AdoHcyase_NAD; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00936; ahcY; 1. DR PROSITE; PS00738; ADOHCYASE_1; 1. DR PROSITE; PS00739; ADOHCYASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; NAD; KW One-carbon metabolism; Reference proteome. FT CHAIN 1 404 Adenosylhomocysteinase. FT /FTId=PRO_0000116995. FT NP_BIND 140 142 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT NP_BIND 203 208 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT NP_BIND 282 284 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT BINDING 114 114 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00563}. FT BINDING 139 139 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00563}. FT BINDING 169 169 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00563}. FT BINDING 173 173 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00563}. FT BINDING 174 174 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT BINDING 226 226 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT BINDING 261 261 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT BINDING 329 329 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT CONFLICT 44 44 A -> R (in Ref. 1; AAC01562). FT {ECO:0000305}. FT CONFLICT 51 51 I -> V (in Ref. 1; AAC01562). FT {ECO:0000305}. FT HELIX 3 13 {ECO:0000244|PDB:3X2F}. FT HELIX 16 25 {ECO:0000244|PDB:3X2F}. FT TURN 26 28 {ECO:0000244|PDB:3X2F}. FT TURN 30 33 {ECO:0000244|PDB:3X2F}. FT STRAND 35 40 {ECO:0000244|PDB:3X2F}. FT HELIX 44 55 {ECO:0000244|PDB:3X2F}. FT STRAND 59 66 {ECO:0000244|PDB:3X2F}. FT HELIX 73 79 {ECO:0000244|PDB:3X2F}. FT TURN 80 82 {ECO:0000244|PDB:3X2F}. FT STRAND 84 86 {ECO:0000244|PDB:3X2F}. FT STRAND 89 91 {ECO:0000244|PDB:3X2F}. FT HELIX 93 104 {ECO:0000244|PDB:3X2F}. FT STRAND 109 116 {ECO:0000244|PDB:3X2F}. FT HELIX 117 124 {ECO:0000244|PDB:3X2F}. FT HELIX 127 132 {ECO:0000244|PDB:3X2F}. FT STRAND 135 138 {ECO:0000244|PDB:3X2F}. FT HELIX 141 152 {ECO:0000244|PDB:3X2F}. FT STRAND 160 162 {ECO:0000244|PDB:3X2F}. FT HELIX 169 172 {ECO:0000244|PDB:3X2F}. FT TURN 175 177 {ECO:0000244|PDB:3X2F}. FT HELIX 178 188 {ECO:0000244|PDB:3X2F}. FT STRAND 198 202 {ECO:0000244|PDB:3X2F}. FT HELIX 206 217 {ECO:0000244|PDB:3X2F}. FT STRAND 221 225 {ECO:0000244|PDB:3X2F}. FT HELIX 229 237 {ECO:0000244|PDB:3X2F}. FT HELIX 245 248 {ECO:0000244|PDB:3X2F}. FT TURN 249 251 {ECO:0000244|PDB:3X2F}. FT STRAND 253 257 {ECO:0000244|PDB:3X2F}. FT HELIX 267 270 {ECO:0000244|PDB:3X2F}. FT STRAND 278 281 {ECO:0000244|PDB:3X2F}. FT STRAND 283 285 {ECO:0000244|PDB:3X2F}. FT TURN 286 290 {ECO:0000244|PDB:3X2F}. FT HELIX 291 297 {ECO:0000244|PDB:3X2F}. FT STRAND 298 305 {ECO:0000244|PDB:3X2F}. FT STRAND 308 313 {ECO:0000244|PDB:3X2F}. FT STRAND 318 322 {ECO:0000244|PDB:3X2F}. FT HELIX 323 325 {ECO:0000244|PDB:3X2F}. FT HELIX 328 331 {ECO:0000244|PDB:3X2F}. FT HELIX 338 358 {ECO:0000244|PDB:3X2F}. FT TURN 359 361 {ECO:0000244|PDB:3X2F}. FT STRAND 364 368 {ECO:0000244|PDB:3X2F}. FT HELIX 371 385 {ECO:0000244|PDB:3X2F}. FT HELIX 394 400 {ECO:0000244|PDB:3X2F}. SQ SEQUENCE 404 AA; 44850 MW; D20DB3BE02826148 CRC64; MNTGEMKINW VSRYMPLLNK IAEEYSREKP LSGFTVGMSI HLEAKTAYLA ITLSKLGAKV VITGSNPLST QDDVAEALRS KGITVYARRT HDESIYRENL MKVLDERPDF IIDDGGDLTV ISHTEREEVL ENLKGVSEET TTGVRRLKAL EETGKLRVPV IAVNDSKMKY LFDNRYGTGQ STWDAIMRNT NLLVAGKNVV VAGYGWCGRG IALRAAGLGA RVIVTEVDPV KAVEAIMDGF TVMPMKEAVK IADFVITASG NTDVLSKEDI LSLKDGAVLA NAGHFNVEIP VRVLEEIAVE KFEARPNVTG YTLENGKTVF LLAEGRLVNL AAGDGHPVEI MDLSFALQIF AVLYLLENHR KMSPKVYMLP DEIDERVARM KLDSLGVKID ELTEKQRRYL RSWQ // ID RSMI_THEMA Reviewed; 222 AA. AC Q9WZG8; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=Ribosomal RNA small subunit methyltransferase I {ECO:0000255|HAMAP-Rule:MF_01877}; DE EC=2.1.1.198 {ECO:0000255|HAMAP-Rule:MF_01877}; DE AltName: Full=16S rRNA 2'-O-ribose C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01877}; DE AltName: Full=rRNA (cytidine-2'-O-)-methyltransferase RsmI {ECO:0000255|HAMAP-Rule:MF_01877}; GN Name=rsmI {ECO:0000255|HAMAP-Rule:MF_01877}; GN OrderedLocusNames=TM_0709; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine CC 1402 (C1402) in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01877}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytidine(1402) in CC 16S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(1402) CC in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01877}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01877}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmI CC family. {ECO:0000255|HAMAP-Rule:MF_01877}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35791.1; -; Genomic_DNA. DR PIR; D72343; D72343. DR RefSeq; NP_228518.1; NC_000853.1. DR RefSeq; WP_004081030.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZG8; -. DR STRING; 243274.TM0709; -. DR DNASU; 898376; -. DR EnsemblBacteria; AAD35791; AAD35791; TM_0709. DR GeneID; 898376; -. DR KEGG; tma:TM0709; -. DR PATRIC; 23936336; VBITheMar51294_0721. DR eggNOG; ENOG4105CU0; Bacteria. DR eggNOG; COG0313; LUCA. DR InParanoid; Q9WZG8; -. DR KO; K07056; -. DR OMA; REFIAFH; -. DR OrthoDB; EOG6677TH; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070677; F:rRNA (cytosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IBA:GO_Central. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 1. DR HAMAP; MF_01877; 16SrRNA_methyltr_I; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR008189; rRNA_ssu_MeTfrase_I. DR InterPro; IPR018063; SAM_MeTrfase_RsmI_CS. DR Pfam; PF00590; TP_methylase; 1. DR PIRSF; PIRSF005917; MTase_YraL; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR00096; TIGR00096; 1. DR PROSITE; PS01296; RSMI; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 222 Ribosomal RNA small subunit FT methyltransferase I. FT /FTId=PRO_0000211959. SQ SEQUENCE 222 AA; 25125 MW; D2AF2E55859EAA90 CRC64; MGKLIIVGTP IGNLEDITIR ALKTLREVDL ILAEDTRRTM VLLNKYRIKK PLLSFNERNS KKRIKEILPL LKEGKKVAIV SDAGMPVISD PGYNLVEECW REGIEVDIVP GPSALTSAVA VSGFPGSKFI FEGFLPRGKN RRRLLKSLKK ENRVIVFFES PERLLSTLRD ILEIIGDREV FIAREMTKLH QEFFRGKVSE AISHFEKKKP LGEITVVLSG KE // ID RUVB_THEMA Reviewed; 334 AA. AC Q56313; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 124. DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB {ECO:0000255|HAMAP-Rule:MF_00016}; DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016}; GN Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016}; GN OrderedLocusNames=TM_1730; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8626340; RA Tong J., Wetmur J.G.; RT "Cloning, sequencing, and expression of ruvB and characterization of RT RuvB proteins from two distantly related thermophilic eubacteria."; RL J. Bacteriol. 178:2695-2700(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures CC cruciform structure in supercoiled DNA with palindromic sequence, CC indicating that it may promote strand exchange reactions in CC homologous recombination. RuvAB is a helicase that mediates the CC Holliday junction migration by localized denaturation and CC reannealing. {ECO:0000255|HAMAP-Rule:MF_00016}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00016}. CC -!- SUBUNIT: Forms a complex with RuvA. CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP- CC Rule:MF_00016}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U38840; AAB03727.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36795.1; -; Genomic_DNA. DR PIR; A72217; A72217. DR RefSeq; NP_229528.1; NC_000853.1. DR RefSeq; WP_004082245.1; NZ_CP011107.1. DR PDB; 1IN4; X-ray; 1.60 A; A=1-334. DR PDB; 1IN5; X-ray; 2.00 A; A=1-334. DR PDB; 1IN6; X-ray; 1.80 A; A=1-334. DR PDB; 1IN7; X-ray; 1.90 A; A=1-334. DR PDB; 1IN8; X-ray; 1.90 A; A=1-334. DR PDB; 1J7K; X-ray; 1.80 A; A=1-334. DR PDBsum; 1IN4; -. DR PDBsum; 1IN5; -. DR PDBsum; 1IN6; -. DR PDBsum; 1IN7; -. DR PDBsum; 1IN8; -. DR PDBsum; 1J7K; -. DR ProteinModelPortal; Q56313; -. DR SMR; Q56313; 17-329. DR STRING; 243274.TM1730; -. DR EnsemblBacteria; AAD36795; AAD36795; TM_1730. DR GeneID; 897204; -. DR KEGG; tma:TM1730; -. DR PATRIC; 23938436; VBITheMar51294_1748. DR eggNOG; ENOG4105CKJ; Bacteria. DR eggNOG; COG2255; LUCA. DR InParanoid; Q56313; -. DR KO; K03551; -. DR OMA; YEPYLMQ; -. DR OrthoDB; EOG6SR93S; -. DR EvolutionaryTrace; Q56313; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00016; DNA_helic_RuvB; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR004605; DNA_helicase_Holl-junc_RuvB. DR InterPro; IPR008823; DNA_helicase_Holl-junc_RuvB_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008824; RuvB_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF05491; RuvB_C; 1. DR Pfam; PF05496; RuvB_N; 1. DR ProDom; PD005323; DNA_helicase_Holl-junc_RuvB_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00635; ruvB; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; DNA damage; KW DNA recombination; DNA repair; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; SOS response. FT CHAIN 1 334 Holliday junction ATP-dependent DNA FT helicase RuvB. FT /FTId=PRO_0000165617. FT NP_BIND 58 65 ATP. {ECO:0000255|HAMAP-Rule:MF_00016}. FT HELIX 24 26 {ECO:0000244|PDB:1IN4}. FT HELIX 31 47 {ECO:0000244|PDB:1IN4}. FT STRAND 54 59 {ECO:0000244|PDB:1IN4}. FT HELIX 64 75 {ECO:0000244|PDB:1IN4}. FT STRAND 79 83 {ECO:0000244|PDB:1IN4}. FT TURN 84 86 {ECO:0000244|PDB:1IN4}. FT HELIX 90 99 {ECO:0000244|PDB:1IN4}. FT STRAND 105 109 {ECO:0000244|PDB:1IN4}. FT HELIX 111 113 {ECO:0000244|PDB:1IN4}. FT HELIX 116 127 {ECO:0000244|PDB:1IN4}. FT STRAND 152 158 {ECO:0000244|PDB:1IN4}. FT HELIX 160 162 {ECO:0000244|PDB:1IN4}. FT HELIX 165 168 {ECO:0000244|PDB:1IN4}. FT STRAND 172 176 {ECO:0000244|PDB:1IN4}. FT HELIX 182 195 {ECO:0000244|PDB:1IN4}. FT HELIX 202 210 {ECO:0000244|PDB:1IN4}. FT HELIX 216 233 {ECO:0000244|PDB:1IN4}. FT STRAND 236 238 {ECO:0000244|PDB:1IN4}. FT HELIX 240 250 {ECO:0000244|PDB:1IN4}. FT HELIX 259 271 {ECO:0000244|PDB:1IN4}. FT HELIX 279 286 {ECO:0000244|PDB:1IN4}. FT HELIX 290 296 {ECO:0000244|PDB:1IN4}. FT HELIX 298 303 {ECO:0000244|PDB:1IN4}. FT STRAND 306 310 {ECO:0000244|PDB:1IN4}. FT STRAND 313 316 {ECO:0000244|PDB:1IN4}. FT HELIX 318 323 {ECO:0000244|PDB:1IN4}. SQ SEQUENCE 334 AA; 37156 MW; 6F4BBFBFA7B9C7A9 CRC64; MSEFLTPERT VYDSGVQFLR PKSLDEFIGQ ENVKKKLSLA LEAAKMRGEV LDHVLLAGPP GLGKTTLAHI IASELQTNIH VTSGPVLVKQ GDMAAILTSL ERGDVLFIDE IHRLNKAVEE LLYSAIEDFQ IDIMIGKGPS AKSIRIDIQP FTLVGATTRS GLLSSPLRSR FGIILELDFY TVKELKEIIK RAASLMDVEI EDAAAEMIAK RSRGTPRIAI RLTKRVRDML TVVKADRINT DIVLKTMEVL NIDDEGLDEF DRKILKTIIE IYRGGPVGLN ALAASLGVEA DTLSEVYEPY LLQAGFLART PRGRIVTEKA YKHLKYEVPE NRLF // ID RUVC_THEMA Reviewed; 168 AA. AC Q9WZ45; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Crossover junction endodeoxyribonuclease RuvC; DE EC=3.1.22.4; DE AltName: Full=Holliday junction nuclease RuvC; DE AltName: Full=Holliday junction resolvase RuvC; GN Name=ruvC; OrderedLocusNames=TM_0575; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Nuclease that resolves Holliday junction intermediates CC in genetic recombination. Cleaves the cruciform structure in CC supercoiled DNA by nicking to strands with the same polarity at CC sites symmetrically opposed at the junction in the homologous arms CC and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl CC group (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage at a junction such as CC a reciprocal single-stranded crossover between two homologous DNA CC duplexes (Holliday junction). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the RuvC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35660.1; -; Genomic_DNA. DR PIR; B72360; B72360. DR RefSeq; NP_228385.1; NC_000853.1. DR RefSeq; WP_010865150.1; NC_000853.1. DR ProteinModelPortal; Q9WZ45; -. DR STRING; 243274.TM0575; -. DR EnsemblBacteria; AAD35660; AAD35660; TM_0575. DR GeneID; 897642; -. DR KEGG; tma:TM0575; -. DR PATRIC; 23936059; VBITheMar51294_0584. DR eggNOG; ENOG4105NHU; Bacteria. DR eggNOG; COG0817; LUCA. DR InParanoid; Q9WZ45; -. DR KO; K01159; -. DR OMA; ILHMIKL; -. DR OrthoDB; EOG6RG044; -. DR BioCyc; TMAR243274:GC6P-599-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central. DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central. DR GO; GO:0071932; P:replication fork reversal; IBA:GO_Central. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00034; RuvC; 1. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR020563; X-over_junc_endoDNase_Mg_BS. DR InterPro; IPR002176; X-over_junc_endoDNase_RuvC. DR Pfam; PF02075; RuvC; 1. DR PRINTS; PR00696; RSOLVASERUVC. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR00228; ruvC; 1. DR PROSITE; PS01321; RUVC; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA recombination; DNA repair; KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 168 Crossover junction endodeoxyribonuclease FT RuvC. FT /FTId=PRO_0000183139. FT METAL 10 10 Magnesium. {ECO:0000250}. FT METAL 70 70 Magnesium. {ECO:0000250}. FT METAL 143 143 Magnesium. {ECO:0000250}. FT METAL 146 146 Magnesium. {ECO:0000250}. SQ SEQUENCE 168 AA; 18705 MW; 8AF26109F3176B56 CRC64; MGSLRILGVD PGYGIVGIGI IEVSGNRISH VFHGTIETPK NLPAEKRLKR IYEEFLKVLE RFSPDECAME KLFFVKNVTT AIGVGEARGV LFLALAEKNI PVFEYAPNEV KVSLSGYGRA SKKQIQENVK RFLNLSEIPR PDDAADALAI AWCHALQSRA RRVTHEKD // ID SECA_THEMA Reviewed; 871 AA. AC Q9X1R4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; GN OrderedLocusNames=TM_1578; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN COMPLEX WITH SECYEG. RX PubMed=18923516; DOI=10.1038/nature07335; RA Zimmer J., Nam Y., Rapoport T.A.; RT "Structure of a complex of the ATPase SecA and the protein- RT translocation channel."; RL Nature 455:936-943(2008). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-816. RX PubMed=19850053; DOI=10.1016/j.jmb.2009.10.024; RA Zimmer J., Rapoport T.A.; RT "Conformational flexibility and peptide interaction of the RT translocation ATPase SecA."; RL J. Mol. Biol. 394:606-612(2009). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts CC with the SecYEG preprotein conducting channel. Has a central role CC in coupling the hydrolysis of ATP to the transfer of proteins into CC and across the cell membrane, serving as an ATP-driven molecular CC motor driving the stepwise translocation of polypeptide chains CC across the membrane. {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- SUBUNIT: Monomer and homodimer (By similarity). Part of the CC essential Sec protein translocation apparatus which comprises CC SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also CC be involved. A single SecA monomer interacts with SecY in the CC channel. {ECO:0000255|HAMAP-Rule:MF_01382, CC ECO:0000269|PubMed:18923516}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_01382}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. CC Note=Distribution is 50-50. {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP- CC Rule:MF_01382}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36645.1; -; Genomic_DNA. DR PIR; C72238; C72238. DR RefSeq; NP_229378.1; NC_000853.1. DR RefSeq; WP_004082002.1; NZ_CP011107.1. DR PDB; 3DIN; X-ray; 4.50 A; A/B=1-871. DR PDB; 3JUX; X-ray; 3.10 A; A=1-816. DR PDB; 4YS0; X-ray; 1.90 A; A=1-816. DR PDBsum; 3DIN; -. DR PDBsum; 3JUX; -. DR PDBsum; 4YS0; -. DR ProteinModelPortal; Q9X1R4; -. DR SMR; Q9X1R4; 496-541. DR DIP; DIP-59806N; -. DR STRING; 243274.TM1578; -. DR EnsemblBacteria; AAD36645; AAD36645; TM_1578. DR GeneID; 897610; -. DR KEGG; tma:TM1578; -. DR PATRIC; 23938120; VBITheMar51294_1597. DR eggNOG; ENOG4105CI6; Bacteria. DR eggNOG; COG0653; LUCA. DR InParanoid; Q9X1R4; -. DR KO; K03070; -. DR OMA; IATERHE; -. DR OrthoDB; EOG654P48; -. DR EvolutionaryTrace; Q9X1R4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0017038; P:protein import; IEA:InterPro. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3060.10; -; 1. DR Gene3D; 3.40.50.300; -; 4. DR Gene3D; 3.90.1440.10; -; 1. DR HAMAP; MF_01382; SecA; 1. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000185; SecA. DR InterPro; IPR020937; SecA_CS. DR InterPro; IPR011115; SecA_DEAD. DR InterPro; IPR014018; SecA_motor_DEAD. DR InterPro; IPR011130; SecA_preprotein_X-link_dom. DR InterPro; IPR011116; SecA_Wing/Scaffold. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF07517; SecA_DEAD; 1. DR Pfam; PF01043; SecA_PP_bind; 1. DR Pfam; PF07516; SecA_SW; 1. DR PRINTS; PR00906; SECA. DR SMART; SM00957; SecA_DEAD; 1. DR SMART; SM00958; SecA_PP_bind; 1. DR SUPFAM; SSF52540; SSF52540; 4. DR SUPFAM; SSF81767; SSF81767; 1. DR SUPFAM; SSF81886; SSF81886; 1. DR PROSITE; PS01312; SECA; 1. DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; KW Complete proteome; Cytoplasm; Membrane; Nucleotide-binding; KW Protein transport; Reference proteome; Translocation; Transport. FT CHAIN 1 871 Protein translocase subunit SecA. FT /FTId=PRO_0000321023. FT NP_BIND 95 102 ATP. {ECO:0000255|HAMAP-Rule:MF_01382}. FT HELIX 6 30 {ECO:0000244|PDB:4YS0}. FT HELIX 33 46 {ECO:0000244|PDB:4YS0}. FT HELIX 50 55 {ECO:0000244|PDB:4YS0}. FT HELIX 57 72 {ECO:0000244|PDB:4YS0}. FT HELIX 78 88 {ECO:0000244|PDB:4YS0}. FT STRAND 92 94 {ECO:0000244|PDB:4YS0}. FT HELIX 101 104 {ECO:0000244|PDB:4YS0}. FT HELIX 106 113 {ECO:0000244|PDB:4YS0}. FT STRAND 120 125 {ECO:0000244|PDB:4YS0}. FT HELIX 126 142 {ECO:0000244|PDB:4YS0}. FT STRAND 147 150 {ECO:0000244|PDB:4YS0}. FT TURN 152 154 {ECO:0000244|PDB:3JUX}. FT STRAND 156 163 {ECO:0000244|PDB:4YS0}. FT HELIX 164 172 {ECO:0000244|PDB:4YS0}. FT STRAND 184 186 {ECO:0000244|PDB:3JUX}. FT HELIX 189 191 {ECO:0000244|PDB:4YS0}. FT HELIX 194 199 {ECO:0000244|PDB:4YS0}. FT STRAND 202 206 {ECO:0000244|PDB:4YS0}. FT HELIX 209 214 {ECO:0000244|PDB:4YS0}. FT STRAND 215 221 {ECO:0000244|PDB:4YS0}. FT HELIX 222 232 {ECO:0000244|PDB:4YS0}. FT HELIX 238 240 {ECO:0000244|PDB:4YS0}. FT STRAND 248 253 {ECO:0000244|PDB:4YS0}. FT HELIX 254 258 {ECO:0000244|PDB:4YS0}. FT HELIX 261 263 {ECO:0000244|PDB:4YS0}. FT STRAND 266 271 {ECO:0000244|PDB:4YS0}. FT HELIX 276 286 {ECO:0000244|PDB:4YS0}. FT TURN 291 293 {ECO:0000244|PDB:4YS0}. FT STRAND 294 298 {ECO:0000244|PDB:4YS0}. FT TURN 299 302 {ECO:0000244|PDB:4YS0}. FT STRAND 303 306 {ECO:0000244|PDB:4YS0}. FT HELIX 308 318 {ECO:0000244|PDB:4YS0}. FT HELIX 326 328 {ECO:0000244|PDB:4YS0}. FT HELIX 329 343 {ECO:0000244|PDB:4YS0}. FT TURN 347 349 {ECO:0000244|PDB:4YS0}. FT STRAND 350 354 {ECO:0000244|PDB:4YS0}. FT STRAND 357 361 {ECO:0000244|PDB:4YS0}. FT TURN 363 365 {ECO:0000244|PDB:4YS0}. FT HELIX 375 377 {ECO:0000244|PDB:3JUX}. FT HELIX 378 385 {ECO:0000244|PDB:4YS0}. FT STRAND 394 400 {ECO:0000244|PDB:4YS0}. FT HELIX 402 406 {ECO:0000244|PDB:4YS0}. FT STRAND 409 417 {ECO:0000244|PDB:4YS0}. FT HELIX 420 422 {ECO:0000244|PDB:4YS0}. FT HELIX 423 430 {ECO:0000244|PDB:4YS0}. FT STRAND 434 436 {ECO:0000244|PDB:4YS0}. FT STRAND 451 455 {ECO:0000244|PDB:4YS0}. FT HELIX 456 473 {ECO:0000244|PDB:4YS0}. FT STRAND 477 482 {ECO:0000244|PDB:4YS0}. FT HELIX 484 497 {ECO:0000244|PDB:4YS0}. FT STRAND 502 504 {ECO:0000244|PDB:4YS0}. FT HELIX 509 516 {ECO:0000244|PDB:4YS0}. FT TURN 517 520 {ECO:0000244|PDB:4YS0}. FT STRAND 525 529 {ECO:0000244|PDB:4YS0}. FT TURN 530 535 {ECO:0000244|PDB:4YS0}. FT TURN 542 544 {ECO:0000244|PDB:4YS0}. FT HELIX 545 547 {ECO:0000244|PDB:4YS0}. FT STRAND 549 556 {ECO:0000244|PDB:4YS0}. FT HELIX 561 568 {ECO:0000244|PDB:4YS0}. FT HELIX 573 575 {ECO:0000244|PDB:4YS0}. FT STRAND 578 585 {ECO:0000244|PDB:4YS0}. FT HELIX 589 593 {ECO:0000244|PDB:4YS0}. FT HELIX 596 605 {ECO:0000244|PDB:4YS0}. FT STRAND 610 612 {ECO:0000244|PDB:3JUX}. FT HELIX 617 664 {ECO:0000244|PDB:4YS0}. FT HELIX 669 688 {ECO:0000244|PDB:4YS0}. FT HELIX 695 701 {ECO:0000244|PDB:4YS0}. FT TURN 702 704 {ECO:0000244|PDB:4YS0}. FT HELIX 720 742 {ECO:0000244|PDB:4YS0}. FT HELIX 743 745 {ECO:0000244|PDB:3JUX}. FT HELIX 746 778 {ECO:0000244|PDB:4YS0}. FT TURN 780 783 {ECO:0000244|PDB:3JUX}. FT HELIX 786 815 {ECO:0000244|PDB:4YS0}. SQ SEQUENCE 871 AA; 100486 MW; 24F661A1799AC89C CRC64; MILFDKNKRI LKKYAKMVSK INQIESDLRS KKNSELIRLS MVLKEKVNSF EDADEHLFEA FALVREAARR TLGMRPFDVQ VMGGIALHEG KVAEMKTGEG KTLAATMPIY LNALIGKGVH LVTVNDYLAR RDALWMGPVY LFLGLRVGVI NSLGKSYEVV WKNPDLARKA IEENWSVWPD GFNGEVLKEE SMNKEAVEAF QVELKEITRK EAYLCDVTYG TNNEFGFDYL RDNLVLDYND KVQRGHFYAI VDEADSVLID EARTPLIISG PSKESPSVYR RFAQIAKKFV KDKDFTVDEK ARTIILTEEG VAKAEKIIGV ENLYDPGNVS LLYHLINALK ALHLFKKDVD YVVMNGEVII VDEFTGRLLP GRRYSGGLHQ AIEAKEGVPI KEESITYATI TFQNYFRMYE KLAGMTGTAK TEESEFVQVY GMEVVVIPTH KPMIRKDHDD LVFRTQKEKY EKIVEEIEKR YKKGQPVLVG TTSIEKSELL SSMLKKKGIP HQVLNAKYHE KEAEIVAKAG QKGMVTIATN MAGRGTDIKL GPGVAELGGL CIIGTERHES RRIDNQLRGR AGRQGDPGES IFFLSLEDDL LRIFGSEQIG KVMNILKIEE GQPIQHPMLS KLIENIQKKV EGINFSIRKT LMEMDDVLDK QRRAVYSLRD QILLEKDYDE YLKDIFEDVV STRVEEFCSG KNWDIESLKN SLSFFPAGLF DLDEKQFSSS EELHDYLFNR LWEEYQRKKQ EIGEDYRKVI RFLMLRIIDD HWRRYLEEVE HVKEAVQLRS YGQKDPIVEF KKETYYMFDE MMRRINDTIA NYVLRVVKVS EKDEKEAKEE LGKIRLVHEE FNLVNRAMRR ATEKKKKKDG LHSFGRIRVK R // ID RUVA_THEMA Reviewed; 188 AA. AC Q9WY12; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 112. DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvA {ECO:0000255|HAMAP-Rule:MF_00031}; DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00031}; GN Name=ruvA {ECO:0000255|HAMAP-Rule:MF_00031}; GN OrderedLocusNames=TM_0165; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures CC cruciform structure in supercoiled DNA with palindromic sequence, CC indicating that it may promote strand exchange reactions in CC homologous recombination. RuvAB is a helicase that mediates the CC Holliday junction migration by localized denaturation and CC reannealing. RuvA stimulates, in the presence of DNA, the weak CC ATPase activity of RuvB. {ECO:0000255|HAMAP-Rule:MF_00031}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00031}. CC -!- SUBUNIT: Forms a complex with RuvB. {ECO:0000255|HAMAP- CC Rule:MF_00031}. CC -!- SIMILARITY: Belongs to the RuvA family. {ECO:0000255|HAMAP- CC Rule:MF_00031}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35258.1; -; Genomic_DNA. DR PIR; C72411; C72411. DR RefSeq; NP_227980.1; NC_000853.1. DR RefSeq; WP_004082791.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY12; -. DR STRING; 243274.TM0165; -. DR DNASU; 897004; -. DR EnsemblBacteria; AAD35258; AAD35258; TM_0165. DR GeneID; 897004; -. DR KEGG; tma:TM0165; -. DR PATRIC; 23935178; VBITheMar51294_0166. DR eggNOG; ENOG4105KA4; Bacteria. DR eggNOG; COG0632; LUCA. DR InParanoid; Q9WY12; -. DR KO; K03550; -. DR OMA; HIIREDA; -. DR OrthoDB; EOG679THG; -. DR BioCyc; TMAR243274:GC6P-166-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009379; C:Holliday junction helicase complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00031; DNA_helic_RuvA; 1. DR InterPro; IPR011114; DNA_helicas_Holl-junc_RuvA_C. DR InterPro; IPR013849; DNA_helicase_Holl-junc_RuvA_I. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000085; RuvA. DR InterPro; IPR010994; RuvA_2-like. DR Pfam; PF07499; RuvA_C; 1. DR Pfam; PF01330; RuvA_N; 1. DR SMART; SM00278; HhH1; 2. DR SUPFAM; SSF46929; SSF46929; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00084; ruvA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA recombination; KW DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; KW Reference proteome; SOS response. FT CHAIN 1 188 Holliday junction ATP-dependent DNA FT helicase RuvA. FT /FTId=PRO_0000094700. SQ SEQUENCE 188 AA; 20818 MW; 28E7F39D67FD61DD CRC64; MIAGISGRVL KKSGNVLLVE TKSGVVFEIV CDVQTSEEVK EGGECFLHTF LSVSQDGITL YGFSNEMKKE LFLSLTKVSR LGPKTALKII SNEDAETLVA MIASQDVEGL SKLPGISKKT AERIVMELKD EFESAGIKDM RIYHESLEAL VSLGYPEKQA REAVKQVYRE GMKTSELIKE ALKFLSHR // ID SAT_THEMA Reviewed; 384 AA. AC Q9X1C0; G4FFD6; DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Serine-pyruvate aminotransferase; DE Short=SAT; DE EC=2.6.1.51; GN OrderedLocusNames=TM_1400; ORFNames=THEMA_07315, Tmari_1407; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RG DOE Joint Genome Institute; RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18156253; DOI=10.1128/JB.01469-07; RA Yang C., Rodionov D.A., Rodionova I.A., Li X., Osterman A.L.; RT "Glycerate 2-kinase of Thermotoga maritima and genomic reconstruction RT of related metabolic pathways."; RL J. Bacteriol. 190:1773-1782(2008). CC -!- FUNCTION: Involved in the degradation of L-serine via 3- CC hydroxypyruvate. Catalyzes the transamination between L-serine and CC pyruvate to yield 3-hydroxypyruvate and alanine. CC {ECO:0000269|PubMed:18156253}. CC -!- CATALYTIC ACTIVITY: L-serine + pyruvate = 3-hydroxypyruvate + L- CC alanine. {ECO:0000269|PubMed:18156253}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36471.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50331.1; -; Genomic_DNA. DR EMBL; CP007013; AHD18704.1; -; Genomic_DNA. DR PIR; A72257; A72257. DR RefSeq; NP_229201.1; NC_000853.1. DR RefSeq; WP_004081619.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1C0; -. DR STRING; 243274.TM1400; -. DR EnsemblBacteria; AAD36471; AAD36471; TM_1400. DR EnsemblBacteria; AGL50331; AGL50331; Tmari_1407. DR EnsemblBacteria; AHD18704; AHD18704; THEMA_07315. DR GeneID; 898076; -. DR KEGG; tma:TM1400; -. DR KEGG; tmi:THEMA_07315; -. DR KEGG; tmm:Tmari_1407; -. DR KEGG; tmw:THMA_1429; -. DR PATRIC; 23937746; VBITheMar51294_1412. DR eggNOG; ENOG4105C5R; Bacteria. DR eggNOG; COG0075; LUCA. DR InParanoid; Q9X1C0; -. DR OMA; MPERGWY; -. DR OrthoDB; EOG6QZMN2; -. DR BioCyc; TMAR243274:GC6P-1437-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004760; F:serine-pyruvate transaminase activity; IDA:UniProtKB. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF000524; SPT; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. PE 1: Evidence at protein level; KW Aminotransferase; Complete proteome; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 384 Serine-pyruvate aminotransferase. FT /FTId=PRO_0000428995. FT MOD_RES 194 194 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 384 AA; 42106 MW; 3A23E83340A26290 CRC64; MGKFLKKHYI MAPGPTPVPN DILTEGAKET IHHRTPQFVS IMEETLESAK YIFQTKHNVY AFASTGTGAM EAAVANLVSP GDKVIVVVAG KFGERWRELC QAYGADIVEI ALEWGDAVTP EQIEEALNKN PDAKVVFTTY SETSTGTVID LEGIARVTKE KDVVLVTDAV SALGAEPLKM DEWGVDLVVT GSQKGLMLPP GLALISLNDK AWGLVEKSRS PRYYFDLRAY RKSYPDNPYT PAVNMIYMLR KALQMIKEEG IENVWERHRI LGDATRAAVK ALGLELLSKR PGNVVTAVKV PEGIDGKQIP KIMRDKYGVT IAGGQAKLKG KIFRIAHLGY MSPFDTITAI SALELTLKEL GYEFELGVGV KAAEAVFAKE FIGE // ID SECY_THEMA Reviewed; 431 AA. AC Q9X1I9; DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Protein translocase subunit SecY; GN Name=secY; OrderedLocusNames=TM_1480; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) OF SECYEG IN COMPLEX WITH SECA. RX PubMed=18923516; DOI=10.1038/nature07335; RA Zimmer J., Nam Y., Rapoport T.A.; RT "Structure of a complex of the ATPase SecA and the protein- RT translocation channel."; RL Nature 455:936-943(2008). CC -!- FUNCTION: The central subunit of the protein translocation channel CC SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These CC two domains form a lateral gate at the front which open onto the CC bilayer between TMs 2 and 7, and are clamped together by SecE at CC the back. The channel is closed by both a pore ring composed of CC hydrophobic SecY resides and a short helix (helix 2A) on the CC extracellular side of the membrane which forms a plug. The plug CC probably moves laterally to allow the channel to open. The ring CC and the pore may move independently. CC -!- SUBUNIT: Component of the Sec protein translocase complex. CC Heterotrimer consisting of SecY, SecE and SecG subunits. The CC heterotrimers can form oligomers, although 1 heterotrimer is CC thought to be able to translocate proteins. Interacts with the CC ribosome. Interacts with SecDF, and other proteins may be CC involved. Interacts with SecA. {ECO:0000269|PubMed:18923516}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36546.1; -; Genomic_DNA. DR PIR; H72247; H72247. DR RefSeq; NP_229280.1; NC_000853.1. DR RefSeq; WP_004081795.1; NZ_CP011107.1. DR PDB; 3DIN; X-ray; 4.50 A; C/F=1-431. DR PDBsum; 3DIN; -. DR ProteinModelPortal; Q9X1I9; -. DR DIP; DIP-59807N; -. DR STRING; 243274.TM1480; -. DR EnsemblBacteria; AAD36546; AAD36546; TM_1480. DR GeneID; 898007; -. DR KEGG; tma:TM1480; -. DR PATRIC; 23937918; VBITheMar51294_1497. DR eggNOG; ENOG4105CGG; Bacteria. DR eggNOG; COG0201; LUCA. DR InParanoid; Q9X1I9; -. DR KO; K03076; -. DR OMA; QTYVISQ; -. DR OrthoDB; EOG651SWP; -. DR BioCyc; TMAR243274:GC6P-1520-MONOMER; -. DR EvolutionaryTrace; Q9X1I9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3370.10; -; 1. DR HAMAP; MF_01465; SecY; 1. DR InterPro; IPR026593; SecY. DR InterPro; IPR002208; SecY/SEC61-alpha. DR InterPro; IPR030659; SecY_CS. DR InterPro; IPR023201; SecY_su_dom. DR PANTHER; PTHR10906; PTHR10906; 1. DR Pfam; PF00344; SecY; 1. DR PIRSF; PIRSF004557; SecY; 1. DR SUPFAM; SSF103491; SSF103491; 1. DR TIGRFAMs; TIGR00967; 3a0501s007; 1. DR PROSITE; PS00755; SECY_1; 1. DR PROSITE; PS00756; SECY_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Protein transport; Reference proteome; Translocation; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 431 Protein translocase subunit SecY. FT /FTId=PRO_0000414213. FT TOPO_DOM 1 17 Cytoplasmic. FT TRANSMEM 18 32 Helical; Name=Helix 1. FT TOPO_DOM 33 73 Periplasmic. FT TRANSMEM 74 95 Discontinuously helical; Name=Helix 2. FT INTRAMEM 74 77 Helical; Name=Helix 2A. FT INTRAMEM 78 84 FT INTRAMEM 85 95 Helical; Name=Helix 2B. FT TOPO_DOM 96 120 Cytoplasmic. FT TRANSMEM 121 133 Helical; Name=Helix 3. FT TOPO_DOM 134 161 Periplasmic. FT TRANSMEM 162 178 Helical; Name=Helix 4. FT TOPO_DOM 179 182 Cytoplasmic. FT TRANSMEM 183 198 Helical; Name=Helix 5. FT TOPO_DOM 199 213 Periplasmic. FT TRANSMEM 214 226 Helical; Name=Helix 6. FT TOPO_DOM 227 270 Cytoplasmic. FT TRANSMEM 271 283 Helical; Name=Helix 7. FT TOPO_DOM 284 302 Periplasmic. FT TRANSMEM 303 315 Helical; Name=Helix 8. FT TOPO_DOM 316 367 Cytoplasmic. FT TRANSMEM 368 382 Helical; Name=Helix 9. FT TOPO_DOM 383 389 Periplasmic. FT TRANSMEM 390 403 Helical; Name=Helix 10. FT TOPO_DOM 404 431 Cytoplasmic. SQ SEQUENCE 431 AA; 48170 MW; 0FFDBBAD1F8F0B61 CRC64; MWQAFKNAFK IPELRDRIIF TFLALIVFRM GIYIPVPGLN LEAWGEIFRR IAETAGVAGI LSFYDVFTGG ALSRFSVFTM SVTPYITASI ILQLLASVMP SLKEMLREGE EGRKKFAKYT RRLTLLIGGF QAFFVSFSLA RSNPDMVAPG VNVLQFTVLS TMSMLAGTMF LLWLGERITE KGIGNGISIL IFAGIVARYP SYIRQAYLGG LNLLEWIFLI AVALITIFGI ILVQQAERRI TIQYARRVTG RRVYGGASTY LPIKVNQGGV IPIIFASAIV SIPSAIASIT NNETLKNLFR AGGFLYLLIY GLLVFFFTYF YSVVIFDPRE ISENIRKYGG YIPGLRPGRS TEQYLHRVLN RVTFIGAVFL VVIALLPYLV QGAIKVNVWI GGTSALIAVG VALDIIQQME THMVMRHYEG FIKKGKIRGR R // ID SIGA_THEMA Reviewed; 399 AA. AC P77994; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 3. DT 11-NOV-2015, entry version 126. DE RecName: Full=RNA polymerase sigma factor SigA {ECO:0000255|HAMAP-Rule:MF_00963}; DE AltName: Full=Sigma-A; GN Name=sigA {ECO:0000255|HAMAP-Rule:MF_00963}; Synonyms=rpoD; GN OrderedLocusNames=TM_1451; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9045836; RA Gruber T.M., Bryant D.A.; RT "Molecular systematic studies of eubacteria, using sigma70-type sigma RT factors of group 1 and group 2."; RL J. Bacteriol. 179:1734-1747(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP STRUCTURE BY NMR OF 313-399. RX PubMed=15257291; DOI=10.1038/sj.emboj.7600312; RA Lambert L.J., Wei Y., Schirf V., Demeler B., Werner M.H.; RT "T4 AsiA blocks DNA recognition by remodeling sigma70 region 4."; RL EMBO J. 23:2952-2962(2004). RN [4] RP STRUCTURE BY NMR OF 29-95, IDENTIFICATION BY MASS SPECTROMETRY, AND RP DOMAIN. RX PubMed=18940669; DOI=10.1016/j.chembiol.2008.09.008; RA Schwartz E.C., Shekhtman A., Dutta K., Pratt M.R., Cowburn D., RA Darst S., Muir T.W.; RT "A full-length group 1 bacterial sigma factor adopts a compact RT structure incompatible with DNA binding."; RL Chem. Biol. 15:1091-1103(2008). CC -!- FUNCTION: Sigma factors are initiation factors that promote the CC attachment of RNA polymerase to specific initiation sites and are CC then released. This sigma factor is the primary sigma factor CC during exponential growth. {ECO:0000255|HAMAP-Rule:MF_00963}. CC -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic CC core. {ECO:0000255|HAMAP-Rule:MF_00963}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00963}. CC -!- DOMAIN: Contains 4 domains, connected by flexible linkers. In the CC active conformation, the domains are in an extended conformation, CC each making extensive interactions with the RNA polymerase CC catalytic core (PubMed:18940669). {ECO:0000269|PubMed:18940669}. CC -!- DOMAIN: In the autoinhibited state, sigma-70 factor domain-1 packs CC closely together with sigma-70 factor domains-2 and -4, contrary CC to the extended conformation that is seen when the protein is part CC of the RNA polymerase holoenzyme. {ECO:0000269|PubMed:18940669}. CC -!- DOMAIN: The sigma-70 factor domain-2 mediates sequence-specific CC interaction with the -10 element in promoter DNA, and plays an CC important role in melting the double-stranded DNA and the CC formation of the transcription bubble. The sigma-70 factor domain- CC 2 mediates interaction with the RNA polymerase subunits RpoB and CC RpoC (By similarity). {ECO:0000250}. CC -!- DOMAIN: The sigma-70 factor domain-4 contains a helix-turn-helix CC (H-T-H) motif that mediates interaction with the -35 element in CC promoter DNA. The domain also mediates interaction with the RNA CC polymerase subunit RpoA. Interactions between sigma-70 factor CC domain-4 and anti-sigma factors prevents interaction of sigma CC factors with the RNA polymerase catalytic core (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00963}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC44889.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U67423; AAC44889.2; ALT_INIT; Genomic_DNA. DR EMBL; AE000512; AAD36519.1; -; Genomic_DNA. DR PIR; G72253; G72253. DR RefSeq; NP_229250.1; NC_000853.1. DR RefSeq; WP_010865345.1; NC_000853.1. DR PDB; 1TTY; NMR; -; A=313-399. DR PDB; 2K6X; NMR; -; A=29-96. DR PDBsum; 1TTY; -. DR PDBsum; 2K6X; -. DR ProteinModelPortal; P77994; -. DR SMR; P77994; 117-287, 313-398. DR STRING; 243274.TM1451; -. DR EnsemblBacteria; AAD36519; AAD36519; TM_1451. DR GeneID; 898025; -. DR KEGG; tma:TM1451; -. DR KEGG; tmi:THEMA_07060; -. DR PATRIC; 23937854; VBITheMar51294_1465. DR eggNOG; ENOG4105DG1; Bacteria. DR eggNOG; COG0568; LUCA. DR InParanoid; P77994; -. DR KO; K03086; -. DR OMA; IDEVYEQ; -. DR OrthoDB; EOG6XHC70; -. DR BioCyc; TMAR243274:GC6P-1489-MONOMER; -. DR EvolutionaryTrace; P77994; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0001123; P:transcription initiation from bacterial-type RNA polymerase promoter; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 2. DR HAMAP; MF_00963; Sigma70_RpoD_SigA; 1. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR000943; RNA_pol_sigma70. DR InterPro; IPR009042; RNA_pol_sigma70_r1_2. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR007624; RNA_pol_sigma70_r3. DR InterPro; IPR007630; RNA_pol_sigma70_r4. DR InterPro; IPR007127; RNA_pol_sigma_70_r1_1. DR InterPro; IPR013325; RNA_pol_sigma_r2. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR012760; RNA_pol_sigma_RpoD_C. DR InterPro; IPR028630; Sigma70_RpoD. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF03979; Sigma70_r1_1; 1. DR Pfam; PF00140; Sigma70_r1_2; 1. DR Pfam; PF04542; Sigma70_r2; 1. DR Pfam; PF04539; Sigma70_r3; 1. DR Pfam; PF04545; Sigma70_r4; 1. DR PRINTS; PR00046; SIGMA70FCT. DR SUPFAM; SSF88659; SSF88659; 2. DR SUPFAM; SSF88946; SSF88946; 1. DR TIGRFAMs; TIGR02393; RpoD_Cterm; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. DR PROSITE; PS00715; SIGMA70_1; 1. DR PROSITE; PS00716; SIGMA70_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; DNA-binding; KW Reference proteome; Sigma factor; Transcription; KW Transcription regulation. FT CHAIN 1 399 RNA polymerase sigma factor SigA. FT /FTId=PRO_0000093929. FT DNA_BIND 353 372 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00963}. FT REGION 30 107 Sigma-70 factor domain-1. FT REGION 159 229 Sigma-70 factor domain-2. FT REGION 238 313 Sigma-70 factor domain-3. FT REGION 327 380 Sigma-70 factor domain-4. FT MOTIF 183 186 Interaction with polymerase core subunit FT RpoC. FT HELIX 29 45 {ECO:0000244|PDB:2K6X}. FT HELIX 50 56 {ECO:0000244|PDB:2K6X}. FT HELIX 66 77 {ECO:0000244|PDB:2K6X}. FT STRAND 92 94 {ECO:0000244|PDB:2K6X}. FT HELIX 323 328 {ECO:0000244|PDB:1TTY}. FT HELIX 333 343 {ECO:0000244|PDB:1TTY}. FT TURN 344 347 {ECO:0000244|PDB:1TTY}. FT HELIX 353 359 {ECO:0000244|PDB:1TTY}. FT HELIX 364 378 {ECO:0000244|PDB:1TTY}. FT STRAND 382 384 {ECO:0000244|PDB:1TTY}. FT HELIX 385 393 {ECO:0000244|PDB:1TTY}. FT TURN 394 396 {ECO:0000244|PDB:1TTY}. SQ SEQUENCE 399 AA; 46534 MW; BF9B519E8C4890A7 CRC64; MNEEQQVLQE QHQEQTQEQT QEQKETLPPQ IERRIKKLIS LGKKKGYITY EDIDKAFPPD FEGFDTNLIE RIHEELEKHG INIVENEPEE EEISASSDEQ ELEELLEKES PEIHDSSNVR DSIKMYLKEI GKIPLLTPAQ ERELARRAQM GDKKAKEKLI TSNLRLVVSI AKRYMGRGLS FQDLIQEGNI GLLKAVEKFD WRKGYKFSTY ATWWIRQAIT RAIADQARTI RIPVHMVETI NKLNRLRREY YQKHGEEPSI EELAKMMGKP PEKIKEILEA AKETISLESP IGEDEDSSIE DFVADDSIAS PKKEAMRMLM REELEKVLKT LSPREAMVLR MRYGLLDGKP KTLEEVGQYF NVTRERIRQI EVKALRKLRH PSRSKYLKSL LSLMDENEG // ID SECG_THEMA Reviewed; 67 AA. AC Q9WYU9; DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 14-OCT-2015, entry version 54. DE RecName: Full=Protein-export membrane protein SecG; GN Name=secG; OrderedLocusNames=TM_0479; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) OF SECYEG IN COMPLEX WITH SECA. RX PubMed=18923516; DOI=10.1038/nature07335; RA Zimmer J., Nam Y., Rapoport T.A.; RT "Structure of a complex of the ATPase SecA and the protein- RT translocation channel."; RL Nature 455:936-943(2008). CC -!- FUNCTION: Subunit of the protein translocation channel SecYEG. CC -!- SUBUNIT: Component of the Sec protein translocase complex. CC Heterotrimer consisting of SecY, SecE and SecG subunits. The CC heterotrimers can form oligomers, although 1 heterotrimer is CC thought to be able to translocate proteins. Interacts with SecDF, CC and other proteins may be involved. The channel interacts with CC SecA via subunit SecY. {ECO:0000269|PubMed:18923516}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the SecG family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35563.1; Type=Frameshift; Positions=34; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35563.1; ALT_FRAME; Genomic_DNA. DR PIR; G72372; G72372. DR RefSeq; NP_228289.1; NC_000853.1. DR RefSeq; WP_010865130.1; NC_000853.1. DR PDB; 3DIN; X-ray; 4.50 A; E/H=1-67. DR PDBsum; 3DIN; -. DR STRING; 243274.TM0479; -. DR EnsemblBacteria; AAD35563; AAD35563; TM_0479. DR GeneID; 897512; -. DR KEGG; tma:TM0479; -. DR PATRIC; 23935857; VBITheMar51294_0486. DR OrthoDB; EOG6DC6SJ; -. DR BioCyc; TMAR243274:GC6P-500-MONOMER; -. DR EvolutionaryTrace; Q9WYU9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 67 Protein-export membrane protein SecG. FT /FTId=PRO_0000414190. FT TOPO_DOM 1 14 Periplasmic. FT TRANSMEM 15 29 Helical; Name=Helix 1. FT TOPO_DOM 30 53 Cytoplasmic. FT TRANSMEM 54 63 Helical; Name=Helix 2. FT TOPO_DOM 64 67 Periplasmic. SQ SEQUENCE 67 AA; 7542 MW; 581A6B0E71E23F47 CRC64; MKTFFLIVHT IISVALIYMV QVQMSKFSEL GGASEVEDFT PFLEEEKAST PVERSLLSCL YSFSFPA // ID SFSA_THEMA Reviewed; 222 AA. AC Q9WZ35; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=Sugar fermentation stimulation protein homolog {ECO:0000255|HAMAP-Rule:MF_00095}; GN Name=sfsA {ECO:0000255|HAMAP-Rule:MF_00095}; GN OrderedLocusNames=TM_0565; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the SfsA family. {ECO:0000255|HAMAP- CC Rule:MF_00095}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35650.1; -; Genomic_DNA. DR PIR; D72361; D72361. DR RefSeq; NP_228375.1; NC_000853.1. DR RefSeq; WP_004081303.1; NZ_CP011107.1. DR STRING; 243274.TM0565; -. DR EnsemblBacteria; AAD35650; AAD35650; TM_0565. DR GeneID; 897629; -. DR KEGG; tma:TM0565; -. DR PATRIC; 23936039; VBITheMar51294_0574. DR eggNOG; ENOG4107ZMQ; Bacteria. DR eggNOG; COG1489; LUCA. DR InParanoid; Q9WZ35; -. DR KO; K06206; -. DR OMA; HVHDPGR; -. DR OrthoDB; EOG6QZMTM; -. DR Proteomes; UP000008183; Chromosome. DR HAMAP; MF_00095; SfsA; 1. DR InterPro; IPR005224; SfsA. DR Pfam; PF03749; SfsA; 1. DR TIGRFAMs; TIGR00230; sfsA; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 222 Sugar fermentation stimulation protein FT homolog. FT /FTId=PRO_0000152313. SQ SEQUENCE 222 AA; 25436 MW; 7CB6DFFD6F4319EA CRC64; MRLILPADTE GIFLERKSRF TGVALVEGKK TLIHIHNTGR LPLLKKGKRV LLKRAESDRR KTGWDLLAVE HRNEFVFVHS GFHSIVAGKI LEELFPGSTI ESEKRFENSR FDFLIDRRTF VEVKGCTYEE DGVAMFPDAP TGRGRRHIEE LIRSVKSGFK ALLLILVFLE SDCFLPNRSV DPAFSEIFWR ALNSGVNIDV FRVKYDGEYL CSTEKLSICE EV // ID SECE_THEMA Reviewed; 65 AA. AC P35874; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422}; GN Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; GN OrderedLocusNames=TM_0452; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=1429627; RA Liao D., Dennis P.P.; RT "The organization and expression of essential transcription RT translation component genes in the extremely thermophilic eubacterium RT Thermotoga maritima."; RL J. Biol. Chem. 267:22787-22797(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) OF SECYEG IN COMPLEX WITH SECA. RX PubMed=18923516; DOI=10.1038/nature07335; RA Zimmer J., Nam Y., Rapoport T.A.; RT "Structure of a complex of the ATPase SecA and the protein- RT translocation channel."; RL Nature 455:936-943(2008). CC -!- FUNCTION: Essential subunit of the protein translocation channel CC SecYEG. Clamps together the 2 halves of SecY. May contact the CC channel plug during translocation. CC -!- SUBUNIT: Component of the Sec protein translocase complex. CC Heterotrimer consisting of SecY, SecE and SecG subunits. The CC heterotrimers can form oligomers, although 1 heterotrimer is CC thought to be able to translocate proteins. Interacts with SecDF, CC and other proteins may be involved. The channel interacts with CC SecA via subunit SecY. {ECO:0000269|PubMed:18923516}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. CC {ECO:0000255|HAMAP-Rule:MF_00422}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z11839; CAA77865.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35535.1; -; Genomic_DNA. DR PIR; E72375; E72375. DR RefSeq; NP_228262.1; NC_000853.1. DR RefSeq; WP_004081514.1; NZ_CP011107.1. DR PDB; 3DIN; X-ray; 4.50 A; D/G=1-65. DR PDBsum; 3DIN; -. DR DIP; DIP-59808N; -. DR STRING; 243274.TM0452; -. DR EnsemblBacteria; AAD35535; AAD35535; TM_0452. DR GeneID; 897478; -. DR KEGG; tma:TM0452; -. DR PATRIC; 23935799; VBITheMar51294_0458. DR eggNOG; ENOG410683Z; Bacteria. DR eggNOG; ENOG410XUXP; LUCA. DR InParanoid; P35874; -. DR KO; K03073; -. DR OMA; ELVNYTA; -. DR OrthoDB; EOG6DRPR4; -. DR EvolutionaryTrace; P35874; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR GO; GO:0006605; P:protein targeting; IEA:InterPro. DR HAMAP; MF_00422; SecE; 1. DR InterPro; IPR022943; SecE. DR InterPro; IPR005807; SecE_bac. DR InterPro; IPR001901; Translocase_SecE/Sec61-g. DR Pfam; PF00584; SecE; 1. DR TIGRFAMs; TIGR00964; secE_bact; 1. DR PROSITE; PS01067; SECE_SEC61G; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Protein transport; Reference proteome; Translocation; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 65 Protein translocase subunit SecE. FT /FTId=PRO_0000104190. FT TOPO_DOM 1 34 Cytoplasmic. FT TRANSMEM 35 51 Helical. FT TOPO_DOM 52 65 Extracellular. FT HELIX 11 22 FT HELIX 33 51 FT HELIX 55 60 SQ SEQUENCE 65 AA; 7314 MW; A9EAC82A8E92947A CRC64; MEKLRKFFRE VIAEAKKISW PSRKELLTSF GVVLVILAVT SVYFFVLDFI FSGVVSAIFK ALGIG // ID SPEE_THEMA Reviewed; 296 AA. AC Q9WZC2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 09-DEC-2015, entry version 117. DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:11731804}; DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:11731804}; DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:11731804}; DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:17585781}; DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:17585781}; DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:17585781}; DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:11731804, ECO:0000269|PubMed:17585781}; GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; GN OrderedLocusNames=TM_0654; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP ENZYME REGULATION. RX PubMed=7641073; DOI=10.1016/1357-2725(95)00007-C; RA Pegg A.E., Poulin R., Coward J.K.; RT "Use of aminopropyltransferase inhibitors and of non-metabolizable RT analogs to study polyamine regulation and function."; RL Int. J. Biochem. Cell Biol. 27:425-442(1995). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-76; ASP-101; ASP-170 RP AND ASP-173, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY. RX PubMed=17585781; DOI=10.1021/bi602498k; RA Wu H., Min J., Ikeguchi Y., Zeng H., Dong A., Loppnau P., Pegg A.E., RA Plotnikov A.N.; RT "Structure and mechanism of spermidine synthases."; RL Biochemistry 46:8331-8339(2007). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF APOENZYME AND COMPLEX WITH RP SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=11731804; DOI=10.1038/nsb737; RA Korolev S., Ikeguchi Y., Skarina T., Beasley S., Arrowsmith C., RA Edwards A., Joachimiak A., Pegg A.E., Savchenko A.; RT "The crystal structure of spermidine synthase with a multisubstrate RT adduct inhibitor."; RL Nat. Struct. Biol. 9:27-31(2002). CC -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine CC group from the amino donor S-adenosylmethioninamine (decarboxy- CC AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. It CC has lower affinity and lower activity towards 1,3-diaminopropane, CC cadaverine (1,5-diaminopentane), agmatine, norspermidine and CC spermidine (in vitro). {ECO:0000255|HAMAP-Rule:MF_00198, CC ECO:0000269|PubMed:11731804, ECO:0000269|PubMed:17585781}. CC -!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine + CC putrescine = 5'-S-methyl-5'-thioadenosine + spermidine. CC {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:11731804, CC ECO:0000269|PubMed:17585781}. CC -!- ENZYME REGULATION: Strongly inhibited by S-adenosyl-1,8-diamino-3- CC thiooctane. {ECO:0000269|PubMed:7641073}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.75 uM for S-adenosylmethioninamine (at pH 7.5 and 37 CC degrees Celsius) {ECO:0000269|PubMed:17585781}; CC KM=19 uM for putrescine (at pH 7.5 and 37 degrees Celsius) CC {ECO:0000269|PubMed:17585781}; CC Note=Kcat is 0.77 sec(-1) for aminopropyltransferase activity CC with putrescine as substrate (at pH 7.5 and 37 degrees Celsius). CC Kcat is 22.7 sec(-1) for aminopropyltransferase activity with CC putrescine as substrate (at pH 7.5 and 80 degrees Celsius). CC {ECO:0000269|PubMed:17585781}; CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:11731804}; CC Temperature dependence: CC Optimum temperature is 90 degrees Celsius. CC {ECO:0000269|PubMed:11731804}; CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine CC biosynthesis; spermidine from putrescine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11731804}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- SIMILARITY: Contains 1 PABS (polyamine biosynthesis) domain. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35738.1; -; Genomic_DNA. DR PIR; C72348; C72348. DR RefSeq; NP_228463.1; NC_000853.1. DR RefSeq; WP_010865176.1; NC_000853.1. DR PDB; 1INL; X-ray; 1.50 A; A/B/C/D=1-296. DR PDB; 1JQ3; X-ray; 1.80 A; A/B/C/D=1-296. DR PDBsum; 1INL; -. DR PDBsum; 1JQ3; -. DR ProteinModelPortal; Q9WZC2; -. DR SMR; Q9WZC2; 2-296. DR STRING; 243274.TM0654; -. DR EnsemblBacteria; AAD35738; AAD35738; TM_0654. DR GeneID; 897762; -. DR KEGG; tma:TM0654; -. DR KEGG; tmi:THEMA_01395; -. DR PATRIC; 23936222; VBITheMar51294_0664. DR eggNOG; ENOG4105CCX; Bacteria. DR eggNOG; COG0421; LUCA. DR InParanoid; Q9WZC2; -. DR KO; K00797; -. DR OMA; SGLWSFT; -. DR OrthoDB; EOG644ZMH; -. DR BioCyc; TMAR243274:GC6P-679-MONOMER; -. DR BRENDA; 2.5.1.16; 6331. DR UniPathway; UPA00248; UER00314. DR EvolutionaryTrace; Q9WZC2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0043919; F:agmatine aminopropyltransferase activity; IDA:UniProtKB. DR GO; GO:0043918; F:cadaverine aminopropyltransferase activity; IDA:UniProtKB. DR GO; GO:0004766; F:spermidine synthase activity; IDA:UniProtKB. DR GO; GO:0050314; F:sym-norspermidine synthase activity; IDA:UniProtKB. DR GO; GO:0010487; F:thermospermine synthase activity; IDA:UniProtKB. DR GO; GO:0008295; P:spermidine biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00198; Spermidine_synth; 1. DR InterPro; IPR030374; PABS. DR InterPro; IPR030373; PABS_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR001045; Spermi_synthase. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00417; speE; 1. DR PROSITE; PS01330; PABS_1; 1. DR PROSITE; PS51006; PABS_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Polyamine biosynthesis; KW Reference proteome; Spermidine biosynthesis; Transferase. FT CHAIN 1 296 Polyamine aminopropyltransferase. FT /FTId=PRO_0000156513. FT DOMAIN 16 251 PABS. {ECO:0000255|HAMAP-Rule:MF_00198}. FT REGION 152 153 S-adenosylmethioninamine binding. FT {ECO:0000269|PubMed:11731804}. FT REGION 171 173 Polyamine binding. FT {ECO:0000269|PubMed:11731804}. FT ACT_SITE 170 170 Proton acceptor. FT {ECO:0000305|PubMed:11731804}. FT BINDING 21 21 Polyamine. {ECO:0000255|HAMAP- FT Rule:MF_00198}. FT BINDING 46 46 S-adenosylmethioninamine. FT {ECO:0000269|PubMed:11731804}. FT BINDING 66 66 Polyamine; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00198}. FT BINDING 77 77 Polyamine. {ECO:0000269|PubMed:11731804}. FT BINDING 101 101 Polyamine. {ECO:0000269|PubMed:11731804}. FT BINDING 121 121 S-adenosylmethioninamine. FT {ECO:0000269|PubMed:11731804}. FT MUTAGEN 76 76 Y->F: Reduces enzyme activity about 1000- FT fold. {ECO:0000269|PubMed:17585781}. FT MUTAGEN 101 101 D->I: Reduces enzyme activity over 10000- FT fold. {ECO:0000269|PubMed:17585781}. FT MUTAGEN 170 170 D->A: Reduces enzyme activity over 10000- FT fold. {ECO:0000269|PubMed:17585781}. FT MUTAGEN 173 173 D->A: Reduces enzyme activity about 500- FT fold. {ECO:0000269|PubMed:17585781}. FT HELIX 4 7 {ECO:0000244|PDB:1INL}. FT STRAND 15 22 {ECO:0000244|PDB:1INL}. FT STRAND 26 33 {ECO:0000244|PDB:1INL}. FT STRAND 35 42 {ECO:0000244|PDB:1INL}. FT STRAND 47 53 {ECO:0000244|PDB:1INL}. FT TURN 54 56 {ECO:0000244|PDB:1INL}. FT STRAND 57 62 {ECO:0000244|PDB:1INL}. FT STRAND 65 69 {ECO:0000244|PDB:1INL}. FT TURN 70 72 {ECO:0000244|PDB:1INL}. FT HELIX 73 87 {ECO:0000244|PDB:1INL}. FT STRAND 88 90 {ECO:0000244|PDB:1INL}. FT STRAND 93 98 {ECO:0000244|PDB:1INL}. FT HELIX 103 108 {ECO:0000244|PDB:1INL}. FT STRAND 115 122 {ECO:0000244|PDB:1INL}. FT HELIX 124 133 {ECO:0000244|PDB:1INL}. FT HELIX 135 138 {ECO:0000244|PDB:1INL}. FT HELIX 139 142 {ECO:0000244|PDB:1INL}. FT STRAND 146 151 {ECO:0000244|PDB:1INL}. FT HELIX 153 156 {ECO:0000244|PDB:1INL}. FT HELIX 157 159 {ECO:0000244|PDB:1INL}. FT STRAND 164 170 {ECO:0000244|PDB:1INL}. FT HELIX 177 179 {ECO:0000244|PDB:1INL}. FT HELIX 181 183 {ECO:0000244|PDB:1JQ3}. FT HELIX 185 194 {ECO:0000244|PDB:1INL}. FT STRAND 195 204 {ECO:0000244|PDB:1INL}. FT TURN 208 211 {ECO:0000244|PDB:1INL}. FT HELIX 212 225 {ECO:0000244|PDB:1INL}. FT STRAND 227 235 {ECO:0000244|PDB:1INL}. FT STRAND 242 252 {ECO:0000244|PDB:1INL}. FT TURN 255 258 {ECO:0000244|PDB:1INL}. FT HELIX 261 265 {ECO:0000244|PDB:1INL}. FT HELIX 276 281 {ECO:0000244|PDB:1INL}. FT HELIX 287 292 {ECO:0000244|PDB:1INL}. SQ SEQUENCE 296 AA; 34142 MW; 9298A156B7481945 CRC64; MRTLKELERE LQPRQHLWYF EYYTGNNVGL FMKMNRVIYS GQSDIQRIDI FENPDLGVVF ALDGITMTTE KDEFMYHEML AHVPMFLHPN PKKVLIIGGG DGGTLREVLK HDSVEKAILC EVDGLVIEAA RKYLKQTSCG FDDPRAEIVI ANGAEYVRKF KNEFDVIIID STDPTAGQGG HLFTEEFYQA CYDALKEDGV FSAETEDPFY DIGWFKLAYR RISKVFPITR VYLGFMTTYP SGMWSYTFAS KGIDPIKDFD PEKVRKFNKE LKYYNEEVHV ASFALPNFVK KELGLM // ID SOR_THEMA Reviewed; 131 AA. AC Q9WZC6; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Putative superoxide reductase; DE Short=SOR; DE EC=1.15.1.2; GN OrderedLocusNames=TM_0658; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Uses electrons from reduced NADP, by way of rubredoxin CC and an oxidoreductase, to catalyze the reduction of superoxide to CC hydrogen peroxide. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Reduced rubredoxin + superoxide + 2 H(+) = CC oxidized rubredoxin + H(2)O(2). {ECO:0000250|UniProtKB:P82385}. CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the desulfoferrodoxin family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35742.1; -; Genomic_DNA. DR PIR; G72348; G72348. DR RefSeq; NP_228467.1; NC_000853.1. DR RefSeq; WP_004081116.1; NZ_CP011107.1. DR PDB; 2AMU; X-ray; 2.00 A; A=1-131. DR PDB; 3QZB; X-ray; 1.10 A; A=1-131. DR PDBsum; 2AMU; -. DR PDBsum; 3QZB; -. DR ProteinModelPortal; Q9WZC6; -. DR SMR; Q9WZC6; 1-131. DR STRING; 243274.TM0658; -. DR EnsemblBacteria; AAD35742; AAD35742; TM_0658. DR GeneID; 897768; -. DR KEGG; tma:TM0658; -. DR PATRIC; 23936230; VBITheMar51294_0668. DR eggNOG; ENOG4108YZ8; Bacteria. DR eggNOG; COG2033; LUCA. DR InParanoid; Q9WZC6; -. DR KO; K05919; -. DR OMA; HVPVIEY; -. DR OrthoDB; EOG6B8XMT; -. DR BRENDA; 1.15.1.2; 6331. DR EvolutionaryTrace; Q9WZC6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050605; F:superoxide reductase activity; IEA:UniProtKB-EC. DR InterPro; IPR002742; Desulfoferrodoxin_Fe-bd_dom. DR Pfam; PF01880; Desulfoferrodox; 1. DR SUPFAM; SSF49367; SSF49367; 1. DR TIGRFAMs; TIGR00332; neela_ferrous; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Electron transport; Iron; KW Metal-binding; Oxidoreductase; Reference proteome; Transport. FT CHAIN 1 131 Putative superoxide reductase. FT /FTId=PRO_0000140876. FT METAL 15 15 Iron. {ECO:0000250}. FT METAL 17 17 Iron. {ECO:0000250}. FT METAL 45 45 Iron. {ECO:0000250}. FT METAL 51 51 Iron. {ECO:0000250}. FT METAL 115 115 Iron. {ECO:0000250}. FT METAL 118 118 Iron. {ECO:0000250}. FT HELIX 3 6 {ECO:0000244|PDB:3QZB}. FT TURN 12 14 {ECO:0000244|PDB:3QZB}. FT STRAND 19 22 {ECO:0000244|PDB:3QZB}. FT STRAND 25 27 {ECO:0000244|PDB:3QZB}. FT STRAND 32 43 {ECO:0000244|PDB:3QZB}. FT STRAND 48 51 {ECO:0000244|PDB:3QZB}. FT STRAND 53 62 {ECO:0000244|PDB:3QZB}. FT STRAND 69 75 {ECO:0000244|PDB:3QZB}. FT STRAND 95 102 {ECO:0000244|PDB:3QZB}. FT STRAND 107 115 {ECO:0000244|PDB:3QZB}. FT TURN 116 118 {ECO:0000244|PDB:3QZB}. FT STRAND 119 129 {ECO:0000244|PDB:3QZB}. SQ SEQUENCE 131 AA; 14935 MW; C5380BF586F124CE CRC64; MKLSDFIKTE DFKKEKHVPV IEAPEKVKKD EKVQIVVTVG KEIPHPNTTE HHIRWIKVFF QPDGDPYVYE VGRYEFNAHG ESVQGPNIGA VYTEPTVTTV VKLNRSGTII ALSYCNIHGL WESSQKITVE E // ID SPEH_THEMA Reviewed; 130 AA. AC Q9WZC3; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 113. DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme; DE Short=AdoMetDC; DE Short=SAMDC; DE EC=4.1.1.50; DE Contains: DE RecName: Full=S-adenosylmethionine decarboxylase beta chain; DE Contains: DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain; DE Flags: Precursor; GN Name=speH; OrderedLocusNames=TM_0655; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-63, RP SUBUNIT, SELF-PROCESSING, ACTIVE SITES, AND MUTAGENESIS OF SER-55; RP SER-63; HIS-68 AND CYS-83. RX PubMed=15150268; DOI=10.1074/jbc.M403369200; RA Toms A.V., Kinsland C., McCloskey D.E., Pegg A.E., Ealick S.E.; RT "Evolutionary links as revealed by the structure of Thermotoga RT maritima S-adenosylmethionine decarboxylase."; RL J. Biol. Chem. 279:33837-33846(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS). RG Joint center for structural genomics (JCSG); RT "Crystal structure of S-adenosylmethionine decarboxylase proenzyme RT (tm0655) from Thermotoga maritima at 1.2-A resolution."; RL Submitted (MAR-2005) to the PDB data bank. CC -!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to CC S-adenosylmethioninamine (dcAdoMet), the propylamine donor CC required for the synthesis of the polyamines spermine and CC spermidine from the diamine putrescine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = S-adenosyl 3- CC (methylthio)propylamine + CO(2). CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000305}; CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000305}; CC -!- PATHWAY: Amine and polyamine biosynthesis; S- CC adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from CC S-adenosyl-L-methionine: step 1/1. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged CC as a dimer of alpha/beta heterodimers. CC {ECO:0000269|PubMed:15150268}. CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation CC of the active enzyme involves a self-maturation process in which CC the active site pyruvoyl group is generated from an internal CC serine residue via an autocatalytic post-translational CC modification. Two non-identical subunits are generated from the CC proenzyme in this reaction, and the pyruvate is formed at the N- CC terminus of the alpha chain, which is derived from the carboxyl CC end of the proenzyme. The post-translation cleavage follows an CC unusual pathway, termed non-hydrolytic serinolysis, in which the CC side chain hydroxyl group of the serine supplies its oxygen atom CC to form the C-terminus of the beta chain, while the remainder of CC the serine residue undergoes an oxidative deamination to produce CC ammonia and the pyruvoyl group blocking the N-terminus of the CC alpha chain (Probable). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1 CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35739.1; -; Genomic_DNA. DR PIR; D72348; D72348. DR RefSeq; NP_228464.1; NC_000853.1. DR RefSeq; WP_004081137.1; NZ_CP011107.1. DR PDB; 1TLU; X-ray; 1.55 A; A/B=1-130. DR PDB; 1TMI; X-ray; 1.70 A; A/B=1-130. DR PDB; 1VR7; X-ray; 1.20 A; A/B=1-130. DR PDB; 3IWB; X-ray; 2.06 A; A/C=64-130, B/D=1-62. DR PDB; 3IWC; X-ray; 1.90 A; A/C=64-130, B/D=1-62. DR PDB; 3IWD; X-ray; 1.90 A; A/C=64-130, B/D=1-62. DR PDBsum; 1TLU; -. DR PDBsum; 1TMI; -. DR PDBsum; 1VR7; -. DR PDBsum; 3IWB; -. DR PDBsum; 3IWC; -. DR PDBsum; 3IWD; -. DR ProteinModelPortal; Q9WZC3; -. DR SMR; Q9WZC3; 2-121. DR STRING; 243274.TM0655; -. DR EnsemblBacteria; AAD35739; AAD35739; TM_0655. DR GeneID; 897764; -. DR KEGG; tma:TM0655; -. DR PATRIC; 23936224; VBITheMar51294_0665. DR eggNOG; ENOG4105X3E; Bacteria. DR eggNOG; COG1586; LUCA. DR InParanoid; Q9WZC3; -. DR KO; K01611; -. DR OMA; INPWDAC; -. DR OrthoDB; EOG6358J6; -. DR BRENDA; 4.1.1.50; 6331. DR UniPathway; UPA00331; UER00451. DR EvolutionaryTrace; Q9WZC3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.90.10; -; 1. DR HAMAP; MF_00464; AdoMetDC_1; 1. DR InterPro; IPR003826; AdoMetDC_fam_prok. DR InterPro; IPR016067; S-AdoMet_deCO2ase_core. DR InterPro; IPR017716; S-AdoMet_deCOase_pro-enz. DR Pfam; PF02675; AdoMet_dc; 1. DR SUPFAM; SSF56276; SSF56276; 1. DR TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 1. PE 1: Evidence at protein level; KW 3D-structure; Autocatalytic cleavage; Complete proteome; KW Decarboxylase; Lyase; Polyamine biosynthesis; Pyruvate; KW Reference proteome; S-adenosyl-L-methionine; Schiff base; KW Spermidine biosynthesis; Zymogen. FT CHAIN 1 62 S-adenosylmethionine decarboxylase beta FT chain. {ECO:0000305}. FT /FTId=PRO_0000030123. FT CHAIN 63 130 S-adenosylmethionine decarboxylase alpha FT chain. {ECO:0000305}. FT /FTId=PRO_0000030124. FT ACT_SITE 63 63 Schiff-base intermediate with substrate; FT via pyruvic acid. {ECO:0000250}. FT ACT_SITE 68 68 Proton acceptor; for processing activity. FT {ECO:0000305|PubMed:15150268}. FT ACT_SITE 83 83 Proton donor; for catalytic activity. FT {ECO:0000305|PubMed:15150268}. FT SITE 62 63 Cleavage (non-hydrolytic); by autolysis. FT {ECO:0000305}. FT MOD_RES 63 63 Pyruvic acid (Ser); by autocatalysis. FT {ECO:0000305}. FT MUTAGEN 55 55 S->A: Cleaves more rapidly than the wild- FT type. {ECO:0000269|PubMed:15150268}. FT MUTAGEN 63 63 S->A: Loss of processing. FT {ECO:0000269|PubMed:15150268}. FT MUTAGEN 68 68 H->A: Cleaves much more slowly than the FT wild-type, but the addition of FT hydroxylamine which is known to cleave FT ester bonds leads to the cleavage of this FT mutant. {ECO:0000269|PubMed:15150268}. FT MUTAGEN 83 83 C->A: Cleaves more rapidly than the wild- FT type. {ECO:0000269|PubMed:15150268}. FT STRAND 3 14 {ECO:0000244|PDB:1VR7}. FT HELIX 17 20 {ECO:0000244|PDB:1VR7}. FT HELIX 23 37 {ECO:0000244|PDB:1VR7}. FT STRAND 41 48 {ECO:0000244|PDB:1VR7}. FT STRAND 50 52 {ECO:0000244|PDB:1VR7}. FT STRAND 54 60 {ECO:0000244|PDB:1VR7}. FT STRAND 63 70 {ECO:0000244|PDB:1VR7}. FT HELIX 71 73 {ECO:0000244|PDB:1VR7}. FT STRAND 75 84 {ECO:0000244|PDB:1VR7}. FT HELIX 89 100 {ECO:0000244|PDB:1VR7}. FT STRAND 103 114 {ECO:0000244|PDB:1VR7}. FT HELIX 115 118 {ECO:0000244|PDB:1VR7}. SQ SEQUENCE 130 AA; 14785 MW; 7659FE20A2019928 CRC64; MKSLGRHLVA EFYECDREVL DNVQLIEQEM KQAAYESGAT IVTSTFHRFL PYGVSGVVVI SESHLTIHTW PEYGYAAIDL FTCGEDVDPW KAFEHLKKAL KAKRVHVVEH ERGRYDEIGI PEDSPHKAAV // ID SSRP_THEMA Reviewed; 150 AA. AC P56944; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=SsrA-binding protein {ECO:0000255|HAMAP-Rule:MF_00023}; DE AltName: Full=Small protein B {ECO:0000255|HAMAP-Rule:MF_00023}; GN Name=smpB {ECO:0000255|HAMAP-Rule:MF_00023}; GN OrderedLocusNames=TM_0254; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Required for rescue of stalled ribosomes mediated by CC trans-translation. Binds to transfer-messenger RNA (tmRNA), CC required for stable association of tmRNA with ribosomes. tmRNA and CC SmpB together mimic tRNA shape, replacing the anticodon stem-loop CC with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold CC to resemble tRNA(Ala) and it encodes a 'tag peptide', a short CC internal open reading frame. During trans-translation Ala- CC aminoacylated tmRNA acts like a tRNA, entering the A-site of CC stalled ribosomes, displacing the stalled mRNA. The ribosome then CC switches to translate the ORF on the tmRNA; the nascent peptide is CC terminated with the 'tag peptide' encoded by the tmRNA and CC targeted for degradation. The ribosome is freed to recommence CC translation, which seems to be the essential function of trans- CC translation. {ECO:0000255|HAMAP-Rule:MF_00023}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00023}. CC Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes. CC {ECO:0000255|HAMAP-Rule:MF_00023}. CC -!- SIMILARITY: Belongs to the SmpB family. {ECO:0000255|HAMAP- CC Rule:MF_00023}. CC -!- SEQUENCE CAUTION: CC Sequence=AE000512; Type=Frameshift; Positions=125; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; WP_011943280.1; NZ_CP011107.1. DR ProteinModelPortal; P56944; -. DR SMR; P56944; 5-124. DR STRING; 243274.TM0254; -. DR KEGG; tmw:THMA_0261; -. DR eggNOG; ENOG4108UH4; Bacteria. DR eggNOG; COG0691; LUCA. DR InParanoid; P56944; -. DR KO; K03664; -. DR OMA; FLLNAHI; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070929; P:trans-translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.280.10; -; 1. DR HAMAP; MF_00023; SmpB; 1. DR InterPro; IPR023620; SmpB. DR InterPro; IPR000037; SsrA-bd_prot. DR InterPro; IPR020081; SsrA-bd_prot_CS. DR Pfam; PF01668; SmpB; 1. DR ProDom; PD004488; SmpB; 1. DR SUPFAM; SSF74982; SSF74982; 1. DR TIGRFAMs; TIGR00086; smpB; 1. DR PROSITE; PS01317; SSRP; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; RNA-binding. FT CHAIN 1 150 SsrA-binding protein. FT /FTId=PRO_0000103054. SQ SEQUENCE 150 AA; 17594 MW; 06519CDBFB328391 CRC64; MVKVVATNKK AYTDYEILET YEAGIVLTGT EVKSLRNGSV NFKDSFCRFK NGELYLLNLH IPPYSHGGVY NHDPERPRKL LLHKRELKRL MGKVQEEGVT IVPLKIYFND RGIAKVEIAV ARGKKKYDKR EAIKKREMER KIREYMKYSR // ID SSB_THEMA Reviewed; 141 AA. AC Q9WZ73; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_00984}; DE Short=SSB {ECO:0000255|HAMAP-Rule:MF_00984}; GN Name=ssb; OrderedLocusNames=TM_0604; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00984}. CC -!- SIMILARITY: Contains 1 SSB domain. {ECO:0000255|HAMAP- CC Rule:MF_00984}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35689.1; -; Genomic_DNA. DR PIR; H72354; H72354. DR RefSeq; NP_228414.1; NC_000853.1. DR RefSeq; WP_004081225.1; NZ_CP011107.1. DR PDB; 1Z9F; X-ray; 2.30 A; A=1-141. DR PDBsum; 1Z9F; -. DR ProteinModelPortal; Q9WZ73; -. DR SMR; Q9WZ73; 1-108. DR STRING; 243274.TM0604; -. DR PRIDE; Q9WZ73; -. DR EnsemblBacteria; AAD35689; AAD35689; TM_0604. DR GeneID; 897685; -. DR KEGG; tma:TM0604; -. DR PATRIC; 23936123; VBITheMar51294_0615. DR eggNOG; ENOG4108UUM; Bacteria. DR eggNOG; COG0629; LUCA. DR InParanoid; Q9WZ73; -. DR KO; K03111; -. DR OMA; QTTDFFR; -. DR OrthoDB; EOG6M9F32; -. DR EvolutionaryTrace; Q9WZ73; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00984; SSB; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000424; Primosome_PriB/ssb. DR InterPro; IPR011344; ssDNA-bd. DR PANTHER; PTHR10302; PTHR10302; 1. DR Pfam; PF00436; SSB; 1. DR PIRSF; PIRSF002070; SSB; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00621; ssb; 1. DR PROSITE; PS50935; SSB; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 141 Single-stranded DNA-binding protein. FT /FTId=PRO_0000096128. FT DOMAIN 4 108 SSB. {ECO:0000255|HAMAP-Rule:MF_00984}. FT STRAND 7 15 {ECO:0000244|PDB:1Z9F}. FT STRAND 18 21 {ECO:0000244|PDB:1Z9F}. FT STRAND 27 36 {ECO:0000244|PDB:1Z9F}. FT STRAND 50 58 {ECO:0000244|PDB:1Z9F}. FT HELIX 59 68 {ECO:0000244|PDB:1Z9F}. FT STRAND 74 84 {ECO:0000244|PDB:1Z9F}. FT STRAND 96 106 {ECO:0000244|PDB:1Z9F}. SQ SEQUENCE 141 AA; 16298 MW; A96A77731553404E CRC64; MSFFNKIILI GRLVRDPEER YTLSGTPVTT FTIAVDRVPR KNAPDDAQTT DFFRIVTFGR LAEFARTYLT KGRLVLVEGE MRMRRWETPT GEKRVSPEVV ANVVRFMDRK PAETVSETEE ELEIPEEDFS SDTFSEDEPP F // ID SURE_THEMA Reviewed; 247 AA. AC P96112; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 127. DE RecName: Full=5'-nucleotidase SurE; DE EC=3.1.3.5; DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase; GN Name=surE; OrderedLocusNames=TM_1662; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 156-247. RX PubMed=9086272; DOI=10.1006/jmbi.1996.0835; RA Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.; RT "A survey of polypeptide deformylase function throughout the RT eubacterial lineage."; RL J. Mol. Biol. 266:939-949(1997). RN [3] RP COFACTOR. RX PubMed=12595266; RA Mura C., Katz J.E., Clarke S.G., Eisenberg D.; RT "Structure and function of an archaeal homolog of survival protein E RT (SurEalpha): an acid phosphatase with purine nucleotide specificity."; RL J. Mol. Biol. 326:1559-1575(2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), CHARACTERIZATION, SUBUNIT, AND RP MUTAGENESIS. RX PubMed=11709173; DOI=10.1016/S0969-2126(01)00675-X; RA Zhang R.-G., Skarina T., Katz J.E., Beasley S., Khachatryan A., RA Vyas S., Arrowsmith C.H., Clarke S., Edwards A., Joachimiak A., RA Savchenko A.; RT "Structure of Thermotoga maritima stationary phase survival protein RT SurE: a novel acid phosphatase."; RL Structure 9:1095-1106(2001). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND CHARACTERIZATION. RX PubMed=11524683; DOI=10.1038/nsb0901-789; RA Lee J.Y., Kwak J.E., Moon J., Eom S.H., Liong E.C., Pedelacq J.-D., RA Berendzen J., Suh S.W.; RT "Crystal structure and functional analysis of the SurE protein RT identify a novel phosphatase family."; RL Nat. Struct. Biol. 8:789-794(2001). CC -!- FUNCTION: Nucleotidase that preferentially dephosphorylates 5'-GMP CC and 5'-AMP. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:12595266}; CC Note=Binds 1 Mg(2+) ion per subunit. In contrast to other surE CC homologs, is essentially inactive with other divalent cations. CC {ECO:0000269|PubMed:12595266}; CC -!- ENZYME REGULATION: Inhibited by vanadate and tungstate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=31.5 mM for pNPP (at 76 degrees Celsius); CC Vmax=51.6 umol/min/mg enzyme with pNPP as substrate (at 76 CC degrees Celsius); CC pH dependence: CC Optimum pH is 5.5-6.2.; CC Temperature dependence: CC Optimum temperature is 80 degrees Celsius. Active up to 95 CC degrees Celsius.; CC -!- SUBUNIT: Homodimer and possibly homotetramer. CC {ECO:0000269|PubMed:11709173}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the SurE nucleotidase family. CC {ECO:0000305}. CC -!- CAUTION: Was originally annotated as an acid phosphatase CC (EC 3.1.3.2). {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36729.1; -; Genomic_DNA. DR EMBL; Y10306; CAA71355.1; -; Genomic_DNA. DR PIR; D72224; D72224. DR RefSeq; NP_229462.1; NC_000853.1. DR RefSeq; WP_004082178.1; NZ_CP011107.1. DR PDB; 1ILV; X-ray; 2.00 A; A/B=1-247. DR PDB; 1J9J; X-ray; 1.90 A; A/B=1-247. DR PDB; 1J9K; X-ray; 2.10 A; A/B=1-247. DR PDB; 1J9L; X-ray; 1.90 A; A/B=1-247. DR PDBsum; 1ILV; -. DR PDBsum; 1J9J; -. DR PDBsum; 1J9K; -. DR PDBsum; 1J9L; -. DR ProteinModelPortal; P96112; -. DR SMR; P96112; 1-247. DR STRING; 243274.TM1662; -. DR DNASU; 897339; -. DR EnsemblBacteria; AAD36729; AAD36729; TM_1662. DR GeneID; 897339; -. DR KEGG; tma:TM1662; -. DR PATRIC; 23938298; VBITheMar51294_1681. DR eggNOG; ENOG4105CV2; Bacteria. DR eggNOG; COG0496; LUCA. DR InParanoid; P96112; -. DR KO; K03787; -. DR OMA; NLNIPPC; -. DR OrthoDB; EOG68WR45; -. DR EvolutionaryTrace; P96112; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.1210.10; -; 1. DR HAMAP; MF_00060; SurE; 1. DR InterPro; IPR030048; SurE. DR InterPro; IPR002828; SurE-like_Pase/nucleotidase. DR Pfam; PF01975; SurE; 1. DR SUPFAM; SSF64167; SSF64167; 1. DR TIGRFAMs; TIGR00087; surE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 247 5'-nucleotidase SurE. FT /FTId=PRO_0000111846. FT METAL 8 8 Magnesium. FT METAL 9 9 Magnesium. FT METAL 39 39 Magnesium. FT METAL 95 95 Magnesium. FT MUTAGEN 8 8 D->N: Loss of activity. FT {ECO:0000269|PubMed:11709173}. FT MUTAGEN 9 9 D->N: Loss of activity. FT {ECO:0000269|PubMed:11709173}. FT MUTAGEN 127 127 S->A: Loss of activity. FT {ECO:0000269|PubMed:11709173}. FT STRAND 2 6 {ECO:0000244|PDB:1J9J}. FT HELIX 14 23 {ECO:0000244|PDB:1J9J}. FT TURN 24 26 {ECO:0000244|PDB:1J9J}. FT STRAND 27 36 {ECO:0000244|PDB:1J9J}. FT STRAND 53 55 {ECO:0000244|PDB:1J9J}. FT STRAND 59 69 {ECO:0000244|PDB:1J9J}. FT HELIX 71 80 {ECO:0000244|PDB:1J9J}. FT STRAND 88 97 {ECO:0000244|PDB:1J9J}. FT HELIX 101 106 {ECO:0000244|PDB:1J9J}. FT HELIX 108 118 {ECO:0000244|PDB:1J9J}. FT STRAND 123 129 {ECO:0000244|PDB:1J9J}. FT STRAND 131 133 {ECO:0000244|PDB:1J9J}. FT HELIX 136 149 {ECO:0000244|PDB:1J9J}. FT HELIX 152 154 {ECO:0000244|PDB:1J9J}. FT STRAND 160 165 {ECO:0000244|PDB:1J9J}. FT STRAND 172 175 {ECO:0000244|PDB:1J9J}. FT STRAND 182 191 {ECO:0000244|PDB:1J9J}. FT STRAND 197 206 {ECO:0000244|PDB:1J9J}. FT STRAND 212 214 {ECO:0000244|PDB:1J9J}. FT HELIX 215 220 {ECO:0000244|PDB:1J9J}. FT STRAND 223 229 {ECO:0000244|PDB:1J9J}. FT HELIX 236 245 {ECO:0000244|PDB:1J9J}. SQ SEQUENCE 247 AA; 28075 MW; 09F4A68A80C0B241 CRC64; MRILVTNDDG IQSKGIIVLA ELLSEEHEVF VVAPDKERSA TGHSITIHVP LWMKKVFISE RVVAYSTTGT PADCVKLAYN VVMDKRVDLI VSGVNRGPNM GMDILHSGTV SGAMEGAMMN IPSIAISSAN YESPDFEGAA RFLIDFLKEF DFSLLDPFTM LNINVPAGEI KGWRFTRQSR RRWNDYFEER VSPFGEKYYW MMGEVIEDDD RDDVDYKAVR EGYVSITPIH PFLTNEQCLK KLREVYD // ID SYA_THEMA Reviewed; 863 AA. AC Q9X1B6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00036}; DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00036}; DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_00036}; GN Name=alaS {ECO:0000255|HAMAP-Rule:MF_00036}; GN OrderedLocusNames=TM_1396; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a CC two-step reaction: alanine is first activated by ATP to form Ala- CC AMP and then transferred to the acceptor end of tRNA(Ala). Also CC edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its CC editing domain. {ECO:0000255|HAMAP-Rule:MF_00036}. CC -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP + CC diphosphate + L-alanyl-tRNA(Ala). {ECO:0000255|HAMAP- CC Rule:MF_00036}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00036}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00036}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00036}. CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic CC domain, the editing domain and the C-terminal C-Ala domain. The CC editing domain removes incorrectly charged amino acids, while the CC C-Ala domain, along with tRNA(Ala), serves as a bridge to CC cooperatively bring together the editing and aminoacylation CC centers thus stimulating deacylation of misacylated tRNAs. CC {ECO:0000255|HAMAP-Rule:MF_00036}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00036}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36467.1; -; Genomic_DNA. DR PIR; E72259; E72259. DR RefSeq; NP_229197.1; NC_000853.1. DR RefSeq; WP_004081612.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1B6; -. DR SMR; Q9X1B6; 4-461. DR STRING; 243274.TM1396; -. DR EnsemblBacteria; AAD36467; AAD36467; TM_1396. DR GeneID; 898080; -. DR KEGG; tma:TM1396; -. DR PATRIC; 23937738; VBITheMar51294_1408. DR eggNOG; ENOG4105CIM; Bacteria. DR eggNOG; COG0013; LUCA. DR InParanoid; Q9X1B6; -. DR KO; K01872; -. DR OMA; EAIKWAW; -. DR OrthoDB; EOG6Q2SQ2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004813; F:alanine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IBA:GO_Central. DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central. DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1. DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc. DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd. DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core. DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N. DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac. DR InterPro; IPR003156; DHHA1_dom. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR012947; tRNA_SAD. DR Pfam; PF02272; DHHA1; 1. DR Pfam; PF01411; tRNA-synt_2c; 1. DR Pfam; PF07973; tRNA_SAD; 1. DR PRINTS; PR00980; TRNASYNTHALA. DR SMART; SM00863; tRNA_SAD; 1. DR SUPFAM; SSF101353; SSF101353; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF55186; SSF55186; 1. DR TIGRFAMs; TIGR00344; alaS; 1. DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; RNA-binding; tRNA-binding; Zinc. FT CHAIN 1 863 Alanine--tRNA ligase. FT /FTId=PRO_0000075232. FT METAL 561 561 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 565 565 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 663 663 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 667 667 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. SQ SEQUENCE 863 AA; 98098 MW; EDDE182B047D8D13 CRC64; MRYMTSEEIR EAFLKFFEKK GHKILPSASL IPDDPQLLFT VAGMVPFKPI FWGKVEPVYT RVATCQKCLR TVDIENVGKT PRHHTFFEML GNFSFGDYFK EEAIEWAWEF LTQVLGVPEE KLWVSVYEED EEAFRIWNEK IGLPEKRILR MGKEDNFWGP AGPTGPCGPD TEIFYDTGYS KGCPEGEGCT PANSEGRFVE IWNLVFTEYY QDEEGKLHPL PRKNIDTGAG LERFCAMMQG VYSNFDTDLF QPIIKRIEEL TGVGYKTDEE KDVSIRVIAD HIRAITFLIS EGVFPSNEGR GYVLRRIIRR AMRHGILLGM SEPFLYRIVD AVVEKMGKVY PEIVRGEGMV KEVLSAEENR FLKTLEQGMK VFDEIVEKKG KIDSEDAFRL YDTYGLPLEL TLEIAKEKGV EVDVQEFNKY MEEQQRKSRA AMGDVEFARR YEYLEKLPKD FRTEFTGYEK LEDEGEVVLV ARDDETVEEA SEGTVEVVFS RTPFYAEKGG QVSDTGMVEW RDGKALVEYV FEASEGVIVH RIKILDGTLR RGQKVILRVD KKRREATMRN HTATHLLHAA LKKVLGDHVR QAGSLVAPDR LRFDFTHFKG LSSAEIEQVE DLVNEWIMEA IPVEVRYTSY EEAVKSGVVA LFTEKYGDVV RVVEVPGVSK ELCGGTHVKN TGQIGLFKII SEESVSSGVR RIEAVTGFSA LELLRNQKKL IDQLKEILGA REDELTDRVL SLREKVKELE KKLSQGRISE ERIAMKQLED GVKVFHGVFE GVEAKHLGGI ADNVLKKEGE GIVILFSKFE NKVSLVVKVS ENLLGKYDAS SIARNIAKEL GGNGGGRKNF AQAGGRHPER IKDVLERLEE FLR // ID SYC_THEMA Reviewed; 460 AA. AC Q9WZH8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=Cysteine--tRNA ligase; DE EC=6.1.1.16; DE AltName: Full=Cysteinyl-tRNA synthetase; DE Short=CysRS; GN Name=cysS; OrderedLocusNames=TM_0719; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP + CC diphosphate + L-cysteinyl-tRNA(Cys). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35801.1; -; Genomic_DNA. DR PIR; E72341; E72341. DR RefSeq; NP_228528.1; NC_000853.1. DR RefSeq; WP_004081016.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZH8; -. DR STRING; 243274.TM0719; -. DR PRIDE; Q9WZH8; -. DR EnsemblBacteria; AAD35801; AAD35801; TM_0719. DR GeneID; 898386; -. DR KEGG; tma:TM0719; -. DR PATRIC; 23936358; VBITheMar51294_0732. DR eggNOG; ENOG4105C8N; Bacteria. DR eggNOG; COG0215; LUCA. DR InParanoid; Q9WZH8; -. DR KO; K01883; -. DR OMA; HENEACQ; -. DR OrthoDB; EOG6RVFXC; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IBA:GO_Central. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00041; Cys_tRNA_synth; 1. DR InterPro; IPR015803; Cys-tRNA-ligase. DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR. DR InterPro; IPR024909; Cys-tRNA/MSH_ligase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR032678; tRNA-synt_1_cat_dom. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR PANTHER; PTHR10890; PTHR10890; 1. DR Pfam; PF09190; DALR_2; 1. DR Pfam; PF01406; tRNA-synt_1e; 1. DR PRINTS; PR00983; TRNASYNTHCYS. DR SMART; SM00840; DALR_2; 1. DR SUPFAM; SSF47323; SSF47323; 1. DR TIGRFAMs; TIGR00435; cysS; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 460 Cysteine--tRNA ligase. FT /FTId=PRO_0000159506. FT MOTIF 29 39 "HIGH" region. FT MOTIF 264 268 "KMSKS" region. FT METAL 27 27 Zinc. {ECO:0000250}. FT METAL 207 207 Zinc. {ECO:0000250}. FT METAL 232 232 Zinc. {ECO:0000250}. FT METAL 236 236 Zinc. {ECO:0000250}. FT BINDING 267 267 ATP. {ECO:0000250}. SQ SEQUENCE 460 AA; 53418 MW; 937C5A0526C4D359 CRC64; MRITNTLTGK KEEFVPIQPG VVRMYVCGPT VYDLIHVGNA RPALVFDVFR RYLEYRGYRV IMVQNFTDID DKIINKANQL GVDYKTVADT FIAEYWRDAH ALGIRPANFH PRTTDFVEDI VEIIEKLVEK GFAYQTETGV YFDVRKFEKY GELSKKKIED LIAGARVEVD ETKKSPLDFS LWKKAKPGEP CWKSPWGEGR PGWHIECTVM SVKILGESFD IHAGGEDLVF PHHENEKAQA EALTGKVFAR YWMHNGMVRF LGDKMSKSTG NIFTVREAVK RYGRDGLRYM ILSKHYRSPM DFSEELLQDY SRAVKRVWEI LGRYEKSGDI GIPKRNAVYE EYVNRFVEAL DDDFNTPVAV SLIFELARNL SKAMDDNDRE DALLYYHLIR REFGPVLGLF DLNEEKKEVS SEELLKLLIE VRDVLRKEKR YDLSDRIRDR LREIGIILKD TPSGTEYTVE // ID SYFA_THEMA Reviewed; 325 AA. AC Q9WZS8; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit; DE EC=6.1.1.20; DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit; DE Short=PheRS; GN Name=pheS; OrderedLocusNames=TM_0821; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Phe-tRNA synthetase alpha subunit type 1 subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35903.1; -; Genomic_DNA. DR PIR; H72329; H72329. DR RefSeq; NP_228630.1; NC_000853.1. DR RefSeq; WP_004080838.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZS8; -. DR SMR; Q9WZS8; 89-325. DR STRING; 243274.TM0821; -. DR EnsemblBacteria; AAD35903; AAD35903; TM_0821. DR GeneID; 898491; -. DR KEGG; tma:TM0821; -. DR PATRIC; 23936566; VBITheMar51294_0833. DR eggNOG; ENOG4105CSS; Bacteria. DR eggNOG; COG0016; LUCA. DR InParanoid; Q9WZS8; -. DR KO; K01889; -. DR OMA; KGTGWLE; -. DR OrthoDB; EOG6WX4QN; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central. DR HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu. DR InterPro; IPR004188; Phe-tRNA_ligase_II_N. DR InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR InterPro; IPR010978; tRNA-bd_arm. DR Pfam; PF02912; Phe_tRNA-synt_N; 1. DR Pfam; PF01409; tRNA-synt_2d; 1. DR SUPFAM; SSF46589; SSF46589; 1. DR TIGRFAMs; TIGR00468; pheS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 325 Phenylalanine--tRNA ligase alpha subunit. FT /FTId=PRO_0000126783. FT METAL 251 251 Magnesium. {ECO:0000250}. SQ SEQUENCE 325 AA; 37875 MW; 30BF5287F068BC3F CRC64; MEIEAVEKEA IEKLSKISNV QELESFRIEF LGKKGKITGL MKNLKNLPPE ERPAYGKRVN ELREKIEKLF EEKRQQIQRI LEQEKMEKMR IDVTVPGARR KLGHSHPVLK VMEEIERIFV SMGFDVVEGP EIETTWHNFD ALNTPEWHPA RDEHDSFYIT DDLLLRTHTS PVQIRTMLER KPPIAIISPG KVYRRDYDAT HLPMFHQVEG LHVDRDLSVA HLKFTLEEFA RRMFGEGAKV RLRPSFFPFT EPSFEVDVYL SGYGWLEILG AGMVDPNVFL NVGYDPEEWT GYAFGMGVER IAMLKYGIAD IREFVRNDVR FLSSY // ID SYE1_THEMA Reviewed; 469 AA. AC Q9X172; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=Glutamate--tRNA ligase 1; DE EC=6.1.1.17; DE AltName: Full=Glutamyl-tRNA synthetase 1; DE Short=GluRS 1; GN Name=gltX1; OrderedLocusNames=TM_1351; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS). RG Joint center for structural genomics (JCSG); RT "Crystal structure of glutamyl-tRNA synthetase 1 (EC 6.1.1.17) RT (glutamate-tRNA ligase 1) (glurS 1) (TM1351) from Thermotoga maritima RT at 2.5 A resolution."; RL Submitted (DEC-2006) to the PDB data bank. CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a CC two-step reaction: glutamate is first activated by ATP to form CC Glu-AMP and then transferred to the acceptor end of tRNA(Glu). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP + CC diphosphate + L-glutamyl-tRNA(Glu). CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36422.1; -; Genomic_DNA. DR PIR; G72264; G72264. DR RefSeq; NP_229152.1; NC_000853.1. DR RefSeq; WP_004081547.1; NZ_CP011107.1. DR PDB; 2O5R; X-ray; 2.34 A; A=1-469. DR PDBsum; 2O5R; -. DR ProteinModelPortal; Q9X172; -. DR SMR; Q9X172; 1-468. DR STRING; 243274.TM1351; -. DR PRIDE; Q9X172; -. DR EnsemblBacteria; AAD36422; AAD36422; TM_1351. DR GeneID; 898129; -. DR KEGG; tma:TM1351; -. DR PATRIC; 23937640; VBITheMar51294_1363. DR eggNOG; ENOG4105C20; Bacteria. DR eggNOG; COG0008; LUCA. DR InParanoid; Q9X172; -. DR KO; K09698; -. DR OMA; AMELMGK; -. DR OrthoDB; EOG6DRPF7; -. DR EvolutionaryTrace; Q9X172; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.350; -; 1. DR Gene3D; 1.10.1160.10; -; 1. DR Gene3D; 1.10.8.70; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00022_B; Glu_tRNA_synth_B; 1. DR InterPro; IPR008925; aa-tRNA-synth_I_codon-bd. DR InterPro; IPR020752; aa-tRNA-synth_I_codon-bd_sub1. DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00749; tRNA-synt_1c; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF48163; SSF48163; 1. DR TIGRFAMs; TIGR00464; gltX_bact; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 469 Glutamate--tRNA ligase 1. FT /FTId=PRO_0000119680. FT MOTIF 8 18 "HIGH" region. FT MOTIF 250 254 "KMSKS" region. FT BINDING 253 253 ATP. {ECO:0000250}. FT STRAND 3 6 {ECO:0000244|PDB:2O5R}. FT HELIX 16 32 {ECO:0000244|PDB:2O5R}. FT STRAND 35 38 {ECO:0000244|PDB:2O5R}. FT HELIX 48 50 {ECO:0000244|PDB:2O5R}. FT HELIX 51 63 {ECO:0000244|PDB:2O5R}. FT STRAND 68 70 {ECO:0000244|PDB:2O5R}. FT TURN 71 73 {ECO:0000244|PDB:2O5R}. FT HELIX 82 85 {ECO:0000244|PDB:2O5R}. FT HELIX 86 98 {ECO:0000244|PDB:2O5R}. FT STRAND 101 105 {ECO:0000244|PDB:2O5R}. FT TURN 110 112 {ECO:0000244|PDB:2O5R}. FT HELIX 113 121 {ECO:0000244|PDB:2O5R}. FT HELIX 130 133 {ECO:0000244|PDB:2O5R}. FT TURN 134 136 {ECO:0000244|PDB:2O5R}. FT HELIX 139 147 {ECO:0000244|PDB:2O5R}. FT STRAND 153 156 {ECO:0000244|PDB:2O5R}. FT STRAND 163 167 {ECO:0000244|PDB:2O5R}. FT TURN 168 170 {ECO:0000244|PDB:2O5R}. FT STRAND 171 175 {ECO:0000244|PDB:2O5R}. FT STRAND 182 186 {ECO:0000244|PDB:2O5R}. FT HELIX 194 204 {ECO:0000244|PDB:2O5R}. FT STRAND 208 213 {ECO:0000244|PDB:2O5R}. FT HELIX 214 216 {ECO:0000244|PDB:2O5R}. FT HELIX 217 229 {ECO:0000244|PDB:2O5R}. FT STRAND 236 240 {ECO:0000244|PDB:2O5R}. FT STRAND 248 250 {ECO:0000244|PDB:2O5R}. FT HELIX 253 255 {ECO:0000244|PDB:2O5R}. FT HELIX 260 266 {ECO:0000244|PDB:2O5R}. FT HELIX 270 278 {ECO:0000244|PDB:2O5R}. FT STRAND 280 282 {ECO:0000244|PDB:2O5R}. FT HELIX 293 299 {ECO:0000244|PDB:2O5R}. FT HELIX 302 304 {ECO:0000244|PDB:2O5R}. FT HELIX 314 327 {ECO:0000244|PDB:2O5R}. FT HELIX 330 343 {ECO:0000244|PDB:2O5R}. FT HELIX 351 361 {ECO:0000244|PDB:2O5R}. FT TURN 362 364 {ECO:0000244|PDB:2O5R}. FT HELIX 368 370 {ECO:0000244|PDB:2O5R}. FT HELIX 371 374 {ECO:0000244|PDB:2O5R}. FT HELIX 376 378 {ECO:0000244|PDB:2O5R}. FT HELIX 389 391 {ECO:0000244|PDB:2O5R}. FT HELIX 392 401 {ECO:0000244|PDB:2O5R}. FT TURN 402 404 {ECO:0000244|PDB:2O5R}. FT HELIX 409 423 {ECO:0000244|PDB:2O5R}. FT HELIX 427 438 {ECO:0000244|PDB:2O5R}. FT STRAND 440 442 {ECO:0000244|PDB:2O5R}. FT HELIX 447 453 {ECO:0000244|PDB:2O5R}. FT HELIX 456 466 {ECO:0000244|PDB:2O5R}. SQ SEQUENCE 469 AA; 54607 MW; F27D3AB4FE070BD8 CRC64; MVRVRFAPSP TGFLHVGGAR TALFNFLFAR KEKGKFILRI EDTDLERSER EYEEKLMESL RWLGLLWDEG PDVGGDHGPY RQSERVEIYR EHAERLVKEG KAYYVYAYPE EIEEMREKLL SEGKAPHYSQ EMFEKFDTPE RRREYEEKGL RPAVFFKMPR KDYVLNDVVK GEVVFKTGAI GDFVIMRSNG LPTYNFACVV DDMLMEITHV IRGDDHLSNT LRQLALYEAF EKAPPVFAHV STILGPDGKK LSKRHGATSV EAFRDMGYLP EALVNYLALL GWSHPEGKEL LTLEELISSF SLDRLSPNPA IFDPQKLKWM NGYYLRNMPI EKLAELAKPF FEKAGIKIID EEYFKKVLEI TKERVEVLSE FPEESRFFFE DPAPVEIPEE MKEVFSQLKE ELQNVRWTME EITPVFKKVL KQHGVKPKEF YMTLRRVLTG REEGPELVNI IPLLGKEIFL RRIERSLGG // ID SYH_THEMA Reviewed; 420 AA. AC Q9X0H5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 110. DE RecName: Full=Histidine--tRNA ligase; DE EC=6.1.1.21; DE AltName: Full=Histidyl-tRNA synthetase; DE Short=HisRS; GN Name=hisS; OrderedLocusNames=TM_1090; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP + CC diphosphate + L-histidyl-tRNA(His). CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36166.1; -; Genomic_DNA. DR PIR; A72298; A72298. DR RefSeq; NP_228896.1; NC_000853.1. DR RefSeq; WP_004080372.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0H5; -. DR STRING; 243274.TM1090; -. DR DNASU; 898676; -. DR EnsemblBacteria; AAD36166; AAD36166; TM_1090. DR GeneID; 898676; -. DR KEGG; tma:TM1090; -. DR PATRIC; 23937111; VBITheMar51294_1104. DR eggNOG; ENOG4105CUT; Bacteria. DR eggNOG; COG0124; LUCA. DR InParanoid; Q9X0H5; -. DR KO; K01892; -. DR OMA; CGGGNFK; -. DR OrthoDB; EOG6BPDH4; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00127; His_tRNA_synth; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR015807; His-tRNA-ligase. DR InterPro; IPR004516; HisRS/HisZ. DR PANTHER; PTHR11476; PTHR11476; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR PIRSF; PIRSF001549; His-tRNA_synth; 1. DR SUPFAM; SSF52954; SSF52954; 1. DR TIGRFAMs; TIGR00442; hisS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 420 Histidine--tRNA ligase. FT /FTId=PRO_0000136282. SQ SEQUENCE 420 AA; 48275 MW; 98C42EADC3F00362 CRC64; MKYRRIKGTN DIFGEEIWYW RYVEETFRNV CESAGIEEIR TPIFEQTELF VRSVGEESDI VQKEMYTFQD KAGRSITLRP EGTAPVVRAF LENSLIDRGF QQRYYYIGPM FRYEKPQSGR LRQFHQVGFE IIGPESPKAD FEVIMLVDTF LRRLGLTKYK IHLNSIGCPV CRKNYREALK EYYGRILDNL CDDCKRRYET NILRLLDCKV DHEYSLNAPK SVDYLCDSCR AHYKKLKEYL NTFEIEYVED HTLVRGLDYY TRTVFEVRHE GLGAQSAIAG GGRYDGLFAE LGGSSVPALG FAGGIERIIL ALKAEGIEIP MKNVHLVYIA TLGEKAFMDG VRLAGELRKK GLSVDVDIMD RKLSGQLKHA SRMGSRYAVI IGDEELEKGI VILRDLETGD QVEIDRDFAA DYIAERVSKD // ID SYS_THEMA Reviewed; 425 AA. AC Q9X199; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=Serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00176}; DE EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00176}; DE Short=SerRS {ECO:0000255|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_00176}; GN Name=serS {ECO:0000255|HAMAP-Rule:MF_00176}; GN OrderedLocusNames=TM_1379; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also CC able to aminoacylate tRNA(Sec) with serine, to form the CC misacylated tRNA L-seryl-tRNA(Sec), which will be further CC converted into selenocysteinyl-tRNA(Sec). {ECO:0000255|HAMAP- CC Rule:MF_00176}. CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate CC + L-seryl-tRNA(Ser). {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate CC + L-seryl-tRNA(Sec). {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a CC N-terminal extension that is involved in tRNA binding. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Type-1 seryl-tRNA synthetase subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36449.1; -; Genomic_DNA. DR PIR; D72261; D72261. DR RefSeq; NP_229180.1; NC_000853.1. DR RefSeq; WP_004081577.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X199; -. DR SMR; Q9X199; 1-424. DR STRING; 243274.TM1379; -. DR EnsemblBacteria; AAD36449; AAD36449; TM_1379. DR GeneID; 898099; -. DR KEGG; tma:TM1379; -. DR PATRIC; 23937700; VBITheMar51294_1391. DR eggNOG; ENOG4105CGR; Bacteria. DR eggNOG; COG0172; LUCA. DR InParanoid; Q9X199; -. DR KO; K01875; -. DR OMA; YRPERHE; -. DR OrthoDB; EOG61KBH9; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.40; -; 1. DR HAMAP; MF_00176; Ser_tRNA_synth_type1; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR002317; Ser-tRNA-ligase_type_1. DR InterPro; IPR015866; Ser-tRNA-synth_1_N. DR InterPro; IPR010978; tRNA-bd_arm. DR PANTHER; PTHR11778; PTHR11778; 1. DR Pfam; PF02403; Seryl_tRNA_N; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1. DR PRINTS; PR00981; TRNASYNTHSER. DR SUPFAM; SSF46589; SSF46589; 1. DR TIGRFAMs; TIGR00414; serS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 425 Serine--tRNA ligase. FT /FTId=PRO_0000122144. FT NP_BIND 264 266 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}. FT NP_BIND 351 354 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}. FT REGION 233 235 Serine binding. {ECO:0000255|HAMAP- FT Rule:MF_00176}. FT BINDING 287 287 Serine. {ECO:0000255|HAMAP- FT Rule:MF_00176}. FT BINDING 387 387 Serine. {ECO:0000255|HAMAP- FT Rule:MF_00176}. SQ SEQUENCE 425 AA; 48892 MW; F0F6D191C21E13BB CRC64; MIDIKLIRQN PDFVKEALRK RGEDPAIIDE ILKIDADWRA TITKTNELRS RRNEISKNVA RLKKEGKNAE AEALIEEGKR LGEEIKALEE KEKELQKKLN DLLLMIPNIP HESVPVGEDE SQNVEVRRWG EPREFDFTPL AHWDLGPAWG LMDFSRASKL SGSRFTVMYG KLARLERALI NFMLDVHTKE HGYTEVWVPH LVKRETITIT GQLPKFEEEL YLAERDDLFL IPTAEVPLAA LHSGEILEEK ELPKKYVSYT PCYRREAGSY GKDVRGMIRQ HQFDKVELVW VTTPERSFED LEELVKDAET ILRKLELPYR VVSLCTGDLG FTSAKTYDIE VWLPSYNAYK EISSCSNVTD FQARRGNMRY RRRSDGKLEY VHTLNGSGIA VGRALVAILE NYQQPDGSVR VPEVLVPYTG FEVIP // ID SYDND_THEMA Reviewed; 579 AA. AC Q9X1F4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 118. DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_00044}; DE EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_00044}; DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044}; DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044}; DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044}; DE Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_00044}; GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; GN OrderedLocusNames=TM_1441; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity CC since it is able to aspartylate not only its cognate tRNA(Asp) but CC also tRNA(Asn). Reaction proceeds in two steps: aspartate is first CC activated by ATP to form Asp-AMP and then transferred to the CC acceptor end of tRNA(Asp/Asn). {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asx) = AMP + CC diphosphate + L-aspartyl-tRNA(Asx). {ECO:0000255|HAMAP- CC Rule:MF_00044}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00044}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36510.1; -; Genomic_DNA. DR PIR; F72252; F72252. DR RefSeq; NP_229240.1; NC_000853.1. DR RefSeq; WP_004081712.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1F4; -. DR STRING; 243274.TM1441; -. DR PRIDE; Q9X1F4; -. DR EnsemblBacteria; AAD36510; AAD36510; TM_1441. DR GeneID; 898034; -. DR KEGG; tma:TM1441; -. DR PATRIC; 23937832; VBITheMar51294_1454. DR eggNOG; ENOG4105C9M; Bacteria. DR eggNOG; COG0173; LUCA. DR InParanoid; Q9X1F4; -. DR KO; K01876; -. DR OMA; YQLDVEM; -. DR OrthoDB; EOG68Q0NX; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.1360.30; -; 1. DR HAMAP; MF_00044; Asp_tRNA_synth; 1. DR InterPro; IPR004364; aa-tRNA-synt_II. DR InterPro; IPR018150; aa-tRNA-synt_II-like. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004524; Asp-tRNA-ligase_bac/mit. DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb. DR InterPro; IPR004115; GAD-like. DR InterPro; IPR029351; GAD_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR PANTHER; PTHR22594; PTHR22594; 2. DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 2. DR Pfam; PF02938; GAD; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR01042; TRNASYNTHASP. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF55261; SSF55261; 1. DR TIGRFAMs; TIGR00459; aspS_bact; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 579 Aspartate--tRNA(Asp/Asn) ligase. FT /FTId=PRO_0000110968. FT NP_BIND 217 219 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT NP_BIND 527 530 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT REGION 195 198 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 171 171 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 217 217 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 226 226 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT BINDING 444 444 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 475 475 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT BINDING 482 482 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT SITE 81 81 Important for tRNA non-discrimination. FT {ECO:0000255|HAMAP-Rule:MF_00044}. SQ SEQUENCE 579 AA; 66495 MW; 84195147100B9A61 CRC64; MLRTHTCGEL RATDEGKKVK LCGWVDRIRD LGGVRFIDLR DRYGETQIVC DVNSEAYSVV DELTRESVVL VEGTVRKRPE GTENPNIETG EIEVVAERIE ILSLADPLPF YPGETPKEEM RLKYRYIDLR SERMKRNIIL RYRISKIIRD YFDELGFLEI ETPFLTRSTP EGARDFLVPS RLRPGKFYAL PQSPQLFKQI LMISGFDRYF QIVRCFRDED LRADRQPEFT QVDVEMSFVD VEDVLNVSEG MVSRVFKESS GIDLKVPFDR IPYDDAMEKY GTDKPDRRYG MELRDFGYAF ETTEFKVIRN VLNEGGSVKG FIVPGFASEM SRKKGEELMA RMKELGLGGL IWFKLDGGIT SPHLKHLEKE FRKIAETENM NEGDVCLIAA HTDRNLLNEA LGTLRLEIGK EHFSHLAKGF DVLWVVDFPY FEWSEEEERF VARHHPFTMP VLETLGDDYT KVRAKAYDLV INGYEVGGGS IRIHRRDIQE KIFELLGLSE EEAQKKFGFF LEAFRYGVPP HGGIAFGLDR LVSIIAGESS IREVIAFPKT GNGVCLLTGA PAEVDERQLR ELRIRIEEG // ID SYT_THEMA Reviewed; 640 AA. AC Q9WZJ9; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=Threonine--tRNA ligase; DE EC=6.1.1.3; DE AltName: Full=Threonyl-tRNA synthetase; DE Short=ThrRS; GN Name=thrS; OrderedLocusNames=TM_0740; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP + CC diphosphate + L-threonyl-tRNA(Thr). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35821.1; -; Genomic_DNA. DR PIR; G72339; G72339. DR RefSeq; NP_228549.1; NC_000853.1. DR RefSeq; WP_004080983.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZJ9; -. DR STRING; 243274.TM0740; -. DR EnsemblBacteria; AAD35821; AAD35821; TM_0740. DR GeneID; 898407; -. DR KEGG; tma:TM0740; -. DR PATRIC; 23936400; VBITheMar51294_0753. DR eggNOG; ENOG4105C22; Bacteria. DR eggNOG; COG0441; LUCA. DR InParanoid; Q9WZJ9; -. DR KO; K01868; -. DR OMA; FYYDFAY; -. DR OrthoDB; EOG61KBFJ; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00184; Thr_tRNA_synth; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR InterPro; IPR002320; Thr-tRNA-ligase_IIa. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR012947; tRNA_SAD. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF02824; TGS; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF07973; tRNA_SAD; 1. DR PRINTS; PR01047; TRNASYNTHTHR. DR SMART; SM00863; tRNA_SAD; 1. DR SUPFAM; SSF52954; SSF52954; 1. DR SUPFAM; SSF55186; SSF55186; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR TIGRFAMs; TIGR00418; thrS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 640 Threonine--tRNA ligase. FT /FTId=PRO_0000101073. FT REGION 240 531 Catalytic. FT METAL 332 332 Zinc; catalytic. {ECO:0000250}. FT METAL 383 383 Zinc; catalytic. {ECO:0000250}. FT METAL 508 508 Zinc; catalytic. {ECO:0000250}. SQ SEQUENCE 640 AA; 74562 MW; 552991A79DBE23AD CRC64; MKIKVKLPDG KEKEYDRGIT PAEIAKELGI KKAIGAVVNG ELWDLKRPIE NDCELRLVTL EDPEAPEFYR HTMAHILAQA VMRLYGKENV KLGIGPTIEN GFYYDFDIKN GRLTEEDLPK IEQEMKKIIK ENLPIERKEI SKEEARELFR DQPYKLELIE EIEGNRVTIY RQGEFVDLCR GPHLPSTGIV KHFKLLSVSG AYWRGSEKNP MLTRVYGTAF AKKEDLDNYL KFLEEAQRRD HRKLGPQLEL FMLNTEYAPG MPFFLPKGVV VLNELMKFSR ELHRERGYQE IFTPLIMNEQ LWKISGHWDH YAENMYFIEK DEERYAVKPM NCPGHILVYK SRTVSYRDLP LRFFEFGRVH RYERSGVLHG LMRVRSFTQD DAHIFCTPDQ IEEEILGVLD LINTIYSQFG FTYRVELSTM PEDHMGDEAI WEKATTALKN ALERAGLSYK VNEGEGAFYG PKIDFHIRDS IGREWQCATI QLDFMMPEKF NVTYIGPDNK EHRAVMIHRA IYGSLERFFG ILIEHFAGAF PTWLAPIQVA VIPISEKHND GAEKVARRIS QEGFRVFFDN RRETLGYRIR QAQTQKIPYM IIIGDKELES GKISVRTRTG KEIKDVDPEH FVETLRNEVL SRKLELSMEG // ID SYE2_THEMA Reviewed; 487 AA. AC Q9X2I8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Glutamate--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00022}; DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022}; DE AltName: Full=Glutamyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00022}; DE Short=GluRS 2 {ECO:0000255|HAMAP-Rule:MF_00022}; GN Name=gltX2 {ECO:0000255|HAMAP-Rule:MF_00022}; GN OrderedLocusNames=TM_1875; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a CC two-step reaction: glutamate is first activated by ATP to form CC Glu-AMP and then transferred to the acceptor end of tRNA(Glu). CC {ECO:0000255|HAMAP-Rule:MF_00022}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP + CC diphosphate + L-glutamyl-tRNA(Glu). {ECO:0000255|HAMAP- CC Rule:MF_00022}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00022}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36937.1; -; Genomic_DNA. DR PIR; F72200; F72200. DR RefSeq; NP_229671.1; NC_000853.1. DR RefSeq; WP_010865423.1; NC_000853.1. DR PDB; 3AFH; X-ray; 2.00 A; A=2-487. DR PDB; 3AKZ; X-ray; 2.90 A; A/B/C/D=1-487. DR PDB; 3AL0; X-ray; 3.37 A; C=1-487. DR PDBsum; 3AFH; -. DR PDBsum; 3AKZ; -. DR PDBsum; 3AL0; -. DR ProteinModelPortal; Q9X2I8; -. DR DIP; DIP-59231N; -. DR STRING; 243274.TM1875; -. DR EnsemblBacteria; AAD36937; AAD36937; TM_1875. DR GeneID; 897796; -. DR KEGG; tma:TM1875; -. DR PATRIC; 23938739; VBITheMar51294_1896. DR eggNOG; ENOG4105C20; Bacteria. DR eggNOG; COG0008; LUCA. DR InParanoid; Q9X2I8; -. DR KO; K01885; -. DR OMA; IDEINDM; -. DR OrthoDB; EOG6DRPF7; -. DR BioCyc; TMAR243274:GC6P-1926-MONOMER; -. DR BRENDA; 6.1.1.24; 6331. DR EvolutionaryTrace; Q9X2I8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.350; -; 1. DR Gene3D; 1.10.1160.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00022_B; Glu_tRNA_synth_B; 1. DR InterPro; IPR008925; aa-tRNA-synth_I_codon-bd. DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00749; tRNA-synt_1c; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF48163; SSF48163; 1. DR TIGRFAMs; TIGR00464; gltX_bact; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 487 Glutamate--tRNA ligase 2. FT /FTId=PRO_0000119681. FT MOTIF 31 41 "HIGH" region. FT MOTIF 254 258 "KMSKS" region. FT BINDING 257 257 ATP. {ECO:0000255|HAMAP-Rule:MF_00022}. FT STRAND 26 29 {ECO:0000244|PDB:3AFH}. FT STRAND 34 36 {ECO:0000244|PDB:3AFH}. FT HELIX 39 55 {ECO:0000244|PDB:3AFH}. FT STRAND 58 61 {ECO:0000244|PDB:3AFH}. FT TURN 68 70 {ECO:0000244|PDB:3AFH}. FT HELIX 73 85 {ECO:0000244|PDB:3AFH}. FT STRAND 91 93 {ECO:0000244|PDB:3AFH}. FT TURN 94 96 {ECO:0000244|PDB:3AFH}. FT HELIX 105 107 {ECO:0000244|PDB:3AFH}. FT HELIX 109 121 {ECO:0000244|PDB:3AFH}. FT STRAND 124 130 {ECO:0000244|PDB:3AFH}. FT STRAND 132 134 {ECO:0000244|PDB:3AFH}. FT STRAND 137 144 {ECO:0000244|PDB:3AFH}. FT HELIX 147 151 {ECO:0000244|PDB:3AFH}. FT STRAND 156 160 {ECO:0000244|PDB:3AFH}. FT STRAND 164 171 {ECO:0000244|PDB:3AFH}. FT TURN 172 174 {ECO:0000244|PDB:3AFH}. FT STRAND 175 180 {ECO:0000244|PDB:3AFH}. FT HELIX 181 183 {ECO:0000244|PDB:3AFH}. FT STRAND 187 190 {ECO:0000244|PDB:3AFH}. FT TURN 192 194 {ECO:0000244|PDB:3AKZ}. FT HELIX 198 208 {ECO:0000244|PDB:3AFH}. FT STRAND 212 217 {ECO:0000244|PDB:3AFH}. FT HELIX 218 223 {ECO:0000244|PDB:3AFH}. FT HELIX 224 234 {ECO:0000244|PDB:3AFH}. FT STRAND 240 244 {ECO:0000244|PDB:3AFH}. FT STRAND 252 254 {ECO:0000244|PDB:3AFH}. FT TURN 257 259 {ECO:0000244|PDB:3AFH}. FT STRAND 261 263 {ECO:0000244|PDB:3AL0}. FT HELIX 264 270 {ECO:0000244|PDB:3AFH}. FT HELIX 274 283 {ECO:0000244|PDB:3AFH}. FT HELIX 296 299 {ECO:0000244|PDB:3AFH}. FT HELIX 300 302 {ECO:0000244|PDB:3AFH}. FT HELIX 305 307 {ECO:0000244|PDB:3AFH}. FT HELIX 317 330 {ECO:0000244|PDB:3AFH}. FT HELIX 333 347 {ECO:0000244|PDB:3AFH}. FT HELIX 356 366 {ECO:0000244|PDB:3AFH}. FT TURN 367 369 {ECO:0000244|PDB:3AKZ}. FT HELIX 373 384 {ECO:0000244|PDB:3AFH}. FT HELIX 392 397 {ECO:0000244|PDB:3AFH}. FT TURN 398 400 {ECO:0000244|PDB:3AFH}. FT HELIX 404 416 {ECO:0000244|PDB:3AFH}. FT HELIX 423 435 {ECO:0000244|PDB:3AFH}. FT HELIX 441 453 {ECO:0000244|PDB:3AFH}. FT STRAND 454 457 {ECO:0000244|PDB:3AKZ}. FT HELIX 461 468 {ECO:0000244|PDB:3AFH}. FT HELIX 470 484 {ECO:0000244|PDB:3AFH}. SQ SEQUENCE 487 AA; 57382 MW; 5E15A2E9E1580791 CRC64; MFITGAFFDI LEVGPKKIRR CFELVRVRFA PSPTGHLHVG GARTALFNWM FARKEGGKFI LRIEDTDTER SSREYEQQIL ESLRWCGLDW DEGPDIGGDF GPYRQSERLE IYREYAEKLV EDKRAYYVVY DKEDPSKELF TTYEYPHEYK EKGHPVTIKF KVLPGKTSFE DLLKGYMEFD NSTLEDFIIM KSNGFPTYNF AVVVDDHLMR ISHVFRGEDH LSNTPKQLMI YEAFGWEAPV FMHIPLILGS DRTPLSKRHG ATSVEHFRRE GILSRALMNY LALLGWRVEG DEIFTIEEKL QSFDPKDISN KGVIFDYQKL EWVNGKHMRR IDLEDLKREF IEWAKYAGKE IPSVDERYFS ETLRICREKV NTLSQLYDIM YPFMNDDYEY EKDYVEKFLK REEAERVLEE AKKAFKDLNS WNMEEIEKTL RDLSEKGLAS KKVVFQLIRG AVTGKLVTPG LFETIEVLGK ERTLKRLERT LQFLKKT // ID SYFB_THEMA Reviewed; 788 AA. AC Q9WZS9; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=Phenylalanine--tRNA ligase beta subunit; DE EC=6.1.1.20; DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit; DE Short=PheRS; GN Name=pheT; OrderedLocusNames=TM_0822; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta CC subunit family. Type 1 subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 B5 domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FDX-ACB domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35904.1; -; Genomic_DNA. DR PIR; A72330; A72330. DR RefSeq; NP_228631.1; NC_000853.1. DR RefSeq; WP_004080832.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZS9; -. DR STRING; 243274.TM0822; -. DR EnsemblBacteria; AAD35904; AAD35904; TM_0822. DR GeneID; 898492; -. DR KEGG; tma:TM0822; -. DR PATRIC; 23936568; VBITheMar51294_0834. DR eggNOG; ENOG4105C6A; Bacteria. DR eggNOG; COG0072; LUCA. DR eggNOG; COG0073; LUCA. DR InParanoid; Q9WZS9; -. DR KO; K01890; -. DR OMA; MKFSEQW; -. DR OrthoDB; EOG6CCH1J; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central. DR GO; GO:0008033; P:tRNA processing; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.56.20; -; 1. DR Gene3D; 3.30.70.380; -; 1. DR Gene3D; 3.50.40.10; -; 1. DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1. DR InterPro; IPR005146; B3/B4_tRNA-bd. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu. DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4. DR InterPro; IPR005121; PheS_beta_Fdx_antiC-bd. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR005147; tRNA_synthase_B5-dom. DR Pfam; PF03483; B3_4; 1. DR Pfam; PF03484; B5; 1. DR Pfam; PF03147; FDX-ACB; 1. DR Pfam; PF01588; tRNA_bind; 1. DR SMART; SM00873; B3_4; 1. DR SMART; SM00874; B5; 1. DR SMART; SM00896; FDX-ACB; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54991; SSF54991; 1. DR SUPFAM; SSF56037; SSF56037; 1. DR TIGRFAMs; TIGR00472; pheT_bact; 1. DR PROSITE; PS51483; B5; 1. DR PROSITE; PS51447; FDX_ACB; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding. FT CHAIN 1 788 Phenylalanine--tRNA ligase beta subunit. FT /FTId=PRO_0000126975. FT DOMAIN 39 147 tRNA-binding. FT DOMAIN 399 472 B5. FT DOMAIN 694 787 FDX-ACB. FT METAL 450 450 Magnesium. {ECO:0000250}. FT METAL 456 456 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 459 459 Magnesium. {ECO:0000250}. FT METAL 460 460 Magnesium. {ECO:0000250}. SQ SEQUENCE 788 AA; 90073 MW; D789875D53FA907B CRC64; MRVPESWLRE FVDLDWDIEQ IAERLTFSGT SVEDILRPFN VSGEIITARV IERFDHPASE KLIVCKVDTG KRIYTVITAD KTVNEGDYVI LALEGATLNN GLKIEPREFK GVISEGMLCS LEELGLEEKS DRVYRFPDPV ELGVNVVEEY GLNERVLDIE ITPNRPDCLS IIGVARELSA LSGRPLNKPQ PDVSFVDEDV QFDVEIEDVE GCPRYSARIM KGVTVKDSPL WMKARLVAAG VRSLNNVVDA TNYVMIELGH PVHAFDLNRL KNKRIVVKSA KGGERVLLLD EKEYELKGGE VLITDGENVL ALGGIMGGME SGVYDDTRDL VLEVAYFDPV RIRKAAKALG ISSESSYRFE RGVDPNDVEL VSLRLAELIQ KLAGGYVLRK FWDVYPRKIE PKKVMLRKAR IEKILGTKVE EPGDILRRLE FQVEDRGDSY EVLVPTFRPD VEREIDLIEE IGRIYGYEKV ESKVISVPAV NRGWGEKQLF RREISQFMKG MGFDEVVTFS FVDSQKVKKW PLVDREPIAL SNPIASDMDV MRTSQFYSLI QVLAENFKRQ NRDLKLFEIG KIYFKENGNF REIETLSAMS CGLENPGDYT DKRSVSFYTI KGVLDELFFR LGVNVVYRAA EIPGLFPTRS ARIYVENREI GFIGMVDPKL LDEYDVKEDT YFFEIDMELL RKYASKRPAY RPTPRFPAVR RDISFLLPKG FESVKIIELF KKSGGDLVEE VGVFDIYEGK GIPENMVSVT LYVVFRHPER TLTDEEVNKI FEEMVQKAER EFGIRRRF // ID SYGB_THEMA Reviewed; 672 AA. AC Q9WY60; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Glycine--tRNA ligase beta subunit; DE EC=6.1.1.14; DE AltName: Full=Glycyl-tRNA synthetase beta subunit; DE Short=GlyRS; GN Name=glyS; OrderedLocusNames=TM_0217; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35309.1; -; Genomic_DNA. DR PIR; C72404; C72404. DR RefSeq; NP_228032.1; NC_000853.1. DR RefSeq; WP_004082897.1; NZ_CP011107.1. DR STRING; 243274.TM0217; -. DR DNASU; 897102; -. DR EnsemblBacteria; AAD35309; AAD35309; TM_0217. DR GeneID; 897102; -. DR KEGG; tma:TM0217; -. DR PATRIC; 23935306; VBITheMar51294_0219. DR eggNOG; ENOG4107RFA; Bacteria. DR eggNOG; COG0751; LUCA. DR InParanoid; Q9WY60; -. DR KO; K01879; -. DR OMA; LPIPKRM; -. DR OrthoDB; EOG661H9S; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3210.10; -; 1. DR Gene3D; 1.10.730.10; -; 1. DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1. DR InterPro; IPR008909; DALR_anticod-bd. DR InterPro; IPR015944; Gly-tRNA-synth_bsu. DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF02092; tRNA_synt_2f; 1. DR PRINTS; PR01045; TRNASYNTHGB. DR SUPFAM; SSF47323; SSF47323; 1. DR TIGRFAMs; TIGR00211; glyS; 1. DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 672 Glycine--tRNA ligase beta subunit. FT /FTId=PRO_0000072934. SQ SEQUENCE 672 AA; 77813 MW; 612B402052DD429A CRC64; MRTALLEVGL EELPASEFHS ILKQLEEKSA ELLKAYRVSS GSVEVFVGSR RFGVILKNLP ERQEDFTEEK KGPPLNVAYD ENGKPTRALE GFLRNNNASL ENVVHREGYV YLSRVVEGKP VEEVLPDLFR DLVLGLNFRK PMRWGSGEHE YIRPVHWIVA MVDGRVLDLE IFGLRSSRIS YGKRYHAGSI EIPDSERYYE SLKKGFVISS HLERKKFVLE QIDEFEKRSS MKIERDEELI EEIVAITEYP RIVVGQFDRK YLELPEEIIV TAVKHHQRSF IAHKGTLTNT FVAFQDGPQP PENVVKGYER VINARLEDAR YYFQKDLETP LEKMNEKLKE IVFQEKLGTL YDKVERIKKI SQRLCEDLKL PGSFTQKVLE AASICKADIA SKVVYEFPEL QGVMGRIYAL REGINEEIAT AIEDHYSEEP QTVIGSILGI ADRIDTIVGN FAIGNVPTSS KDPYGLKSKA DTIFRIIRKN EWDISLEELL TFASSLVGYR LSEELETFFA GRFYQFLINE LGISFDVARA VNHLWKKPLR GILSAEALQE ISEKPEFQDL FVGFERVHNI TKNHDSTKFD GALFEKEEEK KLMNKFYEVK EKVLKALERL NYREALQYLI ELKPYIDEYF DNVFVMVKRD DLRVNRLSFL KNIDELFMMV GDMTYLVKRS QV // ID SYW_THEMA Reviewed; 328 AA. AC Q9WYW2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Tryptophan--tRNA ligase; DE EC=6.1.1.2; DE AltName: Full=Tryptophanyl-tRNA synthetase; DE Short=TrpRS; GN Name=trpS; OrderedLocusNames=TM_0492; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + L-tryptophan + tRNA(Trp) = AMP + CC diphosphate + L-tryptophyl-tRNA(Trp). CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35577.1; -; Genomic_DNA. DR PIR; C72370; C72370. DR RefSeq; NP_228302.1; NC_000853.1. DR RefSeq; WP_004081463.1; NZ_CP011107.1. DR PDB; 2G36; X-ray; 2.50 A; A=1-328. DR PDBsum; 2G36; -. DR ProteinModelPortal; Q9WYW2; -. DR SMR; Q9WYW2; 1-328. DR STRING; 243274.TM0492; -. DR EnsemblBacteria; AAD35577; AAD35577; TM_0492. DR GeneID; 897533; -. DR KEGG; tma:TM0492; -. DR PATRIC; 23935889; VBITheMar51294_0499. DR eggNOG; ENOG4105C31; Bacteria. DR eggNOG; COG0180; LUCA. DR InParanoid; Q9WYW2; -. DR KO; K01867; -. DR OMA; WYLSCFF; -. DR OrthoDB; EOG686NJQ; -. DR EvolutionaryTrace; Q9WYW2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00140_B; Trp_tRNA_synth_B; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002306; Trp-tRNA-ligase. DR InterPro; IPR024109; Trp-tRNA-ligase_bac-type. DR PANTHER; PTHR10055; PTHR10055; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01039; TRNASYNTHTRP. DR TIGRFAMs; TIGR00233; trpS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 328 Tryptophan--tRNA ligase. FT /FTId=PRO_0000136699. FT MOTIF 9 17 "HIGH" region. FT MOTIF 193 197 "KMSKS" region. FT BINDING 196 196 ATP. {ECO:0000250}. FT STRAND 2 7 {ECO:0000244|PDB:2G36}. FT HELIX 15 19 {ECO:0000244|PDB:2G36}. FT HELIX 21 30 {ECO:0000244|PDB:2G36}. FT STRAND 34 39 {ECO:0000244|PDB:2G36}. FT HELIX 41 48 {ECO:0000244|PDB:2G36}. FT HELIX 55 68 {ECO:0000244|PDB:2G36}. FT TURN 73 75 {ECO:0000244|PDB:2G36}. FT STRAND 76 80 {ECO:0000244|PDB:2G36}. FT HELIX 81 83 {ECO:0000244|PDB:2G36}. FT HELIX 86 95 {ECO:0000244|PDB:2G36}. FT HELIX 100 104 {ECO:0000244|PDB:2G36}. FT HELIX 107 110 {ECO:0000244|PDB:2G36}. FT HELIX 124 127 {ECO:0000244|PDB:2G36}. FT HELIX 129 138 {ECO:0000244|PDB:2G36}. FT TURN 139 141 {ECO:0000244|PDB:2G36}. FT STRAND 143 147 {ECO:0000244|PDB:2G36}. FT HELIX 149 151 {ECO:0000244|PDB:2G36}. FT HELIX 152 168 {ECO:0000244|PDB:2G36}. FT STRAND 177 180 {ECO:0000244|PDB:2G36}. FT HELIX 196 198 {ECO:0000244|PDB:2G36}. FT HELIX 208 216 {ECO:0000244|PDB:2G36}. FT HELIX 233 235 {ECO:0000244|PDB:2G36}. FT HELIX 237 244 {ECO:0000244|PDB:2G36}. FT HELIX 249 260 {ECO:0000244|PDB:2G36}. FT HELIX 266 293 {ECO:0000244|PDB:2G36}. FT HELIX 297 323 {ECO:0000244|PDB:2G36}. SQ SEQUENCE 328 AA; 37770 MW; E31EA170720D2857 CRC64; MRILSGMRPT GKLHIGHLVG ALENWVKLQE EGNECFYFVA DWHALTTHYD DVSKLKEYTR DLVRGFLACG IDPEKSVIFV QSGVKEHAEL ALLFSMIVSV SRLERVPTYK EIKSELNYKD LSTAGFLIYP VLQAADILIY KAEGVPVGED QVYHIELTRE IARRFNYLYD EVFPEPEAIL SRVPKLPGTD GRKMSKSYGN IINLEISEKE LEQTILRMMT DPARVRRSDP GNPENCPVWK YHQAFDISEE ESKWVWEGCT TASIGCVDCK KLLLKNMKRK LAPIWENFRK IDEDPHYVDD VIMEGTKKAR EVAAKTMEEV RRAMNLMF // ID SYP_THEMA Reviewed; 577 AA. AC Q9WYY4; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01569}; DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01569}; DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01569}; DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01569}; GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01569}; GN OrderedLocusNames=TM_0514; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a CC two-step reaction: proline is first activated by ATP to form Pro- CC AMP and then transferred to the acceptor end of tRNA(Pro). As CC ProRS can inadvertently accommodate and process non-cognate amino CC acids such as alanine and cysteine, to avoid such errors it has CC two additional distinct editing activities against alanine. One CC activity is designated as 'pretransfer' editing and involves the CC tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other CC activity is designated 'posttransfer' editing and involves CC deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys- CC tRNA(Pro) is not edited by ProRS. {ECO:0000255|HAMAP- CC Rule:MF_01569}. CC -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP + CC diphosphate + L-prolyl-tRNA(Pro). {ECO:0000255|HAMAP- CC Rule:MF_01569}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01569}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01569}. CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic CC domain, the editing domain and the C-terminal anticodon-binding CC domain. {ECO:0000255|HAMAP-Rule:MF_01569}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. ProS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01569}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35599.1; -; Genomic_DNA. DR PIR; H72368; H72368. DR RefSeq; NP_228324.1; NC_000853.1. DR RefSeq; WP_004081418.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYY4; -. DR STRING; 243274.TM0514; -. DR EnsemblBacteria; AAD35599; AAD35599; TM_0514. DR GeneID; 897558; -. DR KEGG; tma:TM0514; -. DR PATRIC; 23935933; VBITheMar51294_0521. DR eggNOG; ENOG4105C90; Bacteria. DR eggNOG; COG0442; LUCA. DR InParanoid; Q9WYY4; -. DR KO; K01881; -. DR OMA; IQPAELW; -. DR OrthoDB; EOG6TTVMR; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.800; -; 1. DR Gene3D; 3.90.960.10; -; 1. DR HAMAP; MF_01569; Pro_tRNA_synth_type1; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR002316; Pro-tRNA-ligase_IIa. DR InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type. DR InterPro; IPR023717; Pro-tRNA-Synthase_IIa_type1. DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom. DR PANTHER; PTHR11451:SF3; PTHR11451:SF3; 2. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF04073; tRNA_edit; 1. DR PRINTS; PR01046; TRNASYNTHPRO. DR SUPFAM; SSF52954; SSF52954; 1. DR SUPFAM; SSF55826; SSF55826; 1. DR TIGRFAMs; TIGR00409; proS_fam_II; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 577 Proline--tRNA ligase. FT /FTId=PRO_0000248802. SQ SEQUENCE 577 AA; 65947 MW; 505B60BA0D512181 CRC64; MRMKDLYAPT LKETPSDVET VSHEYLLRGG FIRKVAAGIY TYLPLGRRVL LKIENIVREE MNRIGAQEIL MPILQPAELW KQSGRWDDYG PEMMKLKDRH ERDFTLGPTH EEIVTDLVKN ELRSYKQLPL TLYQIANKYR DEIRPRFGLL RAREFIMKDA YSFHASWESL DETYEQFKKA YSRIMERLGV RYMIIEAETG AIGGNASHEF VVPAKIGETN VLFCEKCGYQ ASDEKAEYKG EYTQEQEEEK PLKKVPTPGV KTIEEVSEFL GVPPSKIVKS LLYKGREGYV MVLIRGDLEL NEAKLKAHLK DQSLRMATPE EILKDFGVPV GFIGPIGVDV KKVADHSVRG LKNFVVGGME EDTHYVNANH PRDFKVDEWY DLRTVVEGDP CPVCGEPLKA TKGIELGHIF KLGTKYSEAM KAYFMDENGE MKPFIMGCYG WGVSRTMAAV VEHFHDENGM IWPLSIAPYT VVVDILNMND AEQKQVGEKI YQVLSEKGEE VVLDDREVSP GFKFKDADLI GFPIRINVGR SLKEGVVELK KRYSKELVKV NIKNGFGALL ETLEKMKREY DPKEAVR // ID SYR_THEMA Reviewed; 546 AA. AC Q9X0H8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 110. DE RecName: Full=Arginine--tRNA ligase; DE EC=6.1.1.19; DE AltName: Full=Arginyl-tRNA synthetase; DE Short=ArgRS; GN Name=argS; OrderedLocusNames=TM_1093; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP + CC diphosphate + L-arginyl-tRNA(Arg). CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36169.1; -; Genomic_DNA. DR PIR; D72298; D72298. DR RefSeq; NP_228899.1; NC_000853.1. DR RefSeq; WP_004080362.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0H8; -. DR STRING; 243274.TM1093; -. DR EnsemblBacteria; AAD36169; AAD36169; TM_1093. DR GeneID; 898672; -. DR KEGG; tma:TM1093; -. DR PATRIC; 23937117; VBITheMar51294_1107. DR eggNOG; ENOG4105C75; Bacteria. DR eggNOG; COG0018; LUCA. DR InParanoid; Q9X0H8; -. DR KO; K01887; -. DR OMA; HVGHIRN; -. DR OrthoDB; EOG6JB13C; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.30.1360.70; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00123; Arg_tRNA_synth; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR001278; Arg-tRNA-ligase. DR InterPro; IPR005148; Arg-tRNA-synth_N. DR InterPro; IPR008909; DALR_anticod-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR PANTHER; PTHR11956; PTHR11956; 1. DR Pfam; PF03485; Arg_tRNA_synt_N; 1. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF00750; tRNA-synt_1d; 1. DR PRINTS; PR01038; TRNASYNTHARG. DR SMART; SM01016; Arg_tRNA_synt_N; 1. DR SMART; SM00836; DALR_1; 1. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF55190; SSF55190; 1. DR TIGRFAMs; TIGR00456; argS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 546 Arginine--tRNA ligase. FT /FTId=PRO_0000151628. FT MOTIF 122 132 "HIGH" region. SQ SEQUENCE 546 AA; 62482 MW; C255EF5281C0FE93 CRC64; MLVNAIRQKV SEVISKAYGS EIEFEVEIPP RKEFGDLSTN VAMKLAKTLK KNPREIAQEI VKSLDEDPSF DRIEIMGPGF INFFLSNELL RGVVKTVLEK KDEYGRENVG NGMKVQFEYG SANPTGPFTV GHGRQIIIGD VLSEVYKELG YDVTREMYIN DAGKQIRLLA QSLWARYNQL LGVEKEIPEG GYRGEYLVDI ARDLVNEIGD RYKDLWNEEV EEFFKQTALN RILSSMKDTL EKIGSSFDVY FSEKSLIEDG TVEEVLKLLK NKDVVYEKDG AVWLKVSAFI DEEDKVLVRS DGTYTYFMTD IAYHYKKYKR GFRKVYDIWG SDHHGHIPRM KAAMKALDIP DDFFNVILHQ FVTLKRGGEI VRMSTRAGEF VTLDELLDEV GRDATRYFFA MVDPNTHMVF DIDLAKAKSM DNPVYYVQYA HARIHNLFSN AEKKGVKFEE GKHLELLGNE EERVLMRNLG MFNTALKEVA QMFAPNRLTN YLQSLAESFH AFYTKHVIVD PENPELSNAR LNLALATGIV LRKGLKLIGV SAPERM // ID SYGA_THEMA Reviewed; 286 AA. AC Q9WY59; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=Glycine--tRNA ligase alpha subunit; DE EC=6.1.1.14; DE AltName: Full=Glycyl-tRNA synthetase alpha subunit; DE Short=GlyRS; GN Name=glyQ; OrderedLocusNames=TM_0216; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35308.1; -; Genomic_DNA. DR PIR; B72404; B72404. DR RefSeq; NP_228031.1; NC_000853.1. DR RefSeq; WP_004082894.1; NZ_CP011107.1. DR PDB; 1J5W; X-ray; 1.95 A; A/B=1-286. DR PDBsum; 1J5W; -. DR ProteinModelPortal; Q9WY59; -. DR SMR; Q9WY59; 1-280. DR STRING; 243274.TM0216; -. DR EnsemblBacteria; AAD35308; AAD35308; TM_0216. DR GeneID; 897101; -. DR KEGG; tma:TM0216; -. DR PATRIC; 23935304; VBITheMar51294_0218. DR eggNOG; ENOG4108HMW; Bacteria. DR eggNOG; COG0752; LUCA. DR InParanoid; Q9WY59; -. DR KO; K01878; -. DR OMA; LGSYYQF; -. DR OrthoDB; EOG661H9S; -. DR EvolutionaryTrace; Q9WY59; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1. DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer. DR InterPro; IPR002310; Gly-tRNA_ligase_asu. DR Pfam; PF02091; tRNA-synt_2e; 1. DR PRINTS; PR01044; TRNASYNTHGA. DR TIGRFAMs; TIGR00388; glyQ; 1. DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 286 Glycine--tRNA ligase alpha subunit. FT /FTId=PRO_0000072877. FT HELIX 3 16 {ECO:0000244|PDB:1J5W}. FT HELIX 32 34 {ECO:0000244|PDB:1J5W}. FT HELIX 36 39 {ECO:0000244|PDB:1J5W}. FT HELIX 41 43 {ECO:0000244|PDB:1J5W}. FT STRAND 48 57 {ECO:0000244|PDB:1J5W}. FT STRAND 72 83 {ECO:0000244|PDB:1J5W}. FT HELIX 88 98 {ECO:0000244|PDB:1J5W}. FT TURN 103 105 {ECO:0000244|PDB:1J5W}. FT STRAND 108 113 {ECO:0000244|PDB:1J5W}. FT HELIX 118 120 {ECO:0000244|PDB:1J5W}. FT STRAND 122 131 {ECO:0000244|PDB:1J5W}. FT STRAND 134 145 {ECO:0000244|PDB:1J5W}. FT STRAND 155 160 {ECO:0000244|PDB:1J5W}. FT HELIX 161 169 {ECO:0000244|PDB:1J5W}. FT HELIX 174 176 {ECO:0000244|PDB:1J5W}. FT STRAND 178 180 {ECO:0000244|PDB:1J5W}. FT HELIX 185 201 {ECO:0000244|PDB:1J5W}. FT HELIX 206 225 {ECO:0000244|PDB:1J5W}. FT HELIX 229 248 {ECO:0000244|PDB:1J5W}. FT HELIX 254 279 {ECO:0000244|PDB:1J5W}. SQ SEQUENCE 286 AA; 33540 MW; 9B8061D54B1160F2 CRC64; MYLQDVIMKL NDFWASKGCL LEQPYDMEVG AGTFHPATFF GSLRKGPWKV AYVQPSRRPT DGRYGENPNR LQRYFQYQVI IKPSPENSQE LYLESLEYLG INLKEHDIRF VEDNWESPTL GAWGVGWEVW LDGMEITQFT YFQQIGGISL KDIPLEITYG LERIAMYLQG VDNVYEVQWN ENVKYGDVFL ENEREFSVFN FEEANVGLLF RHFDEYEKEF YRLVEKNLYL PAYDYILKCS HTFNLLDARG AISVSQRQTY VKRIQAMARK AARVFLEVQA NENSPA // ID SYM_THEMA Reviewed; 629 AA. AC O33925; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 13-APR-2016, entry version 130. DE RecName: Full=Methionine--tRNA ligase; DE EC=6.1.1.10; DE AltName: Full=Methionyl-tRNA synthetase; DE Short=MetRS; GN Name=metG; Synonyms=metS; OrderedLocusNames=TM_1085; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=9380682; DOI=10.1073/pnas.94.20.10606; RA Guipaud O., Marguet E., Noll K.M., Bouthier de la Tour C., RA Forterre P.; RT "Both DNA gyrase and reverse gyrase are present in the RT hyperthermophilic bacterium Thermotoga maritima."; RL Proc. Natl. Acad. Sci. U.S.A. 94:10606-10611(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Is required not only for elongation of protein synthesis CC but also for the initiation of all mRNA translation through CC initiator tRNA(fMet) aminoacylation. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP + CC diphosphate + L-methionyl-tRNA(Met). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. MetG type 2A subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U76417; AAB87143.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36162.1; -; Genomic_DNA. DR PIR; E72297; E72297. DR RefSeq; NP_228891.1; NC_000853.1. DR RefSeq; WP_004080396.1; NZ_CP011107.1. DR ProteinModelPortal; O33925; -. DR SMR; O33925; 525-629. DR STRING; 243274.TM1085; -. DR DNASU; 897213; -. DR EnsemblBacteria; AAD36162; AAD36162; TM_1085. DR GeneID; 897213; -. DR KEGG; tma:TM1085; -. DR PATRIC; 23937099; VBITheMar51294_1098. DR eggNOG; ENOG4105CKH; Bacteria. DR eggNOG; COG0073; LUCA. DR eggNOG; COG0143; LUCA. DR InParanoid; O33925; -. DR KO; K01874; -. DR OMA; GHVMYVW; -. DR OrthoDB; EOG6CVV9B; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004825; F:methionine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR004495; Met-tRNA-synth_bsu_C. DR InterPro; IPR014758; Met-tRNA_synth. DR InterPro; IPR023457; Met-tRNA_synth_2. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR Pfam; PF01588; tRNA_bind; 1. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00398; metG; 1. DR TIGRFAMs; TIGR00399; metG_C_term; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; RNA-binding; tRNA-binding; Zinc. FT CHAIN 1 629 Methionine--tRNA ligase. FT /FTId=PRO_0000139257. FT DOMAIN 529 629 tRNA-binding. FT MOTIF 10 20 "HIGH" region. FT MOTIF 297 301 "KMSKS" region. FT METAL 125 125 Zinc. {ECO:0000250}. FT METAL 128 128 Zinc. {ECO:0000250}. FT METAL 146 146 Zinc. {ECO:0000250}. FT METAL 149 149 Zinc. {ECO:0000250}. FT BINDING 300 300 ATP. {ECO:0000250}. SQ SEQUENCE 629 AA; 73004 MW; B0E0759F7C78ACEC CRC64; MKFYITTPIY YVNSEPHIGS AYTTIVADII ARYKRFMGYD VFFLTGTDEH GQKVLQAAQQ AGKDPQEFCD ELAEKFKRLW KELKITNDYF IRTTDEMHMK TVQEFVAKMK ENGDVYKGIY KGWYCVPCET FWNEDEVIKE GEERFCPECK RPVKWVEEEN YFFRLSKYRD SLLKYYEEHP DFVEPDFRRN EMLKILEGGL KDLSITRTTF KWGVPMKDDP EHVIYVWVDA LINYISAIGY GWNDEMFNKW WPADLHLIGK EINRFHSIIW PAMLMSVGLP LPKKVFAHGW LTVNGQKISK SLGNAIDPRF FVKRYGNDVV RYYLIRDIMF GKDGDFSEER LVHRLNSDLA NDYGNLLHRI TAMIKKYFNG RLPSPSAQEG FDSWLKERFF ETKDAYHELM DSYRLTEALD KIWEFIADVN KYFNDTKPWI LGKEGNMERL GTVLYNSLEA VFKVALMTLP VMPDTSEEVF RRVSFEEKPS KEHLENWGVL KPGSTVIHGE PLFKKIDAKD FKKVVETVSA EQNAITIDDF SKVDLRIAKV LEAEKVPNSR KLLRLIIDLG TEKRQIVAGI AEHYRPEELV GKLIVVVANL KPAKLMGIES QGMLLAAKSG DTLRLLTVDG EITPGAKVS // ID SYI_THEMA Reviewed; 919 AA. AC P46213; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 123. DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002}; DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002}; DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002}; DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002}; GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002}; GN OrderedLocusNames=TM_1361; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-599. RX PubMed=7708661; DOI=10.1073/pnas.92.7.2441; RA Brown J.R., Doolittle W.F.; RT "Root of the universal tree of life based on ancient aminoacyl-tRNA RT synthetase gene duplications."; RL Proc. Natl. Acad. Sci. U.S.A. 92:2441-2445(1995). CC -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As CC IleRS can inadvertently accommodate and process structurally CC similar amino acids such as valine, to avoid such errors it has CC two additional distinct tRNA(Ile)-dependent editing activities. CC One activity is designated as 'pretransfer' editing and involves CC the hydrolysis of activated Val-AMP. The other activity is CC designated 'posttransfer' editing and involves deacylation of CC mischarged Val-tRNA(Ile). {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP + CC diphosphate + L-isoleucyl-tRNA(Ile). {ECO:0000255|HAMAP- CC Rule:MF_02002}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02002}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_02002}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- DOMAIN: IleRS has two distinct active sites: one for CC aminoacylation and one for editing. The misactivated valine is CC translocated from the active site to the editing site, which CC sterically excludes the correctly activated isoleucine. The single CC editing site contains two valyl binding pockets, one specific for CC each substrate (Val-AMP or Val-tRNA(Ile)). {ECO:0000255|HAMAP- CC Rule:MF_02002}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36431.1; -; Genomic_DNA. DR EMBL; L37104; AAC41448.1; -; Genomic_DNA. DR PIR; B72263; B72263. DR RefSeq; NP_229162.1; NC_000853.1. DR RefSeq; WP_004081557.1; NZ_CP011107.1. DR ProteinModelPortal; P46213; -. DR STRING; 243274.TM1361; -. DR EnsemblBacteria; AAD36431; AAD36431; TM_1361. DR GeneID; 898119; -. DR KEGG; tma:TM1361; -. DR PATRIC; 23937660; VBITheMar51294_1373. DR eggNOG; ENOG4105C07; Bacteria. DR eggNOG; COG0060; LUCA. DR InParanoid; P46213; -. DR KO; K01870; -. DR OMA; THGFIVD; -. DR OrthoDB; EOG644ZM1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002301; Ile-tRNA-ligase. DR InterPro; IPR023585; Ile-tRNA-ligase_type1. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR InterPro; IPR010663; Znf_FPG/IleRS. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR Pfam; PF06827; zf-FPG_IleRS; 1. DR PRINTS; PR00984; TRNASYNTHILE. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50677; SSF50677; 1. DR TIGRFAMs; TIGR00392; ileS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 919 Isoleucine--tRNA ligase. FT /FTId=PRO_0000098494. FT MOTIF 57 67 "HIGH" region. FT MOTIF 594 598 "KMSKS" region. FT METAL 887 887 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 890 890 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 907 907 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 910 910 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT BINDING 553 553 Aminoacyl-adenylate. {ECO:0000255|HAMAP- FT Rule:MF_02002}. FT BINDING 597 597 ATP. {ECO:0000255|HAMAP-Rule:MF_02002}. SQ SEQUENCE 919 AA; 107156 MW; 40E4D0876010C385 CRC64; MEYKNTLNLP KTSFPMKANL VNKEKVFLEE WEKMDLYNYV LEQRKGKPLF VLHDGPPYAN GHIHIGTALN KILKDIVVKY KTMRGYRAPY VPGWDTHGLP IEHRVSQELG EKIKEMSPAE IRKKCEEFAL RFVDIQREEF KRLGVRGDWE NPYITLKPDY EVKILDVFKT LVEQGNVYRS LKPIYWCPRC RTALAEAEIE YHDHKSPSIY VKFRSKEDPN FFIVIWTTTP WTLPANVGIA LHPDYEYSVV KVGEEKWVIA TDLLDAFSKE TGIDCSNVVE KIKGKDLEGK EFVHPIFDDR TSRVILADYV SLETGTGCVH IAPGHGEEDY IYGHVQYGLP IVSPVDEEGR FTEEAGKYKG MFIEDANEVI IEDLKRKGIL VHASSITHSY PHCWRCKGPV IFRATEQWFI SVDHNNLRQK VLEEIDKVKW IPEWGRNRIR SMVEERPDWC ISRQRVWGTP IPAVKCKECG EVVLDPKVIE HFMKIVEKEG TNAWFEKEVE ELIPEDFVCP KCGKRSFEKM LDTLDVWIDS GASFEYITTK REDHPFPLDM YLEGSDQHRG WFHSSIFLAV AKRGSAPYKE VLTHGFIKDE QGRKMSKSLG NVVDPMEVVE KYGAEILRLW LASSDYFNDI KISMRIVEQQ TEVYRKIRNT FRFLLGNLED FDPELDRVPH EKLLTIDRWA LGRLQEIIKR ATEYYDSYEF SKVYNLVVKY CTTELSSLYL DVVKDRLYVE AKDSIYRRSA QTVMHEILIS LMKILAPIMT FTMEEVYSHL HEKDRKYKTV QAEYWPEYRE EFIDRKLMED FEKLLSIRED VLKALEEKRQ QDVIGHSLDA EVVLVPKNDT IKALLEKYRD ILEELFIVSK VSLSDASGEL KGELVEVTVK HAEGEKCQRC WKYTTEISAS EDFPGVCPRC LAVLKGERK // ID SYK_THEMA Reviewed; 502 AA. AC Q9X231; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=Lysine--tRNA ligase; DE EC=6.1.1.6; DE AltName: Full=Lysyl-tRNA synthetase; DE Short=LysRS; GN Name=lysS; OrderedLocusNames=TM_1705; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate CC + L-lysyl-tRNA(Lys). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36772.1; -; Genomic_DNA. DR PIR; C72221; C72221. DR RefSeq; NP_229505.1; NC_000853.1. DR RefSeq; WP_004082221.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X231; -. DR STRING; 243274.TM1705; -. DR EnsemblBacteria; AAD36772; AAD36772; TM_1705. DR GeneID; 897886; -. DR KEGG; tma:TM1705; -. DR PATRIC; 23938384; VBITheMar51294_1722. DR eggNOG; ENOG4105CRK; Bacteria. DR eggNOG; COG1190; LUCA. DR InParanoid; Q9X231; -. DR KO; K04567; -. DR OMA; DMMNLTE; -. DR OrthoDB; EOG69PQ2M; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00252; Lys_tRNA_synth_class2; 1. DR InterPro; IPR004364; aa-tRNA-synt_II. DR InterPro; IPR018150; aa-tRNA-synt_II-like. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR002313; Lys-tRNA-ligase_II. DR InterPro; IPR018149; Lys-tRNA-synth_II_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR PANTHER; PTHR22594; PTHR22594; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PIRSF; PIRSF039101; LysRS2; 1. DR PRINTS; PR00982; TRNASYNTHLYS. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00499; lysS_bact; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 502 Lysine--tRNA ligase. FT /FTId=PRO_0000152696. FT COMPBIAS 490 497 Poly-Glu. FT METAL 398 398 Magnesium 1. {ECO:0000250}. FT METAL 405 405 Magnesium 1. {ECO:0000250}. FT METAL 405 405 Magnesium 2. {ECO:0000250}. SQ SEQUENCE 502 AA; 58998 MW; 4A44749676F82A94 CRC64; MLKEFKEQRL KEIQELRSMG IEPYPYKFEK ELTAREIREK YDYLQAGEVL ESEKLSFAGR VMSIRHHGKT AFFHMKDDTG RIQAYIKADS VGKEKMDLFK RHVKIGDFVG VRGFPFKSKT GELTIYVQEY TLLSKALRPL PEKWHGIKDK EIIYRQRYLE LIVNDEAIER FKKRFKAVRV IREFLNSRGF IEVETPILHY VTGGAEARPF VTHLNVFDID MYLRIAPELY LKRLIVGGFE KIYEIGKNFR NEGISYKHSP EFTSIEIYQA YADYNDMMDL TEELIVEVVK RTCGTLKISY QGKEIDFTPP WKRVRMRDFL KEKLGVDILE DPDEVLLKKL EEHGVELEIK NRAHLIDKLR DLVEEELVNP TFIIDHPVVI SPLAKRHRED PRLTERFELI IFGREIANAF SELNDPVDQY QRFLEQAKMR EEGDEEAHMM DLDFVRALEY GMPPTGGLGI GLDRLFMFIT DSPTIRDVIP FPIVKPKKFE EEEAEFEGGF EE // ID SYL_THEMA Reviewed; 824 AA. AC Q9WY15; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049}; DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049}; DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049}; DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049}; GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; GN OrderedLocusNames=TM_0168; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: ATP + L-leucine + tRNA(Leu) = AMP + CC diphosphate + L-leucyl-tRNA(Leu). {ECO:0000255|HAMAP- CC Rule:MF_00049}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00049}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35261.1; -; Genomic_DNA. DR PIR; F72408; F72408. DR RefSeq; NP_227983.1; NC_000853.1. DR RefSeq; WP_004082796.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY15; -. DR SMR; Q9WY15; 1-761. DR STRING; 243274.TM0168; -. DR PRIDE; Q9WY15; -. DR EnsemblBacteria; AAD35261; AAD35261; TM_0168. DR GeneID; 897007; -. DR KEGG; tma:TM0168; -. DR PATRIC; 23935184; VBITheMar51294_0169. DR eggNOG; ENOG4105C8T; Bacteria. DR eggNOG; COG0495; LUCA. DR InParanoid; Q9WY15; -. DR KO; K01869; -. DR OMA; EGAHRFI; -. DR OrthoDB; EOG63Z74X; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004823; F:leucine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002302; Leu-tRNA-ligase. DR InterPro; IPR025709; Leu_tRNA-synth_edit. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR PANTHER; PTHR11946:SF7; PTHR11946:SF7; 4. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR Pfam; PF13603; tRNA-synt_1_2; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR PRINTS; PR00985; TRNASYNTHLEU. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50677; SSF50677; 1. DR TIGRFAMs; TIGR00396; leuS_bact; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 824 Leucine--tRNA ligase. FT /FTId=PRO_0000152106. FT MOTIF 41 51 "HIGH" region. FT MOTIF 580 584 "KMSKS" region. FT BINDING 583 583 ATP. {ECO:0000255|HAMAP-Rule:MF_00049}. SQ SEQUENCE 824 AA; 95625 MW; 7CB0252A76A844EC CRC64; MKEYRPQEIE KKWQEVWEEK KVFYTPQRSE KPKYYALVMF PYPSGTLHVG HVKNYVIGDI VARYKRMRGY NVLHPFGYDA FGLPAENAAI EKGIHPEEWT RKNIATIRQQ VKKLGISYDW SREIATCDEE YYKWTQWIFL QLYKNGLAYK KKAAVNWCPK CKTVLANEQV KDGKCERCGT SVTIRHLEQW FFKITDYAER LLNDLDKLTG WPEHVKTMQR NWIGKSTGAE IDFPVEGSDT KIRVFTTRPD TLWGVTFMAL APESPLVEEL VPEEKKEELQ EFLERVKQQD RFRRTSVEAE KEGFFLGRYA INPVTGERIP IYVANYILME YGTGAIMGVP AHDQRDFSFA KKYGIPIKVV IKPADKDLDP EKMEEAYEGE GIMVNSGPFD GTPSSEGIEK VINWLEEKGI GKRSVQYKLR DWLISRQRYW GAPIPIIYCE KCGVVPVPEE DLPVRLPKDV EFLPTGQSPL SFHEGFKKTK CPVCGGEAQR ETDTMDTFVD SSWYFLRYVN PHLEDKPFEP DDVNYWLPVD QYIGGVEHAV LHLLYSRFVT KVLHDLGYLN FDEPFTNLFT QGMIYKDGAK MSKSKGNVVS PDEMIEKYGA DTLRMYILFM APPEKDAEWS DAGIEGVHRF VKRLWNTFYT VLPFVKEENT ENLVLKNSTE KELRRKLHSI IKKITEDIEG GFKFNTAISG LMELVNHLSQ YLNSVPQEEW NRKLLREIVE KLTLALSPFA PHLAEEFWHD LGNDSLVVQQ SWPSYDPKAL EVEEVEIAIQ INGKVRDKVV VPVDISEEDL KRIVLERERV KEYVDGKPIR KFIYVKGRIV NIVV // ID SYV_THEMA Reviewed; 865 AA. AC Q9X2D7; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 110. DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004}; DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004}; DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004}; DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004}; GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; GN OrderedLocusNames=TM_1817; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As CC ValRS can inadvertently accommodate and process structurally CC similar amino acids such as threonine, to avoid such errors, it CC has a "posttransfer" editing activity that hydrolyzes mischarged CC Thr-tRNA(Val) in a tRNA-dependent manner. {ECO:0000255|HAMAP- CC Rule:MF_02004}. CC -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate CC + L-valyl-tRNA(Val). {ECO:0000255|HAMAP-Rule:MF_02004}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}. CC -!- DOMAIN: ValRS has two distinct active sites: one for CC aminoacylation and one for editing. The misactivated threonine is CC translocated from the active site to the editing site. CC {ECO:0000255|HAMAP-Rule:MF_02004}. CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for CC aminoacylation activity. {ECO:0000255|HAMAP-Rule:MF_02004}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36880.1; -; Genomic_DNA. DR PIR; D72206; D72206. DR RefSeq; NP_229614.1; NC_000853.1. DR RefSeq; WP_004082363.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2D7; -. DR STRING; 243274.TM1817; -. DR EnsemblBacteria; AAD36880; AAD36880; TM_1817. DR GeneID; 897826; -. DR KEGG; tma:TM1817; -. DR PATRIC; 23938621; VBITheMar51294_1837. DR eggNOG; ENOG4105CA4; Bacteria. DR eggNOG; COG0525; LUCA. DR InParanoid; Q9X2D7; -. DR KO; K01873; -. DR OMA; SQYRFDL; -. DR OrthoDB; EOG644ZM1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.380; -; 1. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR010978; tRNA-bd_arm. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR InterPro; IPR019499; Val-tRNA_synth_tRNA-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR InterPro; IPR002303; Valyl-tRNA_ligase. DR PANTHER; PTHR11946:SF5; PTHR11946:SF5; 2. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR Pfam; PF10458; Val_tRNA-synt_C; 1. DR PRINTS; PR00986; TRNASYNTHVAL. DR SUPFAM; SSF46589; SSF46589; 1. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50677; SSF50677; 1. DR TIGRFAMs; TIGR00422; valS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 865 Valine--tRNA ligase. FT /FTId=PRO_0000106238. FT COILED 797 865 {ECO:0000255|HAMAP-Rule:MF_02004}. FT MOTIF 43 53 "HIGH" region. FT MOTIF 523 527 "KMSKS" region. FT BINDING 526 526 ATP. {ECO:0000255|HAMAP-Rule:MF_02004}. SQ SEQUENCE 865 AA; 101809 MW; 0D4F16060E94648F CRC64; MAELSTRYNP AEIETKWYRY WEEKGYFTPK GVGEKFSIVI PPPNITGRIH MGHALNITLQ DIVVRYKRMK GYDVLWVPGE DHAGIATQNA VEKFLLQTQG KTREEIGREK FLEITWEWAN KYRREIREQI KALGASVDWT RERFTLDEGL SRAVRKVFVE LYRKGLIYRG KYIVNWCPRC KTVLSDEEVE HKEHKSKLYY VKYPVKDSDE YIVVATTRPE TMLGDTAVAV HPEDERYKNF VGKTLILPLV GREIPVVADK YVDPKFGTGA VKVTPAHDPN DYLIAQRHNL PMIEIFDDNA RINENGGKYK GLDRYEAREK IVKDLEEQGF LVKIEDYTHS VGHCYRCDTV IEPKLSDQWF VSTKPLAKRA IEAVENGEIR FFPERWTKVY LNWMYEIRDW CISRQLWWGH RIPVWYCQDC GHLNVSEEDV EKCEKCGSTN LKQDEDVLDT WFSSALWPFS TLGWPEETED LKRYYPTDLL VTGFDIIFFW VARMIMMGYE FMNDKPFSHV YIHQLVRDKY GRKMSKSLGN GIDPLEVIDE YGADPMRFTL AILAAQGRDI KLDPRYFDAY KKFANKIWNA TRFVLMNLED YKEVPLENLK TVDKWILTRL NKTVEEVTNA LENYDFNIAA RTIYNFFWDD FCDWYIEASK PRLKTEERNL VQTVLVKVLD ASLRLLHPFM PFLTEELWQK LPVAGESITI AKWPEIEREL IDETAEKEFT RLMNMVRGVR NVRAEMNLPQ SQRVKVYIKG YEVTEEEELL LKTLGNIEEV SFVNEKPPKT ATAYVEEEIE AYVDLGGLID FEKEKERLKQ IMEKIQKEID RLEKKLANKD FVEKAPEEVV EETKEKLNTN RERLARLESI LRDLE // ID SYY_THEMA Reviewed; 401 AA. AC Q9WYU8; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02007}; DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02007}; DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02007}; DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02007}; GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02007}; GN OrderedLocusNames=TM_0478; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a CC two-step reaction: tyrosine is first activated by ATP to form Tyr- CC AMP and then transferred to the acceptor end of tRNA(Tyr). CC {ECO:0000255|HAMAP-Rule:MF_02007}. CC -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP + CC diphosphate + L-tyrosyl-tRNA(Tyr). {ECO:0000255|HAMAP- CC Rule:MF_02007}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02007}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02007}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. TyrS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02007}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_02007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35566.1; -; Genomic_DNA. DR PIR; F72372; F72372. DR RefSeq; NP_228288.1; NC_000853.1. DR RefSeq; WP_004081488.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYU8; -. DR STRING; 243274.TM0478; -. DR EnsemblBacteria; AAD35566; AAD35566; TM_0478. DR GeneID; 897511; -. DR KEGG; tma:TM0478; -. DR PATRIC; 23935855; VBITheMar51294_0485. DR eggNOG; ENOG4105DA0; Bacteria. DR eggNOG; COG0162; LUCA. DR InParanoid; Q9WYU8; -. DR KO; K01866; -. DR OMA; DMFGKVM; -. DR OrthoDB; EOG6B09VR; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central. DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.290.10; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_02007; Tyr_tRNA_synth_type2; 1. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002942; S4_RNA-bd. DR InterPro; IPR002307; Tyr-tRNA-ligase. DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type. DR InterPro; IPR024108; Tyr-tRNA-ligase_bac_2. DR PANTHER; PTHR11766; PTHR11766; 1. DR Pfam; PF01479; S4; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01040; TRNASYNTHTYR. DR SMART; SM00363; S4; 1. DR TIGRFAMs; TIGR00234; tyrS; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome; KW RNA-binding. FT CHAIN 1 401 Tyrosine--tRNA ligase. FT /FTId=PRO_0000236771. FT DOMAIN 334 395 S4 RNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_02007}. FT MOTIF 41 50 "HIGH" region. FT MOTIF 225 229 "KMSKS" region. FT BINDING 228 228 ATP. {ECO:0000255|HAMAP-Rule:MF_02007}. SQ SEQUENCE 401 AA; 46186 MW; A65F7638A239B210 CRC64; MTPEEQVKIL KRNVVDLISE EELLDRIKRK GKLRVKLGVD PSRPDLHLGH AVVLRKLREF QDLGHTVVLI IGDFTARIGD PSGRNETRPM LTKEEVLENA KTYQEQAFKI LDPKRTELRF NGEWLDRMTF ADVIILASKY TVARMLERDD FAKRFKEGIP IAISEFLYPL AQAYDSVAIQ SDVELGGTDQ LFNLLVGRKI QEEYGQEPQI VMTMPIIEGT DGKLKMSKSY GNYIAFNDPP EEMYGKLMSI PDELIIKYMR LLTDIPEERI EEYERKMKEK TINPRDVKMV LAYEITRFFH GEENAKKAQE HFVKVFQKKE IPDEMPVVEI SQEKNIVDLL VEIGAASSKS EAKRLVSQGG VYIDGERIED IKFTVEPDGE RVLRVGKRKF YRISGGETKK L // ID TDXH_THEMA Reviewed; 215 AA. AC Q9WZR4; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00401}; DE EC=1.11.1.15 {ECO:0000255|HAMAP-Rule:MF_00401}; GN OrderedLocusNames=TM_0807; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Protects cells against oxidative stress. Can reduce CC hydrogen peroxide and/or alkyl hydroperoxides using dithiothreitol CC as an electron donor (in vitro). {ECO:0000255|HAMAP- CC Rule:MF_00401}. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC {ECO:0000255|HAMAP-Rule:MF_00401}. CC -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring CC structure. {ECO:0000255|HAMAP-Rule:MF_00401}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00401}. CC -!- SIMILARITY: Belongs to the AhpC/TSA family. TDXH subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00401}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|HAMAP- CC Rule:MF_00401}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35889.1; -; Genomic_DNA. DR PIR; H72330; H72330. DR RefSeq; NP_228616.1; NC_000853.1. DR RefSeq; WP_004080855.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZR4; -. DR SMR; Q9WZR4; 3-214. DR STRING; 243274.TM0807; -. DR EnsemblBacteria; AAD35889; AAD35889; TM_0807. DR GeneID; 898475; -. DR KEGG; tma:TM0807; -. DR PATRIC; 23936534; VBITheMar51294_0819. DR eggNOG; ENOG4105D3R; Bacteria. DR eggNOG; COG0450; LUCA. DR InParanoid; Q9WZR4; -. DR KO; K03386; -. DR OMA; IPANWPN; -. DR OrthoDB; EOG67X1XH; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-HAMAP. DR GO; GO:0045454; P:cell redox homeostasis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.30.10; -; 1. DR HAMAP; MF_00401; Peroxiredoxin; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR022915; Peroxiredoxin_TDXH. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Antioxidant; Complete proteome; Cytoplasm; Oxidoreductase; KW Redox-active center; Reference proteome. FT CHAIN 1 215 Peroxiredoxin. FT /FTId=PRO_0000135177. FT DOMAIN 6 161 Thioredoxin. {ECO:0000255|HAMAP- FT Rule:MF_00401}. FT ACT_SITE 48 48 Cysteine sulfenic acid (-SOH) FT intermediate. {ECO:0000255|HAMAP- FT Rule:MF_00401}. FT BINDING 124 124 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00401}. SQ SEQUENCE 215 AA; 24764 MW; 4695D5AFB3E3E4C0 CRC64; MEGRIPLIGE EFPRVEVKTT HGKKVLPDDF RGKWFVLFSH PADFTPVCTT EFVAFQKRYD EFRKLNTELI GLSIDQVFSH IKWIEWIKEK LGVEIEFPVI ADDLGEVSRR LGLIHPNKGT NTVRAVFIVD PNGIIRAIVY YPQEVGRNID EILRAVKALQ TSDEKGVAIP ANWPSNELIN DSVIVPPASS VEEARKRLES KDFECYDWWF CYKKV // ID TGT_THEMA Reviewed; 369 AA. AC Q9X1P7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Queuine tRNA-ribosyltransferase; DE EC=2.4.2.29; DE AltName: Full=Guanine insertion enzyme; DE AltName: Full=tRNA-guanine transglycosylase; GN Name=tgt; OrderedLocusNames=TM_1561; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Exchanges the guanine residue with 7-aminomethyl-7- CC deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His CC and -Tyr). After this exchange, a cyclopentendiol moiety is CC attached to the 7-aminomethyl group of 7-deazaguanine, resulting CC in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis- CC dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + queuine = queuosine(34) CC in tRNA + guanine. CC -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + 7-aminomethyl-7- CC carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36627.1; -; Genomic_DNA. DR PIR; D72240; D72240. DR RefSeq; NP_229361.1; NC_000853.1. DR RefSeq; WP_004081969.1; NZ_CP011107.1. DR PDB; 2ASH; X-ray; 1.90 A; A/B/C/D=1-369. DR PDBsum; 2ASH; -. DR ProteinModelPortal; Q9X1P7; -. DR SMR; Q9X1P7; 1-363. DR STRING; 243274.TM1561; -. DR EnsemblBacteria; AAD36627; AAD36627; TM_1561. DR GeneID; 897381; -. DR KEGG; tma:TM1561; -. DR KEGG; tmi:THEMA_06475; -. DR KEGG; tmw:THMA_1596; -. DR PATRIC; 23938084; VBITheMar51294_1579. DR eggNOG; ENOG4105C6U; Bacteria. DR eggNOG; COG0343; LUCA. DR InParanoid; Q9X1P7; -. DR KO; K00773; -. DR OMA; MGVGKPD; -. DR OrthoDB; EOG6SNDVG; -. DR UniPathway; UPA00392; -. DR EvolutionaryTrace; Q9X1P7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central. DR GO; GO:0006400; P:tRNA modification; IEA:InterPro. DR Gene3D; 3.20.20.105; -; 1. DR HAMAP; MF_00168; Q_tRNA_Tgt; 1. DR InterPro; IPR004803; Queuine_tRNA-ribosylTrfase. DR InterPro; IPR002616; tRNA_ribo_trans-like. DR Pfam; PF01702; TGT; 1. DR SUPFAM; SSF51713; SSF51713; 1. DR TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1. DR TIGRFAMs; TIGR00449; tgt_general; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Glycosyltransferase; Metal-binding; KW Queuosine biosynthesis; Reference proteome; Transferase; KW tRNA processing; Zinc. FT CHAIN 1 369 Queuine tRNA-ribosyltransferase. FT /FTId=PRO_0000135545. FT ACT_SITE 89 89 Nucleophile. {ECO:0000250}. FT METAL 299 299 Zinc. {ECO:0000250}. FT METAL 301 301 Zinc. {ECO:0000250}. FT METAL 304 304 Zinc. {ECO:0000250}. FT METAL 330 330 Zinc. {ECO:0000250}. FT BINDING 90 90 Substrate. {ECO:0000250}. FT STRAND 2 9 {ECO:0000244|PDB:2ASH}. FT STRAND 12 19 {ECO:0000244|PDB:2ASH}. FT STRAND 22 37 {ECO:0000244|PDB:2ASH}. FT HELIX 43 49 {ECO:0000244|PDB:2ASH}. FT STRAND 54 56 {ECO:0000244|PDB:2ASH}. FT HELIX 59 63 {ECO:0000244|PDB:2ASH}. FT HELIX 67 72 {ECO:0000244|PDB:2ASH}. FT HELIX 76 80 {ECO:0000244|PDB:2ASH}. FT STRAND 86 88 {ECO:0000244|PDB:2ASH}. FT HELIX 92 96 {ECO:0000244|PDB:2ASH}. FT STRAND 108 111 {ECO:0000244|PDB:2ASH}. FT TURN 113 115 {ECO:0000244|PDB:2ASH}. FT STRAND 118 121 {ECO:0000244|PDB:2ASH}. FT HELIX 123 133 {ECO:0000244|PDB:2ASH}. FT STRAND 136 139 {ECO:0000244|PDB:2ASH}. FT HELIX 151 171 {ECO:0000244|PDB:2ASH}. FT STRAND 178 183 {ECO:0000244|PDB:2ASH}. FT HELIX 189 200 {ECO:0000244|PDB:2ASH}. FT STRAND 205 209 {ECO:0000244|PDB:2ASH}. FT STRAND 213 216 {ECO:0000244|PDB:2ASH}. FT HELIX 218 229 {ECO:0000244|PDB:2ASH}. FT STRAND 238 240 {ECO:0000244|PDB:2ASH}. FT HELIX 246 253 {ECO:0000244|PDB:2ASH}. FT TURN 254 256 {ECO:0000244|PDB:2ASH}. FT STRAND 259 263 {ECO:0000244|PDB:2ASH}. FT HELIX 264 270 {ECO:0000244|PDB:2ASH}. FT STRAND 273 276 {ECO:0000244|PDB:2ASH}. FT STRAND 279 282 {ECO:0000244|PDB:2ASH}. FT HELIX 286 288 {ECO:0000244|PDB:2ASH}. FT HELIX 302 306 {ECO:0000244|PDB:2ASH}. FT HELIX 309 317 {ECO:0000244|PDB:2ASH}. FT HELIX 321 347 {ECO:0000244|PDB:2ASH}. FT HELIX 351 361 {ECO:0000244|PDB:2ASH}. SQ SEQUENCE 369 AA; 41429 MW; 5E9FF9C589347DF2 CRC64; MEFEVKKTFG KARLGVMKLH HGAVETPVFM PVGTNASVKL LTPRDLEEAG AEIILSNTFH LMLKPGVEII KLHRGLHNFM GWKRPILTDS GGFQVFSLPK IRIDDEGVVF RSPIDGSKVF LNPEISMEVQ IALGSDICMV FDHCPVPDAD YEEVKEATER TYRWALRSKK AFKTENQALF GIVQGGIYPD LRRESALQLT SIGFDGYAIG GLSIGEERSL TLEMTEVTVE FLPEDKPRYF MGGGSPELIL ELVDRGVDMF DSVFPTRIAR HGTALTWNGK LNLKASYNKR SLEPVDERCG CYTCKNFTRS YIHHLFDRGE VLGQILLTIH NINFMISLMK EVRRSIESGT FKELKSKVVE VYSSGGVNV // ID THI4_THEMA Reviewed; 250 AA. AC Q9WZP4; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 20-JAN-2016, entry version 92. DE RecName: Full=Putative thiazole biosynthetic enzyme; GN OrderedLocusNames=TM_0787; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in biosynthesis of the thiamine precursor CC thiazole. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35869.1; -; Genomic_DNA. DR PIR; D72333; D72333. DR RefSeq; NP_228596.1; NC_000853.1. DR RefSeq; WP_010865204.1; NC_000853.1. DR ProteinModelPortal; Q9WZP4; -. DR STRING; 243274.TM0787; -. DR DNASU; 898455; -. DR EnsemblBacteria; AAD35869; AAD35869; TM_0787. DR GeneID; 898455; -. DR KEGG; tma:TM0787; -. DR PATRIC; 23936494; VBITheMar51294_0799. DR eggNOG; ENOG4105IQJ; Bacteria. DR eggNOG; COG1635; LUCA. DR InParanoid; Q9WZP4; -. DR KO; K03146; -. DR OMA; RMGPVFG; -. DR OrthoDB; EOG689HV5; -. DR BioCyc; TMAR243274:GC6P-814-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.50.50.60; -; 1. DR HAMAP; MF_00304; Thi4; 1. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR002922; Thi4_fam. DR InterPro; IPR022828; Thi4_putative. DR SUPFAM; SSF51905; SSF51905; 1. DR TIGRFAMs; TIGR00292; TIGR00292; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; NAD; Reference proteome; KW Thiamine biosynthesis. FT CHAIN 1 250 Putative thiazole biosynthetic enzyme. FT /FTId=PRO_0000153955. FT NP_BIND 27 55 FAD or NAD. {ECO:0000255}. SQ SEQUENCE 250 AA; 27073 MW; 54C8BC93F3C286F8 CRC64; MSMRDVLISR LIVERYFEKL RNSLELDVAI VGAGPSGLTA AYELAKNGFR VAVFEERNTP GGGIWGGGMM FNEIVLEKEL ENFLKEVEIE YEVKEDHIVV DSVHFASGLL YRATKAGAIV FNNVSVEDVA VQNGRVCGVV VNWGPTVRLG LHVDPITVKA SFVVDGTGHP ANVVSLLAKR GLVEMKTEFP MDADEAEKFV VDNTGEIFPG LLVSGMAVCA VHGGPRMGPI FGGMILSGQK VARIVSERLR // ID TAL_THEMA Reviewed; 218 AA. AC Q9WYD1; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=Transaldolase; DE EC=2.2.1.2; GN Name=tal; OrderedLocusNames=TM_0295; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=11120740; DOI=10.1074/jbc.M008061200; RA Schuermann M., Sprenger G.A.; RT "Fructose-6-phosphate aldolase is a novel class I aldolase from RT Escherichia coli and is related to a novel group of bacterial RT transaldolases."; RL J. Biol. Chem. 276:11055-11061(2001). CC -!- FUNCTION: Transaldolase is important for the balance of CC metabolites in the pentose-phosphate pathway. Does not show CC fructose-6-P aldolase activity. {ECO:0000269|PubMed:11120740}. CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. CC {ECO:0000269|PubMed:11120740}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D- CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative CC stage): step 2/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3B CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35383.1; -; Genomic_DNA. DR PIR; G72394; G72394. DR RefSeq; NP_228107.1; NC_000853.1. DR RefSeq; WP_004083013.1; NZ_CP011107.1. DR PDB; 1VPX; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-218. DR PDBsum; 1VPX; -. DR ProteinModelPortal; Q9WYD1; -. DR SMR; Q9WYD1; 1-215. DR STRING; 243274.TM0295; -. DR EnsemblBacteria; AAD35383; AAD35383; TM_0295. DR GeneID; 897220; -. DR KEGG; tma:TM0295; -. DR PATRIC; 23935469; VBITheMar51294_0300. DR eggNOG; ENOG4105CW3; Bacteria. DR eggNOG; COG0176; LUCA. DR InParanoid; Q9WYD1; -. DR KO; K00616; -. DR OMA; GRDFYEV; -. DR OrthoDB; EOG6PS600; -. DR BRENDA; 2.2.1.2; 6331. DR UniPathway; UPA00115; UER00414. DR EvolutionaryTrace; Q9WYD1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00494; Transaldolase_3b; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001585; TAL/FSA. DR InterPro; IPR022999; Transaldolase_3B. DR InterPro; IPR004731; Transaldolase_3B/F6P_aldolase. DR InterPro; IPR018225; Transaldolase_AS. DR PANTHER; PTHR10683; PTHR10683; 1. DR Pfam; PF00923; Transaldolase; 1. DR TIGRFAMs; TIGR00875; fsa_talC_mipB; 1. DR PROSITE; PS01054; TRANSALDOLASE_1; 1. DR PROSITE; PS00958; TRANSALDOLASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Pentose shunt; KW Reference proteome; Schiff base; Transferase. FT CHAIN 1 218 Transaldolase. FT /FTId=PRO_0000173687. FT ACT_SITE 83 83 Schiff-base intermediate with substrate. FT {ECO:0000250}. FT STRAND 2 6 {ECO:0000244|PDB:1VPX}. FT HELIX 10 18 {ECO:0000244|PDB:1VPX}. FT STRAND 24 26 {ECO:0000244|PDB:1VPX}. FT HELIX 30 34 {ECO:0000244|PDB:1VPX}. FT HELIX 42 50 {ECO:0000244|PDB:1VPX}. FT STRAND 54 57 {ECO:0000244|PDB:1VPX}. FT HELIX 63 74 {ECO:0000244|PDB:1VPX}. FT STRAND 80 87 {ECO:0000244|PDB:1VPX}. FT HELIX 88 99 {ECO:0000244|PDB:1VPX}. FT STRAND 104 109 {ECO:0000244|PDB:1VPX}. FT HELIX 112 121 {ECO:0000244|PDB:1VPX}. FT STRAND 124 129 {ECO:0000244|PDB:1VPX}. FT HELIX 130 135 {ECO:0000244|PDB:1VPX}. FT HELIX 140 154 {ECO:0000244|PDB:1VPX}. FT STRAND 159 164 {ECO:0000244|PDB:1VPX}. FT HELIX 168 177 {ECO:0000244|PDB:1VPX}. FT STRAND 180 184 {ECO:0000244|PDB:1VPX}. FT HELIX 186 192 {ECO:0000244|PDB:1VPX}. FT HELIX 196 214 {ECO:0000244|PDB:1VPX}. SQ SEQUENCE 218 AA; 24213 MW; 3FF8B0A85CFA6EFA CRC64; MKIFLDTANL EEIKKGVEWG IVDGVTTNPT LISKEGAEFK QRVKEICDLV KGPVSAEVVS LDYEGMVREA RELAQISEYV VIKIPMTPDG IKAVKTLSAE GIKTNVTLVF SPAQAILAAK AGATYVSPFV GRMDDLSNDG MRMLGEIVEI YNNYGFETEI IAASIRHPMH VVEAALMGVD IVTMPFAVLE KLFKHPMTDL GIERFMEDWK KYLENLKK // ID TIG_THEMA Reviewed; 425 AA. AC Q9WZF8; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=Trigger factor; DE Short=TF; DE EC=5.2.1.8; DE AltName: Full=PPIase; GN Name=tig; OrderedLocusNames=TM_0694; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Involved in protein export. Acts as a chaperone by CC maintaining the newly synthesized protein in an open conformation. CC Functions as a peptidyl-prolyl cis-trans isomerase (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- INTERACTION: CC P38526:rpsG; NbExp=5; IntAct=EBI-2463534, EBI-2463521; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to CC the ribosome near the polypeptide exit tunnel while the other half CC is free in the cytoplasm. {ECO:0000250}. CC -!- DOMAIN: Consists of 3 domains; the N-terminus binds the ribosome, CC the middle domain has PPIase activity, while the C-terminus has CC intrinsic chaperone activity on its own. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35776.1; -; Genomic_DNA. DR PIR; D72345; D72345. DR RefSeq; NP_228503.1; NC_000853.1. DR RefSeq; WP_004081061.1; NZ_CP011107.1. DR PDB; 2NSA; X-ray; 1.70 A; A=244-405. DR PDB; 2NSB; X-ray; 3.20 A; A=1-109. DR PDB; 2NSC; X-ray; 2.20 A; A=1-109. DR PDB; 3GTY; X-ray; 3.40 A; X=1-425. DR PDB; 3GU0; X-ray; 3.50 A; A=1-405. DR PDBsum; 2NSA; -. DR PDBsum; 2NSB; -. DR PDBsum; 2NSC; -. DR PDBsum; 3GTY; -. DR PDBsum; 3GU0; -. DR ProteinModelPortal; Q9WZF8; -. DR SMR; Q9WZF8; 1-109, 244-406. DR IntAct; Q9WZF8; 1. DR STRING; 243274.TM0694; -. DR DNASU; 898361; -. DR EnsemblBacteria; AAD35776; AAD35776; TM_0694. DR GeneID; 898361; -. DR KEGG; tma:TM0694; -. DR PATRIC; 23936306; VBITheMar51294_0706. DR eggNOG; ENOG4107XYV; Bacteria. DR eggNOG; COG0544; LUCA. DR InParanoid; Q9WZF8; -. DR KO; K03545; -. DR OMA; PRIIDQR; -. DR OrthoDB; EOG63VBX3; -. DR EvolutionaryTrace; Q9WZF8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3120.10; -; 1. DR Gene3D; 3.30.70.1050; -; 1. DR HAMAP; MF_00303; Trigger_factor_Tig; 1. DR InterPro; IPR005215; Trig_fac. DR InterPro; IPR008880; Trigger_fac_C. DR InterPro; IPR008881; Trigger_fac_ribosome-bd_bac. DR InterPro; IPR027304; Trigger_fact/SurA_dom. DR Pfam; PF05698; Trigger_C; 1. DR Pfam; PF05697; Trigger_N; 1. DR PIRSF; PIRSF003095; Trigger_factor; 1. DR SUPFAM; SSF102735; SSF102735; 1. DR SUPFAM; SSF109998; SSF109998; 1. DR TIGRFAMs; TIGR00115; tig; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Chaperone; Complete proteome; KW Cytoplasm; Isomerase; Reference proteome; Rotamase. FT CHAIN 1 425 Trigger factor. FT /FTId=PRO_0000179452. FT DOMAIN 158 231 PPIase FKBP-type. FT STRAND 2 9 {ECO:0000244|PDB:2NSC}. FT STRAND 12 18 {ECO:0000244|PDB:2NSC}. FT HELIX 21 36 {ECO:0000244|PDB:2NSC}. FT STRAND 42 44 {ECO:0000244|PDB:3GU0}. FT HELIX 51 58 {ECO:0000244|PDB:2NSC}. FT HELIX 59 61 {ECO:0000244|PDB:2NSC}. FT HELIX 62 71 {ECO:0000244|PDB:2NSC}. FT HELIX 74 77 {ECO:0000244|PDB:2NSC}. FT TURN 78 80 {ECO:0000244|PDB:2NSC}. FT STRAND 83 85 {ECO:0000244|PDB:3GTY}. FT STRAND 88 94 {ECO:0000244|PDB:3GTY}. FT STRAND 99 107 {ECO:0000244|PDB:3GTY}. FT STRAND 110 112 {ECO:0000244|PDB:3GTY}. FT HELIX 116 118 {ECO:0000244|PDB:3GTY}. FT STRAND 119 124 {ECO:0000244|PDB:3GTY}. FT HELIX 126 144 {ECO:0000244|PDB:3GTY}. FT STRAND 148 150 {ECO:0000244|PDB:3GTY}. FT STRAND 159 168 {ECO:0000244|PDB:3GTY}. FT STRAND 174 183 {ECO:0000244|PDB:3GTY}. FT HELIX 193 196 {ECO:0000244|PDB:3GTY}. FT STRAND 204 211 {ECO:0000244|PDB:3GTY}. FT STRAND 214 228 {ECO:0000244|PDB:3GTY}. FT HELIX 235 239 {ECO:0000244|PDB:3GTY}. FT STRAND 241 244 {ECO:0000244|PDB:3GU0}. FT HELIX 248 254 {ECO:0000244|PDB:2NSA}. FT HELIX 259 262 {ECO:0000244|PDB:2NSA}. FT HELIX 267 278 {ECO:0000244|PDB:2NSA}. FT HELIX 279 282 {ECO:0000244|PDB:2NSA}. FT STRAND 284 286 {ECO:0000244|PDB:3GTY}. FT HELIX 289 305 {ECO:0000244|PDB:2NSA}. FT HELIX 309 314 {ECO:0000244|PDB:2NSA}. FT HELIX 319 347 {ECO:0000244|PDB:2NSA}. FT HELIX 353 367 {ECO:0000244|PDB:2NSA}. FT HELIX 371 380 {ECO:0000244|PDB:2NSA}. FT HELIX 382 402 {ECO:0000244|PDB:2NSA}. FT STRAND 405 410 {ECO:0000244|PDB:3GTY}. SQ SEQUENCE 425 AA; 49898 MW; BEC16F20ACFDD922 CRC64; MEVKELERDK NRVVLEYVFG AEEIAQAEDK AVRYLNQRVE IPGFRKGRIP KNVLKMKLGE EFQEYTLDFL MDLIPDTLKD RKLILSPIVT ERELKDVTAR VVVEVHEEPE VRIGDISKIE VEKVDEEKVL EKYVERRIED LRESHALLEP KEGPAEAGDL VRVNMEVYNE EGKKLTSREY EYVISEDEDR PFVKDLVGKK KGDVVEIERE YEGKKYTYKL EVEEVYKRTL PEIGDELAKS VNNEFETLEQ LKESLKKEGK EIYDVEMKES MREQLLEKLP EIVEIEISDR TLEILVNEAI NRLKREGRYE QIVSSYESEE KFREELKERI LDDIKRDRVI EVLAQEKGIS VNDEELEKEA EELAPFWGIS PDRAKSLVKA RQDLREELRW AILKRKVLDL LLQEVKVKVV EPKGEGDDSE GKEDN // ID THIC_THEMA Reviewed; 424 AA. AC Q9WZP5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE EC=4.1.99.17 {ECO:0000255|HAMAP-Rule:MF_00089}; DE AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE Short=HMP-P synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE Short=HMP-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE Short=HMPP synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000255|HAMAP-Rule:MF_00089}; GN Name=thiC {ECO:0000255|HAMAP-Rule:MF_00089}; GN OrderedLocusNames=TM_0788; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction. {ECO:0000255|HAMAP-Rule:MF_00089}. CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5- CC (phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + CC formate + CO. {ECO:0000255|HAMAP-Rule:MF_00089}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00089}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine. {ECO:0000255|HAMAP-Rule:MF_00089}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00089}. CC -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000255|HAMAP- CC Rule:MF_00089}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35870.1; -; Genomic_DNA. DR PIR; E72333; E72333. DR RefSeq; NP_228597.1; NC_000853.1. DR RefSeq; WP_004080892.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZP5; -. DR STRING; 243274.TM0788; -. DR DNASU; 898456; -. DR EnsemblBacteria; AAD35870; AAD35870; TM_0788. DR GeneID; 898456; -. DR KEGG; tma:TM0788; -. DR PATRIC; 23936496; VBITheMar51294_0800. DR eggNOG; ENOG4105CBF; Bacteria. DR eggNOG; COG0422; LUCA. DR InParanoid; Q9WZP5; -. DR KO; K03147; -. DR OMA; MTLHCGI; -. DR OrthoDB; EOG6NWBM5; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00089; ThiC; 1. DR InterPro; IPR002817; ThiC. DR Pfam; PF01964; ThiC_Rad_SAM; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine; Thiamine biosynthesis; KW Zinc. FT CHAIN 1 424 Phosphomethylpyrimidine synthase. FT /FTId=PRO_0000152843. FT REGION 185 187 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT REGION 226 229 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT METAL 269 269 Zinc. {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 333 333 Zinc. {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 408 408 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 411 411 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 415 415 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00089}. FT BINDING 66 66 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 95 95 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 124 124 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 163 163 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 265 265 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 292 292 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. SQ SEQUENCE 424 AA; 47155 MW; BFD6E96BBA9458BC CRC64; MTQMEMARKG VVSDEMKKVA EYEGVDVEIV RQKLAEGRAV LPKNKLHRIE RPMIVGEGFS VKVNANIGTS QGFSSLEEEK EKARVAIEYG ADSLMVLSTW GDLREIRRAI VEMSPVPVGS VPIYDSAVRS YQMKKNVVDF SEKDFFDMVI AHAEDGIDFM TIHVGVTRRV LDRIKSSRRV LKIVSRGGAI IAGWMIKNNK ENPFYEHFDE LLDIAKDYDI TLSLGDGMRP GAVVDASDAQ QFEELFVMGE LVERAREKGV QVMLEGPGHV PLNEVEMNVR LMKKIGKGAP IFLLGPLPTD RAMGYDHIAC AIGGALAGYY GADFLCYVTP SEHISLPDVE DVREGVIASK IAAIVADVAR GNKKAWELEK KMALARKNFD WETMFSLSLG KDVAKKKYEE RPYPDKGCSM CGPFCAIKIA EEFS // ID THII_THEMA Reviewed; 388 AA. AC Q9X220; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Probable tRNA sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021}; DE EC=2.8.1.4 {ECO:0000255|HAMAP-Rule:MF_00021}; DE AltName: Full=Sulfur carrier protein ThiS sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021}; DE AltName: Full=Thiamine biosynthesis protein ThiI {ECO:0000255|HAMAP-Rule:MF_00021}; DE AltName: Full=tRNA 4-thiouridine synthase {ECO:0000255|HAMAP-Rule:MF_00021}; GN Name=thiI {ECO:0000255|HAMAP-Rule:MF_00021}; GN OrderedLocusNames=TM_1694; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA CC to produce 4-thiouridine in position 8 of tRNAs, which functions CC as a near-UV photosensor. Also catalyzes the transfer of sulfur to CC the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. CC This is a step in the synthesis of thiazole, in the thiamine CC biosynthesis pathway. The sulfur is donated as persulfide by IscS. CC {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- CATALYTIC ACTIVITY: L-cysteine + 'activated' tRNA = L-serine + CC tRNA containing a thionucleotide. {ECO:0000255|HAMAP- CC Rule:MF_00021}. CC -!- CATALYTIC ACTIVITY: [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + CC [ThiS]-COSH + AMP. {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000255|HAMAP- CC Rule:MF_00021}. CC -!- SIMILARITY: Contains 1 THUMP domain. {ECO:0000255|HAMAP- CC Rule:MF_00021}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36761.1; -; Genomic_DNA. DR PIR; H72223; H72223. DR RefSeq; NP_229494.1; NC_000853.1. DR RefSeq; WP_010865383.1; NC_000853.1. DR PDB; 4KR6; X-ray; 2.85 A; A/B=1-388. DR PDB; 4KR7; X-ray; 3.42 A; A/B=1-388. DR PDB; 4KR9; X-ray; 3.50 A; A/B=1-388. DR PDBsum; 4KR6; -. DR PDBsum; 4KR7; -. DR PDBsum; 4KR9; -. DR ProteinModelPortal; Q9X220; -. DR STRING; 243274.TM1694; -. DR EnsemblBacteria; AAD36761; AAD36761; TM_1694. DR GeneID; 897892; -. DR KEGG; tma:TM1694; -. DR KEGG; tmi:THEMA_05770; -. DR PATRIC; 23938362; VBITheMar51294_1711. DR eggNOG; ENOG4105D8I; Bacteria. DR eggNOG; COG0301; LUCA. DR InParanoid; Q9X220; -. DR KO; K03151; -. DR OMA; PDEDCCT; -. DR OrthoDB; EOG6TBHGR; -. DR BioCyc; TMAR243274:GC6P-1742-MONOMER; -. DR BRENDA; 2.8.1.B3; 6331. DR UniPathway; UPA00060; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00021; ThiI; 1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR020536; ThiI_AANH. DR InterPro; IPR004114; THUMP_dom. DR InterPro; IPR003720; tRNA_STrfase. DR Pfam; PF02568; ThiI; 1. DR Pfam; PF02926; THUMP; 1. DR SMART; SM00981; THUMP; 1. DR TIGRFAMs; TIGR00342; TIGR00342; 1. DR PROSITE; PS51165; THUMP; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome; RNA-binding; KW Thiamine biosynthesis; Transferase; tRNA-binding. FT CHAIN 1 388 Probable tRNA sulfurtransferase. FT /FTId=PRO_0000154880. FT DOMAIN 55 162 THUMP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT NP_BIND 180 181 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT NP_BIND 205 206 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 264 264 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 286 286 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 295 295 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT STRAND 4 10 {ECO:0000244|PDB:4KR6}. FT HELIX 12 14 {ECO:0000244|PDB:4KR6}. FT HELIX 21 36 {ECO:0000244|PDB:4KR6}. FT STRAND 41 43 {ECO:0000244|PDB:4KR6}. FT STRAND 46 50 {ECO:0000244|PDB:4KR6}. FT HELIX 58 61 {ECO:0000244|PDB:4KR6}. FT STRAND 69 76 {ECO:0000244|PDB:4KR6}. FT HELIX 80 95 {ECO:0000244|PDB:4KR6}. FT STRAND 102 111 {ECO:0000244|PDB:4KR6}. FT STRAND 114 116 {ECO:0000244|PDB:4KR7}. FT HELIX 118 132 {ECO:0000244|PDB:4KR6}. FT STRAND 140 142 {ECO:0000244|PDB:4KR6}. FT STRAND 144 152 {ECO:0000244|PDB:4KR6}. FT STRAND 155 162 {ECO:0000244|PDB:4KR6}. FT STRAND 176 180 {ECO:0000244|PDB:4KR6}. FT STRAND 183 185 {ECO:0000244|PDB:4KR6}. FT HELIX 186 196 {ECO:0000244|PDB:4KR6}. FT STRAND 200 207 {ECO:0000244|PDB:4KR6}. FT TURN 209 211 {ECO:0000244|PDB:4KR6}. FT HELIX 216 227 {ECO:0000244|PDB:4KR6}. FT HELIX 228 230 {ECO:0000244|PDB:4KR6}. FT TURN 231 233 {ECO:0000244|PDB:4KR7}. FT STRAND 236 242 {ECO:0000244|PDB:4KR6}. FT HELIX 244 253 {ECO:0000244|PDB:4KR6}. FT HELIX 256 258 {ECO:0000244|PDB:4KR6}. FT HELIX 259 278 {ECO:0000244|PDB:4KR6}. FT STRAND 282 284 {ECO:0000244|PDB:4KR7}. FT STRAND 289 292 {ECO:0000244|PDB:4KR7}. FT HELIX 293 295 {ECO:0000244|PDB:4KR6}. FT HELIX 297 304 {ECO:0000244|PDB:4KR6}. FT TURN 314 317 {ECO:0000244|PDB:4KR6}. FT HELIX 320 329 {ECO:0000244|PDB:4KR6}. FT TURN 333 335 {ECO:0000244|PDB:4KR6}. FT STRAND 346 348 {ECO:0000244|PDB:4KR6}. FT HELIX 358 364 {ECO:0000244|PDB:4KR6}. FT HELIX 365 367 {ECO:0000244|PDB:4KR6}. FT HELIX 371 380 {ECO:0000244|PDB:4KR6}. FT STRAND 383 387 {ECO:0000244|PDB:4KR6}. SQ SEQUENCE 388 AA; 44126 MW; D8BE03E3EFEEB856 CRC64; MKELRVYIVR YSEIGLKGKN RKDFEEALRR NIERVTGMKV KRQWGRFLIP IDENVTLDDK LKKIFGIQNF SKGFLVSHDF EEVKKYSLIA VKEKLEKGNY RTFKVQAKKA YKEYKKGVYE INSELGALIL KNFKELSVDV RNPDFVLGVE VRPEGVLIFT DRVECYGGLP VGTGGKAVLL LSGGIDSPVA GWYALKRGVL IESVTFVSPP FTSEGAVEKV RDILRVLREF SGGHPLRLHI VNLTKLQLEV KKRVPDKYSL IMYRRSMFRI AEKIAEETGA VAFYTGENIG QVASQTLENL WSIESVTTRP VIRPLSGFDK TEIVEKAKEI GTYEISIKPY QDSCVFFAPK NPATRSHPSI LEKLEQQVPD LPVLEEEAFT SRKVEVIE // ID THYX_THEMA Reviewed; 220 AA. AC Q9WYT0; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 114. DE RecName: Full=Thymidylate synthase ThyX; DE Short=TS; DE Short=TSase; DE EC=2.1.1.148; GN Name=thyX; Synonyms=thy1; OrderedLocusNames=TM_0449; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). RX PubMed=12211025; DOI=10.1002/prot.10202; RA Kuhn P., Lesley S.A., Mathews I.I., Canaves J.M., Brinen L.S., Dai X., RA Deacon A.M., Elsliger M.-A., Eshaghi S., Floyd R., Godzik A., RA Grittini C., Grzechnik S.K., Guda C., Hodgson K.O., Jaroszewski L., RA Karlak C., Klock H.E., Koesema E., Kovarik J.M., Kreusch A.T., RA McMullan D., McPhillips T.M., Miller M.A., Miller M., Morse A., RA Moy K., Ouyang J., Robb A., Rodrigues K., Selby T.L., Spraggon G., RA Stevens R.C., Taylor S.S., van den Bedem H., Velasquez J., Vincent J., RA Wang X., West B., Wolf G., Wooley J., Wilson I.A.; RT "Crystal structure of thy1, a thymidylate synthase complementing RT protein from Thermotoga maritima at 2.25 A resolution."; RL Proteins 49:142-145(2002). CC -!- FUNCTION: Catalyzes the formation of dTMP and tetrahydrofolate CC from dUMP and methylenetetrahydrofolate. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP + NADPH CC = dTMP + tetrahydrofolate + NADP(+). CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Note=Binds 1 FAD per subunit.; CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the thymidylate synthase ThyX family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thyX (flavin-dependent thymidylate CC synthase) domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35532.1; -; Genomic_DNA. DR PIR; B72375; B72375. DR RefSeq; NP_228259.1; NC_000853.1. DR RefSeq; WP_004081517.1; NZ_CP011107.1. DR PDB; 1KQ4; X-ray; 2.25 A; A/B/C/D=1-220. DR PDB; 1O24; X-ray; 2.00 A; A/B/C/D=1-220. DR PDB; 1O25; X-ray; 2.40 A; A/B/C/D=1-220. DR PDB; 1O26; X-ray; 1.60 A; A/B/C/D=1-220. DR PDB; 1O27; X-ray; 2.30 A; A/B/C/D=1-220. DR PDB; 1O28; X-ray; 2.10 A; A/B/C/D=1-220. DR PDB; 1O29; X-ray; 2.00 A; A/B/C/D=1-220. DR PDB; 1O2A; X-ray; 1.80 A; A/B/C/D=1-220. DR PDB; 1O2B; X-ray; 2.45 A; A/B/C/D=1-220. DR PDB; 3G4A; X-ray; 1.95 A; A/B/C/D=1-220. DR PDB; 3G4C; X-ray; 2.05 A; A/B/C/D=1-220. DR PDB; 3N0B; X-ray; 2.30 A; A/B/C/D=1-220. DR PDB; 3N0C; X-ray; 2.30 A; A/B/C/D=1-220. DR PDB; 4GT9; X-ray; 1.39 A; A=1-220. DR PDB; 4GTA; X-ray; 1.50 A; A=1-220. DR PDB; 4GTB; X-ray; 1.70 A; A=1-220. DR PDB; 4GTC; X-ray; 1.97 A; A/B/C/D=1-220. DR PDB; 4GTD; X-ray; 1.76 A; A/B/C/D=1-220. DR PDB; 4GTE; X-ray; 1.89 A; A/B/C/D=1-220. DR PDB; 4GTF; X-ray; 1.77 A; A=1-220. DR PDB; 4GTL; X-ray; 2.17 A; A/B/C/D=1-220. DR PDB; 4KAR; X-ray; 2.03 A; A/B/C/D=1-220. DR PDB; 4KAS; X-ray; 1.85 A; A/B/C/D=1-220. DR PDB; 4KAT; X-ray; 2.14 A; A/B/C/D=1-220. DR PDBsum; 1KQ4; -. DR PDBsum; 1O24; -. DR PDBsum; 1O25; -. DR PDBsum; 1O26; -. DR PDBsum; 1O27; -. DR PDBsum; 1O28; -. DR PDBsum; 1O29; -. DR PDBsum; 1O2A; -. DR PDBsum; 1O2B; -. DR PDBsum; 3G4A; -. DR PDBsum; 3G4C; -. DR PDBsum; 3N0B; -. DR PDBsum; 3N0C; -. DR PDBsum; 4GT9; -. DR PDBsum; 4GTA; -. DR PDBsum; 4GTB; -. DR PDBsum; 4GTC; -. DR PDBsum; 4GTD; -. DR PDBsum; 4GTE; -. DR PDBsum; 4GTF; -. DR PDBsum; 4GTL; -. DR PDBsum; 4KAR; -. DR PDBsum; 4KAS; -. DR PDBsum; 4KAT; -. DR ProteinModelPortal; Q9WYT0; -. DR SMR; Q9WYT0; 1-220. DR DIP; DIP-60076N; -. DR STRING; 243274.TM0449; -. DR DrugBank; DB03147; Flavin adenine dinucleotide. DR EnsemblBacteria; AAD35532; AAD35532; TM_0449. DR GeneID; 897468; -. DR KEGG; tma:TM0449; -. DR PATRIC; 23935783; VBITheMar51294_0455. DR eggNOG; ENOG41087GE; Bacteria. DR eggNOG; COG1351; LUCA. DR InParanoid; Q9WYT0; -. DR KO; K03465; -. DR OMA; DAHAQYE; -. DR OrthoDB; EOG661H77; -. DR BioCyc; MetaCyc:MONOMER-15758; -. DR BRENDA; 2.1.1.148; 2604. DR SABIO-RK; Q9WYT0; -. DR EvolutionaryTrace; Q9WYT0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0050797; F:thymidylate synthase (FAD) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01408; ThyX; 1. DR InterPro; IPR003669; Thymidylate_synthase_ThyX. DR Pfam; PF02511; Thy1; 1. DR SUPFAM; SSF69796; SSF69796; 1. DR TIGRFAMs; TIGR02170; thyX; 1. DR PROSITE; PS51331; THYX; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; FAD; Flavoprotein; Methyltransferase; KW NADP; Nucleotide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 220 Thymidylate synthase ThyX. FT /FTId=PRO_0000175579. FT DOMAIN 1 208 ThyX. FT MOTIF 78 88 ThyX motif. FT STRAND 2 5 {ECO:0000244|PDB:4GT9}. FT TURN 6 8 {ECO:0000244|PDB:4GT9}. FT STRAND 9 17 {ECO:0000244|PDB:4GT9}. FT HELIX 20 28 {ECO:0000244|PDB:4GT9}. FT HELIX 29 31 {ECO:0000244|PDB:1O26}. FT HELIX 39 51 {ECO:0000244|PDB:4GT9}. FT HELIX 55 59 {ECO:0000244|PDB:4GT9}. FT STRAND 61 69 {ECO:0000244|PDB:4GT9}. FT HELIX 70 76 {ECO:0000244|PDB:4GT9}. FT STRAND 81 86 {ECO:0000244|PDB:4GT9}. FT TURN 89 91 {ECO:0000244|PDB:4GT9}. FT HELIX 103 106 {ECO:0000244|PDB:4GT9}. FT HELIX 115 138 {ECO:0000244|PDB:4GT9}. FT HELIX 143 146 {ECO:0000244|PDB:4GT9}. FT HELIX 147 149 {ECO:0000244|PDB:4GT9}. FT STRAND 154 163 {ECO:0000244|PDB:4GT9}. FT HELIX 164 174 {ECO:0000244|PDB:4GT9}. FT HELIX 181 197 {ECO:0000244|PDB:4GT9}. FT HELIX 199 208 {ECO:0000244|PDB:4GT9}. FT HELIX 214 216 {ECO:0000244|PDB:1O26}. SQ SEQUENCE 220 AA; 26004 MW; E3B9712014185907 CRC64; MKIDILDKGF VELVDVMGND LSAVRAARVS FDMGLKDEER DRHLIEYLMK HGHETPFEHI VFTFHVKAPI FVARQWFRHR IASYNELSGR YSKLSYEFYI PSPERLEGYK TTIPPERVTE KISEIVDKAY RTYLELIESG VPREVARIVL PLNLYTRFFW TVNARSLMNF LNLRADSHAQ WEIQQYALAI ARIFKEKCPW TFEAFLKYAY KGDILKEVQV // ID THIDN_THEMA Reviewed; 398 AA. AC Q9WZP7; DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=Bifunctional thiamine biosynthesis protein ThiDN; DE Includes: DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; DE EC=2.7.1.49 {ECO:0000250|UniProtKB:P76422}; DE EC=2.7.4.7 {ECO:0000250|UniProtKB:P76422}; DE AltName: Full=Hydroxymethylpyrimidine kinase; DE Short=HMP kinase; DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase; DE Short=HMP-P kinase; DE Short=HMP-phosphate kinase; DE Short=HMPP kinase; DE Includes: DE RecName: Full=Thiamine-phosphate synthase ThiN; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3 {ECO:0000269|PubMed:12794638}; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiDN; OrderedLocusNames=TM_0790; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION AS A THIAMINE-PHOSPHATE SYNTHASE VIA ITS C-TERMINAL DOMAIN, RP AND CATALYTIC ACTIVITY. RX PubMed=12794638; DOI=10.1038/nbt834; RA Morett E., Korbel J.O., Rajan E., Saab-Rincon G., Olvera L., RA Olvera M., Schmidt S., Snel B., Bork P.; RT "Systematic discovery of analogous enzymes in thiamin biosynthesis."; RL Nat. Biotechnol. 21:790-795(2003). CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. CC {ECO:0000250|UniProtKB:P76422}. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). CC {ECO:0000269|PubMed:12794638}. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-5-hydroxymethyl-2- CC methylpyrimidine = ADP + 4-amino-2-methyl-5- CC (phosphomethyl)pyrimidine. {ECO:0000250|UniProtKB:P76422}. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-2-methyl-5- CC (phosphomethyl)pyrimidine = ADP + 4-amino-2-methyl-5- CC (diphosphomethyl)pyrimidine. {ECO:0000250|UniProtKB:P76422}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate CC = diphosphate + thiamine phosphate + CO(2). CC {ECO:0000269|PubMed:12794638}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate + CC thiamine phosphate + CO(2). {ECO:0000269|PubMed:12794638}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine CC phosphate. {ECO:0000269|PubMed:12794638}. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: In the N-terminal section; belongs to the ThiD family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the ThiN family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35872.1; -; Genomic_DNA. DR PIR; G72333; G72333. DR RefSeq; NP_228599.1; NC_000853.1. DR RefSeq; WP_004080887.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZP7; -. DR STRING; 243274.TM0790; -. DR DNASU; 898458; -. DR EnsemblBacteria; AAD35872; AAD35872; TM_0790. DR GeneID; 898458; -. DR KEGG; tma:TM0790; -. DR PATRIC; 23936500; VBITheMar51294_0802. DR eggNOG; ENOG4107ZCS; Bacteria. DR eggNOG; COG0351; LUCA. DR eggNOG; COG1992; LUCA. DR InParanoid; Q9WZP7; -. DR KO; K00941; -. DR OMA; EGATIPW; -. DR OrthoDB; EOG6HMXB7; -. DR BioCyc; TMAR243274:GC6P-817-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1190.20; -; 1. DR Gene3D; 3.40.225.10; -; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR013749; PM/HMP-P_kinase-1. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR019293; ThiN. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF10120; ThiP_synth; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR SUPFAM; SSF53639; SSF53639; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Kinase; Multifunctional enzyme; KW Nucleotide-binding; Reference proteome; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 398 Bifunctional thiamine biosynthesis FT protein ThiDN. FT /FTId=PRO_0000415381. FT REGION 1 216 Hydroxymethylpyrimidine/ FT phosphomethylpyrimidine kinase. FT REGION 217 398 Thiamine-phosphate synthase. FT BINDING 40 40 Hydroxymethylpyrimidine/ FT phosphomethylpyrimidine. {ECO:0000250}. SQ SEQUENCE 398 AA; 45392 MW; DCE6977F471BF649 CRC64; MVLVVAGFDP SGGAGIIQDV KVLSALGVKT HAVISALTVQ NENRVFSVNF RDWEEMRKEI EVLTPPRVIK VGLSAPETVK RLREMFPDSA IVWNVVLESS SGFGFQDPEE VKKFVEYADY VILNSEEAKK LGEYNNFIVT GGHEKGNTVK VKYRDFVFEI PRVPGEFHGT GCAFSSAVSG FLAMSYPVEE AIRSAMELLK KILERSSGVV ETEKLLRDWY RYDTLNTLDE ILPEFLEIGH LTVPEVGQNV SYALPWAKNE FEVGKFPGRI RLKEGKAVAV SCASFKDRSH TARMAVTMMR YHPHMRCVVN VRYEREYVER AKKRGLKVFH YDRSKEPKEV QEKEGQSMVW MIEQAIAELK SPPDVIYDEG WWGKEAMIRV FGRNPKEVLE KIKLMVRE // ID THPR_THEMA Reviewed; 187 AA. AC Q9X2H4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=RNA 2',3'-cyclic phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_01940}; DE Short=RNA 2',3'-CPDase {ECO:0000255|HAMAP-Rule:MF_01940}; DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_01940}; GN OrderedLocusNames=TM_1860; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'- CC phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_01940}. CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. ThpR CC family. {ECO:0000255|HAMAP-Rule:MF_01940}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36922.1; -; Genomic_DNA. DR PIR; E72201; E72201. DR RefSeq; NP_229656.1; NC_000853.1. DR RefSeq; WP_004082411.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2H4; -. DR STRING; 243274.TM1860; -. DR EnsemblBacteria; AAD36922; AAD36922; TM_1860. DR GeneID; 897804; -. DR KEGG; tma:TM1860; -. DR PATRIC; 23938709; VBITheMar51294_1881. DR eggNOG; ENOG41081HM; Bacteria. DR eggNOG; COG1514; LUCA. DR InParanoid; Q9X2H4; -. DR KO; K01975; -. DR OMA; IGVFPNP; -. DR OrthoDB; EOG632D2K; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IEA:InterPro. DR GO; GO:0008664; F:2'-5'-RNA ligase activity; IEA:InterPro. DR Gene3D; 3.90.1140.10; -; 1. DR HAMAP; MF_01940; RNA_CPDase; 1. DR InterPro; IPR004175; RNA_CPDase. DR InterPro; IPR009097; RNA_ligase/cNuc_Pdiesterase. DR SUPFAM; SSF55144; SSF55144; 1. DR TIGRFAMs; TIGR02258; 2_5_ligase; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 187 RNA 2',3'-cyclic phosphodiesterase. FT /FTId=PRO_0000138969. FT MOTIF 40 43 HXTX 1. {ECO:0000255|HAMAP- FT Rule:MF_01940}. FT MOTIF 125 128 HXTX 2. {ECO:0000255|HAMAP- FT Rule:MF_01940}. FT ACT_SITE 40 40 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01940}. FT ACT_SITE 125 125 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01940}. SQ SEQUENCE 187 AA; 22065 MW; 912D041454F0C921 CRC64; MRTFIAIDVN EEVKKQASEI IEKLMKRGFG ATWVSEENMH LTLFFLGEVD EQKISEIAEH LCRRVRGFPS FSFTVKGFGY FKRKMSPRVF WLGVENTDRL MKLYEELRNE LSHHGFSFEE KFVPHITIGR VKYYPDKWEK LIEDIDFPPI EVAVDRFKIY SSTLTPTGPI YKVLYECQFE GGLIRYA // ID TOP1_THEMA Reviewed; 633 AA. AC P46799; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 134. DE RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952}; DE EC=5.99.1.2 {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=Omega-protein; DE AltName: Full=Relaxing enzyme; DE AltName: Full=Swivelase; DE AltName: Full=Untwisting enzyme; GN Name=topA {ECO:0000255|HAMAP-Rule:MF_00952}; GN OrderedLocusNames=TM_0258; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8547314; RA Bouthier de la Tour C., Kaltoum H., Portemer C., Confalonieri F., RA Huber R., Duguet M.; RT "Cloning and sequencing of the gene coding for topoisomerase I from RT the extremely thermophilic eubacterium, Thermotoga maritima."; RL Biochim. Biophys. Acta 1264:279-283(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3-633, AND DISULFIDE BOND. RX PubMed=16600296; DOI=10.1016/j.jmb.2006.03.012; RA Hansen G., Harrenga A., Wieland B., Schomburg D., Reinemer P.; RT "Crystal structure of full length topoisomerase I from Thermotoga RT maritima."; RL J. Mol. Biol. 358:1328-1340(2006). CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, CC which is introduced during the DNA replication and transcription, CC by transiently cleaving and rejoining one strand of the DNA CC duplex. Introduces a single-strand break via transesterification CC at a target site in duplex DNA. The scissile phosphodiester is CC attacked by the catalytic tyrosine of the enzyme, resulting in the CC formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the CC expulsion of a 3'-OH DNA strand. The free DNA strand then CC undergoes passage around the unbroken strand, thus removing DNA CC supercoils. Finally, in the religation step, the DNA 3'-OH attacks CC the covalent intermediate to expel the active-site tyrosine and CC restore the DNA phosphodiester backbone. {ECO:0000255|HAMAP- CC Rule:MF_00952}. CC -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded CC DNA, followed by passage and rejoining. {ECO:0000255|HAMAP- CC Rule:MF_00952}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00952}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00952}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00952}. CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00952}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00952}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U27841; AAA68949.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35346.1; -; Genomic_DNA. DR PIR; S62737; S62737. DR RefSeq; NP_228071.1; NC_000853.1. DR RefSeq; WP_004082962.1; NZ_CP011107.1. DR PDB; 2GAI; X-ray; 1.70 A; A/B=3-633. DR PDB; 2GAJ; X-ray; 1.95 A; A/B=3-633. DR PDBsum; 2GAI; -. DR PDBsum; 2GAJ; -. DR ProteinModelPortal; P46799; -. DR SMR; P46799; 7-601. DR STRING; 243274.TM0258; -. DR EnsemblBacteria; AAD35346; AAD35346; TM_0258. DR GeneID; 897168; -. DR KEGG; tma:TM0258; -. DR PATRIC; 23935393; VBITheMar51294_0262. DR eggNOG; ENOG4105C73; Bacteria. DR eggNOG; COG0550; LUCA. DR eggNOG; COG0551; LUCA. DR InParanoid; P46799; -. DR KO; K03168; -. DR OMA; WHISEEL; -. DR OrthoDB; EOG6S7XQ9; -. DR BRENDA; 5.99.1.2; 6331. DR EvolutionaryTrace; P46799; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.460.10; -; 2. DR Gene3D; 2.70.20.10; -; 2. DR Gene3D; 3.40.50.140; -; 1. DR HAMAP; MF_00952; Topoisom_1_prok; 1. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR023406; Topo_IA_AS. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. DR InterPro; IPR013825; Topo_IA_cen_sub2. DR InterPro; IPR023405; Topo_IA_core_domain. DR InterPro; IPR003602; Topo_IA_DNA-bd_dom. DR InterPro; IPR005733; TopoI_bac-type. DR InterPro; IPR028612; Topoisom_1_IA. DR InterPro; IPR006171; Toprim_domain. DR PANTHER; PTHR11390; PTHR11390; 1. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF56712; SSF56712; 1. DR TIGRFAMs; TIGR01051; topA_bact; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; DNA-binding; KW Isomerase; Magnesium; Metal-binding; Reference proteome; KW Topoisomerase; Zinc; Zinc-finger. FT CHAIN 1 633 DNA topoisomerase 1. FT /FTId=PRO_0000145169. FT DOMAIN 6 115 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT ZN_FING 559 580 C4-type. FT REGION 164 169 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT ACT_SITE 288 288 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 12 12 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 84 84 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 84 84 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT METAL 86 86 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 36 36 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 140 140 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 141 141 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 144 144 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 149 149 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 156 156 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 290 290 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 475 475 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT DISULFID 559 578 {ECO:0000269|PubMed:16600296}. FT DISULFID 561 580 {ECO:0000269|PubMed:16600296}. FT STRAND 8 12 {ECO:0000244|PDB:2GAI}. FT HELIX 14 24 {ECO:0000244|PDB:2GAI}. FT HELIX 25 27 {ECO:0000244|PDB:2GAI}. FT STRAND 28 32 {ECO:0000244|PDB:2GAI}. FT STRAND 37 40 {ECO:0000244|PDB:2GAI}. FT STRAND 42 44 {ECO:0000244|PDB:2GAI}. FT STRAND 51 55 {ECO:0000244|PDB:2GAI}. FT HELIX 64 76 {ECO:0000244|PDB:2GAI}. FT STRAND 79 81 {ECO:0000244|PDB:2GAI}. FT HELIX 87 99 {ECO:0000244|PDB:2GAI}. FT HELIX 116 124 {ECO:0000244|PDB:2GAI}. FT HELIX 131 159 {ECO:0000244|PDB:2GAI}. FT HELIX 166 185 {ECO:0000244|PDB:2GAI}. FT STRAND 190 198 {ECO:0000244|PDB:2GAI}. FT STRAND 201 205 {ECO:0000244|PDB:2GAI}. FT HELIX 215 222 {ECO:0000244|PDB:2GAI}. FT STRAND 227 239 {ECO:0000244|PDB:2GAI}. FT HELIX 247 258 {ECO:0000244|PDB:2GAI}. FT HELIX 262 274 {ECO:0000244|PDB:2GAI}. FT STRAND 279 283 {ECO:0000244|PDB:2GAI}. FT HELIX 298 311 {ECO:0000244|PDB:2GAI}. FT HELIX 314 316 {ECO:0000244|PDB:2GAI}. FT HELIX 346 349 {ECO:0000244|PDB:2GAI}. FT TURN 350 352 {ECO:0000244|PDB:2GAI}. FT HELIX 355 371 {ECO:0000244|PDB:2GAI}. FT STRAND 376 386 {ECO:0000244|PDB:2GAI}. FT STRAND 393 403 {ECO:0000244|PDB:2GAI}. FT HELIX 405 408 {ECO:0000244|PDB:2GAI}. FT STRAND 431 438 {ECO:0000244|PDB:2GAI}. FT HELIX 447 456 {ECO:0000244|PDB:2GAI}. FT TURN 462 464 {ECO:0000244|PDB:2GAI}. FT HELIX 465 474 {ECO:0000244|PDB:2GAI}. FT STRAND 477 481 {ECO:0000244|PDB:2GAI}. FT STRAND 484 488 {ECO:0000244|PDB:2GAI}. FT HELIX 489 501 {ECO:0000244|PDB:2GAI}. FT TURN 503 506 {ECO:0000244|PDB:2GAI}. FT HELIX 508 522 {ECO:0000244|PDB:2GAI}. FT HELIX 528 540 {ECO:0000244|PDB:2GAI}. FT STRAND 553 558 {ECO:0000244|PDB:2GAI}. FT STRAND 560 562 {ECO:0000244|PDB:2GAJ}. FT STRAND 564 570 {ECO:0000244|PDB:2GAI}. FT STRAND 573 577 {ECO:0000244|PDB:2GAI}. FT STRAND 579 581 {ECO:0000244|PDB:2GAI}. FT STRAND 593 595 {ECO:0000244|PDB:2GAI}. FT STRAND 598 600 {ECO:0000244|PDB:2GAI}. SQ SEQUENCE 633 AA; 72695 MW; F7262A044060CFE9 CRC64; MSKKVKKYIV VESPAKAKTI KSILGNEYEV FASMGHIIDL PKSKFGVDLE KDFEPEFAVI KGKEKVVEKL KDLAKKGELL IASDMDREGE AIAWHIARVT NTLGRKNRIV FSEITPRVIR EAVKNPREID MKKVRAQLAR RILDRIVGYS LSPVLWRNFK SNLSAGRVQS ATLKLVCDRE REILRFVPKK YHRITVNFDG LTAEIDVKEK KFFDAETLKE IQSIDELVVE EKKVSVKKFA PPEPFKTSTL QQEAYSKLGF SVSKTMMIAQ QLYEGVETKD GHIAFITYMR TDSTRVSDYA KEEARNLITE VFGEEYVGSK RERRKSNAKI QDAHEAIRPT NVFMTPEEAG KYLNSDQKKL YELIWKRFLA SQMKPSQYEE TRFVLRTKDG KYRFKGTVLK KIFDGYEKVW KTERNTGEFP FEEGESVKPV VVKIEEQETK PKPRYTEGSL VKEMERLGIG RPSTYASTIK LLLNRGYIKK IRGYLYPTIV GSVVMDYLEK KYSDVVSVSF TAEMEKDLDE VEQGKKTDKI VLREFYESFS SVFDRNDRIV VDFPTNQKCS CGKEMRLSFG KYGFYLKCEC GKTRSVKNDE IAVIDDGKIF LGRKDSESGS PDGRSVEGKG NLSEKRRKGK KGS // ID TRMB_THEMA Reviewed; 313 AA. AC Q9X027; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_01057}; DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; GN Name=trmB {ECO:0000255|HAMAP-Rule:MF_01057}; GN OrderedLocusNames=TM_0925; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at CC position 46 (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_01057}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(46) in tRNA CC = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_01057}. CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01057}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. TrmB family. {ECO:0000255|HAMAP- CC Rule:MF_01057}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36006.1; -; Genomic_DNA. DR PIR; F72317; F72317. DR RefSeq; NP_228733.1; NC_000853.1. DR RefSeq; WP_004080637.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X027; -. DR STRING; 243274.TM0925; -. DR PRIDE; Q9X027; -. DR EnsemblBacteria; AAD36006; AAD36006; TM_0925. DR GeneID; 898599; -. DR KEGG; tma:TM0925; -. DR PATRIC; 23936781; VBITheMar51294_0939. DR eggNOG; ENOG4105CZ1; Bacteria. DR eggNOG; COG0220; LUCA. DR InParanoid; Q9X027; -. DR KO; K03439; -. DR OMA; TRYERKW; -. DR OrthoDB; EOG6K6VBC; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central. DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01057; tRNA_methyltr_TrmB; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb. DR Pfam; PF02390; Methyltransf_4; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00091; TIGR00091; 1. DR PROSITE; PS51625; SAM_MT_TRMB; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 313 tRNA (guanine-N(7)-)-methyltransferase. FT /FTId=PRO_0000171413. FT REGION 177 180 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01057}. FT BINDING 33 33 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 58 58 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 85 85 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 112 112 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01057}. FT BINDING 144 144 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01057}. SQ SEQUENCE 313 AA; 36770 MW; 34EE4D3669AD2CF3 CRC64; MVVTEYELKP QNFPRFPLDW SEIFGRKAKI VVEIGFGNGE FLAELARRHP EKDFVGFEVS ITSFVKAQKK FKRYNLKNVR LVKVDARFGL RELFPDNSVE KVYINFPCPW PKKRHESRRI TSYDFLQTLS AVLEMDGTVE FATDEEWYAR EVLDTFESSE YFVVDVFEEN FKRDVETRYE RKWKSQGKKT FLIVARKVKN GTVKRLMEGE NTMAHSVFEG NVTWEKLKEL EGKVFKDKNK IFVVKKVYRD GDYLLKVIST DEGGFQQVYY LNLSGRDGKW VLKLDEGSDP YRTPALKWSL RRIPEELTAQ GSP // ID TILS_THEMA Reviewed; 414 AA. AC Q9WZ48; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 104. DE RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000255|HAMAP-Rule:MF_01161}; DE EC=6.3.4.19 {ECO:0000255|HAMAP-Rule:MF_01161}; DE AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000255|HAMAP-Rule:MF_01161}; DE AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000255|HAMAP-Rule:MF_01161}; GN Name=tilS {ECO:0000255|HAMAP-Rule:MF_01161}; GN OrderedLocusNames=TM_0579; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Ligates lysine onto the cytidine present at position 34 CC of the AUA codon-specific tRNA(Ile) that contains the anticodon CC CAU, in an ATP-dependent manner. Cytidine is converted to CC lysidine, thus changing the amino acid specificity of the tRNA CC from methionine to isoleucine. {ECO:0000255|HAMAP-Rule:MF_01161}. CC -!- CATALYTIC ACTIVITY: (tRNA(Ile2))-cytidine(34) + L-lysine + ATP = CC (tRNA(Ile2))-lysidine(34) + AMP + diphosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01161}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01161}. CC -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS CC motif, predicted to be a P-loop motif involved in ATP binding. CC -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01161}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35664.1; -; Genomic_DNA. DR PIR; D72358; D72358. DR RefSeq; NP_228389.1; NC_000853.1. DR RefSeq; WP_010865151.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ48; -. DR STRING; 243274.TM0579; -. DR EnsemblBacteria; AAD35664; AAD35664; TM_0579. DR GeneID; 897648; -. DR KEGG; tma:TM0579; -. DR PATRIC; 23936069; VBITheMar51294_0588. DR eggNOG; ENOG4105D3U; Bacteria. DR eggNOG; COG0037; LUCA. DR InParanoid; Q9WZ48; -. DR KO; K04075; -. DR OMA; NIKCITR; -. DR OrthoDB; EOG693GNP; -. DR BioCyc; TMAR243274:GC6P-604-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-HAMAP. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01161; tRNA_Ile_lys_synt; 1. DR InterPro; IPR012796; Lysidine-tRNA-synth_C. DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR011063; TilS/TtcA_N. DR InterPro; IPR012094; tRNA_Ile_lys_synt. DR InterPro; IPR012795; tRNA_Ile_lys_synt_N. DR PANTHER; PTHR11807:SF2; PTHR11807:SF2; 1. DR Pfam; PF01171; ATP_bind_3; 1. DR Pfam; PF11734; TilS_C; 1. DR SMART; SM00977; TilS_C; 1. DR SUPFAM; SSF56037; SSF56037; 1. DR TIGRFAMs; TIGR02433; lysidine_TilS_C; 1. DR TIGRFAMs; TIGR02432; lysidine_TilS_N; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome; tRNA processing. FT CHAIN 1 414 tRNA(Ile)-lysidine synthase. FT /FTId=PRO_0000181791. FT NP_BIND 13 18 ATP. {ECO:0000255|HAMAP-Rule:MF_01161}. SQ SEQUENCE 414 AA; 48834 MW; 6ADE577F137D8423 CRC64; MLEEGEHVLV AVSGGIDSMT LLYVLRKFSP LLKIKITAAH LDHRIRESSR RDREFVERIC RQWNIPVETS EVDVPSLWKD SGKTLEEIAR EVRYDFLKRT AKKVGASKIA LAHHKNDLLE TVVHRLIRGT GPLGLACISP KREEFIRPFL VFKRSEIEEY ARKNNVPYVV DETNYNVKYT RNFIRHRIVP LMKELNPTVE DAVYRLVSVT HLLRNFVERT VQDFVERNVY FYKDYAVFVE PEDLFLFLEV TRWVLKEMYG RVPEYEKLIG TLKSKRVELW SGIFVERSFG YVAVGKTVFK KKYRVEVKGD MLEMEGFKIR VVNNRNDMKF WVRNRKEGDR IIVNGRERKL KDVFIEKKVP TFYRDRVPLL VDEEDRVLWV PGIARSDFLP EDVVVELLEY PVGYVKGGTY FEQV // ID TRMD_THEMA Reviewed; 245 AA. AC Q9X1Q5; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=tRNA (guanine-N(1)-)-methyltransferase; DE EC=2.1.1.228; DE AltName: Full=M1G-methyltransferase; DE AltName: Full=tRNA [GM37] methyltransferase; GN Name=trmD; OrderedLocusNames=TM_1569; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(37) in tRNA CC = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36636.1; -; Genomic_DNA. DR PIR; B72237; B72237. DR RefSeq; NP_229369.1; NC_000853.1. DR RefSeq; WP_004081985.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1Q5; -. DR STRING; 243274.TM1569; -. DR EnsemblBacteria; AAD36636; AAD36636; TM_1569. DR GeneID; 897961; -. DR KEGG; tma:TM1569; -. DR KEGG; tmi:THEMA_06435; -. DR KEGG; tmw:THMA_1604; -. DR PATRIC; 23938100; VBITheMar51294_1587. DR eggNOG; ENOG4105D6X; Bacteria. DR eggNOG; COG0336; LUCA. DR InParanoid; Q9X1Q5; -. DR KO; K00554; -. DR OMA; NRYDLYL; -. DR OrthoDB; EOG6J48RZ; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0030488; P:tRNA methylation; IBA:GOC. DR Gene3D; 1.10.1270.20; -; 1. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_00605; TrmD; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR002649; tRNA_m1G_MeTrfase_bac. DR InterPro; IPR023148; tRNA_m1G_MeTrfase_C. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10. DR Pfam; PF01746; tRNA_m1G_MT; 1. DR PIRSF; PIRSF000386; tRNA_mtase; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00088; trmD; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 245 tRNA (guanine-N(1)-)-methyltransferase. FT /FTId=PRO_0000060484. FT REGION 131 136 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 112 112 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000250}. SQ SEQUENCE 245 AA; 28493 MW; 6D3D2255526CE2D9 CRC64; MRITIVTIFP EMVEVIKKYG VIARAVERGI VEINVENLRD YTTDRHRTVD DYQYGGGYGM VMKPEPFFRF YESYVEKYGK PYVILTSPQG RIFNYKIAEE LSKKDDIVIF CGRYEGIDER VMSIVDDEIS IGDYILTGGE LPAMVITDAV VRLVPGVVER ESVERESFHQ GLLDHPVYTR PYEYKGMKVP DVLLSGDHEK VELWRRKESI KKTLAKRPDL FLAKELDEMD KLAIIELFRE LMEKC // ID TRPA_THEMA Reviewed; 239 AA. AC P50908; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-APR-2016, entry version 117. DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131}; DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131}; GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131}; GN OrderedLocusNames=TM_0137; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7556082; RA Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.; RT "(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the RT hyperthermophile Thermotoga maritima."; RL EMBO J. 14:4395-4402(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage CC of indoleglycerol phosphate to indole and glyceraldehyde 3- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3- CC phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. CC {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X92729; CAA63392.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35230.1; -; Genomic_DNA. DR PIR; S59050; S59050. DR RefSeq; NP_227952.1; NC_000853.1. DR RefSeq; WP_004082732.1; NZ_CP011107.1. DR ProteinModelPortal; P50908; -. DR STRING; 243274.TM0137; -. DR DNASU; 896967; -. DR EnsemblBacteria; AAD35230; AAD35230; TM_0137. DR GeneID; 896967; -. DR KEGG; tma:TM0137; -. DR PATRIC; 23935116; VBITheMar51294_0136. DR eggNOG; ENOG4105F6H; Bacteria. DR eggNOG; COG0159; LUCA. DR InParanoid; P50908; -. DR KO; K01695; -. DR OMA; PVFICPP; -. DR OrthoDB; EOG6RVG0K; -. DR BioCyc; MetaCyc:MONOMER-344; -. DR SABIO-RK; P50908; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00131; Trp_synth_alpha; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR InterPro; IPR018204; Trp_synthase_alpha_AS. DR InterPro; IPR002028; Trp_synthase_suA. DR Pfam; PF00290; Trp_syntA; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00262; trpA; 1. DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 239 Tryptophan synthase alpha chain. FT /FTId=PRO_0000098864. FT ACT_SITE 34 34 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00131}. FT ACT_SITE 45 45 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00131}. FT CONFLICT 189 189 F -> L (in Ref. 1; CAA63392). FT {ECO:0000305}. SQ SEQUENCE 239 AA; 26759 MW; F6B06FBCA83294FA CRC64; MKGFIAYIPA GFPDLETTRK ILIALNELGI TGVEIGVPFS DPVADGPVIQ LAHSVALRNG VTIKKILEML SEISVDYDLY LMSYLNPIVN YPEGKEKLLD ELKKLGVKGL IIPDLPLREV KNVDIAYPIV PFVAPNTKDE EIDLINSVQA PFVYYISRYG VTGEREDLPF ADHIKRVKER IKLPLFVGFG ISRHEQVKKV WEIADGVIVG SALVRIMEEN PKDEIPRKVV EKVKELLGK // ID TRPB1_THEMA Reviewed; 389 AA. AC P50909; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 13-APR-2016, entry version 119. DE RecName: Full=Tryptophan synthase beta chain 1; DE EC=4.2.1.20; GN Name=trpB1; Synonyms=trpB; OrderedLocusNames=TM_0138; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7556082; RA Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.; RT "(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the RT hyperthermophile Thermotoga maritima."; RL EMBO J. 14:4395-4402(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L- CC tryptophan from indole and L-serine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3- CC phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X92729; CAA63391.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35231.1; -; Genomic_DNA. DR PIR; S59049; S59049. DR RefSeq; NP_227953.1; NC_000853.1. DR RefSeq; WP_004082734.1; NZ_CP011107.1. DR ProteinModelPortal; P50909; -. DR SMR; P50909; 4-379. DR STRING; 243274.TM0138; -. DR EnsemblBacteria; AAD35231; AAD35231; TM_0138. DR GeneID; 896968; -. DR KEGG; tma:TM0138; -. DR PATRIC; 23935118; VBITheMar51294_0137. DR eggNOG; ENOG4105CG0; Bacteria. DR eggNOG; COG0133; LUCA. DR InParanoid; P50909; -. DR KO; K01696; -. DR OMA; IPEMLYP; -. DR OrthoDB; EOG6GFGH7; -. DR BioCyc; MetaCyc:MONOMER-345; -. DR SABIO-RK; P50909; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central. DR HAMAP; MF_00133; Trp_synth_beta; 1. DR InterPro; IPR006653; Trp_synth_b_CS. DR InterPro; IPR006654; Trp_synth_beta. DR InterPro; IPR023026; Trp_synth_beta/beta-like. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR PANTHER; PTHR10314:SF3; PTHR10314:SF3; 1. DR Pfam; PF00291; PALP; 1. DR PIRSF; PIRSF001413; Trp_syn_beta; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR00263; trpB; 1. DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1 389 Tryptophan synthase beta chain 1. FT /FTId=PRO_0000099013. FT MOD_RES 83 83 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 389 AA; 42917 MW; 23AF62465A3E1CDE CRC64; MKGYFGPYGG QYVPEILMPA LEELEAAYEE IMKDESFWKE FNDLLRDYAG RPTPLYFARR LSEKYGARIY LKREDLLHTG AHKINNAIGQ VLLAKKMGKT RIIAETGAGQ HGVATATAAA LFGMECVIYM GEEDTIRQKP NVERMKLLGA KVVPVKSGSR TLKDAINEAL RDWITNLQTT YYVIGSVVGP HPYPIIVRNF QKVIGEETKK QILEKEGRLP DYIVACVGGG SNAAGIFYPF IDSGVKLIGV EAGGEGLETG KHAASLLKGK IGYLHGSKTF VLQDDWGQVQ VTHSVSAGLD YSGVGPEHAY WRETGKVLYD AVTDEEALDA FIELSRLEGI IPALESSHAL AYLKKINIKG KVVVVNLSGR GDKDLESVLN HPYVRERIR // ID TRMFO_THEMA Reviewed; 435 AA. AC Q9WZJ3; DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO {ECO:0000255|HAMAP-Rule:MF_01037}; DE EC=2.1.1.74 {ECO:0000255|HAMAP-Rule:MF_01037}; DE AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01037}; DE AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01037}; GN Name=trmFO {ECO:0000255|HAMAP-Rule:MF_01037}; Synonyms=gid; GN OrderedLocusNames=TM_0734; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP CRYSTALLIZATION. RX PubMed=18323606; DOI=10.1107/S1744309108003825; RA Cicmil N.; RT "Crystallization and preliminary X-ray crystallographic RT characterization of TrmFO, a folate-dependent tRNA methyltransferase RT from Thermotoga maritima."; RL Acta Crystallogr. F 64:193-195(2008). CC -!- FUNCTION: Catalyzes the folate-dependent formation of 5-methyl- CC uridine at position 54 (M-5-U54) in all tRNAs. {ECO:0000255|HAMAP- CC Rule:MF_01037}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + uracil(54) in CC tRNA + FADH(2) = tetrahydrofolate + 5-methyluracil(54) in tRNA + CC FAD. {ECO:0000255|HAMAP-Rule:MF_01037}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01037}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01037}. CC -!- SIMILARITY: Belongs to the MnmG family. TrmFO subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01037}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35815.1; -; Genomic_DNA. DR PIR; A72339; A72339. DR RefSeq; NP_228543.1; NC_000853.1. DR RefSeq; WP_004080992.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZJ3; -. DR STRING; 243274.TM0734; -. DR EnsemblBacteria; AAD35815; AAD35815; TM_0734. DR GeneID; 898401; -. DR KEGG; tma:TM0734; -. DR PATRIC; 23936388; VBITheMar51294_0747. DR eggNOG; ENOG4107QXI; Bacteria. DR eggNOG; COG1206; LUCA. DR InParanoid; Q9WZJ3; -. DR KO; K04094; -. DR OMA; DYLNCPM; -. DR OrthoDB; EOG6J74VT; -. DR BRENDA; 2.1.1.74; 6331. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030698; F:5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:UniProtKB-EC. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 4. DR HAMAP; MF_01037; TrmFO; 1. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR002218; MnmG-rel. DR InterPro; IPR004417; TrmFO. DR Pfam; PF01134; GIDA; 1. DR SUPFAM; SSF51905; SSF51905; 1. DR TIGRFAMs; TIGR00137; gid_trmFO; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase; KW Reference proteome; Transferase; tRNA processing. FT CHAIN 1 435 Methylenetetrahydrofolate--tRNA-(uracil- FT 5-)-methyltransferase TrmFO. FT /FTId=PRO_0000117284. FT NP_BIND 7 12 FAD. {ECO:0000255|HAMAP-Rule:MF_01037}. SQ SEQUENCE 435 AA; 49689 MW; 768BFBAB0C97D57F CRC64; MIVNVIGAGL AGSEVAYNLG KRGIRVRLFE MRPKKMTEVH KTGYFAELVC SNSLKSEDIT NAEGLLKAEM RLMGSITLEA AEKARVPSGK ALAVDRNIFA KEVTEVIERL ESVEIIREEV TEFDPEEGIW VVATGPATSD GLLPFLKKLL GDDLLFFFDA VSPIVTFESI DMECAFWGDR FGKGKDYINC PLTKEEYEEF WKALVEAEVI EMEDFDRKLL FERCQPIEEI ARSGKDALRY GPLRPTGLVD PRTGKEPYAV VQLRREDKEG RFYSLVGFQT RLKWSEQKRV LRKIPCLRNA EIVRYGVMHR NVYINSPKLL DIFFRLKKHP NIFFAGQITG VEGYMESAAS GIYVAYNVHR ILKGLSPLKL PEETMMGALF SYIIEKVEGD LKPMYANFGL LPPLKVRVKD KFEKRKKLAE RAIETMKKFL EENPW // ID TRPB2_THEMA Reviewed; 422 AA. AC Q9WZ09; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Tryptophan synthase beta chain 2; DE EC=4.2.1.20; GN Name=trpB2; OrderedLocusNames=TM_0539; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L- CC tryptophan from indole and L-serine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3- CC phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35624.1; -; Genomic_DNA. DR PIR; H72363; H72363. DR RefSeq; NP_228349.1; NC_000853.1. DR RefSeq; WP_004081366.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ09; -. DR STRING; 243274.TM0539; -. DR EnsemblBacteria; AAD35624; AAD35624; TM_0539. DR GeneID; 897593; -. DR KEGG; tma:TM0539; -. DR PATRIC; 23935985; VBITheMar51294_0547. DR eggNOG; ENOG4108JEB; Bacteria. DR eggNOG; COG1350; LUCA. DR InParanoid; Q9WZ09; -. DR KO; K06001; -. DR OMA; NHVMLHQ; -. DR OrthoDB; EOG6RVFW8; -. DR BioCyc; MetaCyc:MONOMER-3543; -. DR SABIO-RK; Q9WZ09; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0052684; F:L-serine hydro-lyase (adding indole, L-tryptophan-forming) activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR HAMAP; MF_00133; Trp_synth_beta; 1. DR InterPro; IPR006316; Trp_synth_b-like. DR InterPro; IPR006653; Trp_synth_b_CS. DR InterPro; IPR023026; Trp_synth_beta/beta-like. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR PANTHER; PTHR10314:SF21; PTHR10314:SF21; 2. DR Pfam; PF00291; PALP; 1. DR PIRSF; PIRSF001413; Trp_syn_beta; 1. DR PIRSF; PIRSF500824; TrpB_prok; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR01415; trpB_rel; 1. DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1 422 Tryptophan synthase beta chain 2. FT /FTId=PRO_0000099014. FT MOD_RES 111 111 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 422 AA; 46387 MW; 1A32AE27E22B5A8D CRC64; MRIVVNLKPE EIPKHWYNVL ADLPFKLDPP LDPETKQPIS PEKLSVIFPM SLIEQEVSEE RFIEIPEPVL KEYAVYRPTP LIRATFLEEY LQTPARIYYK YEGVSPTGSH KPNTAIAQAY YNKIEGVKRL VTETGAGQWG SALSYAGAKF GLEVKVFMVK VSYQQKPMRK YMMNLFGGKV TPSPSEETNF GRKILSEDPD NPGSLGIAIS EALEVAVSDP NTKYSLGSVL NHVLLHQTVI GLEIKKQLEL IGEKPDILLG CHGGGSNFGG TILPFVPDKL SGRDIRFVAC EPAACPSLTK GNYDYDFGDT AGLTPLLKMY TLGKDFIPPK IHAGGLRYHG SAPIIARLVK EGLVEAQAFD QDETFEAAKI FAKLEGIIPA PESAHAIAGA IREAKKAKEE GKERVIVFTL SGHGLLDLTA YV // ID TRPC_THEMA Reviewed; 252 AA. AC Q56319; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 3. DT 13-APR-2016, entry version 117. DE RecName: Full=Indole-3-glycerol phosphate synthase; DE Short=IGPS; DE EC=4.1.1.48; GN Name=trpC; OrderedLocusNames=TM_0140; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=7556082; RA Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.; RT "(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the RT hyperthermophile Thermotoga maritima."; RL EMBO J. 14:4395-4402(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5- CC phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 4/5. CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35233.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X92729; CAA63389.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35233.1; ALT_INIT; Genomic_DNA. DR PIR; S59047; S59047. DR RefSeq; NP_227955.1; NC_000853.1. DR PDB; 1I4N; X-ray; 2.50 A; A/B=2-252. DR PDB; 1J5T; X-ray; 3.00 A; A=24-252. DR PDBsum; 1I4N; -. DR PDBsum; 1J5T; -. DR ProteinModelPortal; Q56319; -. DR SMR; Q56319; 2-252. DR STRING; 243274.TM0140; -. DR EnsemblBacteria; AAD35233; AAD35233; TM_0140. DR GeneID; 896970; -. DR KEGG; tma:TM0140; -. DR PATRIC; 23935122; VBITheMar51294_0139. DR eggNOG; ENOG4105DK0; Bacteria. DR eggNOG; COG0134; LUCA. DR InParanoid; Q56319; -. DR KO; K01609; -. DR OMA; GISYITD; -. DR OrthoDB; EOG6WT8JX; -. DR BioCyc; MetaCyc:MONOMER-343; -. DR BRENDA; 4.1.1.48; 6331. DR UniPathway; UPA00035; UER00043. DR EvolutionaryTrace; Q56319; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00134_B; IGPS_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013798; Indole-3-glycerol_P_synth. DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00218; IGPS; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR PROSITE; PS00614; IGPS; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Complete proteome; Decarboxylase; KW Direct protein sequencing; Lyase; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1 252 Indole-3-glycerol phosphate synthase. FT /FTId=PRO_0000154266. FT CONFLICT 226 226 N -> K (in Ref. 1; CAA63389). FT {ECO:0000305}. FT HELIX 4 14 {ECO:0000244|PDB:1I4N}. FT HELIX 15 17 {ECO:0000244|PDB:1I4N}. FT HELIX 20 22 {ECO:0000244|PDB:1I4N}. FT HELIX 31 36 {ECO:0000244|PDB:1I4N}. FT STRAND 39 41 {ECO:0000244|PDB:1I4N}. FT STRAND 43 48 {ECO:0000244|PDB:1I4N}. FT STRAND 53 55 {ECO:0000244|PDB:1I4N}. FT HELIX 64 74 {ECO:0000244|PDB:1I4N}. FT STRAND 76 81 {ECO:0000244|PDB:1I4N}. FT STRAND 85 87 {ECO:0000244|PDB:1I4N}. FT HELIX 92 98 {ECO:0000244|PDB:1I4N}. FT STRAND 105 108 {ECO:0000244|PDB:1I4N}. FT HELIX 115 122 {ECO:0000244|PDB:1I4N}. FT STRAND 126 131 {ECO:0000244|PDB:1I4N}. FT HELIX 132 134 {ECO:0000244|PDB:1I4N}. FT HELIX 137 148 {ECO:0000244|PDB:1I4N}. FT TURN 149 151 {ECO:0000244|PDB:1I4N}. FT STRAND 153 158 {ECO:0000244|PDB:1I4N}. FT HELIX 161 168 {ECO:0000244|PDB:1I4N}. FT STRAND 174 179 {ECO:0000244|PDB:1I4N}. FT TURN 183 185 {ECO:0000244|PDB:1I4N}. FT HELIX 192 196 {ECO:0000244|PDB:1I4N}. FT HELIX 197 199 {ECO:0000244|PDB:1I4N}. FT STRAND 204 210 {ECO:0000244|PDB:1I4N}. FT HELIX 215 217 {ECO:0000244|PDB:1I4N}. FT HELIX 218 221 {ECO:0000244|PDB:1I4N}. FT TURN 222 224 {ECO:0000244|PDB:1I4N}. FT STRAND 226 230 {ECO:0000244|PDB:1I4N}. FT HELIX 232 236 {ECO:0000244|PDB:1I4N}. FT STRAND 237 239 {ECO:0000244|PDB:1J5T}. FT HELIX 240 250 {ECO:0000244|PDB:1I4N}. SQ SEQUENCE 252 AA; 28660 MW; AA60B8E28BC043DF CRC64; MRRLWEIVEA KKKDILEIDG ENLIVQRRNH RFLEVLSGKE RVKIIAEFKK ASPSAGDINA DASLEDFIRM YDELADAISI LTEKHYFKGD PAFVRAARNL TCRPILAKDF YIDTVQVKLA SSVGADAILI IARILTAEQI KEIYEAAEEL GMDSLVEVHS REDLEKVFSV IRPKIIGINT RDLDTFEIKK NVLWELLPLV PDDTVVVAES GIKDPRELKD LRGKVNAVLV GTSIMKAENP RRFLEEMRAW SE // ID TRPE_THEMA Reviewed; 461 AA. AC Q08653; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 20-JAN-2016, entry version 122. DE RecName: Full=Anthranilate synthase component 1; DE Short=AS; DE Short=ASI; DE EC=4.1.3.27; GN Name=trpE; OrderedLocusNames=TM_0142; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7685830; DOI=10.1006/jmbi.1993.1345; RA Kim C.W., Markiewicz P.G., Lee J.J., Schierle C.F., Miller J.H.; RT "Studies of the hyperthermophile Thermotoga maritima by random RT sequencing of cDNA and genomic libraries. Identification and RT sequencing of the trpEG (D) operon."; RL J. Mol. Biol. 231:960-981(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the CC two-step biosynthesis of anthranilate, an intermediate in the CC biosynthesis of L-tryptophan. In the first step, the glutamine- CC binding beta subunit (TrpG) of anthranilate synthase (AS) provides CC the glutamine amidotransferase activity which generates ammonia as CC a substrate that, along with chorismate, is used in the second CC step, catalyzed by the large alpha subunit of AS (TrpE) to produce CC anthranilate. In the absence of TrpG, TrpE can synthesize CC anthranilate directly from chorismate and high concentrations of CC ammonia (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate + CC pyruvate + L-glutamate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P00897}; CC Note=Binds 1 Mg(2+) ion per subunit. CC {ECO:0000250|UniProtKB:P00897}; CC -!- ENZYME REGULATION: Feedback inhibited by tryptophan. CC {ECO:0000250}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: CC a beta subunit (TrpG) and a large alpha subunit (TrpE). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the anthranilate synthase component I CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA52202.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X74075; CAA52202.1; ALT_INIT; Genomic_DNA. DR EMBL; AE000512; AAD35235.1; -; Genomic_DNA. DR PIR; D72414; D72414. DR RefSeq; NP_227957.1; NC_000853.1. DR RefSeq; WP_010865059.1; NC_000853.1. DR ProteinModelPortal; Q08653; -. DR STRING; 243274.TM0142; -. DR EnsemblBacteria; AAD35235; AAD35235; TM_0142. DR GeneID; 896972; -. DR KEGG; tma:TM0142; -. DR KEGG; tmi:THEMA_04095; -. DR PATRIC; 23935126; VBITheMar51294_0141. DR eggNOG; ENOG4105CRQ; Bacteria. DR eggNOG; COG0147; LUCA. DR InParanoid; Q08653; -. DR KO; K01657; -. DR OMA; TMQVVAD; -. DR OrthoDB; EOG6D5G6B; -. DR BioCyc; MetaCyc:MONOMER-281; -. DR BioCyc; TMAR243274:GC6P-142-MONOMER; -. DR UniPathway; UPA00035; UER00040. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.60.120.10; -; 1. DR InterPro; IPR005801; ADC_synthase. DR InterPro; IPR019999; Anth_synth_I-like. DR InterPro; IPR006805; Anth_synth_I_N. DR InterPro; IPR015890; Chorismate_C. DR Pfam; PF04715; Anth_synt_I_N; 1. DR Pfam; PF00425; Chorismate_bind; 1. DR PRINTS; PR00095; ANTSNTHASEI. DR SUPFAM; SSF56322; SSF56322; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Magnesium; Metal-binding; KW Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 461 Anthranilate synthase component 1. FT /FTId=PRO_0000154116. FT REGION 234 236 Tryptophan binding. FT {ECO:0000250|UniProtKB:P00897}. FT REGION 269 270 Chorismate binding. FT {ECO:0000250|UniProtKB:P00897}. FT REGION 423 425 Chorismate binding. FT {ECO:0000250|UniProtKB:P00897}. FT METAL 296 296 Magnesium. FT {ECO:0000250|UniProtKB:P00897}. FT METAL 438 438 Magnesium. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 36 36 Tryptophan. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 384 384 Chorismate. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 409 409 Chorismate. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 425 425 Chorismate; via amide nitrogen. FT {ECO:0000250|UniProtKB:P00897}. FT CONFLICT 104 104 A -> R (in Ref. 1; CAA52202). FT {ECO:0000305}. SQ SEQUENCE 461 AA; 52240 MW; DEA00256445C568C CRC64; MGDSMHVLKL VSDLETPVST FMKVSRGEEF AFLLESVELG SAFGRHSFIG IGKKDVLVFE KGILRTSNQQ LDYTSSPLKA IKDWLEVYRY SVKHDELPSF RGGAVGFVSY DYISYIEKVK VKASVFPTFY FVVPEHLIIF DHLKNNVFII SDSPEELTSK VLSPFEEKPE KNVFVTEPES NFEREQFYKV VEKAKKYIVE GDIFQVVLSQ AFTFKTTLDP FYIYRALRMI NPSPYMFYLK FGDTVVLGSS PETMAKVEGD KATVKPIAGT RPRGRTVEED LKLERELLND EKEIAEHVML VDLGRNDLGR VCKEGTVRVE KKMVIERYSH VMHIVSQVSG ELKDDKDAVD VFEATFPAGT VSGAPKVRAM EIIEELEPTP RGPYAGAVGY FSFPDDKGRM NMDSAITIRS FFFKGKQGWL QAGAGIVYDS VPEREYQETL NKLRALFRSL EVAQKIQGGL F // ID TSAB_THEMA Reviewed; 206 AA. AC Q9WZX7; G4FCV1; DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaB; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB; GN Name=tsaB; OrderedLocusNames=TM_0874; ORFNames=Tmari_0876; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), AND SUBUNIT. RX PubMed=20944216; DOI=10.1107/S1744309109022192; RA Xu Q., McMullan D., Jaroszewski L., Krishna S.S., Elsliger M.A., RA Yeh A.P., Abdubek P., Astakhova T., Axelrod H.L., Carlton D., RA Chiu H.J., Clayton T., Duan L., Feuerhelm J., Grant J., Han G.W., RA Jin K.K., Klock H.E., Knuth M.W., Miller M.D., Morse A.T., RA Nigoghossian E., Okach L., Oommachen S., Paulsen J., Reyes R., RA Rife C.L., van den Bedem H., Hodgson K.O., Wooley J., Deacon A.M., RA Godzik A., Lesley S.A., Wilson I.A.; RT "Structure of an essential bacterial protein YeaZ (TM0874) from RT Thermotoga maritima at 2.5 A resolution."; RL Acta Crystallogr. F 66:1230-1236(2010). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Is involved in the transfer of the CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the CC N6 group of A37, together with TsaD and TsaE; this reaction does CC not require ATP in vitro. TsaB seems to play an indirect role in CC the t(6)A biosynthesis pathway, possibly in regulating the core CC enzymatic function of TsaD (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20944216}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. TsaB subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35955.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49801.1; -; Genomic_DNA. DR PIR; D72323; D72323. DR RefSeq; NP_228682.1; NC_000853.1. DR RefSeq; WP_004080725.1; NZ_CP011107.1. DR PDB; 2A6A; X-ray; 2.50 A; A/B=1-206. DR PDBsum; 2A6A; -. DR ProteinModelPortal; Q9WZX7; -. DR SMR; Q9WZX7; 1-193. DR STRING; 243274.TM0874; -. DR DNASU; 898547; -. DR EnsemblBacteria; AAD35955; AAD35955; TM_0874. DR EnsemblBacteria; AGL49801; AGL49801; Tmari_0876. DR GeneID; 898547; -. DR KEGG; tma:TM0874; -. DR KEGG; tmi:THEMA_00265; -. DR KEGG; tmm:Tmari_0876; -. DR KEGG; tmw:THMA_0896; -. DR PATRIC; 23936679; VBITheMar51294_0888. DR eggNOG; COG1214; LUCA. DR InParanoid; Q9WZX7; -. DR OMA; STIKGFC; -. DR OrthoDB; EOG6JDWDD; -. DR BioCyc; TMAR243274:GC6P-904-MONOMER; -. DR EvolutionaryTrace; Q9WZX7; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IBA:GO_Central. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR022496; T6A_YeaZ. DR Pfam; PF00814; Peptidase_M22; 1. DR TIGRFAMs; TIGR03725; T6A_YeaZ; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Reference proteome; KW tRNA processing. FT CHAIN 1 206 tRNA threonylcarbamoyladenosine FT biosynthesis protein TsaB. FT /FTId=PRO_0000423848. FT STRAND 2 7 {ECO:0000244|PDB:2A6A}. FT STRAND 9 18 {ECO:0000244|PDB:2A6A}. FT STRAND 21 29 {ECO:0000244|PDB:2A6A}. FT HELIX 31 35 {ECO:0000244|PDB:2A6A}. FT HELIX 36 48 {ECO:0000244|PDB:2A6A}. FT HELIX 52 54 {ECO:0000244|PDB:2A6A}. FT STRAND 56 61 {ECO:0000244|PDB:2A6A}. FT HELIX 67 81 {ECO:0000244|PDB:2A6A}. FT HELIX 82 84 {ECO:0000244|PDB:2A6A}. FT STRAND 88 91 {ECO:0000244|PDB:2A6A}. FT HELIX 93 99 {ECO:0000244|PDB:2A6A}. FT STRAND 105 112 {ECO:0000244|PDB:2A6A}. FT STRAND 117 128 {ECO:0000244|PDB:2A6A}. FT STRAND 130 139 {ECO:0000244|PDB:2A6A}. FT HELIX 140 150 {ECO:0000244|PDB:2A6A}. FT STRAND 153 159 {ECO:0000244|PDB:2A6A}. FT HELIX 164 176 {ECO:0000244|PDB:2A6A}. FT HELIX 183 185 {ECO:0000244|PDB:2A6A}. FT HELIX 188 191 {ECO:0000244|PDB:2A6A}. SQ SEQUENCE 206 AA; 22987 MW; F5A341FBA22E66E7 CRC64; MNVLALDTSQ RIRIGLRKGE DLFEISYTGE KKHAEILPVV VKKLLDELDL KVKDLDVVGV GIGPGGLTGL RVGIATVVGL VSPYDIPVAP LNSFEMTAKS CPADGVVLVA RRARKGYHYC AVYLKDKGLN PLKEPSVVSD EELEEITKEF SPKIVLKDDL LISPAVLVEE SERLFREKKT IHYYEIEPLY LQKSIAELNW EKKKRG // ID TRPGD_THEMA Reviewed; 589 AA. AC Q08654; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 17-FEB-2016, entry version 129. DE RecName: Full=Bifunctional protein TrpGD; DE Includes: DE RecName: Full=Anthranilate synthase component 2; DE Short=AS; DE Short=ASII; DE EC=4.1.3.27; DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component; DE Includes: DE RecName: Full=Anthranilate phosphoribosyltransferase; DE EC=2.4.2.18; GN Name=trpGD; Synonyms=trpD; OrderedLocusNames=TM_0141; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7685830; DOI=10.1006/jmbi.1993.1345; RA Kim C.W., Markiewicz P.G., Lee J.J., Schierle C.F., Miller J.H.; RT "Studies of the hyperthermophile Thermotoga maritima by random RT sequencing of cDNA and genomic libraries. Identification and RT sequencing of the trpEG (D) operon."; RL J. Mol. Biol. 231:960-981(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 494-589. RX PubMed=7556082; RA Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.; RT "(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the RT hyperthermophile Thermotoga maritima."; RL EMBO J. 14:4395-4402(1995). CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the CC two-step biosynthesis of anthranilate, an intermediate in the CC biosynthesis of L-tryptophan. In the first step, the glutamine- CC binding beta subunit (TrpG) of anthranilate synthase (AS) provides CC the glutamine amidotransferase activity which generates ammonia as CC a substrate that, along with chorismate, is used in the second CC step, catalyzed by the large alpha subunit of AS (TrpE) to produce CC anthranilate. In the absence of TrpG, TrpE can synthesize CC anthranilate directly from chorismate and high concentrations of CC ammonia. In addition to synthesizing anthranilate, it also CC catalyzes the second step of the pathway, the transfer of the CC phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) CC to anthranilate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate + CC pyruvate + L-glutamate. CC -!- CATALYTIC ACTIVITY: N-(5-phospho-D-ribosyl)-anthranilate + CC diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1- CC diphosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 2/5. CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: CC a beta subunit (TrpG) and a large alpha subunit (TrpE). CC {ECO:0000250}. CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate CC phosphoribosyltransferase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X74075; CAA52203.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35234.1; -; Genomic_DNA. DR EMBL; X92729; CAA63388.1; -; Genomic_DNA. DR PIR; C72414; C72414. DR RefSeq; NP_227956.1; NC_000853.1. DR RefSeq; WP_010865058.1; NC_000853.1. DR ProteinModelPortal; Q08654; -. DR STRING; 243274.TM0141; -. DR MEROPS; C26.955; -. DR EnsemblBacteria; AAD35234; AAD35234; TM_0141. DR GeneID; 896971; -. DR KEGG; tma:TM0141; -. DR PATRIC; 23935124; VBITheMar51294_0140. DR eggNOG; ENOG4105DDQ; Bacteria. DR eggNOG; COG0512; LUCA. DR eggNOG; COG0547; LUCA. DR InParanoid; Q08654; -. DR KO; K13497; -. DR OMA; VIYRNHV; -. DR OrthoDB; EOG6D5G6B; -. DR BioCyc; MetaCyc:MONOMER-282; -. DR BioCyc; TMAR243274:GC6P-141-MONOMER; -. DR UniPathway; UPA00035; UER00040. DR UniPathway; UPA00035; UER00041. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1030.10; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00211; TrpD; 1. DR InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR000312; Glycosyl_Trfase_fam3. DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom. DR InterPro; IPR006221; TrpG/PapA_dom. DR Pfam; PF00117; GATase; 1. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR SUPFAM; SSF47648; SSF47648; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52418; SSF52418; 1. DR TIGRFAMs; TIGR01245; trpD; 1. DR TIGRFAMs; TIGR00566; trpG_papA; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Glutamine amidotransferase; Glycosyltransferase; KW Lyase; Multifunctional enzyme; Reference proteome; Transferase; KW Tryptophan biosynthesis. FT CHAIN 1 589 Bifunctional protein TrpGD. FT /FTId=PRO_0000056901. FT DOMAIN 46 241 Glutamine amidotransferase type-1. FT REGION 99 101 Glutamine binding. FT {ECO:0000250|UniProtKB:P00900}. FT REGION 176 177 Glutamine binding. FT {ECO:0000250|UniProtKB:P00900}. FT REGION 253 589 Anthranilate phosphoribosyltransferase. FT ACT_SITE 126 126 Nucleophile; for GATase activity. FT {ECO:0000250|UniProtKB:P00900}. FT ACT_SITE 215 215 For GATase activity. {ECO:0000250}. FT ACT_SITE 217 217 For GATase activity. {ECO:0000250}. FT BINDING 130 130 Glutamine. FT {ECO:0000250|UniProtKB:P00900}. FT CONFLICT 384 384 E -> G (in Ref. 1; CAA52203). FT {ECO:0000305}. SQ SEQUENCE 589 AA; 64269 MW; 8DF80E6DA0C68610 CRC64; MAPGRSGYRL RFRSGARISG DSEQTQGFVQ EPGSCAEDPG GIVLKRVIVI DNYDSFVYNI VQYIGEVEPD CEIEVFRNDE ITIEEIERKN PTHIVISPGP GRPEEAGISV DVVRHFSGKV PILGVCLGHQ VIGYAFGGKI VHAKRILHGK TSKIVHNGKG VFSGVKNPLV ATRYHSLVVE EASLPEVLEI TAKSDDGEIM GLQHKEHPTF GVQFHPESVL TEEGKRIIKN FLNIQDIQVK KVSEETEIDI VSALKKLVEF EDLTFEESRQ VMNFIMSGNA TDAQIAGFLV ALRMKEETGD ELGGMASVMR EKSIHIKAPS PRTVDTCGTG GDGFGTFNIS TTTAFVVAAA GIPVAKHGNR SVSSKVGSAD VLEAGGYKLE KTPEEMEREL KETGFSFLFA PLLHPAMKHV MPARRQLKIR TAFNLLGPIT NPARVKYQVV GVFDLSFASK LATALQRLGT ERSAVVNGGF TDELTTCGKN NLLLVTQEEI VPMVLDPEEL GLKSGDPEEL KGPSDPKEAY RMMESVLKGE ASRTQVETVA LNAGVVFWLV GECDTIKDGV GKALDLIRTG EAYKKLREVM DYQKTLGNS // ID TRUA_THEMA Reviewed; 245 AA. AC Q9X1R0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=tRNA pseudouridine synthase A {ECO:0000255|HAMAP-Rule:MF_00171}; DE EC=5.4.99.12 {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA pseudouridine(38-40) synthase {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA pseudouridylate synthase I {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA-uridine isomerase I {ECO:0000255|HAMAP-Rule:MF_00171}; GN Name=truA {ECO:0000255|HAMAP-Rule:MF_00171}; GN OrderedLocusNames=TM_1574; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in CC the anticodon stem and loop of transfer RNAs. {ECO:0000255|HAMAP- CC Rule:MF_00171}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(38-40) = tRNA pseudouridine(38- CC 40). {ECO:0000255|HAMAP-Rule:MF_00171}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00171}. CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA CC family. {ECO:0000255|HAMAP-Rule:MF_00171}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36641.1; -; Genomic_DNA. DR PIR; G72237; G72237. DR RefSeq; NP_229374.1; NC_000853.1. DR RefSeq; WP_004081995.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1R0; -. DR STRING; 243274.TM1574; -. DR EnsemblBacteria; AAD36641; AAD36641; TM_1574. DR GeneID; 897640; -. DR KEGG; tma:TM1574; -. DR PATRIC; 23938110; VBITheMar51294_1592. DR eggNOG; ENOG4105DI7; Bacteria. DR eggNOG; COG0101; LUCA. DR InParanoid; Q9X1R0; -. DR KO; K06173; -. DR OMA; YKLTIEY; -. DR OrthoDB; EOG6Z9B4R; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.580; -; 1. DR Gene3D; 3.30.70.660; -; 1. DR HAMAP; MF_00171; TruA; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR001406; PsdUridine_synth_TruA. DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom. DR InterPro; IPR020095; PsdUridine_synth_TruA_C. DR InterPro; IPR020094; PsdUridine_synth_TruA_N. DR PANTHER; PTHR11142; PTHR11142; 1. DR Pfam; PF01416; PseudoU_synth_1; 2. DR PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00071; hisT_truA; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; tRNA processing. FT CHAIN 1 245 tRNA pseudouridine synthase A. FT /FTId=PRO_0000057474. FT ACT_SITE 52 52 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00171}. FT BINDING 111 111 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00171}. SQ SEQUENCE 245 AA; 28609 MW; BDEC449A33C268E2 CRC64; MKRVAAVIEY DGSNFFGYQG QPDVRTVQGV IEDALERIFK QRIYTQAAGR TDTGVHANGQ LIAFNCPNDR MTTEDIRNAM NANLPDDVYV KEVFEVPVNF HPRFDVTKRI YHYFILTSRQ KNVFLRKYVW WFPYELDLDA MRKAVKYLEG THDFTSFKTG SDERDPVRTI YRIRILRLKN DLVLIRVEGR SFLRRMVRNI VAALVKVGLK QWEPEKMKEV LEARDRSAAA GTAPAHGLYF YKVLF // ID TRUB_THEMA Reviewed; 309 AA. AC Q9WZW0; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 121. DE RecName: Full=tRNA pseudouridine synthase B {ECO:0000255|HAMAP-Rule:MF_01080}; DE EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01080}; DE AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000255|HAMAP-Rule:MF_01080, ECO:0000303|PubMed:12499554}; DE Short=Psi55 synthase {ECO:0000255|HAMAP-Rule:MF_01080}; DE AltName: Full=tRNA pseudouridylate synthase {ECO:0000255|HAMAP-Rule:MF_01080}; DE AltName: Full=tRNA-uridine isomerase {ECO:0000255|HAMAP-Rule:MF_01080}; GN Name=truB {ECO:0000255|HAMAP-Rule:MF_01080, GN ECO:0000303|PubMed:14566049}; OrderedLocusNames=TM_0856; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP CRYSTALLIZATION. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=12499554; RA Wouters J., Tricot C., Durbecq V., Roovers M., Stalon V., RA Droogmans L.; RT "Preliminary X-ray crystallographic analysis of tRNA pseudouridine 55 RT synthase from the thermophilic eubacterium Thermotoga maritima."; RL Acta Crystallogr. D 59:152-154(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF COMPLEX WITH RNA. RX PubMed=14566049; DOI=10.1073/pnas.2135585100; RA Pan H., Agarwalla S., Moustakas D.T., Finer-Moore J., Stroud R.M.; RT "Structure of tRNA pseudouridine synthase TruB and its RNA complex: RT RNA recognition through a combination of rigid docking and induced RT fit."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12648-12653(2003). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil- CC 55 in the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP- CC Rule:MF_01080}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(55) = tRNA pseudouridine(55). CC {ECO:0000255|HAMAP-Rule:MF_01080}. CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01080}. CC -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000255|HAMAP- CC Rule:MF_01080}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35938.1; -; Genomic_DNA. DR PIR; A72325; A72325. DR RefSeq; NP_228665.1; NC_000853.1. DR RefSeq; WP_004080766.1; NZ_CP011107.1. DR PDB; 1R3E; X-ray; 2.10 A; A=1-309. DR PDB; 1ZE1; X-ray; 2.90 A; A/B/C/D=1-309. DR PDB; 1ZE2; X-ray; 3.00 A; A/B=1-309. DR PDB; 2AB4; X-ray; 2.40 A; A=1-309. DR PDBsum; 1R3E; -. DR PDBsum; 1ZE1; -. DR PDBsum; 1ZE2; -. DR PDBsum; 2AB4; -. DR ProteinModelPortal; Q9WZW0; -. DR SMR; Q9WZW0; 1-308. DR STRING; 243274.TM0856; -. DR EnsemblBacteria; AAD35938; AAD35938; TM_0856. DR GeneID; 898529; -. DR KEGG; tma:TM0856; -. DR PATRIC; 23936640; VBITheMar51294_0869. DR eggNOG; ENOG4105D0T; Bacteria. DR eggNOG; COG0130; LUCA. DR InParanoid; Q9WZW0; -. DR KO; K03177; -. DR OMA; ENDLITW; -. DR OrthoDB; EOG6358D3; -. DR BRENDA; 5.4.99.25; 6331. DR EvolutionaryTrace; Q9WZW0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central. DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.130.10; -; 1. DR HAMAP; MF_01080; TruB_bact; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR002501; PsdUridine_synth_N. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB. DR InterPro; IPR032819; TruB_C. DR PANTHER; PTHR13767; PTHR13767; 1. DR Pfam; PF01472; PUA; 1. DR Pfam; PF16198; TruB_C_2; 1. DR Pfam; PF01509; TruB_N; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00431; TruB; 1. DR PROSITE; PS50890; PUA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isomerase; Reference proteome; KW tRNA processing. FT CHAIN 1 309 tRNA pseudouridine synthase B. FT /FTId=PRO_0000121929. FT DOMAIN 229 306 PUA. {ECO:0000255|HAMAP-Rule:MF_01080}. FT ACT_SITE 39 39 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01080}. FT STRAND 4 10 {ECO:0000244|PDB:1R3E}. FT STRAND 12 14 {ECO:0000244|PDB:1R3E}. FT HELIX 16 26 {ECO:0000244|PDB:1R3E}. FT STRAND 32 36 {ECO:0000244|PDB:1R3E}. FT STRAND 43 50 {ECO:0000244|PDB:1R3E}. FT HELIX 51 60 {ECO:0000244|PDB:1R3E}. FT STRAND 65 73 {ECO:0000244|PDB:1R3E}. FT STRAND 75 81 {ECO:0000244|PDB:1R3E}. FT STRAND 86 89 {ECO:0000244|PDB:1R3E}. FT HELIX 96 104 {ECO:0000244|PDB:1R3E}. FT STRAND 105 112 {ECO:0000244|PDB:1R3E}. FT STRAND 116 119 {ECO:0000244|PDB:1R3E}. FT STRAND 121 126 {ECO:0000244|PDB:2AB4}. FT HELIX 127 132 {ECO:0000244|PDB:1R3E}. FT STRAND 137 139 {ECO:0000244|PDB:1ZE1}. FT STRAND 142 155 {ECO:0000244|PDB:1R3E}. FT STRAND 158 165 {ECO:0000244|PDB:1R3E}. FT HELIX 171 181 {ECO:0000244|PDB:1R3E}. FT STRAND 186 196 {ECO:0000244|PDB:1R3E}. FT HELIX 201 203 {ECO:0000244|PDB:1R3E}. FT TURN 207 209 {ECO:0000244|PDB:1R3E}. FT HELIX 212 218 {ECO:0000244|PDB:1R3E}. FT HELIX 222 224 {ECO:0000244|PDB:1R3E}. FT STRAND 231 233 {ECO:0000244|PDB:1R3E}. FT TURN 236 238 {ECO:0000244|PDB:1R3E}. FT HELIX 239 242 {ECO:0000244|PDB:1R3E}. FT TURN 243 245 {ECO:0000244|PDB:1R3E}. FT STRAND 248 252 {ECO:0000244|PDB:1R3E}. FT STRAND 253 255 {ECO:0000244|PDB:1ZE1}. FT STRAND 264 268 {ECO:0000244|PDB:1R3E}. FT STRAND 270 272 {ECO:0000244|PDB:1R3E}. FT STRAND 274 282 {ECO:0000244|PDB:1R3E}. FT HELIX 287 290 {ECO:0000244|PDB:1ZE1}. FT STRAND 291 294 {ECO:0000244|PDB:1ZE1}. FT STRAND 298 305 {ECO:0000244|PDB:1R3E}. SQ SEQUENCE 309 AA; 35459 MW; 04825FD6D643CE9C CRC64; MKHGILVAYK PKGPTSHDVV DEVRKKLKTR KVGHGGTLDP FACGVLIIGV NQGTRILEFY KDLKKVYWVK MRLGLITETF DITGEVVEER ECNVTEEEIR EAIFSFVGEY DQVPPAYSAK KYKGERLYKL AREGKIINLP PKRVKIFKIW DVNIEGRDVS FRVEVSPGTY IRSLCMDIGY KLGCGATAVE LVRESVGPHT IEESLNVFEA APEEIENRII PLEKCLEWLP RVVVHQESTK MILNGSQIHL EMLKEWDGFK KGEVVRVFNE EGRLLALAEA ERNSSFLETL RKHERNERVL TLRKVFNTR // ID TRPF_THEMA Reviewed; 205 AA. AC Q56320; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase; DE Short=PRAI; DE EC=5.3.1.24; GN Name=trpF; OrderedLocusNames=TM_0139; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7556082; RA Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.; RT "(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the RT hyperthermophile Thermotoga maritima."; RL EMBO J. 14:4395-4402(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=9166771; DOI=10.1021/bi962718q; RA Hennig M., Sterner R., Kirschner K., Jansonius J.N.; RT "Crystal structure at 2.0-A resolution of phosphoribosyl anthranilate RT isomerase from the hyperthermophile Thermotoga maritima: possible RT determinants of protein stability."; RL Biochemistry 36:6009-6016(1997). CC -!- CATALYTIC ACTIVITY: N-(5-phospho-beta-D-ribosyl)anthranilate = 1- CC (2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X92729; CAA63390.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35232.1; -; Genomic_DNA. DR PIR; S59048; S59048. DR RefSeq; NP_227954.1; NC_000853.1. DR RefSeq; WP_004082737.1; NZ_CP011107.1. DR PDB; 1DL3; X-ray; 2.70 A; A/B=1-205. DR PDB; 1LBM; X-ray; 2.80 A; A=1-205. DR PDB; 1NSJ; X-ray; 2.00 A; A=1-205. DR PDBsum; 1DL3; -. DR PDBsum; 1LBM; -. DR PDBsum; 1NSJ; -. DR ProteinModelPortal; Q56320; -. DR SMR; Q56320; 1-205. DR STRING; 243274.TM0139; -. DR EnsemblBacteria; AAD35232; AAD35232; TM_0139. DR GeneID; 896969; -. DR KEGG; tma:TM0139; -. DR PATRIC; 23935120; VBITheMar51294_0138. DR eggNOG; ENOG4108ZGB; Bacteria. DR eggNOG; COG0135; LUCA. DR InParanoid; Q56320; -. DR KO; K01817; -. DR OMA; FVNASRC; -. DR OrthoDB; EOG6N94DF; -. DR BioCyc; MetaCyc:MONOMER-301; -. DR BRENDA; 5.3.1.24; 6331. DR UniPathway; UPA00035; UER00042. DR EvolutionaryTrace; Q56320; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00135; PRAI; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001240; PRAI. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00697; PRAI; 1. DR SUPFAM; SSF51366; SSF51366; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Complete proteome; Isomerase; KW Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 205 N-(5'-phosphoribosyl)anthranilate FT isomerase. FT /FTId=PRO_0000154390. FT STRAND 3 6 {ECO:0000244|PDB:1NSJ}. FT HELIX 12 21 {ECO:0000244|PDB:1NSJ}. FT STRAND 24 29 {ECO:0000244|PDB:1NSJ}. FT HELIX 40 49 {ECO:0000244|PDB:1NSJ}. FT STRAND 52 62 {ECO:0000244|PDB:1NSJ}. FT HELIX 65 75 {ECO:0000244|PDB:1NSJ}. FT STRAND 78 82 {ECO:0000244|PDB:1NSJ}. FT HELIX 88 95 {ECO:0000244|PDB:1NSJ}. FT STRAND 98 108 {ECO:0000244|PDB:1NSJ}. FT HELIX 109 115 {ECO:0000244|PDB:1NSJ}. FT HELIX 116 118 {ECO:0000244|PDB:1NSJ}. FT STRAND 123 128 {ECO:0000244|PDB:1NSJ}. FT STRAND 130 134 {ECO:0000244|PDB:1NSJ}. FT HELIX 141 143 {ECO:0000244|PDB:1NSJ}. FT HELIX 145 150 {ECO:0000244|PDB:1NSJ}. FT STRAND 154 159 {ECO:0000244|PDB:1NSJ}. FT TURN 162 164 {ECO:0000244|PDB:1NSJ}. FT HELIX 165 172 {ECO:0000244|PDB:1NSJ}. FT STRAND 175 180 {ECO:0000244|PDB:1NSJ}. FT HELIX 181 183 {ECO:0000244|PDB:1NSJ}. FT STRAND 184 186 {ECO:0000244|PDB:1NSJ}. FT HELIX 192 203 {ECO:0000244|PDB:1NSJ}. SQ SEQUENCE 205 AA; 23041 MW; 9E1D76948C7EAE5E CRC64; MVRVKICGIT NLEDALFSVE SGADAVGFVF YPKSKRYISP EDARRISVEL PPFVFRVGVF VNEEPEKILD VASYVQLNAV QLHGEEPIEL CRKIAERILV IKAVGVSNER DMERALNYRE FPILLDTKTP EYGGSGKTFD WSLILPYRDR FRYLVLSGGL NPENVRSAID VVRPFAVDVS SGVEAFPGKK DHDSIKMFIK NAKGL // ID TSAD_THEMA Reviewed; 327 AA. AC Q9WXZ2; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01445}; DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01445}; DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_01445}; DE Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_01445}; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445}; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445}; GN Name=tsaD {ECO:0000255|HAMAP-Rule:MF_01445}; Synonyms=gcp; GN OrderedLocusNames=TM_0145; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Is involved in the transfer of the CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the CC N6 group of A37, together with TsaE and TsaB. TsaD likely plays a CC direct catalytic role in this reaction. {ECO:0000255|HAMAP- CC Rule:MF_01445}. CC -!- CATALYTIC ACTIVITY: L-threonylcarbamoyladenylate + adenine(37) in CC tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_01445}. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01445}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01445}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445}. CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP- CC Rule:MF_01445}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35238.1; -; Genomic_DNA. DR PIR; G72411; G72411. DR RefSeq; NP_227960.1; NC_000853.1. DR RefSeq; WP_004082750.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXZ2; -. DR STRING; 243274.TM0145; -. DR DNASU; 896976; -. DR EnsemblBacteria; AAD35238; AAD35238; TM_0145. DR GeneID; 896976; -. DR KEGG; tma:TM0145; -. DR PATRIC; 23935134; VBITheMar51294_0144. DR eggNOG; ENOG4105CPM; Bacteria. DR eggNOG; COG0533; LUCA. DR InParanoid; Q9WXZ2; -. DR KO; K01409; -. DR OMA; ICIDHIL; -. DR OrthoDB; EOG6K402S; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase; IEA:UniProtKB-EC. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IBA:GO_Central. DR HAMAP; MF_01445; TsaD; 1. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR017861; KAE1/TsaD. DR InterPro; IPR022450; TsaD. DR Pfam; PF00814; Peptidase_M22; 1. DR PRINTS; PR00789; OSIALOPTASE. DR TIGRFAMs; TIGR00329; gcp_kae1; 1. DR TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Iron; Metal-binding; KW Reference proteome; Transferase; tRNA processing. FT CHAIN 1 327 tRNA N6-adenosine FT threonylcarbamoyltransferase. FT /FTId=PRO_0000303595. FT REGION 132 136 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT METAL 109 109 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT METAL 113 113 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT METAL 296 296 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT BINDING 165 165 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT BINDING 178 178 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01445}. FT BINDING 182 182 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT BINDING 268 268 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. SQ SEQUENCE 327 AA; 35628 MW; F8373046AED4858C CRC64; MRVLGIETSC DETAVAVLDD GKNVVVNFTV SQIEVHQKFG GVVPEVAARH HLKNLPILLK KAFEKVPPET VDVVAATYGP GLIGALLVGL SAAKGLAISL EKPFVGVNHV EAHVQAVFLA NPDLKPPLVV LMVSGGHTQL MKVDEDYSME VLGETLDDSA GEAFDKVARL LGLGYPGGPV IDRVAKKGDP EKYSFPRPML DDDSYNFSFA GLKTSVLYFL QREKGYKVED VAASFQKAVV DILVEKTFRL ARNLGIRKIA FVGGVAANSM LREEVRKRAE RWNYEVFFPP LELCTDNALM VAKAGYEKAK RGMFSPLSLN ADPNLNV // ID UPPP_THEMA Reviewed; 237 AA. AC Q9WZZ5; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=Undecaprenyl-diphosphatase {ECO:0000255|HAMAP-Rule:MF_01006}; DE EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006}; DE AltName: Full=Bacitracin resistance protein {ECO:0000255|HAMAP-Rule:MF_01006}; DE AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_01006}; GN Name=uppP {ECO:0000255|HAMAP-Rule:MF_01006}; Synonyms=bacA, upk; GN OrderedLocusNames=TM_0893; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl CC diphosphate (UPP). Confers resistance to bacitracin. CC {ECO:0000255|HAMAP-Rule:MF_01006}. CC -!- CATALYTIC ACTIVITY: Ditrans,octacis-undecaprenyl diphosphate + CC H(2)O = ditrans,octacis-undecaprenyl phosphate + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01006}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01006}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01006}. CC -!- MISCELLANEOUS: Bacitracin is thought to be involved in the CC inhibition of peptidoglycan synthesis by sequestering undecaprenyl CC diphosphate, thereby reducing the pool of lipid carrier available. CC -!- SIMILARITY: Belongs to the UppP family. {ECO:0000255|HAMAP- CC Rule:MF_01006}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35974.1; -; Genomic_DNA. DR PIR; F72321; F72321. DR RefSeq; NP_228701.1; NC_000853.1. DR RefSeq; WP_004080690.1; NZ_CP011107.1. DR STRING; 243274.TM0893; -. DR EnsemblBacteria; AAD35974; AAD35974; TM_0893. DR GeneID; 898567; -. DR KEGG; tma:TM0893; -. DR PATRIC; 23936717; VBITheMar51294_0907. DR eggNOG; ENOG4105DWR; Bacteria. DR eggNOG; COG1968; LUCA. DR InParanoid; Q9WZZ5; -. DR KO; K06153; -. DR OMA; GFRFGIN; -. DR OrthoDB; EOG6QP13M; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01006; Undec_diphosphatase; 1. DR InterPro; IPR003824; UppP. DR Pfam; PF02673; BacA; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Hydrolase; KW Membrane; Peptidoglycan synthesis; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 237 Undecaprenyl-diphosphatase. FT /FTId=PRO_0000151227. FT TRANSMEM 38 58 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 65 85 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 92 112 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 126 146 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 166 186 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 191 211 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. FT TRANSMEM 217 237 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01006}. SQ SEQUENCE 237 AA; 26036 MW; 759239335C5FE10F CRC64; MDLLLGIVQG LTEFLPISSS GHLTLLSHLL KTDLNAYQTA VLHLGTLVSV VLFALDGIRR SLRSWRIILN LIVSTIPAGV FGVLFEKQID QLFSSPRFLP LFFSATALIL MFTRYSSSGE KRMENMSFLD ALLVGIAQLF ALFPGISRSG ITVSSLLFMK YRSEDALQYS FLMSIPVVLG AGILGLGKGN VTILAPIFAF LSGLFALYVL SRSVRSGKIW QFSYYCLFVA ILSYLAG // ID UPP_THEMA Reviewed; 209 AA. AC Q9WZI0; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01218}; DE EC=2.4.2.9 {ECO:0000255|HAMAP-Rule:MF_01218}; DE AltName: Full=UMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01218}; DE AltName: Full=UPRTase {ECO:0000255|HAMAP-Rule:MF_01218}; GN Name=upp {ECO:0000255|HAMAP-Rule:MF_01218}; OrderedLocusNames=TM_0721; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RG Joint center for structural genomics (JCSG); RT "Crystal structure of uracil phosphoribosyltransferase (TM0721) from RT Thermotoga maritima at 2.30 A resolution."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha- CC D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01218}. CC -!- CATALYTIC ACTIVITY: UMP + diphosphate = uracil + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_01218}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01218}; CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg- CC PRPP. {ECO:0000255|HAMAP-Rule:MF_01218}; CC -!- ENZYME REGULATION: Allosterically activated by GTP. CC {ECO:0000255|HAMAP-Rule:MF_01218}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage CC pathway; UMP from uracil: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01218}. CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000255|HAMAP- CC Rule:MF_01218}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35803.1; -; Genomic_DNA. DR PIR; G72341; G72341. DR RefSeq; NP_228530.1; NC_000853.1. DR RefSeq; WP_004081012.1; NZ_CP011107.1. DR PDB; 1O5O; X-ray; 2.30 A; A/B/C/D=1-209. DR PDBsum; 1O5O; -. DR ProteinModelPortal; Q9WZI0; -. DR SMR; Q9WZI0; 1-209. DR STRING; 243274.TM0721; -. DR EnsemblBacteria; AAD35803; AAD35803; TM_0721. DR GeneID; 898388; -. DR KEGG; tma:TM0721; -. DR PATRIC; 23936362; VBITheMar51294_0734. DR eggNOG; ENOG4105CZ5; Bacteria. DR eggNOG; COG0035; LUCA. DR InParanoid; Q9WZI0; -. DR KO; K00761; -. DR OMA; TIEGWCG; -. DR OrthoDB; EOG6HF5WX; -. DR UniPathway; UPA00574; UER00636. DR EvolutionaryTrace; Q9WZI0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004849; F:uridine kinase activity; IBA:GO_Central. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IBA:GO_Central. DR GO; GO:0043097; P:pyrimidine nucleoside salvage; IBA:GO_Central. DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0006223; P:uracil salvage; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01218_B; Upp_B; 1. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005765; Ura_phspho_trans. DR Pfam; PF14681; UPRTase; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01091; upp; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Complete proteome; KW Glycosyltransferase; GTP-binding; Magnesium; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 209 Uracil phosphoribosyltransferase. FT /FTId=PRO_0000120904. FT REGION 131 139 5-phospho-alpha-D-ribose 1-diphosphate FT binding. {ECO:0000255|HAMAP- FT Rule:MF_01218}. FT REGION 199 201 Uracil binding. {ECO:0000255|HAMAP- FT Rule:MF_01218}. FT BINDING 79 79 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 104 104 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 194 194 Uracil; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 200 200 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT STRAND 4 6 {ECO:0000244|PDB:1O5O}. FT HELIX 10 20 {ECO:0000244|PDB:1O5O}. FT HELIX 26 44 {ECO:0000244|PDB:1O5O}. FT TURN 45 47 {ECO:0000244|PDB:1O5O}. FT STRAND 51 56 {ECO:0000244|PDB:1O5O}. FT STRAND 61 66 {ECO:0000244|PDB:1O5O}. FT STRAND 72 78 {ECO:0000244|PDB:1O5O}. FT HELIX 81 91 {ECO:0000244|PDB:1O5O}. FT STRAND 99 104 {ECO:0000244|PDB:1O5O}. FT TURN 106 108 {ECO:0000244|PDB:1O5O}. FT STRAND 111 117 {ECO:0000244|PDB:1O5O}. FT STRAND 126 130 {ECO:0000244|PDB:1O5O}. FT STRAND 132 137 {ECO:0000244|PDB:1O5O}. FT HELIX 138 149 {ECO:0000244|PDB:1O5O}. FT STRAND 154 158 {ECO:0000244|PDB:1O5O}. FT STRAND 160 162 {ECO:0000244|PDB:1O5O}. FT HELIX 164 173 {ECO:0000244|PDB:1O5O}. FT STRAND 178 184 {ECO:0000244|PDB:1O5O}. FT STRAND 186 188 {ECO:0000244|PDB:1O5O}. FT STRAND 194 197 {ECO:0000244|PDB:1O5O}. FT HELIX 201 206 {ECO:0000244|PDB:1O5O}. SQ SEQUENCE 209 AA; 23320 MW; BD306120FF64D586 CRC64; MKNLVVVDHP LIKHKLTIMR DKNTGPKEFR ELLREITLLL AYEATRHLKC EEVEVETPIT KTIGYRINDK DIVVVPILRA GLVMADGILE LLPNASVGHI GIYRDPETLQ AVEYYAKLPP LNDDKEVFLL DPMLATGVSS IKAIEILKEN GAKKITLVAL IAAPEGVEAV EKKYEDVKIY VAALDERLND HGYIIPGLGD AGDRLFRTK // ID UXUA_THEMA Reviewed; 360 AA. AC Q9WXS4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Mannonate dehydratase; DE EC=4.2.1.8; DE AltName: Full=D-mannonate hydro-lyase; GN Name=uxuA; OrderedLocusNames=TM_0069; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the dehydration of D-mannonate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + CC H(2)O. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate CC interconversion. CC -!- SIMILARITY: Belongs to the mannonate dehydratase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35163.1; -; Genomic_DNA. DR PIR; A72423; A72423. DR RefSeq; NP_227885.1; NC_000853.1. DR RefSeq; WP_004082566.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXS4; -. DR SMR; Q9WXS4; 1-354. DR STRING; 243274.TM0069; -. DR EnsemblBacteria; AAD35163; AAD35163; TM_0069. DR GeneID; 896894; -. DR KEGG; tma:TM0069; -. DR PATRIC; 23934978; VBITheMar51294_0067. DR eggNOG; ENOG4105CHZ; Bacteria. DR eggNOG; COG1312; LUCA. DR InParanoid; Q9WXS4; -. DR KO; K01686; -. DR OMA; GRHLWGE; -. DR OrthoDB; EOG6ZSP6Z; -. DR BioCyc; MetaCyc:MONOMER-17955; -. DR UniPathway; UPA00246; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central. DR GO; GO:0008927; F:mannonate dehydratase activity; IBA:GO_Central. DR GO; GO:0042840; P:D-glucuronate catabolic process; IBA:GO_Central. DR Gene3D; 3.20.20.150; -; 1. DR HAMAP; MF_00106; UxuA; 1. DR InterPro; IPR004628; Man_deHydtase. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF03786; UxuA; 1. DR PIRSF; PIRSF016049; Man_dehyd; 1. DR SUPFAM; SSF51658; SSF51658; 1. DR TIGRFAMs; TIGR00695; uxuA; 1. PE 3: Inferred from homology; KW Complete proteome; Iron; Lyase; Manganese; Reference proteome. FT CHAIN 1 360 Mannonate dehydratase. FT /FTId=PRO_0000170689. SQ SEQUENCE 360 AA; 41890 MW; 08C9771F1DCBFA3E CRC64; MKLVFRWYGE KHDTVTLEQI RQIPGVEGVV GALFDIPVGE VWPFEEIMKL KETVEKAGLK LEVIESVNVH EDIKLGLPTR DRYIENYKKT IRNLAKAGVK VVCYNFMPVF DWMRTDLHKK LPDGSETMEY DHRLIEGVTP DELIKRVKEG SQGFVLPGWE WDRLEKLRET FELYKNVDEE KLFENLVYFL ERVIPVCEEC DVKLAIHPDD PPWSIFGLPR IITNKENIER MLKAVDSPYN GITFCMGSLG ANPENNIPEM IRYFGKMGRI HFAHVRNLKF TGEKSFYETA HPSFCGSHDL FEVMKAFHDI GYEGYIRPDH GRLIWGEKAR PGYGLYDRAL GATYILGLWE AIDKMKKRYC // ID UVRC_THEMA Reviewed; 557 AA. AC Q9WYA3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 120. DE RecName: Full=UvrABC system protein C {ECO:0000255|HAMAP-Rule:MF_00203}; DE Short=Protein UvrC {ECO:0000255|HAMAP-Rule:MF_00203}; DE AltName: Full=Excinuclease ABC subunit C {ECO:0000255|HAMAP-Rule:MF_00203}; GN Name=uvrC {ECO:0000255|HAMAP-Rule:MF_00203}; GN OrderedLocusNames=TM_0265; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. UvrC both incises the 5' and 3' sides CC of the lesion. The N-terminal half is responsible for the 3' CC incision and the C-terminal half is responsible for the 5' CC incision. {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SUBUNIT: Interacts with UvrB in an incision complex. CC {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC -!- SIMILARITY: Contains 1 GIY-YIG domain. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC -!- SIMILARITY: Contains 1 UVR domain. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35353.1; -; Genomic_DNA. DR PIR; H72400; H72400. DR RefSeq; NP_228078.1; NC_000853.1. DR RefSeq; WP_004082969.1; NZ_CP011107.1. DR PDB; 1YCZ; X-ray; 1.80 A; A=1-96. DR PDB; 1YD0; X-ray; 1.50 A; A=1-96. DR PDB; 1YD1; X-ray; 1.80 A; A=1-96. DR PDB; 1YD2; X-ray; 1.60 A; A=1-96. DR PDB; 1YD3; X-ray; 1.60 A; A=1-96. DR PDB; 1YD4; X-ray; 1.90 A; A=1-96. DR PDB; 1YD5; X-ray; 1.80 A; A=1-96. DR PDB; 2NRR; X-ray; 1.20 A; A=345-502. DR PDB; 2NRT; X-ray; 1.50 A; A=339-557. DR PDB; 2NRV; X-ray; 1.80 A; A/B=339-557. DR PDB; 2NRW; X-ray; 2.30 A; A=339-557. DR PDB; 2NRX; X-ray; 1.90 A; A/B=339-557. DR PDB; 2NRZ; X-ray; 2.00 A; A/B=339-557. DR PDBsum; 1YCZ; -. DR PDBsum; 1YD0; -. DR PDBsum; 1YD1; -. DR PDBsum; 1YD2; -. DR PDBsum; 1YD3; -. DR PDBsum; 1YD4; -. DR PDBsum; 1YD5; -. DR PDBsum; 2NRR; -. DR PDBsum; 2NRT; -. DR PDBsum; 2NRV; -. DR PDBsum; 2NRW; -. DR PDBsum; 2NRX; -. DR PDBsum; 2NRZ; -. DR ProteinModelPortal; Q9WYA3; -. DR SMR; Q9WYA3; 1-89, 340-557. DR STRING; 243274.TM0265; -. DR EnsemblBacteria; AAD35353; AAD35353; TM_0265. DR GeneID; 897176; -. DR KEGG; tma:TM0265; -. DR PATRIC; 23935407; VBITheMar51294_0269. DR eggNOG; ENOG4105CII; Bacteria. DR eggNOG; COG0322; LUCA. DR InParanoid; Q9WYA3; -. DR KO; K03703; -. DR OMA; LFPIRQC; -. DR OrthoDB; EOG6K13R9; -. DR EvolutionaryTrace; Q9WYA3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1440.10; -; 1. DR Gene3D; 4.10.860.10; -; 1. DR HAMAP; MF_00203; UvrC; 1. DR InterPro; IPR027299; GIY-YIG_dom. DR InterPro; IPR000305; GIY-YIG_SF. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR001943; UVR_dom. DR InterPro; IPR004791; UvrC. DR InterPro; IPR001162; UvrC_homol_region. DR Pfam; PF01541; GIY-YIG; 1. DR Pfam; PF02151; UVR; 1. DR Pfam; PF08459; UvrC_HhH_N; 1. DR SMART; SM00465; GIYc; 1. DR SUPFAM; SSF46600; SSF46600; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF82771; SSF82771; 1. DR TIGRFAMs; TIGR00194; uvrC; 1. DR PROSITE; PS50164; GIY_YIG; 1. DR PROSITE; PS50151; UVR; 1. DR PROSITE; PS50165; UVRC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; DNA damage; DNA excision; KW DNA repair; Excision nuclease; Reference proteome; SOS response. FT CHAIN 1 557 UvrABC system protein C. FT /FTId=PRO_0000138354. FT DOMAIN 14 89 GIY-YIG. {ECO:0000255|HAMAP- FT Rule:MF_00203}. FT DOMAIN 194 229 UVR. {ECO:0000255|HAMAP-Rule:MF_00203}. FT HELIX 3 11 {ECO:0000244|PDB:1YD0}. FT STRAND 17 23 {ECO:0000244|PDB:1YD0}. FT STRAND 26 35 {ECO:0000244|PDB:1YD0}. FT HELIX 36 41 {ECO:0000244|PDB:1YD0}. FT HELIX 42 44 {ECO:0000244|PDB:1YD0}. FT HELIX 49 57 {ECO:0000244|PDB:1YD0}. FT STRAND 59 65 {ECO:0000244|PDB:1YD0}. FT HELIX 69 83 {ECO:0000244|PDB:1YD0}. FT HELIX 346 353 {ECO:0000244|PDB:2NRR}. FT STRAND 362 369 {ECO:0000244|PDB:2NRR}. FT TURN 372 374 {ECO:0000244|PDB:2NRT}. FT STRAND 376 384 {ECO:0000244|PDB:2NRR}. FT HELIX 390 392 {ECO:0000244|PDB:2NRR}. FT STRAND 394 398 {ECO:0000244|PDB:2NRR}. FT HELIX 405 417 {ECO:0000244|PDB:2NRR}. FT STRAND 424 430 {ECO:0000244|PDB:2NRR}. FT HELIX 432 444 {ECO:0000244|PDB:2NRR}. FT STRAND 451 454 {ECO:0000244|PDB:2NRR}. FT TURN 456 458 {ECO:0000244|PDB:2NRT}. FT STRAND 461 463 {ECO:0000244|PDB:2NRR}. FT STRAND 466 468 {ECO:0000244|PDB:2NRR}. FT HELIX 475 492 {ECO:0000244|PDB:2NRR}. FT HELIX 493 495 {ECO:0000244|PDB:2NRT}. FT HELIX 496 508 {ECO:0000244|PDB:2NRT}. FT STRAND 511 513 {ECO:0000244|PDB:2NRW}. FT HELIX 516 526 {ECO:0000244|PDB:2NRT}. FT HELIX 529 533 {ECO:0000244|PDB:2NRT}. FT HELIX 537 544 {ECO:0000244|PDB:2NRT}. FT HELIX 547 556 {ECO:0000244|PDB:2NRT}. SQ SEQUENCE 557 AA; 64821 MW; 16B7F10C99212892 CRC64; MKEKIRKKIL LAPEEPGVYI FKNKGVPIYI GKAKRLSNRL RSYLNPQTEK VFRIGEEADE LETIVVMNER EAFILEANLI KKYRPKYNVR LKDTDFYPYI RISDDEIPYV EIVKRKLWDG TYFGPYTSVQ FVRNLLEILQ KIMGFRTCKS DLKRIKRPCF LYHLGRCIGP CIGNIESHEE AIRKLREFLS GNMEEVFDYL KEKMETHSKM LDFENAAKYR DLLLNLSNVL ESQGVVFEEN INCDVLVHAH DLFVVLRVRN GYLVGKISFE MEGGNVEDFI REYYISGRGD IPKTLILESD LDEMDYSSLG FEYVGPPRST TEEDLLEKAK KNLENELKMR GLRKEALEEL MKLLNMKDFP YRIEGIDISH LQGKYTVASL VVFEDGFPKK GDYRRYKIEQ DHPDDYESIR TVVKRRYSKH PLPNLLFVDG GIGQVNAAIE ALKEIGKDCP VVGLAKKEET VVFENREIHL PHDHPVLRLL VQIRDETHRF AVSYHRKRRE KESLRSVLDN VPGIGPIRKK KLIEHFGSLE NIRSASLEEI ARVIGSTEIA RRVLDIL // ID UVRA_THEMA Reviewed; 916 AA. AC Q9WYV0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 125. DE RecName: Full=UvrABC system protein A {ECO:0000255|HAMAP-Rule:MF_00205}; DE Short=UvrA protein {ECO:0000255|HAMAP-Rule:MF_00205}; DE AltName: Full=Excinuclease ABC subunit A {ECO:0000255|HAMAP-Rule:MF_00205}; GN Name=uvrA {ECO:0000255|HAMAP-Rule:MF_00205}; GN OrderedLocusNames=TM_0480; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. UvrA is an ATPase and a DNA-binding CC protein. A damage recognition complex composed of 2 UvrA and 2 CC UvrB subunits scans DNA for abnormalities. When the presence of a CC lesion has been verified by UvrB, the UvrA molecules dissociate. CC {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for CC lesions. {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA CC family. {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|HAMAP-Rule:MF_00205}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35564.1; -; Genomic_DNA. DR PIR; H72372; H72372. DR RefSeq; NP_228290.1; NC_000853.1. DR RefSeq; WP_004081486.1; NZ_CP011107.1. DR PDB; 3PIH; X-ray; 2.90 A; A=1-916. DR PDBsum; 3PIH; -. DR ProteinModelPortal; Q9WYV0; -. DR SMR; Q9WYV0; 1-916. DR DIP; DIP-59073N; -. DR STRING; 243274.TM0480; -. DR EnsemblBacteria; AAD35564; AAD35564; TM_0480. DR GeneID; 897514; -. DR KEGG; tma:TM0480; -. DR PATRIC; 23935859; VBITheMar51294_0487. DR eggNOG; ENOG4105C5U; Bacteria. DR eggNOG; COG0178; LUCA. DR InParanoid; Q9WYV0; -. DR KO; K03701; -. DR OMA; GAIKGWD; -. DR OrthoDB; EOG6QK4PS; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1490.20; -; 2. DR Gene3D; 3.40.50.300; -; 4. DR HAMAP; MF_00205; UvrA; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004602; UvrA. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00630; uvra; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; DNA damage; KW DNA excision; DNA repair; DNA-binding; Excision nuclease; KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat; KW SOS response; Zinc; Zinc-finger. FT CHAIN 1 916 UvrABC system protein A. FT /FTId=PRO_0000093107. FT DOMAIN 308 566 ABC transporter 1. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT DOMAIN 586 913 ABC transporter 2. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT NP_BIND 31 38 ATP. {ECO:0000255|HAMAP-Rule:MF_00205}. FT ZN_FING 252 279 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT NP_BIND 617 624 ATP. {ECO:0000255|HAMAP-Rule:MF_00205}. FT ZN_FING 716 742 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT STRAND 3 9 {ECO:0000244|PDB:3PIH}. FT STRAND 20 22 {ECO:0000244|PDB:3PIH}. FT STRAND 25 32 {ECO:0000244|PDB:3PIH}. FT STRAND 35 37 {ECO:0000244|PDB:3PIH}. FT HELIX 38 41 {ECO:0000244|PDB:3PIH}. FT TURN 42 44 {ECO:0000244|PDB:3PIH}. FT HELIX 45 54 {ECO:0000244|PDB:3PIH}. FT STRAND 74 77 {ECO:0000244|PDB:3PIH}. FT STRAND 82 85 {ECO:0000244|PDB:3PIH}. FT HELIX 98 101 {ECO:0000244|PDB:3PIH}. FT HELIX 104 114 {ECO:0000244|PDB:3PIH}. FT STRAND 117 119 {ECO:0000244|PDB:3PIH}. FT TURN 121 123 {ECO:0000244|PDB:3PIH}. FT HELIX 132 142 {ECO:0000244|PDB:3PIH}. FT STRAND 148 152 {ECO:0000244|PDB:3PIH}. FT STRAND 206 209 {ECO:0000244|PDB:3PIH}. FT HELIX 212 214 {ECO:0000244|PDB:3PIH}. FT HELIX 215 229 {ECO:0000244|PDB:3PIH}. FT STRAND 231 237 {ECO:0000244|PDB:3PIH}. FT TURN 238 240 {ECO:0000244|PDB:3PIH}. FT STRAND 243 249 {ECO:0000244|PDB:3PIH}. FT TURN 253 255 {ECO:0000244|PDB:3PIH}. FT HELIX 264 267 {ECO:0000244|PDB:3PIH}. FT TURN 272 274 {ECO:0000244|PDB:3PIH}. FT TURN 277 281 {ECO:0000244|PDB:3PIH}. FT STRAND 282 288 {ECO:0000244|PDB:3PIH}. FT HELIX 306 308 {ECO:0000244|PDB:3PIH}. FT HELIX 312 322 {ECO:0000244|PDB:3PIH}. FT TURN 323 325 {ECO:0000244|PDB:3PIH}. FT HELIX 342 346 {ECO:0000244|PDB:3PIH}. FT HELIX 354 363 {ECO:0000244|PDB:3PIH}. FT HELIX 371 376 {ECO:0000244|PDB:3PIH}. FT STRAND 379 383 {ECO:0000244|PDB:3PIH}. FT TURN 385 387 {ECO:0000244|PDB:3PIH}. FT HELIX 396 398 {ECO:0000244|PDB:3PIH}. FT STRAND 399 401 {ECO:0000244|PDB:3PIH}. FT HELIX 406 411 {ECO:0000244|PDB:3PIH}. FT HELIX 414 422 {ECO:0000244|PDB:3PIH}. FT TURN 428 433 {ECO:0000244|PDB:3PIH}. FT HELIX 434 449 {ECO:0000244|PDB:3PIH}. FT TURN 450 452 {ECO:0000244|PDB:3PIH}. FT HELIX 462 464 {ECO:0000244|PDB:3PIH}. FT HELIX 467 480 {ECO:0000244|PDB:3PIH}. FT STRAND 487 491 {ECO:0000244|PDB:3PIH}. FT TURN 493 496 {ECO:0000244|PDB:3PIH}. FT HELIX 499 501 {ECO:0000244|PDB:3PIH}. FT HELIX 502 511 {ECO:0000244|PDB:3PIH}. FT TURN 512 516 {ECO:0000244|PDB:3PIH}. FT STRAND 518 522 {ECO:0000244|PDB:3PIH}. FT HELIX 526 530 {ECO:0000244|PDB:3PIH}. FT STRAND 533 542 {ECO:0000244|PDB:3PIH}. FT HELIX 543 545 {ECO:0000244|PDB:3PIH}. FT STRAND 547 553 {ECO:0000244|PDB:3PIH}. FT HELIX 555 560 {ECO:0000244|PDB:3PIH}. FT HELIX 566 572 {ECO:0000244|PDB:3PIH}. FT STRAND 573 575 {ECO:0000244|PDB:3PIH}. FT STRAND 587 595 {ECO:0000244|PDB:3PIH}. FT STRAND 602 616 {ECO:0000244|PDB:3PIH}. FT HELIX 623 629 {ECO:0000244|PDB:3PIH}. FT HELIX 631 640 {ECO:0000244|PDB:3PIH}. FT STRAND 650 653 {ECO:0000244|PDB:3PIH}. FT HELIX 655 657 {ECO:0000244|PDB:3PIH}. FT STRAND 660 664 {ECO:0000244|PDB:3PIH}. FT HELIX 677 680 {ECO:0000244|PDB:3PIH}. FT HELIX 683 691 {ECO:0000244|PDB:3PIH}. FT HELIX 695 699 {ECO:0000244|PDB:3PIH}. FT HELIX 704 707 {ECO:0000244|PDB:3PIH}. FT TURN 712 714 {ECO:0000244|PDB:3PIH}. FT TURN 717 721 {ECO:0000244|PDB:3PIH}. FT STRAND 722 727 {ECO:0000244|PDB:3PIH}. FT STRAND 735 738 {ECO:0000244|PDB:3PIH}. FT TURN 740 744 {ECO:0000244|PDB:3PIH}. FT HELIX 751 753 {ECO:0000244|PDB:3PIH}. FT HELIX 761 765 {ECO:0000244|PDB:3PIH}. FT STRAND 766 768 {ECO:0000244|PDB:3PIH}. FT HELIX 769 775 {ECO:0000244|PDB:3PIH}. FT TURN 776 778 {ECO:0000244|PDB:3PIH}. FT HELIX 780 791 {ECO:0000244|PDB:3PIH}. FT HELIX 794 796 {ECO:0000244|PDB:3PIH}. FT HELIX 808 820 {ECO:0000244|PDB:3PIH}. FT STRAND 826 834 {ECO:0000244|PDB:3PIH}. FT TURN 835 838 {ECO:0000244|PDB:3PIH}. FT HELIX 841 856 {ECO:0000244|PDB:3PIH}. FT STRAND 860 864 {ECO:0000244|PDB:3PIH}. FT HELIX 868 871 {ECO:0000244|PDB:3PIH}. FT STRAND 875 884 {ECO:0000244|PDB:3PIH}. FT HELIX 885 887 {ECO:0000244|PDB:3PIH}. FT STRAND 890 896 {ECO:0000244|PDB:3PIH}. FT HELIX 897 901 {ECO:0000244|PDB:3PIH}. FT HELIX 907 912 {ECO:0000244|PDB:3PIH}. FT TURN 913 915 {ECO:0000244|PDB:3PIH}. SQ SEQUENCE 916 AA; 102967 MW; 54FBAA620783791A CRC64; MNEIVVKGAR VHNLKNITVR IPKNRLVVIT GVSGSGKSSL AMDTIYAEGQ RRYLESLSTY ARQFLGNLKK PDVDEIEGLS PAIAIDQKTV SHNPRSTVGT VTEIYDYLRV LYARIGKAHC PECGRPLEKK SIDEILQDLF NSFKEGSRIY ILAPVATEKK GTFKKEIEEF ISKGFARIEI DGEIYRLEEV PELDKNKRHT VKLVVDRLIL ETRNEHRILD SLELAMREGK GFVEIRNVDT GESKIFSENL MCPVCGIGFP EITPKLFSFN SPYGACPNCH GLGFTFEVDP SLVIDEEKSV LEGAIIPYRW DRRLSRWVAR EIEKRGVSPH LPFKDLPEDV KEFILYGDDR FEGVVPKVQR WHRETESPEM KEWLEKNFIV QRTCSVCGGR RLNREALSVK INGLNIHEFT ELSISEELEF LKNLNLTERE REIVGELLKE IEKRLEFLVD VGLEYLTLSR SATTLSGGES QRIRLATQIG SGLTGVIYVL DEPTIGLHPR DTERLIKTLK KLRDLGNTVI VVEHDEEVIR NADHIIDIGP GGGTNGGRVV FQGTVDELLK NPDSSLTGEY LSGKRKITVN KTRRLPYASL KIKGVRHNNL KNIDVEIPLG VFVCVTGVSG SGKSSLVMET LYPALMNLLH KTKLPAGEFD SIEGHENIDK MIAIDQSPIG RTPRSNPATY TKVFDEIRSL FAMTPAAKAR GYNKSRFSFN LKGGRCEACQ GQGYVKIEML FLPDVYVECD VCKGKRYNRE TLEITYKGKN ISDILDMTVD EALEFFKNIP SIKRTLQVLH DVGLGYVKLG QPATTLSGGE AQRIKLASEL RKRDTGRTLY ILDEPTVGLH FEDVRKLVEV LHRLVDRGNT VIVIEHNLDV IKNADHIIDL GPEGGKEGGY IVATGTPEEI AKNPHSYTGR FLKNVL // ID UXAC_THEMA Reviewed; 451 AA. AC Q9WXR9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=Uronate isomerase; DE EC=5.3.1.12; DE AltName: Full=Glucuronate isomerase; DE AltName: Full=Uronic isomerase; GN Name=uxaC; OrderedLocusNames=TM_0064; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS). RX PubMed=12945057; DOI=10.1002/prot.10462; RA Schwarzenbacher R., Canaves J.M., Brinen L.S., Dai X., Deacon A.M., RA Elsliger M.-A., Eshaghi S., Floyd R., Godzik A., Grittini C., RA Grzechnik S.K., Guda C., Jaroszewski L., Karlak C., Klock H.E., RA Koesema E., Kovarik J.S., Kreusch A., Kuhn P., Lesley S.A., RA McMullan D., McPhillips T.M., Miller M.A., Miller M.D., Morse A., RA Moy K., Ouyang J., Robb A., Rodrigues K., Selby T.L., Spraggon G., RA Stevens R.C., van den Bedem H., Velasquez J., Vincent J., Wang X., RA West B., Wolf G., Hodgson K.O., Wooley J., Wilson I.A.; RT "Crystal structure of uronate isomerase (TM0064) from Thermotoga RT maritima at 2.85 A resolution."; RL Proteins 53:142-145(2003). CC -!- CATALYTIC ACTIVITY: D-glucuronate = D-fructuronate. CC -!- CATALYTIC ACTIVITY: D-galacturonate = D-tagaturonate. CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate CC interconversion. CC -!- SUBUNIT: Homotrimer. CC -!- SIMILARITY: Belongs to the uronate isomerase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35158.1; -; Genomic_DNA. DR PIR; D72422; D72422. DR RefSeq; NP_227880.1; NC_000853.1. DR RefSeq; WP_004082556.1; NZ_CP011107.1. DR PDB; 1J5S; X-ray; 2.85 A; A/B/C=1-451. DR PDBsum; 1J5S; -. DR ProteinModelPortal; Q9WXR9; -. DR SMR; Q9WXR9; 1-450. DR STRING; 243274.TM0064; -. DR EnsemblBacteria; AAD35158; AAD35158; TM_0064. DR GeneID; 896888; -. DR KEGG; tma:TM0064; -. DR PATRIC; 23934968; VBITheMar51294_0062. DR eggNOG; ENOG4105D2H; Bacteria. DR eggNOG; COG1904; LUCA. DR InParanoid; Q9WXR9; -. DR KO; K01812; -. DR OMA; GHTDPRW; -. DR OrthoDB; EOG6J1D95; -. DR BioCyc; MetaCyc:MONOMER-17959; -. DR UniPathway; UPA00246; -. DR EvolutionaryTrace; Q9WXR9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008880; F:glucuronate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro. DR Gene3D; 1.10.2020.10; -; 1. DR HAMAP; MF_00675; UxaC; 1. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR003766; Uronate_isomerase. DR InterPro; IPR023177; Uronate_isomerase_dom2. DR Pfam; PF02614; UxaC; 1. DR SUPFAM; SSF51556; SSF51556; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isomerase; Reference proteome. FT CHAIN 1 451 Uronate isomerase. FT /FTId=PRO_0000172789. FT TURN 5 8 {ECO:0000244|PDB:1J5S}. FT HELIX 12 21 {ECO:0000244|PDB:1J5S}. FT STRAND 26 29 {ECO:0000244|PDB:1J5S}. FT HELIX 35 40 {ECO:0000244|PDB:1J5S}. FT HELIX 47 51 {ECO:0000244|PDB:1J5S}. FT TURN 52 54 {ECO:0000244|PDB:1J5S}. FT HELIX 56 64 {ECO:0000244|PDB:1J5S}. FT HELIX 69 71 {ECO:0000244|PDB:1J5S}. FT STRAND 74 76 {ECO:0000244|PDB:1J5S}. FT HELIX 78 88 {ECO:0000244|PDB:1J5S}. FT HELIX 89 92 {ECO:0000244|PDB:1J5S}. FT HELIX 96 108 {ECO:0000244|PDB:1J5S}. FT HELIX 117 130 {ECO:0000244|PDB:1J5S}. FT HELIX 136 142 {ECO:0000244|PDB:1J5S}. FT STRAND 145 149 {ECO:0000244|PDB:1J5S}. FT HELIX 159 167 {ECO:0000244|PDB:1J5S}. FT STRAND 172 174 {ECO:0000244|PDB:1J5S}. FT HELIX 180 183 {ECO:0000244|PDB:1J5S}. FT HELIX 190 201 {ECO:0000244|PDB:1J5S}. FT HELIX 208 223 {ECO:0000244|PDB:1J5S}. FT TURN 224 226 {ECO:0000244|PDB:1J5S}. FT STRAND 229 236 {ECO:0000244|PDB:1J5S}. FT HELIX 244 254 {ECO:0000244|PDB:1J5S}. FT TURN 255 257 {ECO:0000244|PDB:1J5S}. FT HELIX 262 283 {ECO:0000244|PDB:1J5S}. FT STRAND 286 291 {ECO:0000244|PDB:1J5S}. FT HELIX 299 304 {ECO:0000244|PDB:1J5S}. FT STRAND 307 310 {ECO:0000244|PDB:1J5S}. FT HELIX 320 330 {ECO:0000244|PDB:1J5S}. FT TURN 332 334 {ECO:0000244|PDB:1J5S}. FT STRAND 337 343 {ECO:0000244|PDB:1J5S}. FT HELIX 344 346 {ECO:0000244|PDB:1J5S}. FT HELIX 347 356 {ECO:0000244|PDB:1J5S}. FT STRAND 360 362 {ECO:0000244|PDB:1J5S}. FT HELIX 372 383 {ECO:0000244|PDB:1J5S}. FT HELIX 388 390 {ECO:0000244|PDB:1J5S}. FT HELIX 403 424 {ECO:0000244|PDB:1J5S}. FT HELIX 430 441 {ECO:0000244|PDB:1J5S}. FT HELIX 443 449 {ECO:0000244|PDB:1J5S}. SQ SEQUENCE 451 AA; 52306 MW; FC0B3221F740B927 CRC64; MFLGEDYLLT NRAAVRLFNE VKDLPIVDPH NHLDAKDIVE NKPWNDIWEV EGATDHYVWE LMRRCGVSEE YITGSRSNKE KWLALAKVFP RFVGNPTYEW IHLDLWRRFN IKKVISEETA EEIWEETKKK LPEMTPQKLL RDMKVEILCT TDDPVSTLEH HRKAKEAVEG VTILPTWRPD RAMNVDKEGW REYVEKMGER YGEDTSTLDG FLNALWKSHE HFKEHGCVAS DHALLEPSVY YVDENRARAV HEKAFSGEKL TQDEINDYKA FMMVQFGKMN QETNWVTQLH IGALRDYRDS LFKTLGPDSG GDISTNFLRI AEGLRYFLNE FDGKLKIVLY VLDPTHLPTI STIARAFPNV YVGAPWWFND SPFGMEMHLK YLASVDLLYN LAGMVTDSRK LLSFGSRTEM FRRVLSNVVG EMVEKGQIPI KEARELVKHV SYDGPKALFF G // ID UVRB_THEMA Reviewed; 664 AA. AC Q9X282; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 117. DE RecName: Full=UvrABC system protein B {ECO:0000255|HAMAP-Rule:MF_00204}; DE Short=Protein UvrB {ECO:0000255|HAMAP-Rule:MF_00204}; DE AltName: Full=Excinuclease ABC subunit B {ECO:0000255|HAMAP-Rule:MF_00204}; GN Name=uvrB {ECO:0000255|HAMAP-Rule:MF_00204}; GN OrderedLocusNames=TM_1761; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. A damage recognition complex composed CC of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon CC binding of the UvrA(2)B(2) complex to a putative damaged site, the CC DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP CC binding by UvrB and probably causes local melting of the DNA CC helix, facilitating insertion of UvrB beta-hairpin between the DNA CC strands. Then UvrB probes one DNA strand for the presence of a CC lesion. If a lesion is found the UvrA subunits dissociate and the CC UvrB-DNA preincision complex is formed. This complex is CC subsequently bound by UvrC and the second UvrB is released. If no CC lesion is found, the DNA wraps around the other UvrB subunit that CC will check the other stand for damage. {ECO:0000255|HAMAP- CC Rule:MF_00204}. CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for CC lesions. Interacts with UvrC in an incision complex. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000255|HAMAP- CC Rule:MF_00204}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SIMILARITY: Contains 1 UVR domain. {ECO:0000255|HAMAP- CC Rule:MF_00204}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36825.1; -; Genomic_DNA. DR PIR; A72215; A72215. DR RefSeq; NP_229558.1; NC_000853.1. DR RefSeq; WP_004082307.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X282; -. DR SMR; Q9X282; 2-588. DR STRING; 243274.TM1761; -. DR EnsemblBacteria; AAD36825; AAD36825; TM_1761. DR GeneID; 897857; -. DR KEGG; tma:TM1761; -. DR PATRIC; 23938502; VBITheMar51294_1780. DR eggNOG; ENOG4105CCW; Bacteria. DR eggNOG; COG0556; LUCA. DR InParanoid; Q9X282; -. DR KO; K03702; -. DR OMA; QEYVDRM; -. DR OrthoDB; EOG6B360R; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 4. DR Gene3D; 4.10.860.10; -; 1. DR HAMAP; MF_00204; UvrB; 1. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001943; UVR_dom. DR InterPro; IPR004807; UvrB. DR InterPro; IPR024759; UvrB_YAD/RRR_dom. DR PANTHER; PTHR24029; PTHR24029; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF04851; ResIII; 1. DR Pfam; PF02151; UVR; 1. DR Pfam; PF12344; UvrB; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF46600; SSF46600; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00631; uvrb; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50151; UVR; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA excision; KW DNA repair; Excision nuclease; Nucleotide-binding; Reference proteome; KW SOS response. FT CHAIN 1 664 UvrABC system protein B. FT /FTId=PRO_0000138439. FT DOMAIN 23 412 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00204}. FT DOMAIN 429 588 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_00204}. FT DOMAIN 622 657 UVR. {ECO:0000255|HAMAP-Rule:MF_00204}. FT NP_BIND 36 43 ATP. {ECO:0000255|HAMAP-Rule:MF_00204}. FT MOTIF 89 112 Beta-hairpin. SQ SEQUENCE 664 AA; 76684 MW; 7DF847C942D1EAC9 CRC64; MFKLVSEFEP TGDQPQAIEK LVEGLNRGMR FQTLLGVTGS GKTFTMANVI ARVNRPALVI SPNKTLAAQL YQEFKTFFPE NRVEFFISYY DYYQPEAYIP TKDLYIEKNA DINDVIVRMR MSTLKSVRTR RDVVVVASVS CIYATGDPND FDRMNINLAV GDRIDVLELA ERLARIGYQR TEDVSLSGCF RLKGDTVEIY PTYQDEGIRI EFFGDEVDSI TLIDRFNRTT LEHLDKIIIY PAVEFITTEE KLKRAVESIR EELNERLSEL KKQGKILEYE RLKQRTLNDI ELLETMGYCP GIENYSRHFD GRKPGEPPYT LLDYFDKDFI VFIDESHITV PQLRAMYNGD RSRKKNLVEY GFRLPSAYDN RPLTFEEFLK KTGQIIFVSA TPGDFELSIS EQVVEQIIRP TGLVDPEVEV RPTAGQVDDL VNEIVKVKER GERALVTVLT KKTAELLSEH LTELGIRSLY LHSELDAIER VEVLKKLRRG DVDVVVGVNL LREGLDLPEV SLVAIMDADV EGFLRSETTL IQIIGRTARN VNGKVIMYAD RITNAMKRAI EETNRRRRIQ LEYNRKHGIT PRSVIKPLEI EVFEQFMVKE EPERYGDTVK NIFEMKKTLS PEEYMAVLEE EMYRAASELR YEDAAALRDE LFRIREEIKK KKGL // ID XYLA_THEMA Reviewed; 444 AA. AC Q9X1Z5; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 109. DE RecName: Full=Xylose isomerase {ECO:0000255|HAMAP-Rule:MF_00455}; DE EC=5.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00455}; GN Name=xylA {ECO:0000255|HAMAP-Rule:MF_00455}; GN OrderedLocusNames=TM_1667; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: D-xylopyranose = D-xylulose. CC {ECO:0000255|HAMAP-Rule:MF_00455}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00455}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00455}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00455}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00455}. CC -!- SIMILARITY: Belongs to the xylose isomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00455}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36734.1; -; Genomic_DNA. DR PIR; A72225; A72225. DR RefSeq; NP_229467.1; NC_000853.1. DR RefSeq; WP_004082185.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1Z5; -. DR SMR; Q9X1Z5; 2-444. DR STRING; 243274.TM1667; -. DR PRIDE; Q9X1Z5; -. DR EnsemblBacteria; AAD36734; AAD36734; TM_1667. DR GeneID; 897906; -. DR KEGG; tma:TM1667; -. DR PATRIC; 23938308; VBITheMar51294_1686. DR eggNOG; ENOG4105C93; Bacteria. DR eggNOG; COG2115; LUCA. DR InParanoid; Q9X1Z5; -. DR KO; K01805; -. DR OMA; HTFQHEL; -. DR OrthoDB; EOG62NX4R; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009045; F:xylose isomerase activity; IBA:GO_Central. DR GO; GO:0042843; P:D-xylose catabolic process; IBA:GO_Central. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.150; -; 1. DR HAMAP; MF_00455; Xylose_isom_A; 1. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR InterPro; IPR013452; Xylose_isom_bac. DR InterPro; IPR001998; Xylose_isomerase. DR Pfam; PF01261; AP_endonuc_2; 1. DR PRINTS; PR00688; XYLOSISMRASE. DR SUPFAM; SSF51658; SSF51658; 1. DR TIGRFAMs; TIGR02630; xylose_isom_A; 1. DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase; KW Magnesium; Metal-binding; Pentose shunt; Reference proteome; KW Xylose metabolism. FT CHAIN 1 444 Xylose isomerase. FT /FTId=PRO_0000195813. FT ACT_SITE 101 101 {ECO:0000255|HAMAP-Rule:MF_00455}. FT ACT_SITE 104 104 {ECO:0000255|HAMAP-Rule:MF_00455}. FT METAL 232 232 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00455}. FT METAL 268 268 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00455}. FT METAL 268 268 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00455}. FT METAL 271 271 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00455}. FT METAL 296 296 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00455}. FT METAL 307 307 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00455}. FT METAL 309 309 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00455}. FT METAL 339 339 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00455}. SQ SEQUENCE 444 AA; 50835 MW; E18F92E67600F53A CRC64; MAEFFPEIPK IQFEGKESTN PLAFRFYDPN EVIDGKPLKD HLKFSVAFWH TFVNEGRDPF GDPTAERPWN RFSDPMDKAF ARVDALFEFC EKLNIEYFCF HDRDIAPEGK TLRETNKILD KVVERIKERM KDSNVKLLWG TANLFSHPRY MHGAATTCSA DVFAYAAAQV KKALEITKEL GGEGYVFWGG REGYETLLNT DLGLELENLA RFLRMAVEYA KKIGFTGQFL IEPKPKEPTK HQYDFDVATA YAFLKNHGLD EYFKFNIEAN HATLAGHTFQ HELRMARILG KLGSIDANQG DLLLGWDTDQ FPTNIYDTTL AMYEVIKAGG FTKGGLNFDA KVRRASYKVE DLFIGHIAGM DTFALGFKIA YKLAKDGVFD KFIEEKYRSF KEGIGKEIVE GKTDFEKLEE YIIDKEDIEL PSGKQEYLES LLNSYIVKTI AELR // ID Y1081_THEMA Reviewed; 113 AA. AC Q9X0H0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Putative anti-sigma factor antagonist TM_1081; GN OrderedLocusNames=TM_1081; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: In the phosphorylated form it could act as an anti-anti- CC sigma factor that counteracts an anti-sigma factor and thus CC releases a sigma factor from inhibition. {ECO:0000250}. CC -!- PTM: Phosphorylated on a serine residue. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the anti-sigma-factor antagonist family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 STAS domain. {ECO:0000255|PROSITE- CC ProRule:PRU00198}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36158.1; -; Genomic_DNA. DR PIR; A72297; A72297. DR RefSeq; NP_228887.1; NC_000853.1. DR RefSeq; WP_004080402.1; NZ_CP011107.1. DR PDB; 2KA5; NMR; -; A=1-113. DR PDB; 3F43; X-ray; 1.59 A; A=1-113. DR PDBsum; 2KA5; -. DR PDBsum; 3F43; -. DR ProteinModelPortal; Q9X0H0; -. DR STRING; 243274.TM1081; -. DR EnsemblBacteria; AAD36158; AAD36158; TM_1081. DR GeneID; 897065; -. DR KEGG; tma:TM1081; -. DR PATRIC; 23937091; VBITheMar51294_1094. DR eggNOG; ENOG410682B; Bacteria. DR eggNOG; ENOG410XUXE; LUCA. DR InParanoid; Q9X0H0; -. DR OMA; VVILMPN; -. DR OrthoDB; EOG6J48NK; -. DR EvolutionaryTrace; Q9X0H0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 3.30.750.24; -; 1. DR InterPro; IPR003658; Anti-sigma_ant. DR InterPro; IPR002645; STAS_dom. DR Pfam; PF01740; STAS; 1. DR SUPFAM; SSF52091; SSF52091; 1. DR TIGRFAMs; TIGR00377; ant_ant_sig; 1. DR PROSITE; PS50801; STAS; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Phosphoprotein; Reference proteome. FT CHAIN 1 113 Putative anti-sigma factor antagonist FT TM_1081. FT /FTId=PRO_0000194206. FT DOMAIN 1 110 STAS. {ECO:0000255|PROSITE- FT ProRule:PRU00198}. FT MOD_RES 55 55 Phosphoserine. {ECO:0000250}. FT STRAND 4 7 {ECO:0000244|PDB:3F43}. FT STRAND 10 13 {ECO:0000244|PDB:3F43}. FT TURN 21 23 {ECO:0000244|PDB:3F43}. FT HELIX 24 34 {ECO:0000244|PDB:3F43}. FT HELIX 36 38 {ECO:0000244|PDB:3F43}. FT STRAND 42 46 {ECO:0000244|PDB:3F43}. FT HELIX 55 71 {ECO:0000244|PDB:3F43}. FT STRAND 74 78 {ECO:0000244|PDB:3F43}. FT HELIX 82 90 {ECO:0000244|PDB:3F43}. FT HELIX 93 95 {ECO:0000244|PDB:3F43}. FT STRAND 97 102 {ECO:0000244|PDB:3F43}. FT HELIX 103 111 {ECO:0000244|PDB:3F43}. SQ SEQUENCE 113 AA; 12973 MW; 88603AF80637DA4E CRC64; MFPYKIVDDV VILMPNKELN IENAHLFKKW VFDEFLNKGY NKIFLVLSDV ESIDSFSLGV IVNILKSISS SGGFFALVSP NEKVERVLSL TNLDRIVKIY DTISEAMEEV RRK // ID XYNA_THEMA Reviewed; 1059 AA. AC Q60037; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 128. DE RecName: Full=Endo-1,4-beta-xylanase A; DE Short=Xylanase A; DE EC=3.2.1.8; DE AltName: Full=1,4-beta-D-xylan xylanohydrolase A; DE Flags: Precursor; GN Name=xynA; OrderedLocusNames=TM_0061; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=7783614; DOI=10.1111/j.1365-2958.1995.tb02257.x; RA Winterhalter C., Heinrich P., Candussio A., Wich G., Liebl W.; RT "Identification of a novel cellulose-binding domain within the RT multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium RT Thermotoga maritima."; RL Mol. Microbiol. 15:431-444(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic CC linkages in xylans. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6.2.; CC Temperature dependence: CC Optimum temperature is 90 degrees Celsius. Thermostable.; CC -!- DOMAIN: The C-terminal CBM-CenC domains mediate the binding of CC XynA to microcrystalline cellulose. CBM-CenC 2 alone can also CC promote cellulose binding. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 CBM-cenC (cenC-type cellulose-binding) CC domains. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GH10 (glycosyl hydrolase family 10) domain. CC {ECO:0000255|PROSITE-ProRule:PRU01096}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z46264; CAA86406.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35155.1; -; Genomic_DNA. DR PIR; S61311; S61311. DR RefSeq; NP_227877.1; NC_000853.1. DR RefSeq; WP_004082550.1; NZ_CP011107.1. DR PDB; 1I82; X-ray; 1.90 A; A=871-1059. DR PDB; 1I8A; X-ray; 1.90 A; A=871-1059. DR PDB; 1I8U; X-ray; 1.90 A; A=871-1059. DR PDBsum; 1I82; -. DR PDBsum; 1I8A; -. DR PDBsum; 1I8U; -. DR ProteinModelPortal; Q60037; -. DR SMR; Q60037; 871-1059. DR STRING; 243274.TM0061; -. DR CAZy; CBM22; Carbohydrate-Binding Module Family 22. DR CAZy; CBM9; Carbohydrate-Binding Module Family 9. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR PRIDE; Q60037; -. DR EnsemblBacteria; AAD35155; AAD35155; TM_0061. DR GeneID; 896885; -. DR KEGG; tma:TM0061; -. DR PATRIC; 23934962; VBITheMar51294_0059. DR eggNOG; ENOG4105D9F; Bacteria. DR eggNOG; COG3693; LUCA. DR InParanoid; Q60037; -. DR KO; K01181; -. DR OMA; QNPTLEF; -. DR OrthoDB; EOG6B363F; -. DR BioCyc; MetaCyc:MONOMER-16897; -. DR BRENDA; 3.2.1.8; 6331. DR EvolutionaryTrace; Q60037; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.260; -; 2. DR Gene3D; 2.60.40.1190; -; 2. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR010502; Carb-bd_dom_fam9. DR InterPro; IPR003305; CenC_carb-bd. DR InterPro; IPR008979; Galactose-bd-like. DR InterPro; IPR001000; GH10. DR InterPro; IPR031158; GH10_AS. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF06452; CBM9_1; 2. DR Pfam; PF02018; CBM_4_9; 2. DR Pfam; PF00331; Glyco_hydro_10; 1. DR PRINTS; PR00134; GLHYDRLASE10. DR SMART; SM00633; Glyco_10; 1. DR SUPFAM; SSF49785; SSF49785; 2. DR SUPFAM; SSF51445; SSF51445; 1. DR PROSITE; PS00591; GH10_1; 1. DR PROSITE; PS51760; GH10_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Complete proteome; Glycosidase; KW Hydrolase; Polysaccharide degradation; Reference proteome; Repeat; KW Signal; Xylan degradation. FT SIGNAL 1 30 {ECO:0000255}. FT CHAIN 31 1059 Endo-1,4-beta-xylanase A. FT /FTId=PRO_0000007986. FT DOMAIN 364 692 GH10. {ECO:0000255|PROSITE- FT ProRule:PRU01096}. FT DOMAIN 700 870 CBM-cenC 1. FT DOMAIN 871 1059 CBM-cenC 2. FT REGION 47 199 A-1. FT REGION 200 354 A-2. FT ACT_SITE 502 502 Proton donor. {ECO:0000250}. FT ACT_SITE 608 608 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU10061}. FT STRAND 872 877 {ECO:0000244|PDB:1I82}. FT STRAND 882 885 {ECO:0000244|PDB:1I82}. FT HELIX 888 892 {ECO:0000244|PDB:1I82}. FT STRAND 895 897 {ECO:0000244|PDB:1I82}. FT STRAND 900 904 {ECO:0000244|PDB:1I82}. FT TURN 906 908 {ECO:0000244|PDB:1I82}. FT STRAND 911 918 {ECO:0000244|PDB:1I82}. FT STRAND 920 930 {ECO:0000244|PDB:1I82}. FT STRAND 938 940 {ECO:0000244|PDB:1I82}. FT HELIX 941 943 {ECO:0000244|PDB:1I82}. FT STRAND 944 952 {ECO:0000244|PDB:1I82}. FT STRAND 965 971 {ECO:0000244|PDB:1I82}. FT STRAND 976 978 {ECO:0000244|PDB:1I82}. FT HELIX 984 986 {ECO:0000244|PDB:1I82}. FT STRAND 987 994 {ECO:0000244|PDB:1I82}. FT STRAND 997 1005 {ECO:0000244|PDB:1I82}. FT STRAND 1015 1026 {ECO:0000244|PDB:1I82}. FT STRAND 1032 1039 {ECO:0000244|PDB:1I82}. FT STRAND 1041 1043 {ECO:0000244|PDB:1I82}. FT TURN 1045 1047 {ECO:0000244|PDB:1I82}. FT HELIX 1049 1051 {ECO:0000244|PDB:1I82}. FT STRAND 1052 1058 {ECO:0000244|PDB:1I82}. SQ SEQUENCE 1059 AA; 119643 MW; 045936844A2D72E2 CRC64; MQVRKRRGLL DVSTAVLVGI LAGFLGVVLA ASGVLSFGKE ASSKGDSSLE TVLALSFEGT TEGVVPFGKD VVLTASQDVA ADGEYSLKVE NRTSPWDGVE IDLTGKVKSG ADYLLSFQVY QSSDAPQLFN VVARTEDEKG ERYDVILDKV VVSDHWKEIL VPFSPTFEGT PAKYSLIIVA SKNTNFNFYL DKVQVLAPKE SGPKVIYETS FENGVGDWQP RGDVNIEASS EVAHSGKSSL FISNRQKGWQ GAQINLKGIL KTGKTYAFEA WVYQNSGQDQ TIIMTMQRKY SSDASTQYEW IKSATVPSGQ WVQLSGTYTI PAGVTVEDLT LYFESQNPTL EFYVDDVKIV DTTSAEIKIE MEPEKEIPAL KEVLKDYFKV GVALPSKVFL NPKDIELITK HFNSITAENE MKPESLLAGI ENGKLKFRFE TADKYIQFVE ENGMVIRGHT LVWHNQTPDW FFKDENGNLL SKEAMTERLK EYIHTVVGHF KGKVYAWDVV NEAVDPNQPD GLRRSTWYQI MGPDYIELAF KFAREADPDA KLFYNDYNTF EPRKRDIIYN LVKDLKEKGL IDGIGMQCHI SLATDIKQIE EAIKKFSTIP GIEIHITELD MSVYRDSSSN YPEAPRTALI EQAHKMMQLF EIFKKYSNVI TNVTFWGLKD DYSWRATRRN DWPLIFDKDH QAKLAYWAIV APEVLPPLPK ESRISEGEAV VVGMMDDSYL MSKPIEILDE EGNVKATIRA VWKDSTIYIY GEVQDKTKKP AEDGVAIFIN PNNERTPYLQ PDDTYAVLWT NWKTEVNRED VQVKKFVGPG FRRYSFEMSI TIPGVEFKKD SYIGFDAAVI DDGKWYSWSD TTNSQKTNTM NYGTLKLEGI MVATAKYGTP VIDGEIDEIW NTTEEIETKA VAMGSLDKNA TAKVRVLWDE NYLYVLAIVK DPVLNKDNSN PWEQDSVEIF IDENNHKTGY YEDDDAQFRV NYMNEQTFGT GGSPARFKTA VKLIEGGYIV EAAIKWKTIK PTPNTVIGFN IQVNDANEKG QRVGIISWSD PTNNSWRDPS KFGNLRLIK // ID Y1311_THEMA Reviewed; 70 AA. AC Q9X137; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 78. DE RecName: Full=UPF0150 protein TM_1311; GN OrderedLocusNames=TM_1311; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0150 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36385.1; -; Genomic_DNA. DR PIR; A72271; A72271. DR RefSeq; NP_229115.1; NC_000853.1. DR RefSeq; WP_004079908.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X137; -. DR STRING; 243274.TM1311; -. DR EnsemblBacteria; AAD36385; AAD36385; TM_1311. DR GeneID; 898171; -. DR KEGG; tma:TM1311; -. DR PATRIC; 23937560; VBITheMar51294_1326. DR eggNOG; ENOG4105ZVY; Bacteria. DR eggNOG; ENOG411224B; LUCA. DR InParanoid; Q9X137; -. DR OMA; CHFGEEA; -. DR OrthoDB; EOG6GFGQ9; -. DR Proteomes; UP000008183; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 70 UPF0150 protein TM_1311. FT /FTId=PRO_0000157938. SQ SEQUENCE 70 AA; 8086 MW; 5FD2194F692568BD CRC64; METQKEIVFI AVESEDGGYI EKTERYSIFT QGDTWEELLE MIKDAVKCHF DEGAPKYVHA RFVKDVTIAV // ID Y1323_THEMA Reviewed; 60 AA. AC Q9WW67; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein TM_1323/TM_1333; GN OrderedLocusNames=TM_1323; GN and GN OrderedLocusNames=TM_1333; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36395.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36405.1; -; Genomic_DNA. DR PIR; A72268; A72268. DR RefSeq; NP_229125.1; NC_000853.1. DR RefSeq; NP_229135.1; NC_000853.1. DR RefSeq; WP_010865311.1; NC_000853.1. DR STRING; 243274.TM1333; -. DR EnsemblBacteria; AAD36395; AAD36395; TM_1323. DR EnsemblBacteria; AAD36405; AAD36405; TM_1333. DR GeneID; 898149; -. DR GeneID; 898159; -. DR KEGG; tma:TM1323; -. DR KEGG; tma:TM1333; -. DR KEGG; tmi:THEMA_07680; -. DR KEGG; tmi:THEMA_07730; -. DR OrthoDB; EOG6RC3W1; -. DR BioCyc; TMAR243274:GC6P-1354-MONOMER; -. DR BioCyc; TMAR243274:GC6P-1364-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 60 Uncharacterized protein TM_1323/TM_1333. FT /FTId=PRO_0000216219. SQ SEQUENCE 60 AA; 6589 MW; D733C38162F60142 CRC64; MIIFLILVLL STIIFADKVK TDNETHSWKS EITEQVQVAP KSAATCEVTF KGSTAGNQSF // ID Y1349_THEMA Reviewed; 338 AA. AC Q9X170; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=UPF0118 membrane protein TM_1349; GN OrderedLocusNames=TM_1349; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0118 (PerM) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36420.1; -; Genomic_DNA. DR PIR; E72264; E72264. DR RefSeq; NP_229150.1; NC_000853.1. DR RefSeq; WP_004081545.1; NZ_CP011107.1. DR STRING; 243274.TM1349; -. DR EnsemblBacteria; AAD36420; AAD36420; TM_1349. DR GeneID; 898131; -. DR KEGG; tma:TM1349; -. DR PATRIC; 23937636; VBITheMar51294_1361. DR eggNOG; ENOG4107Z0G; Bacteria. DR eggNOG; COG0628; LUCA. DR InParanoid; Q9X170; -. DR OMA; ISAYSWG; -. DR OrthoDB; EOG67Q997; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002549; AI-2E-like. DR PANTHER; PTHR21716; PTHR21716; 1. DR Pfam; PF01594; UPF0118; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 338 UPF0118 membrane protein TM_1349. FT /FTId=PRO_0000148323. FT TRANSMEM 20 40 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 147 167 Helical. {ECO:0000255}. FT TRANSMEM 203 223 Helical. {ECO:0000255}. FT TRANSMEM 239 259 Helical. {ECO:0000255}. FT TRANSMEM 263 283 Helical. {ECO:0000255}. FT TRANSMEM 297 317 Helical. {ECO:0000255}. SQ SEQUENCE 338 AA; 39387 MW; 9B21A19682078ADD CRC64; MKEFRKILED KAFFFTTLYI LISFLVFKIF PDVFAVIVLM VFFTLLLDPV IRFLEKLKFG KYFSRVAALL LFFFVMVYSL YMIIPPVFNE FGSFIEFMTK VFESKIWKDY IKSPELMPVF DKIMNFLEPK LTDFLNYVFS LVTTNFVSVT TIIVFTLFGL GYTVFYIREI ASFFVLIYPK SVRAEAREFF RDVYASMGRY IRVIFINAVI IGLSYWIVFE AFNLKYSAII SLWAFVTNFI PIVGVVLEYI PVLLFSLTLG VKGVLLIALF AILIHAVAFV VFIQLMKGLE KLNPVYIILS ILFFGKLFGL FGSFVGVPLA LFFKVFWRKF LRPLFEAG // ID Y124_THEMA Reviewed; 240 AA. AC Q9WXX8; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Probable metal transport system ATP-binding protein TM_0124; GN OrderedLocusNames=TM_0124; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Part of an ATP-driven transport system CC TM_0123/TM_0124/TM_0125 for a metal. Probably responsible for CC energy coupling to the transport system. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35218.1; -; Genomic_DNA. DR PIR; D72415; D72415. DR RefSeq; NP_227940.1; NC_000853.1. DR RefSeq; WP_004082707.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXX8; -. DR STRING; 243274.TM0124; -. DR DNASU; 896951; -. DR EnsemblBacteria; AAD35218; AAD35218; TM_0124. DR GeneID; 896951; -. DR KEGG; tma:TM0124; -. DR PATRIC; 23935088; VBITheMar51294_0122. DR eggNOG; ENOG4105FDK; Bacteria. DR eggNOG; COG1121; LUCA. DR InParanoid; Q9WXX8; -. DR KO; K09817; -. DR OMA; ARITHDI; -. DR OrthoDB; EOG6VXF80; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 240 Probable metal transport system ATP- FT binding protein TM_0124. FT /FTId=PRO_0000093278. FT DOMAIN 4 223 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 36 43 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 240 AA; 27586 MW; 134E023F78AF7B91 CRC64; MKIVEVKNLT YRINDFEILK NVTFSVEEGE FVGIIGPNGA GKTTLVRILV GDIKNYEGKV EVRGKIGYLP QLHQVQREFP ITVKEFAAMG MYGRYRKIDW EKVRSTLKDV GILHKENDPI KNLSGGEFQR LSLARALLSD PDILVLDEPE AGVDEMGKAS FYELLNRLRK EKNITVIMVS HDIGMVFKEC STIMCLNRTL HCHGPTETIN PEDLKKIFTD FDIWIRGTRH YEIYHGRERD // ID Y125_THEMA Reviewed; 282 AA. AC Q9WXX9; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=Probable metal transport system membrane protein TM_0125; GN OrderedLocusNames=TM_0125; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Part of an ATP-driven transport system CC TM_0123/TM_0124/TM_0125 for a metal. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC-3 integral membrane protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35219.1; -; Genomic_DNA. DR PIR; E72415; E72415. DR RefSeq; NP_227941.1; NC_000853.1. DR RefSeq; WP_010865057.1; NC_000853.1. DR ProteinModelPortal; Q9WXX9; -. DR STRING; 243274.TM0125; -. DR EnsemblBacteria; AAD35219; AAD35219; TM_0125. DR GeneID; 896952; -. DR KEGG; tma:TM0125; -. DR PATRIC; 23935090; VBITheMar51294_0123. DR eggNOG; ENOG41080V6; Bacteria. DR eggNOG; COG1108; LUCA. DR InParanoid; Q9WXX9; -. DR KO; K09816; -. DR OMA; HFYTSYA; -. DR OrthoDB; EOG600DND; -. DR BioCyc; TMAR243274:GC6P-125-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central. DR Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR001626; ABC_3. DR InterPro; IPR029022; ABC_BtuC-like. DR Pfam; PF00950; ABC-3; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 282 Probable metal transport system membrane FT protein TM_0125. FT /FTId=PRO_0000171174. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 79 99 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. FT TRANSMEM 148 168 Helical. {ECO:0000255}. FT TRANSMEM 184 204 Helical. {ECO:0000255}. FT TRANSMEM 210 230 Helical. {ECO:0000255}. FT TRANSMEM 234 254 Helical. {ECO:0000255}. FT TRANSMEM 259 279 Helical. {ECO:0000255}. SQ SEQUENCE 282 AA; 30769 MW; 90915278A9749E99 CRC64; MDQRNKTLRD LPWEGERLSF FHDLVEYSFL RTAFVGGILV ASLSGLVSPI VVFRRMEFIG DGTAHAVFAG LAAATLIGAD HRLIAFATAL LFAFAVSLFS RSRISESSAI GILLPFFMAV GVVLFSVSGR YQTDVMGYLF GDVLLVNSTD VAITAVVLAL SVILTVVFRW DIKYFIVDEK MARFYGIKTD LIRFLITSFI AITVVTTVKV VGVILTGALL ILPGLVSKIF GKSFWSLTTI SVIFSTGVFF AGFLTAYTLD LPPGPVIVII AFVSFLPMLK FS // ID Y1608_THEMA Reviewed; 212 AA. AC Q9X1U4; DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=DegV domain-containing protein TM_1608; GN OrderedLocusNames=TM_1608; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: May bind long-chain fatty acids, such as palmitate, and CC may play a role in lipid transport or fatty acid metabolism. CC {ECO:0000250}. CC -!- SIMILARITY: Contains 1 DegV domain. {ECO:0000255|PROSITE- CC ProRule:PRU00815}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36675.1; -; Genomic_DNA. DR PIR; D72235; D72235. DR RefSeq; NP_229408.1; NC_000853.1. DR RefSeq; WP_004082055.1; NC_000853.1. DR ProteinModelPortal; Q9X1U4; -. DR STRING; 243274.TM1608; -. DR EnsemblBacteria; AAD36675; AAD36675; TM_1608. DR GeneID; 897937; -. DR KEGG; tma:TM1608; -. DR KEGG; tmi:THEMA_06210; -. DR PATRIC; 23938190; VBITheMar51294_1627. DR eggNOG; ENOG4105EPR; Bacteria. DR eggNOG; COG1307; LUCA. DR OMA; HTGPEVF; -. DR OrthoDB; EOG6B8XGD; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR InterPro; IPR003797; DegV. DR Pfam; PF02645; DegV; 1. DR TIGRFAMs; TIGR00762; DegV; 1. DR PROSITE; PS51482; DEGV; 1. PE 3: Inferred from homology; KW Complete proteome; Lipid-binding; Reference proteome. FT CHAIN 1 212 DegV domain-containing protein TM_1608. FT /FTId=PRO_0000209817. FT DOMAIN 1 211 DegV. {ECO:0000255|PROSITE- FT ProRule:PRU00815}. FT BINDING 26 26 Fatty acid. {ECO:0000250}. SQ SEQUENCE 212 AA; 24128 MW; 622264916C4806EA CRC64; MERVLRDIIS EGCTRIYCVH LSSKLSAFYN VMKSVTERLK EKFPSVTFRV IDTRQVSIGA GYVLLKLMES VKDGREDLER VVQEANERIK IRFSVLEFDY LMKSGRVKAI TGMLGNLIKI HPILSIEDGE LRVVAKKRGL KNVVEKIVQD LKIDGRKMLG LVYAGEEMKE IVLEIEEKLK DEHIERVDIV RLPPTLAVHS GPKMFGAGVF IL // ID WECA_THEMA Reviewed; 291 AA. AC Q9X1N5; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase; DE EC=2.7.8.33; DE AltName: Full=UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase; DE AltName: Full=Undecaprenyl-phosphate GlcNAc-1-phosphate transferase; GN Name=wecA; OrderedLocusNames=TM_1549; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION AS A TRANSFERASE, COFACTOR, ENZYME REGULATION, SUBSTRATE RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18723618; DOI=10.1128/JB.00676-08; RA Al-Dabbagh B., Mengin-Lecreulx D., Bouhss A.; RT "Purification and characterization of the bacterial UDP- RT GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA."; RL J. Bacteriol. 190:7141-7146(2008). RN [3] RP CATALYTIC ACTIVITY. RX PubMed=19442646; DOI=10.1016/j.ab.2009.05.011; RA Al-Dabbagh B., Blanot D., Mengin-Lecreulx D., Bouhss A.; RT "Preparative enzymatic synthesis of polyprenyl-pyrophosphoryl- RT Nacetylglucosamine, an essential lipid intermediate for the RT biosynthesis of various bacterial cell envelope polymers."; RL Anal. Biochem. 391:163-165(2009). CC -!- FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety CC from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate CC (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP- CC C55), the lipid intermediate involved in the synthesis of various CC bacterial cell envelope components. The enzyme is highly active CC when tested with C35-P, instead of its natural C55-P lipid CC substrate, suggesting that at least a 35-carbon chain is required CC for the lipid to be a substrate of WecA. CC {ECO:0000269|PubMed:18723618}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + CC ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D- CC glucosaminyl-diphospho-ditrans,octacis-undecaprenol. CC {ECO:0000269|PubMed:19442646}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:18723618}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:18723618}; CC -!- ENZYME REGULATION: Partially inhibited by magnesium at CC concentration higher than 10 mM and totally inhibited at CC concentration higher than 250 mM. Also inhibited by tunicamycin, CC NaCl and KCl. {ECO:0000269|PubMed:18723618}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.12 mM for C55-P (at pH 8 and at 65 degrees Celsius) CC {ECO:0000269|PubMed:18723618}; CC KM=0.62 mM for UDP-GlcNAc (at pH 8 and at 65 degrees Celsius) CC {ECO:0000269|PubMed:18723618}; CC pH dependence: CC Optimum pH is 8. {ECO:0000269|PubMed:18723618}; CC Temperature dependence: CC Optimum temperature is 65 degrees Celsius. At 30 degrees Celsius CC activity is only 7% of the optimal value and at 80 degrees CC Celsius, the enzyme is totally inactive. CC {ECO:0000269|PubMed:18723618}; CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36631.1; -; Genomic_DNA. DR PIR; H72238; H72238. DR RefSeq; NP_229349.1; NC_000853.1. DR RefSeq; WP_004081942.1; NZ_CP011107.1. DR STRING; 243274.TM1549; -. DR BindingDB; Q9X1N5; -. DR ChEMBL; CHEMBL1932901; -. DR EnsemblBacteria; AAD36631; AAD36631; TM_1549. DR GeneID; 897567; -. DR KEGG; tma:TM1549; -. DR eggNOG; ENOG4107UKG; Bacteria. DR eggNOG; COG0472; LUCA. DR InParanoid; Q9X1N5; -. DR KO; K02851; -. DR OMA; FYEVVAS; -. DR OrthoDB; EOG69GZPZ; -. DR BRENDA; 2.7.8.33; 6331. DR UniPathway; UPA00963; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro. DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:UniProtKB. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IDA:UniProtKB. DR GO; GO:0071555; P:cell wall organization; IDA:UniProtKB. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:UniProtKB. DR InterPro; IPR000715; Glycosyl_transferase_4. DR PANTHER; PTHR22926; PTHR22926; 1. DR Pfam; PF00953; Glycos_transf_4; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Glycosyltransferase; Magnesium; KW Manganese; Membrane; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1 291 Undecaprenyl-phosphate alpha-N- FT acetylglucosaminyl 1-phosphate FT transferase. FT /FTId=PRO_0000395353. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 57 77 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. FT TRANSMEM 110 130 Helical. {ECO:0000255}. FT TRANSMEM 138 160 Helical. {ECO:0000255}. FT TRANSMEM 167 189 Helical. {ECO:0000255}. FT TRANSMEM 194 216 Helical. {ECO:0000255}. FT TRANSMEM 237 257 Helical. {ECO:0000255}. FT TRANSMEM 262 282 Helical. {ECO:0000255}. FT SITE 72 72 Important in orienting the substrate. FT {ECO:0000250}. FT SITE 73 73 Important in orienting the substrate; FT probably interacts with magnesium or FT manganese. {ECO:0000250}. FT SITE 128 128 Could be required for catalysis. FT {ECO:0000250}. FT SITE 131 131 Could be required for catalysis. FT {ECO:0000250}. SQ SEQUENCE 291 AA; 32778 MW; 0B328CC164C9B85F CRC64; MWEAIISFFL TSVLSVFAKK TEFLDRPDSR KSHGRAVPPV GGVSIFLTLL IFERDNPFFL FSIPLFLLGL LDDLFDLSYR IKLAVTALVA VWFSTAVTIE VSIFGARIHP VFFVIWFVGM VNAFNVVDGL DGLLSGISLF SSLMIGERSL AFSIIGFLPW NLPDAKVFLG NSGSFLLGAY LSTASVVFFE GDLGYATLFL GFPFYEIVFS FVRRLVVKKN PFSPDEKHTH HVFSRKIGKW KTLLILVSFS LMFNLLGLSQ KFYFIFLYVV LCCVLLFTYC VLQRGNGNLK L // ID Y123_THEMA Reviewed; 267 AA. AC Q9WXX7; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=Uncharacterized periplasmic metal-binding protein TM_0123; DE Flags: Precursor; GN OrderedLocusNames=TM_0123; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Part of an ATP-driven transport system CC TM_0123/TM_0124/TM_0125 for a metal. Metal-binding component. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35217.1; -; Genomic_DNA. DR PIR; C72415; C72415. DR RefSeq; NP_227939.1; NC_000853.1. DR RefSeq; WP_004082706.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXX7; -. DR STRING; 243274.TM0123; -. DR EnsemblBacteria; AAD35217; AAD35217; TM_0123. DR GeneID; 896950; -. DR KEGG; tma:TM0123; -. DR PATRIC; 23935086; VBITheMar51294_0121. DR eggNOG; ENOG4107XSR; Bacteria. DR eggNOG; COG0803; LUCA. DR InParanoid; Q9WXX7; -. DR KO; K09815; -. DR OMA; SGHEHST; -. DR OrthoDB; EOG6TR0BR; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central. DR InterPro; IPR006127; ZnuA-like. DR Pfam; PF01297; ZnuA; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Periplasm; Reference proteome; KW Signal; Transport. FT SIGNAL 1 15 {ECO:0000255}. FT CHAIN 16 267 Uncharacterized periplasmic metal-binding FT protein TM_0123. FT /FTId=PRO_0000031906. SQ SEQUENCE 267 AA; 30144 MW; 35ADDF60033C22A6 CRC64; MKKILLLLVL IVAVLNFGKT IVTTINPYYL IVSQLLGDTA SVKLLVPPGA NPHLFSLKPS DAKTLEEADL IVANGLGLEP YLEKYREKTV FVSDFIPALL LIDDNPHIWL DPFFLKYYIV PGLYQVLIEK FPEKQSEIKQ KAEEIVSGLD TVIRDSFKAL LPYTGKTVVM AHPSFTYFFK EFGLELITLS SGHEHSTSFS TIKEILRKKE QIVALFREPQ QPAEILSSLE KELRMKSFVL DPLGVNGEKT IVELLRKNLS VIQEALK // ID Y1420_THEMA Reviewed; 75 AA. AC Q9X1D7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 2. DT 11-MAY-2016, entry version 96. DE RecName: Full=Protein TM_1420; GN OrderedLocusNames=TM_1420; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP MASS SPECTROMETRY, PRESENCE OF A [2FE--2S] CLUSTER, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=12605255; DOI=10.1007/s00775-002-0439-y; RA Pan G., Menon A.L., Adams M.W.W.; RT "Characterization of a [2Fe-2S] protein encoded in the iron- RT hydrogenase operon of Thermotoga maritima."; RL J. Biol. Inorg. Chem. 8:469-474(2003). CC -!- FUNCTION: Might be part of a multi-protein complex, possibly CC involved in metal cluster assembly. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Note=Binds 1 [2Fe-2S] cluster.; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Redox potential: CC E(0) is 233 mV at pH 6.5 and 25 degrees Celsius, -296 mV at 80 CC degrees Celsius. {ECO:0000269|PubMed:12605255}; CC Temperature dependence: CC Not very thermostable. {ECO:0000269|PubMed:12605255}; CC -!- MASS SPECTROMETRY: Mass=8537; Mass_error=3; Method=Unknown; CC Range=1-75; Evidence={ECO:0000269|PubMed:12605255}; CC -!- SEQUENCE CAUTION: CC Sequence=AAD36490.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36490.1; ALT_INIT; Genomic_DNA. DR PIR; A72256; A72256. DR RefSeq; NP_229220.1; NC_000853.1. DR RefSeq; WP_012311059.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1D7; -. DR STRING; 243274.TM1420; -. DR EnsemblBacteria; AAD36490; AAD36490; TM_1420. DR GeneID; 898055; -. DR KEGG; tma:TM1420; -. DR KEGG; tmi:THEMA_07210; -. DR KEGG; tmw:THMA_1451; -. DR PATRIC; 23937788; VBITheMar51294_1432. DR eggNOG; ENOG4105Y5S; Bacteria. DR eggNOG; ENOG411227E; LUCA. DR OMA; ELKADFC; -. DR OrthoDB; EOG63VC47; -. DR BioCyc; TMAR243274:GC6P-1458-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central. DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR012336; Thioredoxin-like_fold. DR SUPFAM; SSF52833; SSF52833; 1. PE 1: Evidence at protein level; KW 2Fe-2S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 75 Protein TM_1420. FT /FTId=PRO_0000318590. FT METAL 6 6 Iron-sulfur (2Fe-2S). {ECO:0000250}. FT METAL 11 11 Iron-sulfur (2Fe-2S). {ECO:0000250}. FT METAL 39 39 Iron-sulfur (2Fe-2S). {ECO:0000250}. FT METAL 43 43 Iron-sulfur (2Fe-2S). {ECO:0000250}. SQ SEQUENCE 75 AA; 8536 MW; CCF5BDDBB2F3AA93 CRC64; MIVRVCMGSS CHLKGSYEVV RRFQELQKKY NFKLYGSLCF GNCSQGVCVE IDGRLFSRVT PENAEEILKK VLQNG // ID Y1567_THEMA Reviewed; 75 AA. AC Q9X1Q3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=UPF0109 protein TM_1567; GN OrderedLocusNames=TM_1567; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0109 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36634.1; -; Genomic_DNA. DR PIR; H72236; H72236. DR RefSeq; NP_229367.1; NC_000853.1. DR RefSeq; WP_004081981.1; NZ_CP011107.1. DR STRING; 243274.TM1567; -. DR EnsemblBacteria; AAD36634; AAD36634; TM_1567. DR GeneID; 897962; -. DR KEGG; tma:TM1567; -. DR PATRIC; 23938096; VBITheMar51294_1585. DR eggNOG; ENOG41084QK; Bacteria. DR eggNOG; COG1837; LUCA. DR InParanoid; Q9X1Q3; -. DR KO; K06960; -. DR OMA; NSEDVGQ; -. DR OrthoDB; EOG6XDH3R; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00088; UPF0109; 1. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR009019; KH_prok-type. DR InterPro; IPR020627; UPF0109. DR SUPFAM; SSF54814; SSF54814; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; RNA-binding. FT CHAIN 1 75 UPF0109 protein TM_1567. FT /FTId=PRO_0000163236. FT DOMAIN 29 75 KH. SQ SEQUENCE 75 AA; 8494 MW; 0AB23DD5DE3DB16E CRC64; MKELLEKILR GIVKHPEEVV VMEFDEEGKK VYEIVVNEED VGQVIGKDGR TIKSLKILLS ALMGDSKEIT IKVVR // ID Y019_THEMA Reviewed; 256 AA. AC Q56318; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 101. DE RecName: Full=Uncharacterized oxidoreductase TM_0019; DE EC=1.-.-.-; GN OrderedLocusNames=TM_0019; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8550425; RA Kletzin A., Adams M.W.W.; RT "Molecular and phylogenetic characterization of pyruvate and 2- RT ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus RT and pyruvate ferredoxin oxidoreductase from Thermotoga maritima."; RL J. Bacteriol. 178:248-257(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X85171; CAA59459.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35113.1; -; Genomic_DNA. DR PIR; E72427; E72427. DR RefSeq; NP_227835.1; NC_000853.1. DR RefSeq; WP_004082464.1; NZ_CP011107.1. DR ProteinModelPortal; Q56318; -. DR STRING; 243274.TM0019; -. DR EnsemblBacteria; AAD35113; AAD35113; TM_0019. DR GeneID; 896834; -. DR KEGG; tma:TM0019; -. DR PATRIC; 23934878; VBITheMar51294_0017. DR eggNOG; ENOG4107EXU; Bacteria. DR eggNOG; COG1028; LUCA. DR InParanoid; Q56318; -. DR KO; K00540; -. DR OMA; PEAIWDM; -. DR OrthoDB; EOG6N3CR8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 256 Uncharacterized oxidoreductase TM_0019. FT /FTId=PRO_0000054866. FT NP_BIND 9 33 NADP. {ECO:0000250}. FT ACT_SITE 153 153 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10001}. FT BINDING 140 140 Substrate. {ECO:0000250}. FT CONFLICT 130 136 RGGGVII -> TRWRSDH (in Ref. 1; CAA59459). FT {ECO:0000305}. SQ SEQUENCE 256 AA; 28078 MW; D68160B1D7980C6B CRC64; MLEGKVAVVT GGGQGIGAAI AQLFAENGMK VVIAEIDEEA GVEREEMLRE RGLDVTFVKT DVADENSVKN MVRKTVEIYG GVDVLVNNAA VMSVKSIFER PLEEWERVIR VNLTGPYICS RYCAEEMIKR GGGVIINIAS TRAFQSEPDT EPYSASKGGL VALTHSLAVS LSRYHIRVVS ISPGWIETSE WKKKSLRKKP DLRPIDHEQH PAGRVGNPLD IAHLCVFLAD DEKAGFITGT NFIVDGGMTV KMIYEE // ID Y021_THEMA Reviewed; 102 AA. AC Q9WXM9; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=UPF0166 protein TM_0021; GN OrderedLocusNames=TM_0021; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0166 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35115.1; -; Genomic_DNA. DR PIR; G72427; G72427. DR RefSeq; NP_227837.1; NC_000853.1. DR RefSeq; WP_004082468.1; NZ_CP011107.1. DR PDB; 1O51; X-ray; 2.50 A; A=1-102. DR PDBsum; 1O51; -. DR ProteinModelPortal; Q9WXM9; -. DR SMR; Q9WXM9; 1-100. DR STRING; 243274.TM0021; -. DR EnsemblBacteria; AAD35115; AAD35115; TM_0021. DR GeneID; 896836; -. DR KEGG; tma:TM0021; -. DR PATRIC; 23934882; VBITheMar51294_0019. DR eggNOG; ENOG4105KJJ; Bacteria. DR eggNOG; COG1993; LUCA. DR InParanoid; Q9WXM9; -. DR KO; K09137; -. DR OMA; FIGESDK; -. DR OrthoDB; EOG66MQRH; -. DR EvolutionaryTrace; Q9WXM9; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.30.70.120; -; 1. DR InterPro; IPR003793; DUF190. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C. DR Pfam; PF02641; DUF190; 1. DR SUPFAM; SSF54913; SSF54913; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 102 UPF0166 protein TM_0021. FT /FTId=PRO_0000185232. FT STRAND 1 9 {ECO:0000244|PDB:1O51}. FT HELIX 19 29 {ECO:0000244|PDB:1O51}. FT STRAND 36 39 {ECO:0000244|PDB:1O51}. FT STRAND 63 70 {ECO:0000244|PDB:1O51}. FT HELIX 72 83 {ECO:0000244|PDB:1O51}. FT STRAND 89 97 {ECO:0000244|PDB:1O51}. SQ SEQUENCE 102 AA; 11804 MW; 69EF5F156B6F400F CRC64; MKLLKIYLGE KDKHSGKPLF EYLVKRAYEL GMKGVTVYRG IMGFGHKRHM HRSDFFSLSP DLPIVLEIVD EEERINLFLK EIDNIDFDGL VFTADVNVVK MG // ID Y1034_THEMA Reviewed; 378 AA. AC Q9X0C4; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 95. DE RecName: Full=Putative UDP-N-acetylglucosamine 2-epimerase; DE EC=5.1.3.14; DE AltName: Full=UDP-GlcNAc-2-epimerase; GN OrderedLocusNames=TM_1034; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine = UDP-N- CC acetyl-alpha-D-mannosamine. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36111.1; -; Genomic_DNA. DR PIR; A72304; A72304. DR RefSeq; NP_228840.1; NC_000853.1. DR RefSeq; WP_004080488.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0C4; -. DR SMR; Q9X0C4; 2-368. DR STRING; 243274.TM1034; -. DR EnsemblBacteria; AAD36111; AAD36111; TM_1034. DR GeneID; 897719; -. DR KEGG; tma:TM1034; -. DR PATRIC; 23936997; VBITheMar51294_1047. DR eggNOG; ENOG4105EAG; Bacteria. DR eggNOG; COG0381; LUCA. DR InParanoid; Q9X0C4; -. DR KO; K01791; -. DR OMA; IMKERQT; -. DR OrthoDB; EOG6HXJ6F; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom. DR InterPro; IPR029767; WecB-like. DR PANTHER; PTHR18964:SF2; PTHR18964:SF2; 1. DR Pfam; PF02350; Epimerase_2; 1. DR TIGRFAMs; TIGR00236; wecB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Isomerase; KW Lipopolysaccharide biosynthesis; Reference proteome. FT CHAIN 1 378 Putative UDP-N-acetylglucosamine 2- FT epimerase. FT /FTId=PRO_0000208534. SQ SEQUENCE 378 AA; 42846 MW; 0EF1F9F9A0BC4B80 CRC64; MIRVLSVFGT RPEAIKMAPL VKKLEEEQNV ESLVCVTAQH RQMLDQVLEV FDIKPDFDLN IMKERQNLSD ITVNALSGLY DLIGELKPDI VLVQGDTTTT FAGALAAFYH RIPVGHVEAG LRTNDRYSPF PEEINRRLTG VLSTLHFAPT KRNRENLLKE NVMGKIYVTG NTVIDALRYT VKENHVFEDP ILRNMDFSDG RYILLTSHRR ENIGKPLENI CRAVRRIVEG FEDVKVIYPV HMNPAVREIV FPMLENVERV FLIDPVNVID MHNLMARSYL IMTDSGGIQE EAPALGKPVI VLRKETERPE AIEAGVAVLG GVEEERIFEL AKKLLVDREE YEKMAKAVNP FGDGRASERI VKAILHEFGL SDPPEEFC // ID Y1094_THEMA Reviewed; 439 AA. AC Q9X0H9; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Uncharacterized RNA methyltransferase TM_1094; DE EC=2.1.1.-; GN OrderedLocusNames=TM_1094; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RNA M5U methyltransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU01024}. CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|PROSITE- CC ProRule:PRU00208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36170.1; -; Genomic_DNA. DR PIR; E72298; E72298. DR RefSeq; NP_228900.1; NC_000853.1. DR RefSeq; WP_004080361.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0H9; -. DR STRING; 243274.TM1094; -. DR EnsemblBacteria; AAD36170; AAD36170; TM_1094. DR GeneID; 898671; -. DR KEGG; tma:TM1094; -. DR PATRIC; 23937119; VBITheMar51294_1108. DR eggNOG; ENOG4105BZT; Bacteria. DR eggNOG; COG2265; LUCA. DR InParanoid; Q9X0H9; -. DR KO; K03215; -. DR OMA; DLDPFGQ; -. DR OrthoDB; EOG6V4GKM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR001566; 23S_rRNA_MeTrfase_RlmD. DR InterPro; IPR030390; MeTrfase_TrmA_AS. DR InterPro; IPR030391; MeTrfase_TrmA_CS. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR002792; TRAM_dom. DR InterPro; IPR010280; U5_MeTrfase_fam. DR Pfam; PF05958; tRNA_U5-meth_tr; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00479; rumA; 1. DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1. DR PROSITE; PS50926; TRAM; 1. DR PROSITE; PS01230; TRMA_1; 1. DR PROSITE; PS01231; TRMA_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 439 Uncharacterized RNA methyltransferase FT TM_1094. FT /FTId=PRO_0000162046. FT DOMAIN 1 55 TRAM. {ECO:0000255|PROSITE- FT ProRule:PRU00208}. FT ACT_SITE 394 394 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU01024}. FT METAL 68 68 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 74 74 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 77 77 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 149 149 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT BINDING 272 272 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU01024}. FT BINDING 301 301 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|PROSITE- FT ProRule:PRU01024}. FT BINDING 322 322 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU01024}. FT BINDING 367 367 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU01024}. SQ SEQUENCE 439 AA; 50257 MW; 598E66897CF64619 CRC64; MLEQVRIQKM VNGGYGLAHL SNGKVVLVEG AYPGEEVLIK TYREKRDFSF GKVVSLLKES EDRIKPPCRY FGRCGGCHWM DVKYETQLRY KKEVLIDLFE RSNLKVEVED VEPSDLVFHY RTKMEFHFQG RKLGLKKRNS DFVIDIKDCE VAPEGTGEIL NTVKEAVQVL NVPVYNWETR KGVLKHLVIR YAFSTDQFMV IFVTKTESFP WGRDLVRAVL KRFPKIHSII HVMNSKDSVV LRGPYKTLYG EGVIVEEFDW ERFQIPPTAF FQSNYSITSK LIDHVYREQA LQGNEVVLDL YAGIGTFSVR TSFSAARVIS VESSRVAVKA GKANANINSR KNIEYVEQDV LDFLKNYSGR ADRIILDPPR SGAGPEVMKE IARLSPERIV YVSCDPSTLV RDLKVLVENG YSIVRVKPFD MFPQTYHVET AVTLVKGDR // ID Y1187_THEMA Reviewed; 324 AA. AC Q9X0R9; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 20-JAN-2016, entry version 94. DE RecName: Full=UPF0118 membrane protein TM_1187; GN OrderedLocusNames=TM_1187; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0118 (PerM) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36262.1; -; Genomic_DNA. DR PIR; A72285; A72285. DR RefSeq; NP_228992.1; NC_000853.1. DR RefSeq; WP_010865277.1; NC_000853.1. DR STRING; 243274.TM1187; -. DR DNASU; 898298; -. DR EnsemblBacteria; AAD36262; AAD36262; TM_1187. DR GeneID; 898298; -. DR KEGG; tma:TM1187; -. DR KEGG; tmi:THEMA_08400; -. DR PATRIC; 23937314; VBITheMar51294_1205. DR eggNOG; ENOG4107WSY; Bacteria. DR eggNOG; COG0628; LUCA. DR InParanoid; Q9X0R9; -. DR OMA; GFLFAER; -. DR OrthoDB; EOG61S2X5; -. DR BioCyc; TMAR243274:GC6P-1216-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002549; AI-2E-like. DR PANTHER; PTHR21716; PTHR21716; 1. DR Pfam; PF01594; UPF0118; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 324 UPF0118 membrane protein TM_1187. FT /FTId=PRO_0000148322. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT TRANSMEM 131 151 Helical. {ECO:0000255}. FT TRANSMEM 190 210 Helical. {ECO:0000255}. FT TRANSMEM 227 247 Helical. {ECO:0000255}. FT TRANSMEM 252 272 Helical. {ECO:0000255}. FT TRANSMEM 285 305 Helical. {ECO:0000255}. SQ SEQUENCE 324 AA; 36043 MW; 13D7CA5EA201C327 CRC64; MKNLKNKHFA LLYLVLFLVL AKLSPFIITA LIMGLYLSII IDYVARFLEV FIKKPRVLPR VISNVLVFLT IAYSAVNFFP VIVREAQKVF SEIDRIRSGL ENIDIPGWLS SILSSISASF SEGALSLVNK IVGYVPSFIT AAILIVITAF IVSSLKRLIK ENVHYLFPTN PSDGKEFLKT TYTEFERFVG GQVLVAIFVG LFVGFGAFIF KIPSAFFLGM LAFVTDFVPY LGVVISAIPL LMLAFSVHGL SGLLIGTIIL VAANQLEMWV LAPKIQSNTL NVHWFIILIM ILILGDLFSF GGVLIALPFL IFLKNFWKQY VMGG // ID Y1321_THEMA Reviewed; 72 AA. AC Q9X145; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 78. DE RecName: Full=UPF0150 protein TM_1321; GN OrderedLocusNames=TM_1321; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0150 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36393.1; -; Genomic_DNA. DR PIR; G72268; G72268. DR RefSeq; NP_229123.1; NC_000853.1. DR RefSeq; WP_004083352.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X145; -. DR STRING; 243274.TM1321; -. DR EnsemblBacteria; AAD36393; AAD36393; TM_1321. DR GeneID; 898161; -. DR KEGG; tma:TM1321; -. DR PATRIC; 23937579; VBITheMar51294_1335. DR eggNOG; ENOG4106HX1; Bacteria. DR eggNOG; COG1598; LUCA. DR InParanoid; Q9X145; -. DR OMA; GFPGAHS; -. DR OrthoDB; EOG6X113J; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR031807; HicB-like. DR Pfam; PF15919; HicB_lk_antitox; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 72 UPF0150 protein TM_1321. FT /FTId=PRO_0000157940. SQ SEQUENCE 72 AA; 8215 MW; 5F7974EB7F92AB98 CRC64; MRKIFTAIIE YDPETKQYVG MVPDVPGVHT VGSSLEEVRR NLKEVLELVL EEAGDEINHQ EFVALEMIEV ET // ID Y253_THEMA Reviewed; 108 AA. AC Q9WY95; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=UPF0102 protein TM_0253; GN OrderedLocusNames=TM_0253; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0102 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35343.1; -; Genomic_DNA. DR PIR; F72399; F72399. DR RefSeq; NP_228067.1; NC_000853.1. DR RefSeq; WP_004082957.1; NZ_CP011107.1. DR STRING; 243274.TM0253; -. DR EnsemblBacteria; AAD35343; AAD35343; TM_0253. DR GeneID; 897162; -. DR KEGG; tma:TM0253; -. DR KEGG; tmi:THEMA_03460; -. DR KEGG; tmw:THMA_0260; -. DR PATRIC; 23935381; VBITheMar51294_0256. DR eggNOG; ENOG41085R6; Bacteria. DR eggNOG; COG0792; LUCA. DR InParanoid; Q9WY95; -. DR KO; K07460; -. DR OMA; HKQKGLK; -. DR OrthoDB; EOG6PP9TH; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.1350.10; -; 1. DR HAMAP; MF_00048; UPF0102; 1. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR InterPro; IPR003509; UPF0102. DR Pfam; PF02021; UPF0102; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 108 UPF0102 protein TM_0253. FT /FTId=PRO_0000167383. SQ SEQUENCE 108 AA; 12650 MW; DB5B77A4F72945EE CRC64; MMDWKEAEEL ACKFLKKKGY KILERNYRTK YGEIDIVARD GREIVFVEVK SGSGKVDPLE RIDLKKVRNL EQTARFYMIQ NKLKGPARVD FVRVTPEGID HFEGIWLG // ID Y1513_THEMA Reviewed; 418 AA. AC Q9X1K1; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 74. DE RecName: Full=UPF0348 protein TM_1513 {ECO:0000255|HAMAP-Rule:MF_01539}; GN OrderedLocusNames=TM_1513; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0348 family. {ECO:0000255|HAMAP- CC Rule:MF_01539}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36580.1; -; Genomic_DNA. DR PIR; B72245; B72245. DR RefSeq; NP_229313.1; NC_000853.1. DR RefSeq; WP_004081862.1; NZ_CP011107.1. DR STRING; 243274.TM1513; -. DR EnsemblBacteria; AAD36580; AAD36580; TM_1513. DR GeneID; 897346; -. DR KEGG; tma:TM1513; -. DR PATRIC; 23937984; VBITheMar51294_1530. DR eggNOG; ENOG4105CDE; Bacteria. DR eggNOG; COG1323; LUCA. DR InParanoid; Q9X1K1; -. DR OMA; NPFHSGH; -. DR OrthoDB; EOG6PS5WF; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01539; UPF0348; 1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR008513; UPF0348. DR Pfam; PF05636; HIGH_NTase1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 418 UPF0348 protein TM_1513. FT /FTId=PRO_0000147197. SQ SEQUENCE 418 AA; 48592 MW; 60C1196BE5C933C1 CRC64; MEYNPFHNGH LYHLTSAREL VKPDYTIAVM SGNFCQRGEP AVIDKFARAE IALRMGVDVV LELPVVFATQ DAGGFAFGAV CVLDATGVVT DVVFGSESND IEFLQRVARI LYEQPDEYQK FLHEELKKGY SFPNARKYAL MRYFSMKGWN EEEVLKLEKS NDILGVEYIH SALKIGSNIR FHTIKRVGAE EKDTSFRGRF SSATAIRNLM REKRWEEVRD SLPEDSFEIL MREINEGRGP VFLENMGDFL LSFFRLKNMD FFEKIHGFSE GLEKRFHVCA RQTGSYRDFL ECVKAKRFTF SRIRRLALFS VFEVNKEFVE KSNTKGPQYI RILGFTEKGR EILSLMRKKA KLPIVTNMSL YRKVLEKTDL PVDKQLFLEQ IDLDVKATNF YSMFFPSVEQ RCGERDFSIH PIFLRTEM // ID Y1551_THEMA Reviewed; 174 AA. AC Q9X1N7; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Protein TM_1551 {ECO:0000255|HAMAP-Rule:MF_00645}; GN OrderedLocusNames=TM_1551; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains 1 AMMECR1 domain. {ECO:0000255|HAMAP- CC Rule:MF_00645}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36617.1; -; Genomic_DNA. DR PIR; B72239; B72239. DR RefSeq; NP_229351.1; NC_000853.1. DR RefSeq; WP_004081947.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1N7; -. DR STRING; 243274.TM1551; -. DR EnsemblBacteria; AAD36617; AAD36617; TM_1551. DR GeneID; 897568; -. DR KEGG; tma:TM1551; -. DR PATRIC; 23938064; VBITheMar51294_1569. DR eggNOG; ENOG4105NBF; Bacteria. DR eggNOG; COG2078; LUCA. DR InParanoid; Q9X1N7; -. DR KO; K09141; -. DR OMA; RAGCFVT; -. DR OrthoDB; EOG6WDSHC; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.30.700.20; -; 1. DR HAMAP; MF_00645; AMMECR1; 1. DR InterPro; IPR023473; AMMECR1. DR InterPro; IPR002733; AMMECR1_domain. DR InterPro; IPR027485; AMMECR1_N. DR InterPro; IPR027623; AmmeMemoSam_A. DR InterPro; IPR023472; Uncharacterised_MJ0810. DR PANTHER; PTHR13016; PTHR13016; 1. DR Pfam; PF01871; AMMECR1; 1. DR SUPFAM; SSF143447; SSF143447; 1. DR TIGRFAMs; TIGR04335; AmmeMemoSam_A; 1. DR TIGRFAMs; TIGR00296; TIGR00296; 1. DR PROSITE; PS51112; AMMECR1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 174 Protein TM_1551. FT /FTId=PRO_0000142393. FT DOMAIN 2 174 AMMECR1. {ECO:0000255|HAMAP- FT Rule:MF_00645}. SQ SEQUENCE 174 AA; 19789 MW; AF23814EEC99267D CRC64; MIGEHPYVKW AIRVIENYVR YGKVIEPDES VPEELFKRRA GAFVTLHKTD GSLRGCIGTY LPTKPNLALE IRDNAIAAAT QDPRFPPVSP DELDDIVVHV DILSPPEPVR DISELDPKKY GVIVVKGWRR GLLLPDIEGV DTVEEQLRIA KLKAGIPEWD DDVEIYRFTV ERYK // ID Y1556_THEMA Reviewed; 204 AA. AC Q9X1P2; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=Maf-like protein TM_1556 {ECO:0000255|HAMAP-Rule:MF_00528}; GN OrderedLocusNames=TM_1556; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528}. CC -!- SIMILARITY: Belongs to the maf family. {ECO:0000255|HAMAP- CC Rule:MF_00528}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36622.1; -; Genomic_DNA. DR PIR; G72239; G72239. DR RefSeq; NP_229356.1; NC_000853.1. DR RefSeq; WP_010865361.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1P2; -. DR STRING; 243274.TM1556; -. DR EnsemblBacteria; AAD36622; AAD36622; TM_1556. DR GeneID; 897968; -. DR KEGG; tma:TM1556; -. DR PATRIC; 23938074; VBITheMar51294_1574. DR eggNOG; ENOG4108Z03; Bacteria. DR eggNOG; COG0424; LUCA. DR InParanoid; Q9X1P2; -. DR KO; K06287; -. DR OMA; VITGYCI; -. DR OrthoDB; EOG6SV5F0; -. DR BioCyc; TMAR243274:GC6P-1597-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_00528; Maf; 1. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR003697; Maf. DR Pfam; PF02545; Maf; 1. DR PIRSF; PIRSF006305; Maf; 1. DR SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00172; maf; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 204 Maf-like protein TM_1556. FT /FTId=PRO_0000123066. FT ACT_SITE 32 32 {ECO:0000255|HAMAP-Rule:MF_00528}. SQ SEQUENCE 204 AA; 23323 MW; A93845BF2C9AB71C CRC64; MRIILASSSP RRRQLMELLG IEFEVEKPDV EEEFLESPEE TVRELSLRKA EWVFKKRKEE EILVIGSDTV VVLDGNILGK PESLEEAKGM LKKLSGKWHV VYTGVAFVSS ETKDVIVSST KVRFRELPES VIDYYVEKYR PLDKAGAYGI QDFAAVFVEK IEGDFFTVVG FPLGMVWQYL YEKGWWKVAS KREDDKGGAR VAFG // ID Y1313_THEMA Reviewed; 75 AA. AC Q9X139; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=UPF0150 protein TM_1313; GN OrderedLocusNames=TM_1313; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0150 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36387.1; -; Genomic_DNA. DR PIR; C72271; C72271. DR RefSeq; NP_229117.1; NC_000853.1. DR RefSeq; WP_010865306.1; NC_000853.1. DR ProteinModelPortal; Q9X139; -. DR STRING; 243274.TM1313; -. DR EnsemblBacteria; AAD36387; AAD36387; TM_1313. DR GeneID; 898169; -. DR KEGG; tma:TM1313; -. DR PATRIC; 23937562; VBITheMar51294_1327. DR eggNOG; ENOG4106HX1; Bacteria. DR eggNOG; COG1598; LUCA. DR InParanoid; Q9X139; -. DR OrthoDB; EOG6X113J; -. DR BioCyc; TMAR243274:GC6P-1344-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR031807; HicB-like. DR Pfam; PF15919; HicB_lk_antitox; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 75 UPF0150 protein TM_1313. FT /FTId=PRO_0000157939. SQ SEQUENCE 75 AA; 8560 MW; 692320DC1CDE7EB5 CRC64; MKNVRKIFTA IIEYDPEKKQ YVGMVPDVPG VHTVGSSLEE VRRNLKEVLE LVLEEAGDEI NLQEFVALEM IEVET // ID Y1468_THEMA Reviewed; 288 AA. AC Q9X1H9; DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=Fatty acid-binding protein TM_1468; GN OrderedLocusNames=TM_1468; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PALMITATE, RP FUNCTION, AND SUBUNIT. RX PubMed=12577257; DOI=10.1002/prot.10305; RA Schulze-Gahmen U., Pelaschier J., Yokota H., Kim R., Kim S.-H.; RT "Crystal structure of a hypothetical protein, TM841 of Thermotoga RT maritima, reveals its function as a fatty acid-binding protein."; RL Proteins 50:526-530(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH PALMITATE. RG Joint center for structural genomics (JCSG); RT "Crystal structure of UPF0230 protein TM1468 (TM1468) from Thermotoga RT maritima at 2.45 A resolution."; RL Submitted (JUL-2011) to the PDB data bank. CC -!- FUNCTION: Binds long-chain fatty acids, such as palmitate, and may CC play a role in lipid transport or fatty acid metabolism. CC {ECO:0000269|PubMed:12577257}. CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:12577257, CC ECO:0000305|Ref.3}. CC -!- SIMILARITY: Contains 1 DegV domain. {ECO:0000255|PROSITE- CC ProRule:PRU00815}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36536.1; -; Genomic_DNA. DR PIR; E72246; E72246. DR RefSeq; NP_229268.1; NC_000853.1. DR RefSeq; WP_004081771.1; NZ_CP011107.1. DR PDB; 1MGP; X-ray; 2.00 A; A=1-288. DR PDB; 1VPV; X-ray; 2.45 A; A/B=1-288. DR PDBsum; 1MGP; -. DR PDBsum; 1VPV; -. DR ProteinModelPortal; Q9X1H9; -. DR SMR; Q9X1H9; 1-287. DR STRING; 243274.TM1468; -. DR DNASU; 897743; -. DR EnsemblBacteria; AAD36536; AAD36536; TM_1468. DR GeneID; 897743; -. DR KEGG; tma:TM1468; -. DR PATRIC; 23937892; VBITheMar51294_1484. DR eggNOG; ENOG4105EPR; Bacteria. DR eggNOG; COG1307; LUCA. DR InParanoid; Q9X1H9; -. DR OMA; ITIERIN; -. DR OrthoDB; EOG6CP3W7; -. DR EvolutionaryTrace; Q9X1H9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR InterPro; IPR003797; DegV. DR Pfam; PF02645; DegV; 1. DR TIGRFAMs; TIGR00762; DegV; 1. DR PROSITE; PS51482; DEGV; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Lipid-binding; Reference proteome. FT CHAIN 1 288 Fatty acid-binding protein TM_1468. FT /FTId=PRO_0000209816. FT DOMAIN 3 283 DegV. {ECO:0000255|PROSITE- FT ProRule:PRU00815}. FT BINDING 63 63 Fatty acid. FT BINDING 96 96 Fatty acid. FT STRAND 3 8 {ECO:0000244|PDB:1MGP}. FT HELIX 9 11 {ECO:0000244|PDB:1MGP}. FT HELIX 17 20 {ECO:0000244|PDB:1MGP}. FT STRAND 23 26 {ECO:0000244|PDB:1MGP}. FT STRAND 29 31 {ECO:0000244|PDB:1MGP}. FT STRAND 37 39 {ECO:0000244|PDB:1MGP}. FT HELIX 44 56 {ECO:0000244|PDB:1MGP}. FT STRAND 62 64 {ECO:0000244|PDB:1MGP}. FT HELIX 68 80 {ECO:0000244|PDB:1MGP}. FT STRAND 84 91 {ECO:0000244|PDB:1MGP}. FT TURN 93 95 {ECO:0000244|PDB:1MGP}. FT HELIX 98 108 {ECO:0000244|PDB:1MGP}. FT STRAND 109 111 {ECO:0000244|PDB:1MGP}. FT STRAND 113 117 {ECO:0000244|PDB:1MGP}. FT HELIX 122 124 {ECO:0000244|PDB:1MGP}. FT HELIX 126 137 {ECO:0000244|PDB:1MGP}. FT HELIX 142 154 {ECO:0000244|PDB:1MGP}. FT STRAND 158 165 {ECO:0000244|PDB:1MGP}. FT HELIX 168 173 {ECO:0000244|PDB:1MGP}. FT STRAND 189 196 {ECO:0000244|PDB:1MGP}. FT STRAND 199 208 {ECO:0000244|PDB:1MGP}. FT HELIX 209 221 {ECO:0000244|PDB:1MGP}. FT STRAND 229 238 {ECO:0000244|PDB:1MGP}. FT HELIX 240 250 {ECO:0000244|PDB:1MGP}. FT TURN 251 253 {ECO:0000244|PDB:1MGP}. FT STRAND 254 263 {ECO:0000244|PDB:1MGP}. FT HELIX 266 272 {ECO:0000244|PDB:1MGP}. FT STRAND 277 284 {ECO:0000244|PDB:1MGP}. SQ SEQUENCE 288 AA; 32575 MW; 1CF1D341AF278E2E CRC64; MKVKILVDST ADVPFSWMEK YDIDSIPLYV VWEDGRSEPD EREPEEIMNF YKRIREAGSV PKTSQPSVED FKKRYLKYKE EDYDVVLVLT LSSKLSGTYN SAVLASKEVD IPVYVVDTLL ASGAIPLPAR VAREMLENGA TIEEVLKKLD ERMKNKDFKA IFYVSNFDYL VKGGRVSKFQ GFVGNLLKIR VCLHIENGEL IPYRKVRGDK KAIEALIEKL REDTPEGSKL RVIGVHADNE AGVVELLNTL RKSYEVVDEI ISPMGKVITT HVGPGTVGFG IEVLERKR // ID Y288_THEMA Reviewed; 598 AA. AC Q9WYC4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 122. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein TM_0288; GN OrderedLocusNames=TM_0288; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35376.1; -; Genomic_DNA. DR PIR; F72396; F72396. DR RefSeq; NP_228100.1; NC_000853.1. DR RefSeq; WP_004083002.1; NZ_CP011107.1. DR PDB; 3QF4; X-ray; 2.90 A; B=1-598. DR PDB; 4Q4A; X-ray; 2.60 A; B=1-598. DR PDB; 4Q4H; X-ray; 2.53 A; B=1-598. DR PDB; 4Q4J; X-ray; 3.20 A; B=1-598. DR PDB; 4Q7L; X-ray; 2.35 A; A/B/C=353-598. DR PDB; 4Q7M; X-ray; 2.30 A; B=353-598. DR PDBsum; 3QF4; -. DR PDBsum; 4Q4A; -. DR PDBsum; 4Q4H; -. DR PDBsum; 4Q4J; -. DR PDBsum; 4Q7L; -. DR PDBsum; 4Q7M; -. DR ProteinModelPortal; Q9WYC4; -. DR STRING; 243274.TM0288; -. DR TCDB; 3.A.1.135.5; the atp-binding cassette (abc) superfamily. DR DNASU; 897208; -. DR EnsemblBacteria; AAD35376; AAD35376; TM_0288. DR GeneID; 897208; -. DR KEGG; tma:TM0288; -. DR PATRIC; 23935455; VBITheMar51294_0293. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR InParanoid; Q9WYC4; -. DR KO; K06147; -. DR OMA; LRNWGWN; -. DR OrthoDB; EOG6T7N3V; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 598 Uncharacterized ABC transporter ATP- FT binding protein TM_0288. FT /FTId=PRO_0000093279. FT TRANSMEM 40 60 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 80 100 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 150 170 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 177 197 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 273 293 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 39 322 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 355 589 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 388 395 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT HELIX 21 28 {ECO:0000244|PDB:4Q4H}. FT TURN 29 31 {ECO:0000244|PDB:4Q4H}. FT HELIX 33 35 {ECO:0000244|PDB:4Q4H}. FT HELIX 36 66 {ECO:0000244|PDB:4Q4H}. FT TURN 67 71 {ECO:0000244|PDB:4Q4H}. FT HELIX 73 75 {ECO:0000244|PDB:4Q4A}. FT HELIX 76 122 {ECO:0000244|PDB:4Q4H}. FT HELIX 125 130 {ECO:0000244|PDB:4Q4H}. FT HELIX 133 152 {ECO:0000244|PDB:4Q4H}. FT HELIX 154 175 {ECO:0000244|PDB:4Q4H}. FT HELIX 177 183 {ECO:0000244|PDB:4Q4H}. FT HELIX 186 224 {ECO:0000244|PDB:4Q4H}. FT HELIX 226 231 {ECO:0000244|PDB:4Q4H}. FT TURN 232 234 {ECO:0000244|PDB:4Q4J}. FT HELIX 235 259 {ECO:0000244|PDB:4Q4H}. FT TURN 260 262 {ECO:0000244|PDB:3QF4}. FT HELIX 263 287 {ECO:0000244|PDB:4Q4H}. FT HELIX 293 301 {ECO:0000244|PDB:4Q4H}. FT TURN 302 306 {ECO:0000244|PDB:4Q4H}. FT HELIX 308 333 {ECO:0000244|PDB:4Q4H}. FT STRAND 355 362 {ECO:0000244|PDB:4Q7M}. FT STRAND 364 368 {ECO:0000244|PDB:4Q7M}. FT STRAND 370 378 {ECO:0000244|PDB:4Q7M}. FT STRAND 383 387 {ECO:0000244|PDB:4Q7M}. FT HELIX 394 401 {ECO:0000244|PDB:4Q7M}. FT STRAND 408 414 {ECO:0000244|PDB:4Q7M}. FT HELIX 419 421 {ECO:0000244|PDB:4Q7M}. FT HELIX 424 429 {ECO:0000244|PDB:4Q7M}. FT STRAND 431 434 {ECO:0000244|PDB:4Q7M}. FT STRAND 442 444 {ECO:0000244|PDB:4Q7M}. FT HELIX 445 449 {ECO:0000244|PDB:4Q7M}. FT TURN 450 452 {ECO:0000244|PDB:4Q7M}. FT HELIX 458 467 {ECO:0000244|PDB:4Q7M}. FT HELIX 471 475 {ECO:0000244|PDB:4Q7M}. FT HELIX 480 482 {ECO:0000244|PDB:4Q7M}. FT HELIX 486 489 {ECO:0000244|PDB:4Q7M}. FT HELIX 494 507 {ECO:0000244|PDB:4Q7M}. FT STRAND 511 516 {ECO:0000244|PDB:4Q7M}. FT STRAND 520 522 {ECO:0000244|PDB:4Q7L}. FT HELIX 524 538 {ECO:0000244|PDB:4Q7M}. FT STRAND 541 546 {ECO:0000244|PDB:4Q7M}. FT HELIX 552 555 {ECO:0000244|PDB:4Q7M}. FT STRAND 557 563 {ECO:0000244|PDB:4Q7M}. FT STRAND 566 571 {ECO:0000244|PDB:4Q7M}. FT HELIX 573 579 {ECO:0000244|PDB:4Q7M}. FT HELIX 582 591 {ECO:0000244|PDB:4Q7M}. FT HELIX 592 596 {ECO:0000244|PDB:3QF4}. SQ SEQUENCE 598 AA; 67708 MW; BDFA5A242F18393E CRC64; MPEIRRRPHG PILEKPALKN PTATLRRLLG YLRPHTFTLI MVFVFVTVSS ILGVLSPYLI GKTIDVVFVP RRFDLLPRYM LILGTIYALT SLLFWLQGKI MLTLSQDVVF RLRKELFEKL QRVPVGFFDR TPHGDIISRV INDVDNINNV LGNSIIQFFS GIVTLAGAVI MMFRVNVILS LVTLSIVPLT VLITQIVSSQ TRKYFYENQR VLGQLNGIIE EDISGLTVIK LFTREEKEME KFDRVNESLR KVGTKAQIFS GVLPPLMNMV NNLGFALISG FGGWLALKDI ITVGTIATFI GYSRQFTRPL NELSNQFNMI QMALASAERI FEILDLEEEK DDPDAVELRE VRGEIEFKNV WFSYDKKKPV LKDITFHIKP GQKVALVGPT GSGKTTIVNL LMRFYDVDRG QILVDGIDIR KIKRSSLRSS IGIVLQDTIL FSTTVKENLK YGNPGATDEE IKEAAKLTHS DHFIKHLPEG YETVLTDNGE DLSQGQRQLL AITRAFLANP KILILDEATS NVDTKTEKSI QAAMWKLMEG KTSIIIAHRL NTIKNADLII VLRDGEIVEM GKHDELIQKR GFYYELFTSQ YGLVVEKE // ID Y087_THEMA Reviewed; 277 AA. AC Q9WXU2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 92. DE RecName: Full=MEMO1 family protein TM_0087 {ECO:0000255|HAMAP-Rule:MF_00055}; GN OrderedLocusNames=TM_0087; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the MEMO1 family. {ECO:0000255|HAMAP- CC Rule:MF_00055}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35181.1; -; Genomic_DNA. DR PIR; A72420; A72420. DR RefSeq; NP_227903.1; NC_000853.1. DR RefSeq; WP_004082616.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXU2; -. DR STRING; 243274.TM0087; -. DR EnsemblBacteria; AAD35181; AAD35181; TM_0087. DR GeneID; 896914; -. DR KEGG; tma:TM0087; -. DR PATRIC; 23935014; VBITheMar51294_0085. DR eggNOG; ENOG41074MP; Bacteria. DR eggNOG; COG1355; LUCA. DR InParanoid; Q9WXU2; -. DR KO; K06990; -. DR OMA; ISMCGYG; -. DR OrthoDB; EOG63C0TM; -. DR Proteomes; UP000008183; Chromosome. DR HAMAP; MF_00055; MEMO1; 1. DR InterPro; IPR002737; MEMO1_fam. DR PANTHER; PTHR11060; PTHR11060; 1. DR Pfam; PF01875; Memo; 1. DR TIGRFAMs; TIGR04336; AmmeMemoSam_B; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 277 MEMO1 family protein TM_0087. FT /FTId=PRO_0000134374. SQ SEQUENCE 277 AA; 30476 MW; 1CC8129A9DA017FA CRC64; MKRKPAVAGL FYPSRRDELI EQIRMCFLDK RIGPGKLPGP VETKLQNPIG LVSPHAGYIY SGPVAAWGFL EAVKFGEPSV VVIIGPNHTG LGRPVGVWPE GEWETPLGTV PVNERAVEIV LSNSRYAEED FMSHIREHSI EVQIPFLQFV FGEVSIVPIC LMDQSPAVAE DLASALAKLV AEFPGVLIIA STDLNHYEDQ RTTLRKDSYI IEAIEGMDPS LLYEYLVRED ISMCGYGGVA TLLNMDFENV RILKHATSGD VSGDTLEVVG YLSAILF // ID Y1162_THEMA Reviewed; 226 AA. AC Q9X0P5; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=UPF0173 metal-dependent hydrolase TM_1162 {ECO:0000255|HAMAP-Rule:MF_00457}; GN OrderedLocusNames=TM_1162; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0173 family. {ECO:0000255|HAMAP- CC Rule:MF_00457}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36238.1; -; Genomic_DNA. DR PIR; H72287; H72287. DR RefSeq; NP_228968.1; NC_000853.1. DR RefSeq; WP_004080208.1; NZ_CP011107.1. DR PDB; 3X2X; X-ray; 3.42 A; A/B/C=1-226. DR PDB; 3X2Y; X-ray; 2.67 A; A/B/C=1-226. DR PDB; 3X2Z; X-ray; 2.33 A; A/B/C=1-226. DR PDB; 3X30; X-ray; 1.92 A; A=1-226. DR PDBsum; 3X2X; -. DR PDBsum; 3X2Y; -. DR PDBsum; 3X2Z; -. DR PDBsum; 3X30; -. DR ProteinModelPortal; Q9X0P5; -. DR STRING; 243274.TM1162; -. DR EnsemblBacteria; AAD36238; AAD36238; TM_1162. DR GeneID; 898324; -. DR KEGG; tma:TM1162; -. DR PATRIC; 23937261; VBITheMar51294_1179. DR eggNOG; ENOG4105E8R; Bacteria. DR eggNOG; COG2220; LUCA. DR InParanoid; Q9X0P5; -. DR OMA; IGMNIGG; -. DR OrthoDB; EOG6PCPVR; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.15.10; -; 1. DR HAMAP; MF_00457; UPF0173; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR022877; UPF0173. DR Pfam; PF12706; Lactamase_B_2; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 226 UPF0173 metal-dependent hydrolase FT TM_1162. FT /FTId=PRO_0000156388. FT STRAND 1 5 {ECO:0000244|PDB:3X30}. FT STRAND 11 22 {ECO:0000244|PDB:3X30}. FT HELIX 35 37 {ECO:0000244|PDB:3X30}. FT STRAND 42 45 {ECO:0000244|PDB:3X30}. FT HELIX 51 54 {ECO:0000244|PDB:3X30}. FT HELIX 57 64 {ECO:0000244|PDB:3X30}. FT STRAND 67 71 {ECO:0000244|PDB:3X30}. FT HELIX 72 80 {ECO:0000244|PDB:3X30}. FT STRAND 84 88 {ECO:0000244|PDB:3X30}. FT STRAND 93 96 {ECO:0000244|PDB:3X30}. FT STRAND 99 105 {ECO:0000244|PDB:3X30}. FT STRAND 111 114 {ECO:0000244|PDB:3X30}. FT STRAND 117 120 {ECO:0000244|PDB:3X30}. FT STRAND 125 131 {ECO:0000244|PDB:3X30}. FT STRAND 134 138 {ECO:0000244|PDB:3X30}. FT HELIX 146 154 {ECO:0000244|PDB:3X30}. FT STRAND 157 162 {ECO:0000244|PDB:3X30}. FT STRAND 166 168 {ECO:0000244|PDB:3X2Z}. FT HELIX 171 181 {ECO:0000244|PDB:3X30}. FT STRAND 184 190 {ECO:0000244|PDB:3X30}. FT STRAND 192 194 {ECO:0000244|PDB:3X30}. FT HELIX 195 197 {ECO:0000244|PDB:3X30}. FT HELIX 201 210 {ECO:0000244|PDB:3X30}. FT STRAND 223 226 {ECO:0000244|PDB:3X30}. SQ SEQUENCE 226 AA; 24644 MW; FB10EA6E72E873FF CRC64; MKVTFLGHAV VLIEGKKNII IDPFISGNPV CPVKLEGLPK IDYILVTHGH GDHLGDAVEI AKKNDATVIS NYEICHYLGK KGVKTHAMHI GGSYLFDFGR VKMTPAVHGS GILDGDSMIY GGNPSGFLIT IEGKKIYHAG DTGLTREMEL LAEENVDVAF LPIGGNFVMD VEDAVRAAVM IKPKKVVPMH YGTWELIFAD VELFKKKVEE KGVECVILEP GESLEL // ID Y1410_THEMA Reviewed; 323 AA. AC Q9X1D0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Uncharacterized protein TM_1410; GN OrderedLocusNames=TM_1410; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36481.1; -; Genomic_DNA. DR PIR; C72258; C72258. DR RefSeq; NP_229211.1; NC_000853.1. DR RefSeq; WP_004081643.1; NZ_CP011107.1. DR PDB; 2AAM; X-ray; 2.20 A; A/B/C/D/E/F=27-323. DR PDBsum; 2AAM; -. DR ProteinModelPortal; Q9X1D0; -. DR SMR; Q9X1D0; 27-313. DR STRING; 243274.TM1410; -. DR EnsemblBacteria; AAD36481; AAD36481; TM_1410. DR GeneID; 898066; -. DR KEGG; tma:TM1410; -. DR PATRIC; 23937766; VBITheMar51294_1422. DR eggNOG; ENOG4105GSQ; Bacteria. DR eggNOG; COG2342; LUCA. DR InParanoid; Q9X1D0; -. DR KO; K01884; -. DR OMA; PIAYISI; -. DR OrthoDB; EOG680WZX; -. DR EvolutionaryTrace; Q9X1D0; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR016063; Extracellular_prot. DR InterPro; IPR004352; GH114_TIM-barrel. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR016062; TM1410-rel. DR Pfam; PF03537; Glyco_hydro_114; 1. DR PRINTS; PR01545; THEMAYE10DUF. DR SUPFAM; SSF51445; SSF51445; 1. DR TIGRFAMs; TIGR01370; TIGR01370; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 323 Uncharacterized protein TM_1410. FT /FTId=PRO_0000107361. FT STRAND 38 40 {ECO:0000244|PDB:2AAM}. FT HELIX 46 50 {ECO:0000244|PDB:2AAM}. FT STRAND 55 59 {ECO:0000244|PDB:2AAM}. FT STRAND 61 66 {ECO:0000244|PDB:2AAM}. FT HELIX 67 69 {ECO:0000244|PDB:2AAM}. FT HELIX 73 81 {ECO:0000244|PDB:2AAM}. FT STRAND 85 96 {ECO:0000244|PDB:2AAM}. FT HELIX 105 108 {ECO:0000244|PDB:2AAM}. FT STRAND 114 118 {ECO:0000244|PDB:2AAM}. FT STRAND 121 127 {ECO:0000244|PDB:2AAM}. FT HELIX 132 147 {ECO:0000244|PDB:2AAM}. FT STRAND 151 156 {ECO:0000244|PDB:2AAM}. FT HELIX 160 167 {ECO:0000244|PDB:2AAM}. FT HELIX 172 193 {ECO:0000244|PDB:2AAM}. FT STRAND 198 203 {ECO:0000244|PDB:2AAM}. FT HELIX 205 210 {ECO:0000244|PDB:2AAM}. FT HELIX 214 218 {ECO:0000244|PDB:2AAM}. FT STRAND 220 230 {ECO:0000244|PDB:2AAM}. FT HELIX 237 252 {ECO:0000244|PDB:2AAM}. FT STRAND 256 264 {ECO:0000244|PDB:2AAM}. FT HELIX 270 285 {ECO:0000244|PDB:2AAM}. FT STRAND 288 294 {ECO:0000244|PDB:2AAM}. FT TURN 306 308 {ECO:0000244|PDB:2AAM}. SQ SEQUENCE 323 AA; 37719 MW; D6A16F72F8BBC93B CRC64; MSHLKNILFI IIVSLFFISS CSTVMSTEGW FMPFDNWLYQ LQNADPVEIS SSGFEIAVID YSKDGSESGE YSPEEIKIMV DAGVVPVAYV NIGQAEDYRF YWKESWYTNT PEWLGEEDPA WPGNYFVKYW YNEWKEIVFS YLDRVIDQGF KGIYLDRIDS FEYWAQEGVI SRRSAARKMI NFVLEIAEYV RERKPDMLII PQNGENILDF DDGQLASTVS GWAVENLFYL KTIPLEENET KSRLEYLIRL NRKGKFILSV DYVDDGSDSF ENISRILDYY EKAKRNGCIP YAARSDLELD EMNVIEGIQP PEALKDYESR TYR // ID Y1442_THEMA Reviewed; 110 AA. AC Q9X1F5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=Putative anti-sigma factor antagonist TM_1442; GN OrderedLocusNames=TM_1442; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: In the phosphorylated form it could act as an anti-anti- CC sigma factor that counteracts an anti-sigma factor and thus CC releases a sigma factor from inhibition. {ECO:0000250}. CC -!- PTM: Phosphorylated on a serine residue. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the anti-sigma-factor antagonist family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 STAS domain. {ECO:0000255|PROSITE- CC ProRule:PRU00198}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36511.1; -; Genomic_DNA. DR PIR; G72252; G72252. DR RefSeq; NP_229241.1; NC_000853.1. DR RefSeq; WP_004081714.1; NZ_CP011107.1. DR PDB; 1SBO; NMR; -; A=1-110. DR PDB; 1T6R; NMR; -; A=1-110. DR PDB; 1VC1; X-ray; 2.00 A; A/B=1-110. DR PDBsum; 1SBO; -. DR PDBsum; 1T6R; -. DR PDBsum; 1VC1; -. DR ProteinModelPortal; Q9X1F5; -. DR SMR; Q9X1F5; 1-110. DR STRING; 243274.TM1442; -. DR EnsemblBacteria; AAD36511; AAD36511; TM_1442. DR GeneID; 898033; -. DR KEGG; tma:TM1442; -. DR PATRIC; 23937834; VBITheMar51294_1455. DR eggNOG; ENOG41084GC; Bacteria. DR eggNOG; COG1366; LUCA. DR InParanoid; Q9X1F5; -. DR KO; K04749; -. DR OMA; FPIANSV; -. DR OrthoDB; EOG6J48NK; -. DR EvolutionaryTrace; Q9X1F5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 3.30.750.24; -; 1. DR InterPro; IPR003658; Anti-sigma_ant. DR InterPro; IPR002645; STAS_dom. DR Pfam; PF01740; STAS; 1. DR SUPFAM; SSF52091; SSF52091; 1. DR TIGRFAMs; TIGR00377; ant_ant_sig; 1. DR PROSITE; PS50801; STAS; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Phosphoprotein; Reference proteome. FT CHAIN 1 110 Putative anti-sigma factor antagonist FT TM_1442. FT /FTId=PRO_0000194208. FT DOMAIN 4 110 STAS. {ECO:0000255|PROSITE- FT ProRule:PRU00198}. FT MOD_RES 59 59 Phosphoserine. {ECO:0000250}. FT STRAND 5 11 {ECO:0000244|PDB:1VC1}. FT STRAND 14 21 {ECO:0000244|PDB:1VC1}. FT TURN 25 27 {ECO:0000244|PDB:1VC1}. FT HELIX 28 41 {ECO:0000244|PDB:1VC1}. FT STRAND 45 53 {ECO:0000244|PDB:1VC1}. FT HELIX 59 74 {ECO:0000244|PDB:1VC1}. FT STRAND 78 83 {ECO:0000244|PDB:1VC1}. FT HELIX 86 94 {ECO:0000244|PDB:1VC1}. FT HELIX 97 99 {ECO:0000244|PDB:1VC1}. FT STRAND 101 106 {ECO:0000244|PDB:1VC1}. FT TURN 107 109 {ECO:0000244|PDB:1VC1}. SQ SEQUENCE 110 AA; 12300 MW; EA1036F91820AC5D CRC64; MNNLKLDIVE QDDKAIVRVQ GDIDAYNSSE LKEQLRNFIS TTSKKKIVLD LSSVSYMDSA GLGTLVVILK DAKINGKEFI LSSLKESISR ILKLTHLDKI FKITDTVEEA // ID Y1557_THEMA Reviewed; 222 AA. AC Q9X1P3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 09-DEC-2015, entry version 91. DE RecName: Full=UPF0758 protein TM_1557; GN OrderedLocusNames=TM_1557; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36623.1; -; Genomic_DNA. DR PIR; H72239; H72239. DR RefSeq; NP_229357.1; NC_000853.1. DR RefSeq; WP_010865362.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1P3; -. DR STRING; 243274.TM1557; -. DR EnsemblBacteria; AAD36623; AAD36623; TM_1557. DR GeneID; 897343; -. DR KEGG; tma:TM1557; -. DR KEGG; tmw:THMA_1592; -. DR PATRIC; 23938076; VBITheMar51294_1575. DR eggNOG; ENOG4105W5Q; Bacteria. DR eggNOG; COG2003; LUCA. DR InParanoid; Q9X1P3; -. DR KO; K03630; -. DR OMA; PHEEFWV; -. DR OrthoDB; EOG6RRKTV; -. DR BioCyc; TMAR243274:GC6P-1598-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR001405; RadC. DR InterPro; IPR025657; RadC_JAB. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR020891; UPF0758_CS. DR Pfam; PF04002; RadC; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR TIGRFAMs; TIGR00608; radc; 1. DR PROSITE; PS01302; UPF0758; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 222 UPF0758 protein TM_1557. FT /FTId=PRO_0000190747. SQ SEQUENCE 222 AA; 24776 MW; D0276495753ED7F1 CRC64; MKRDGGRLLP RERMIKAGPE SLSVEELVAI VLRTGKKGKH VLELSKDLLE RFDGSLIKLS NASLEEIASV EGVGMVKAIT LKAALELGKR LHRELERIPE KLDSSVKVYK YCQEMVYLER EIVKVICLDT KLNVIGENTL TVGTSDRSLI HPRDVFRTAI RANASGVIVV HNHPSGDPTP SKEDRLITER LKQAGEILGV SLVDHVIVSR RGYFSFREEG EL // ID Y1690_THEMA Reviewed; 92 AA. AC Q9X216; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 76. DE RecName: Full=UPF0296 protein TM_1690 {ECO:0000255|HAMAP-Rule:MF_01503}; GN OrderedLocusNames=TM_1690; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0296 family. {ECO:0000255|HAMAP- CC Rule:MF_01503}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36757.1; -; Genomic_DNA. DR PIR; D72223; D72223. DR RefSeq; NP_229490.1; NC_000853.1. DR RefSeq; WP_004082206.1; NZ_CP011107.1. DR STRING; 243274.TM1690; -. DR EnsemblBacteria; AAD36757; AAD36757; TM_1690. DR GeneID; 897242; -. DR KEGG; tma:TM1690; -. DR PATRIC; 23938354; VBITheMar51294_1707. DR eggNOG; ENOG4105KC4; Bacteria. DR eggNOG; COG2052; LUCA. DR InParanoid; Q9X216; -. DR KO; K09777; -. DR OMA; NIGFGNM; -. DR OrthoDB; EOG62K20V; -. DR Proteomes; UP000008183; Chromosome. DR HAMAP; MF_01503; UPF0296; 1. DR InterPro; IPR007169; UPF0296. DR Pfam; PF04025; DUF370; 1. DR ProDom; PD063023; DUF370; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 92 UPF0296 protein TM_1690. FT /FTId=PRO_0000050239. SQ SEQUENCE 92 AA; 10437 MW; 71B7DBA29E9FF916 CRC64; MYGLINIGFG NVVAGDRVIA IVNPESSPLK RMKDEAKLEG KLIDATYGRK TRSIIITDSN HIILSAIQPE TIAQRFMENF YEIERVLRET KK // ID Y325_THEMA Reviewed; 251 AA. AC Q9WYG0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=Uncharacterized oxidoreductase TM_0325; DE EC=1.-.-.-; GN OrderedLocusNames=TM_0325; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35412.1; -; Genomic_DNA. DR PIR; G72389; G72389. DR RefSeq; NP_228136.1; NC_000853.1. DR RefSeq; WP_004083078.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYG0; -. DR STRING; 243274.TM0325; -. DR PRIDE; Q9WYG0; -. DR EnsemblBacteria; AAD35412; AAD35412; TM_0325. DR GeneID; 897270; -. DR KEGG; tma:TM0325; -. DR PATRIC; 23935529; VBITheMar51294_0330. DR eggNOG; ENOG41061TZ; Bacteria. DR eggNOG; COG1028; LUCA. DR InParanoid; Q9WYG0; -. DR KO; K00540; -. DR OMA; KGPWLAM; -. DR OrthoDB; EOG6N3CR8; -. DR BioCyc; RETL1328306-WGS:GSTH-3778-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 251 Uncharacterized oxidoreductase TM_0325. FT /FTId=PRO_0000054867. FT NP_BIND 10 34 NADP. {ECO:0000250}. FT ACT_SITE 152 152 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10001}. FT BINDING 139 139 Substrate. {ECO:0000250}. SQ SEQUENCE 251 AA; 26635 MW; 61C736A0F13564A5 CRC64; MNFQGKVVLI TGAGSGIGKK AAVMFAERGA KVAINDISEE KGKETVELIK SMGGEAAFIF GDVAKDAEQI VKKTVETFGR LDILVNNAGI VPYGNIEETS EEDFDKTMAV NVKGPFLLSK YAVEQMKKQG GGVIVNVSSE AGLIGIPRRC VYSVSKAALL GLTRSLAVDY VDYGIRVNAV CPGTTQSEGL MARVKASPNP EELLKKMTSR IPMKRLGKEE EIAFAILFAA CDEAGFMTGS IINIDGGSTA V // ID Y508_THEMA Reviewed; 599 AA. AC Q9WYX8; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Uncharacterized protein TM_0508; GN OrderedLocusNames=TM_0508; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase CC family. RarA/MGS1/WRNIP1 subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Macro domain. {ECO:0000255|PROSITE- CC ProRule:PRU00490}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35593.1; -; Genomic_DNA. DR PIR; B72368; B72368. DR RefSeq; NP_228318.1; NC_000853.1. DR RefSeq; WP_004081432.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYX8; -. DR STRING; 243274.TM0508; -. DR EnsemblBacteria; AAD35593; AAD35593; TM_0508. DR GeneID; 897552; -. DR KEGG; tma:TM0508; -. DR PATRIC; 23935921; VBITheMar51294_0515. DR eggNOG; ENOG4105D1H; Bacteria. DR eggNOG; COG2110; LUCA. DR eggNOG; COG2256; LUCA. DR InParanoid; Q9WYX8; -. DR KO; K07478; -. DR OMA; YRYDHDE; -. DR OrthoDB; EOG64FKG0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009378; F:four-way junction helicase activity; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR032423; AAA_assoc_2. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR002589; Macro_dom. DR InterPro; IPR021886; MgsA_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008824; RuvB_N. DR Pfam; PF16193; AAA_assoc_2; 1. DR Pfam; PF01661; Macro; 1. DR Pfam; PF12002; MgsA_C; 1. DR Pfam; PF05496; RuvB_N; 1. DR SMART; SM00506; A1pp; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF48019; SSF48019; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51154; MACRO; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 599 Uncharacterized protein TM_0508. FT /FTId=PRO_0000089221. FT DOMAIN 416 599 Macro. {ECO:0000255|PROSITE- FT ProRule:PRU00490}. FT NP_BIND 49 56 ATP. {ECO:0000255}. SQ SEQUENCE 599 AA; 67418 MW; B0FB5CB877155BC7 CRC64; MSISEKPLSE LLRPKDFEDF VGQDHIFGNK GILRRTLKTG NMFSSILYGP PGSGKTSVFS LLKRYFNGEV VYLSSTVHGV SEIKNVLKRG EQLRKYGKKL LLFLDEIHRL NKNQQMVLVS HVERGDIVLV ATTTENPSFV IVPALLSRCR ILYFKKLSDE DLMKILKKAT EVLNIDLEES VEKAIVRHSE GDARKLLNTL EIVHQAFKNK RVTLEDLETL LGNVSGYTKE SHYDFASAFI KSMRGSDPNA AVYYLVKMIE MGEDPRFIAR RMIIFASEDV GLADPNALHI AVSTSIAVEH VGLPECLMNL VECAVYLSLA PKSNSVYLAM KKVQELPVED VPLFLRNPVT EEMKKRGYGE GYLYPHDFGG FVKTNYLPEK LKNEVIFQPK RVGFEEELFE RLRKLWPEKY GGESMAEVRK ELEYKGKKIR IVKGDITREE VDAIVNAANE YLKHGGGVAG AIVRAGGSVI QEESDRIVQE RGRVPTGEAV VTSAGKLKAK YVIHTVGPVW RGGSHGEDEL LYKAVYNALL RAHELKLKSI SMPAISTGIF GFPKERAVGI FSKAIRDFID QHPDTTLEEI RICNIDEETT KIFEEKFSV // ID Y562A_THEMA Reviewed; 192 AA. AC P58008; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 1. DT 13-APR-2016, entry version 64. DE RecName: Full=Uncharacterized protein TM_0562.1; GN OrderedLocusNames=TM_0562.1; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP IDENTIFICATION. RA Medigue C., Bocs S.; RL Unpublished observations (APR-2001). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR InParanoid; P58008; -. DR OMA; GYFIFWL; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 192 Uncharacterized protein TM_0562.1. FT /FTId=PRO_0000216214. FT TRANSMEM 31 51 Helical. {ECO:0000255}. FT TRANSMEM 119 139 Helical. {ECO:0000255}. SQ SEQUENCE 192 AA; 22686 MW; 4A6C60F80E81FF80 CRC64; MLVKEREEKL NRVLVALLGI PVVFSIIRAK IVETIGYFIF WLGGFSPYVY EKITHQEIPE RTKLMLSSSV FLHSVMGQFL NFYEKIFFWD KILHFYGSFV ITYFFYQILT KKSRFWDEVP GAVLMAFLLG VFSGVLWEIA EFTTDKILPD YNTQKGLDDT MLDLIFDLLG CYTMAKIVYR KKTGRFFWRP RS // ID Y1570_THEMA Reviewed; 192 AA. AC Q9X1Q6; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 78. DE RecName: Full=Uncharacterized protein TM_1570; GN OrderedLocusNames=TM_1570; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: To A.aeolicus AQ_054. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36637.1; -; Genomic_DNA. DR PIR; C72237; C72237. DR RefSeq; NP_229370.1; NC_000853.1. DR RefSeq; WP_004081987.1; NZ_CP011107.1. DR PDB; 3DCM; X-ray; 2.00 A; X=1-192. DR PDBsum; 3DCM; -. DR ProteinModelPortal; Q9X1Q6; -. DR STRING; 243274.TM1570; -. DR EnsemblBacteria; AAD36637; AAD36637; TM_1570. DR GeneID; 897550; -. DR KEGG; tma:TM1570; -. DR PATRIC; 23938102; VBITheMar51294_1588. DR eggNOG; ENOG4108WTY; Bacteria. DR eggNOG; COG4752; LUCA. DR InParanoid; Q9X1Q6; -. DR OMA; DYILEPI; -. DR OrthoDB; EOG6J48RZ; -. DR EvolutionaryTrace; Q9X1Q6; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR019230; RNA_MeTrfase_dom. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF09936; Methyltrn_RNA_4; 1. DR SUPFAM; SSF75217; SSF75217; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 192 Uncharacterized protein TM_1570. FT /FTId=PRO_0000186836. FT STRAND 4 10 {ECO:0000244|PDB:3DCM}. FT STRAND 12 15 {ECO:0000244|PDB:3DCM}. FT STRAND 20 22 {ECO:0000244|PDB:3DCM}. FT HELIX 28 40 {ECO:0000244|PDB:3DCM}. FT STRAND 44 49 {ECO:0000244|PDB:3DCM}. FT HELIX 53 67 {ECO:0000244|PDB:3DCM}. FT HELIX 70 73 {ECO:0000244|PDB:3DCM}. FT STRAND 76 78 {ECO:0000244|PDB:3DCM}. FT HELIX 79 82 {ECO:0000244|PDB:3DCM}. FT STRAND 85 90 {ECO:0000244|PDB:3DCM}. FT HELIX 91 102 {ECO:0000244|PDB:3DCM}. FT STRAND 107 110 {ECO:0000244|PDB:3DCM}. FT HELIX 122 131 {ECO:0000244|PDB:3DCM}. FT STRAND 136 140 {ECO:0000244|PDB:3DCM}. FT HELIX 148 151 {ECO:0000244|PDB:3DCM}. FT STRAND 155 158 {ECO:0000244|PDB:3DCM}. FT TURN 161 164 {ECO:0000244|PDB:3DCM}. FT HELIX 172 183 {ECO:0000244|PDB:3DCM}. FT TURN 184 186 {ECO:0000244|PDB:3DCM}. SQ SEQUENCE 192 AA; 21978 MW; E6AD7DC7C3CA53B3 CRC64; MLEKVYVALI HYPIKGKDGS IISTAVTNLD VHDIARTART YNLKGYYIVT NLRAQQDMVS KMLKFWREGF GSRYNPSRAE SLKLVKLKSY LEDVLEDIES VEGERPLIFF TSAKKRENDI SFEEGRRIII ETEKPVLILL GTGWGLPDEI LEISDYVLEP IRAQSDFNHL SVRAAAAIII DRLIGENYAR RD // ID Y370_THEMA Reviewed; 242 AA. AC Q9WYK4; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 15-AUG-2003, sequence version 2. DT 11-MAY-2016, entry version 99. DE RecName: Full=UPF0273 protein TM_0370 {ECO:0000255|HAMAP-Rule:MF_01076}; GN OrderedLocusNames=TM_0370; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0273 family. {ECO:0000255|HAMAP- CC Rule:MF_01076}. CC -!- SIMILARITY: Contains 1 kaiC domain. {ECO:0000255|HAMAP- CC Rule:MF_01076}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35457.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35457.1; ALT_INIT; Genomic_DNA. DR PIR; H72384; H72384. DR RefSeq; NP_228181.1; NC_000853.1. DR RefSeq; WP_004083183.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYK4; -. DR SMR; Q9WYK4; 3-237. DR STRING; 243274.TM0370; -. DR EnsemblBacteria; AAD35457; AAD35457; TM_0370. DR GeneID; 897329; -. DR KEGG; tma:TM0370; -. DR PATRIC; 23935621; VBITheMar51294_0375. DR eggNOG; ENOG4105EHU; Bacteria. DR eggNOG; COG0467; LUCA. DR InParanoid; Q9WYK4; -. DR OMA; EEHPVQI; -. DR OrthoDB; EOG6ZPSVX; -. DR BioCyc; TMAR243274:GC6P-384-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central. DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central. DR GO; GO:0000150; F:recombinase activity; IBA:GO_Central. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central. DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central. DR GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central. DR GO; GO:0042148; P:strand invasion; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01076; UPF0273; 1. DR InterPro; IPR004504; DNA_repair_RadA. DR InterPro; IPR014774; KaiC-like_dom. DR InterPro; IPR010624; KaiC_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022475; UPF0273_KaiC-like. DR Pfam; PF06745; ATPase; 1. DR PRINTS; PR01874; DNAREPAIRADA. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03877; thermo_KaiC_1; 1. DR PROSITE; PS51146; KAIC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 242 UPF0273 protein TM_0370. FT /FTId=PRO_0000184583. FT DOMAIN 3 242 KaiC. {ECO:0000255|HAMAP-Rule:MF_01076}. FT NP_BIND 30 37 ATP. {ECO:0000255|HAMAP-Rule:MF_01076}. SQ SEQUENCE 242 AA; 26813 MW; 396431D4D5E48837 CRC64; MIKRVKTGIP GMDEILHGGI PERNIVLISG GPGTGKTIFS QQFIWNGLQM GEPGIYVALE EHPVQVKKNM EVFGWNVDPF EKEGKFAIVD AFTGGIGEYA EKEKYVVRDI DDVRELAEVL KRAVRETQAK RVVIDSVTTL YITKPAMARS IIFQLKRILS GLGCTSLFVS QVSVTEKGFG GPGVEHGVDG IIRLDLDEID GELKRSLIVW KMRGTSHSMR RHPFEITDKG IVIYPSEGGE GR // ID Y398_THEMA Reviewed; 377 AA. AC Q9WYM9; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=Uncharacterized protein TM_0398; GN OrderedLocusNames=TM_0398; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00609}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35483.1; -; Genomic_DNA. DR PIR; G72382; G72382. DR RefSeq; NP_228208.1; NC_000853.1. DR RefSeq; WP_004083231.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYM9; -. DR STRING; 243274.TM0398; -. DR MEROPS; C44.A09; -. DR EnsemblBacteria; AAD35483; AAD35483; TM_0398. DR GeneID; 897390; -. DR KEGG; tma:TM0398; -. DR PATRIC; 23935677; VBITheMar51294_0403. DR eggNOG; ENOG4105EYU; Bacteria. DR eggNOG; COG0067; LUCA. DR InParanoid; Q9WYM9; -. DR OMA; SYGINKR; -. DR OrthoDB; EOG6BKJ53; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GOC. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR012375; Glu_synth_lsu_1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR Pfam; PF00310; GATase_2; 1. DR PIRSF; PIRSF018774; GOGAT_lg_dom1; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Glutamine amidotransferase; Reference proteome. FT CHAIN 1 377 Uncharacterized protein TM_0398. FT /FTId=PRO_0000107292. FT DOMAIN 20 377 Glutamine amidotransferase type-2. FT {ECO:0000255|PROSITE-ProRule:PRU00609}. FT ACT_SITE 20 20 For GATase activity. {ECO:0000250}. SQ SEQUENCE 377 AA; 42651 MW; A69DFA1946792248 CRC64; MSYDLPRLTP DKDFKVPSAC GVSGIMNTSG KRFSGSVIVE SMALMRERGN GLGAGYAAYG IYPELKDLYC FHMLYDSDLD KKNAEEYIKD HYEIIESEPI PTRKNPHIKE VHILWRYFLK PKFIPEDMSE EDFVVSTVMF INEKINGAFV MSSGKNMGVF KGVGFPEDIA DFYRIDEYKG YIWTAHNRFP TNTVGWWGGA HPFGILDWTV VHNGEISSYG INRRFLEAYG YKCTLMTDTE VVAYLVDLFM RRFGYSPQLT AKILAAPLWK DIDLMPEEER KLYTALRMNY GGALLNGPFA IIVANNNMMM GLNDRIKLRP LVAATKDDFL YIASEESAIR VVCPEPDEVW APKAGDPVVG VLKSARKTQV VLEGENG // ID Y326_THEMA Reviewed; 280 AA. AC Q9WYG1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator TM_0326; GN OrderedLocusNames=TM_0326; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains 1 HTH rpiR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00390}. CC -!- SIMILARITY: Contains 1 SIS domain. {ECO:0000255|PROSITE- CC ProRule:PRU00797}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35413.1; -; Genomic_DNA. DR PIR; H72389; H72389. DR RefSeq; NP_228137.1; NC_000853.1. DR RefSeq; WP_004083079.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYG1; -. DR STRING; 243274.TM0326; -. DR EnsemblBacteria; AAD35413; AAD35413; TM_0326. DR GeneID; 897271; -. DR KEGG; tma:TM0326; -. DR PATRIC; 23935531; VBITheMar51294_0331. DR eggNOG; ENOG4106KNT; Bacteria. DR eggNOG; COG1737; LUCA. DR InParanoid; Q9WYG1; -. DR OMA; LRPAAMS; -. DR OrthoDB; EOG6HMXHM; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR000281; HTH_RpiR. DR InterPro; IPR001347; SIS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01418; HTH_6; 1. DR Pfam; PF01380; SIS; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS51071; HTH_RPIR; 1. DR PROSITE; PS51464; SIS; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 280 Uncharacterized HTH-type transcriptional FT regulator TM_0326. FT /FTId=PRO_0000068632. FT DOMAIN 1 78 HTH rpiR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00390}. FT DOMAIN 123 263 SIS. {ECO:0000255|PROSITE- FT ProRule:PRU00797}. FT DNA_BIND 37 57 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00390}. SQ SEQUENCE 280 AA; 31117 MW; AA7D3C0212BCBD30 CRC64; MDVIQRIKEK YDEFTNAEKK IADTILSDPK GIIESSISDL SEKAGVKSEA SVVKFYKKLG LNSFQQFKVL LAQSISRAPL EIVYEDVSSE DDTKTITEKI FKATVRAILD TLNWLDIDSI ERTVDLFKNA QRIIFIGFAA SAAVAFDAFH KFTRIGKNCL FSNDEHIIAA ILATASPSDL LVAISHTGET ISVVNFAKKA KEMKMPVVTI TGNRKSTLAK YSDVVLATNT KETKIRTDAM TSRIVQLVIL DTIYTLLAAR DPRAIENLNK SRLAVSELKY // ID Y352_THEMA Reviewed; 234 AA. AC Q9WYI7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein TM_0352; GN OrderedLocusNames=TM_0352; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35439.1; -; Genomic_DNA. DR PIR; H72385; H72385. DR RefSeq; NP_228163.1; NC_000853.1. DR RefSeq; WP_004083143.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYI7; -. DR SMR; Q9WYI7; 5-224. DR STRING; 243274.TM0352; -. DR EnsemblBacteria; AAD35439; AAD35439; TM_0352. DR GeneID; 897308; -. DR KEGG; tma:TM0352; -. DR PATRIC; 23935585; VBITheMar51294_0357. DR eggNOG; ENOG4105D6C; Bacteria. DR eggNOG; COG1136; LUCA. DR InParanoid; Q9WYI7; -. DR KO; K02003; -. DR OMA; QISHIRC; -. DR OrthoDB; EOG6T7N3V; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 234 Uncharacterized ABC transporter ATP- FT binding protein TM_0352. FT /FTId=PRO_0000093280. FT DOMAIN 5 234 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 41 48 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 234 AA; 26254 MW; 8A762A4852BF08D5 CRC64; MKKVMELVDV WKIYDLGEVK VEALRGVSFE VFEGEYVIII GPSGSGKSTL LHILGCLDRP TKGKVLIEGE EVSRMGDRRL AQVRNRKIGF VFQSYNLLPR LTALENVELP MIYAGVPAKE RKRRAKELLE LVGLGDRLHH RPNQLSGGQQ QRVAIARALA NDPVFILADE PTGNLDTKTG EEILELFRKL HEMGKTLVVV THNLEMVDEG TCIVRIRDGR IEGIERRGVV YGDT // ID Y416_THEMA Reviewed; 270 AA. AC Q9WYP7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=Uncharacterized protein TM_0416; GN OrderedLocusNames=TM_0416; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35501.1; -; Genomic_DNA. DR PIR; F72381; F72381. DR RefSeq; NP_228226.1; NC_000853.1. DR RefSeq; WP_004083268.1; NZ_CP011107.1. DR PDB; 2ZVR; X-ray; 2.20 A; A/B=1-270. DR PDBsum; 2ZVR; -. DR ProteinModelPortal; Q9WYP7; -. DR STRING; 243274.TM0416; -. DR EnsemblBacteria; AAD35501; AAD35501; TM_0416. DR GeneID; 897418; -. DR KEGG; tma:TM0416; -. DR PATRIC; 23935715; VBITheMar51294_0421. DR eggNOG; ENOG4107S8A; Bacteria. DR eggNOG; COG1082; LUCA. DR InParanoid; Q9WYP7; -. DR OMA; LADTFHM; -. DR OrthoDB; EOG6NKQXM; -. DR BioCyc; MetaCyc:MONOMER-17951; -. DR EvolutionaryTrace; Q9WYP7; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF01261; AP_endonuc_2; 1. DR SUPFAM; SSF51658; SSF51658; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 270 Uncharacterized protein TM_0416. FT /FTId=PRO_0000209114. FT STRAND 2 7 {ECO:0000244|PDB:2ZVR}. FT HELIX 20 33 {ECO:0000244|PDB:2ZVR}. FT STRAND 36 41 {ECO:0000244|PDB:2ZVR}. FT HELIX 45 47 {ECO:0000244|PDB:2ZVR}. FT HELIX 50 60 {ECO:0000244|PDB:2ZVR}. FT STRAND 64 68 {ECO:0000244|PDB:2ZVR}. FT HELIX 71 74 {ECO:0000244|PDB:2ZVR}. FT HELIX 85 105 {ECO:0000244|PDB:2ZVR}. FT STRAND 108 112 {ECO:0000244|PDB:2ZVR}. FT HELIX 113 115 {ECO:0000244|PDB:2ZVR}. FT HELIX 123 140 {ECO:0000244|PDB:2ZVR}. FT STRAND 146 148 {ECO:0000244|PDB:2ZVR}. FT TURN 153 155 {ECO:0000244|PDB:2ZVR}. FT HELIX 162 172 {ECO:0000244|PDB:2ZVR}. FT STRAND 177 182 {ECO:0000244|PDB:2ZVR}. FT HELIX 183 189 {ECO:0000244|PDB:2ZVR}. FT HELIX 193 200 {ECO:0000244|PDB:2ZVR}. FT HELIX 201 203 {ECO:0000244|PDB:2ZVR}. FT STRAND 204 209 {ECO:0000244|PDB:2ZVR}. FT STRAND 214 216 {ECO:0000244|PDB:2ZVR}. FT HELIX 224 233 {ECO:0000244|PDB:2ZVR}. FT STRAND 238 242 {ECO:0000244|PDB:2ZVR}. FT TURN 247 249 {ECO:0000244|PDB:2ZVR}. FT HELIX 251 265 {ECO:0000244|PDB:2ZVR}. SQ SEQUENCE 270 AA; 30464 MW; 10948413A7624158 CRC64; MKLSLVISTS DAAFDALAFK GDLRKGMELA KRVGYQAVEI AVRDPSIVDW NEVKILSEEL NLPICAIGTG QAYLADGLSL THPNDEIRKK AIERVVKHTE VAGMFGALVI IGLVRGRREG RSYEETEELF IESMKRLLEL TEHAKFVIEP LNRYETDFIN TIDDALRILR KINSNRVGIL ADTFHMNIEE VNIPESLKRA GEKLYHFHVA DSNRWAPGCG HFDFRSVFNT LKEIGYNRYV SVECLPLPGG MEEAAEIAFK TLKELIIKLT // ID Y687_THEMA Reviewed; 118 AA. AC Q9WZF3; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Nucleoid-associated protein TM_0687 {ECO:0000255|HAMAP-Rule:MF_00274}; GN OrderedLocusNames=TM_0687; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Binds to DNA and alters its conformation. May be CC involved in regulation of gene expression, nucleoid organization CC and DNA protection. {ECO:0000255|HAMAP-Rule:MF_00274}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00274}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP- CC Rule:MF_00274}. CC -!- SIMILARITY: Belongs to the YbaB/EbfC family. {ECO:0000255|HAMAP- CC Rule:MF_00274}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35769.1; -; Genomic_DNA. DR PIR; E72344; E72344. DR RefSeq; NP_228496.1; NC_000853.1. DR RefSeq; WP_004081076.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZF3; -. DR STRING; 243274.TM0687; -. DR EnsemblBacteria; AAD35769; AAD35769; TM_0687. DR GeneID; 898354; -. DR KEGG; tma:TM0687; -. DR PATRIC; 23936292; VBITheMar51294_0699. DR eggNOG; ENOG41085TI; Bacteria. DR eggNOG; COG0718; LUCA. DR InParanoid; Q9WZF3; -. DR KO; K09747; -. DR OMA; MQQEMLK; -. DR OrthoDB; EOG6DVJWP; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043590; C:bacterial nucleoid; IEA:UniProtKB-HAMAP. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1310.10; -; 1. DR HAMAP; MF_00274; DNA_YbaB_EbfC; 1. DR InterPro; IPR004401; YbaB/EbfC. DR Pfam; PF02575; YbaB_DNA_bd; 1. DR PIRSF; PIRSF004555; UCP004555; 1. DR SUPFAM; SSF82607; SSF82607; 1. DR TIGRFAMs; TIGR00103; DNA_YbaB_EbfC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome. FT CHAIN 1 118 Nucleoid-associated protein TM_0687. FT /FTId=PRO_0000170458. SQ SEQUENCE 118 AA; 13394 MW; 73FAF4EF8A6C4593 CRC64; MKKIKSFGGK SLGGGKQEKI LKDFARMQEE LQKKIQELEE SFSQIEVEAS VGGGAVRIVA TCDRRVKDIE IDEDLKEDFD TLKDLLIAGM NEVMEKIEKR REEEMSKITQ QFGIPGLM // ID Y928_THEMA Reviewed; 246 AA. AC P56728; P46803; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Uncharacterized protein TM_0928; GN OrderedLocusNames=TM_0928; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8168477; RA Darimont B., Sterner R.; RT "Sequence, assembly and evolution of a primordial ferredoxin from RT Thermotoga maritima."; RL EMBO J. 13:1772-1781(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CAUTION: Was originally proposed to be fused with TM_0929. CC {ECO:0000305|PubMed:8168477}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA65436.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA57668.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U24145; AAA65436.1; ALT_INIT; Genomic_DNA. DR EMBL; X82178; CAA57668.1; ALT_INIT; Genomic_DNA. DR EMBL; AE000512; AAD36009.1; -; Genomic_DNA. DR PIR; H72314; H72314. DR RefSeq; NP_228736.1; NC_000853.1. DR RefSeq; WP_004080634.1; NZ_CP011107.1. DR STRING; 243274.TM0928; -. DR EnsemblBacteria; AAD36009; AAD36009; TM_0928. DR GeneID; 898602; -. DR KEGG; tma:TM0928; -. DR PATRIC; 23936787; VBITheMar51294_0942. DR eggNOG; ENOG41063SX; Bacteria. DR eggNOG; ENOG4112C5G; LUCA. DR OMA; REPCIYR; -. DR OrthoDB; EOG6FZ4CR; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR032606; DUF4895. DR Pfam; PF16236; DUF4895; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 246 Uncharacterized protein TM_0928. FT /FTId=PRO_0000216215. SQ SEQUENCE 246 AA; 29365 MW; 2A32302C773042C9 CRC64; MKRELELLLK ETSVHNPLKD YESKLDNVHL HTFVLRIKRH RFPSLFLMID TSDRRLLNLS VEDPFDREPC IYRVEADVPE SMVSFYTKLF EKVDSVSAGI FRMPLKVKVL RSAGNESWLQ KIFLQEKVKN MEFFLFQNRV SDENLEKMMK LLKSRLKIVL RNEGIDVFLE TPEWVDKEHI SLLHEMGVVL RKKKGIQPAQ NPMEQAFLTL RVGYDQFFEE DFDMEYFAKD FMEKLKRMYE VLVSML // ID Y337_THEMA Reviewed; 567 AA. AC Q9WYH2; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 2. DT 11-MAY-2016, entry version 84. DE RecName: Full=UPF0313 protein TM_0337 {ECO:0000255|HAMAP-Rule:MF_01251}; GN OrderedLocusNames=TM_0337; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01251}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01251}; CC -!- SIMILARITY: Belongs to the UPF0313 family. {ECO:0000255|HAMAP- CC Rule:MF_01251}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35424.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35424.1; ALT_INIT; Genomic_DNA. DR PIR; C72391; C72391. DR RefSeq; NP_228148.1; NC_000853.1. DR RefSeq; WP_004083105.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYH2; -. DR STRING; 243274.TM0337; -. DR EnsemblBacteria; AAD35424; AAD35424; TM_0337. DR GeneID; 897292; -. DR KEGG; tma:TM0337; -. DR PATRIC; 23935555; VBITheMar51294_0342. DR eggNOG; ENOG4105CCT; Bacteria. DR eggNOG; COG1032; LUCA. DR InParanoid; Q9WYH2; -. DR OMA; NLNTDHS; -. DR OrthoDB; EOG6742TW; -. DR BioCyc; TMAR243274:GC6P-351-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.80.30.20; -; 1. DR HAMAP; MF_01251; UPF0313; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR022946; UPF0313. DR InterPro; IPR024560; UPF0313_C. DR InterPro; IPR013704; UPF0313_N. DR Pfam; PF11842; DUF3362; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF08497; Radical_SAM_N; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR03904; SAM_YgiQ; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 567 UPF0313 protein TM_0337. FT /FTId=PRO_0000076397. FT METAL 303 303 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01251}. FT METAL 307 307 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01251}. FT METAL 310 310 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01251}. SQ SEQUENCE 567 AA; 64967 MW; 8ED2B2F52606555F CRC64; MFLPTTREEM RKLGWKELDI ILVTGDAYVD HPSFGVAFIG HYLVSHGFKV GIIAQPDWRT EKDITRLGRP RLFFGVTAGN VDSMVANYTA SKKKRKTDDY TPGGIGGKRP DRATIVYTNL IKRFFPEVPV VLGGLEASLR RFAHYDWWSD RVRKSVLVDS KADLLVYGMG EKAVLGIAQI LSRTGDIEKC KSIRGVVWWA SQKPEEGIEL PSYDEISENP EKYAEALKLQ TWYTDPYKNI PIYQRQDTRY VVQNPPQPPL SQEELDRLYL LPFEREVHPF YAKMGKVKAI ETVKFSITAV RGCFGNCSFC ALTQHQTTHV SYRSKDSILE EVRILTKKKD FKGTITDVGG PTANLYGSGC SIRETKGQCQ KFCLYPIVCK VVRPNHDEFI SLLESIRQIP GVRNVFVSSG IRHDFVFAEK DPDVFIRELV KYTPGQLKLA PEHAHPKVLS LMRKPPVELF LEFKKRFETL AKKMGKRKYV IGYFIVGHPG EGWRENNYLR DFILKHLGYF PQQIQIFTPT PGTVSTAMYY SGVDPFTGEK VHVERSLKVR NKMKENVLFK KKGREKR // ID Y890_THEMA Reviewed; 501 AA. AC Q9WZZ2; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=Putative zinc metalloprotease TM_0890; DE EC=3.4.24.-; GN OrderedLocusNames=TM_0890; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. {ECO:0000255|PROSITE- CC ProRule:PRU00143}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35971.1; -; Genomic_DNA. DR PIR; C72321; C72321. DR RefSeq; NP_228698.1; NC_000853.1. DR RefSeq; WP_004080697.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZZ2; -. DR STRING; 243274.TM0890; -. DR MEROPS; M50.004; -. DR EnsemblBacteria; AAD35971; AAD35971; TM_0890. DR GeneID; 898564; -. DR KEGG; tma:TM0890; -. DR PATRIC; 23936711; VBITheMar51294_0904. DR eggNOG; ENOG4105DZP; Bacteria. DR eggNOG; COG0750; LUCA. DR InParanoid; Q9WZZ2; -. DR KO; K11749; -. DR OMA; NEAYAFV; -. DR OrthoDB; EOG66F07W; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 2.30.42.10; -; 1. DR InterPro; IPR001478; PDZ. DR InterPro; IPR008915; Peptidase_M50. DR Pfam; PF13180; PDZ_2; 1. DR Pfam; PF02163; Peptidase_M50; 1. DR SMART; SM00228; PDZ; 2. DR SUPFAM; SSF50156; SSF50156; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Metal-binding; Metalloprotease; Protease; KW Reference proteome; Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1 501 Putative zinc metalloprotease TM_0890. FT /FTId=PRO_0000088473. FT TRANSMEM 93 115 Helical. {ECO:0000255}. FT TRANSMEM 401 420 Helical. {ECO:0000255}. FT TRANSMEM 427 449 Helical. {ECO:0000255}. FT TRANSMEM 474 496 Helical. {ECO:0000255}. FT DOMAIN 96 180 PDZ. {ECO:0000255|PROSITE- FT ProRule:PRU00143}. FT ACT_SITE 18 18 {ECO:0000255|PROSITE-ProRule:PRU10095}. FT METAL 17 17 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 21 21 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. SQ SEQUENCE 501 AA; 55876 MW; CE3E581117DC2A9A CRC64; MVIVYFILIL TGVIMVHELG HYLFARLFKV KVLEFAIGFG PKIFSVKGRE TTFRLNVFPI GGYVRMLGEE GEEIADEEEK EKSFYAKPAW QRFLITLAGP LFSILAGYLL FLPITLNWGI ALPGIDEVVP GSPAEEAGLR RGDIIYSIND KIAFDTSIIS NEIQKGLPVE LVIIRNGEKK SLRLTPRMYP ETYEFVLESA EGTPSGKLVS VNGNRDTSVL KEFVNEYVVL EFEGGTVKGI LKQFNEIPAR YMIGISFSGL APVFKKDIYF KEGLFVFKKG DRIVRVEDQE IEGWQDLVVL YQRLTLGKDT MIVSLQGENI EWWRGLSGSV RVVIKRGDST IEKNVEASFL KNILETPDLL EMGVPRYKPK NPLEAVNLSV KACNYVLLTT ASSLKNFFRN VQTGQIVGVV GLAGVISAAS KTGLEAVLTV VAVITISLGV LNLLPLPALD GGRIIFSLVE MITRKKLNPQ VENIIHFLGF IFLMILFLYI TFLDIGRMMG I // ID YB5A_THEMA Reviewed; 240 AA. AC P58009; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Uncharacterized protein TM_1158.1; GN OrderedLocusNames=TM_1158.1; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP IDENTIFICATION. RA Medigue C., Bocs S.; RL Unpublished observations (APR-2001). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; WP_004080218.1; NZ_CP011107.1. DR ProteinModelPortal; P58009; -. DR KEGG; tmi:THEMA_08545; -. DR KEGG; tmw:THMA_1183; -. DR InParanoid; P58009; -. DR OMA; ILMFDEY; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR Gene3D; 3.40.800.10; -; 1. DR InterPro; IPR006035; Ureohydrolase. DR InterPro; IPR023696; Ureohydrolase_domain. DR PANTHER; PTHR11358; PTHR11358; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 240 Uncharacterized protein TM_1158.1. FT /FTId=PRO_0000216218. SQ SEQUENCE 240 AA; 27773 MW; 1BEF66C1C8BD2700 CRC64; MIPPHIHILD FNGIYEEQRI LKSLAEFVFS KKIEGIRYMV LPEKIPEIEN ILPSHLGVTF LGDGEFHHLT YFIIKKIKRP FVLVVFDNHL DAREEEFLTC DSWIRKALKL KHLVKVVVVG TQEQEKIHRV FYSETDPQKI LKLLGRHPVY LSIDKDVLDI GITGWESGRV SLEDLLNVLR HIPLRKILGA DICGEPDPLE FWKMQESEKV NLSILSALFF EKLHYVPGSE HLEGKPAHVT // ID YE6A_THEMA Reviewed; 168 AA. AC P58010; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein TM_1467.1; GN OrderedLocusNames=TM_1467.1; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP IDENTIFICATION. RA Medigue C., Bocs S.; RL Unpublished observations (APR-2001). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; WP_004081768.1; NZ_CP011107.1. DR KEGG; tmi:THEMA_06965; -. DR KEGG; tmw:THMA_1499; -. DR OMA; YREILMP; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 168 Uncharacterized protein TM_1467.1. FT /FTId=PRO_0000216220. FT TRANSMEM 41 61 Helical. {ECO:0000255}. FT TRANSMEM 133 153 Helical. {ECO:0000255}. SQ SEQUENCE 168 AA; 19408 MW; A3747AE2270D7B12 CRC64; MMIDVFLIAL LLSILTGNIK NVLKYNYKGL YLFAIPFVLQ LLPWKEILVP LSFVMLFLFF IWNRNIPGFK LMAIGAVLNG FTMSVNGGKM PVWEPTLKLL NLDLDFKHTA FTEFSWKTLL ADYIPVYLPW GRKFVISVGD ILVFIGVFIF FVLKPRFQTQ PSRVPHES // ID Y466_THEMA Reviewed; 253 AA. AC Q9WYT7; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 04-AUG-2003, sequence version 2. DT 13-APR-2016, entry version 93. DE RecName: Full=Probable transcriptional regulatory protein TM_0466 {ECO:0000255|HAMAP-Rule:MF_00693}; GN OrderedLocusNames=TM_0466; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00693}. CC -!- SIMILARITY: Belongs to the TACO1 family. {ECO:0000255|HAMAP- CC Rule:MF_00693}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD35550.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35550.1; ALT_INIT; Genomic_DNA. DR PIR; B72374; B72374. DR RefSeq; NP_228276.1; NC_000853.1. DR RefSeq; WP_004081500.1; NZ_CP011107.1. DR RefSeq; WP_010865126.1; NC_000853.1. DR ProteinModelPortal; Q9WYT7; -. DR SMR; Q9WYT7; 5-246. DR STRING; 243274.TM0466; -. DR EnsemblBacteria; AAD35550; AAD35550; TM_0466. DR GeneID; 897497; -. DR KEGG; tma:TM0466; -. DR PATRIC; 23935829; VBITheMar51294_0473. DR eggNOG; ENOG4105CDY; Bacteria. DR eggNOG; COG0217; LUCA. DR InParanoid; Q9WYT7; -. DR OMA; MTRNGGS; -. DR OrthoDB; EOG6HJ29R; -. DR BioCyc; TMAR243274:GC6P-486-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.200; -; 1. DR Gene3D; 3.30.1270.10; -; 2. DR Gene3D; 3.30.70.980; -; 1. DR HAMAP; MF_00693; Transcrip_reg_TACO1; 1. DR InterPro; IPR017856; Integrase_Zn-bd_dom-like_N. DR InterPro; IPR002876; Transcrip_reg_TACO1-like. DR InterPro; IPR026563; Transcrip_reg_TACO1-like_dom2. DR InterPro; IPR026564; Transcrip_reg_TACO1-like_dom3. DR InterPro; IPR029072; YebC-like. DR PANTHER; PTHR12532; PTHR12532; 1. DR Pfam; PF01709; Transcrip_reg; 1. DR SUPFAM; SSF75625; SSF75625; 1. DR TIGRFAMs; TIGR01033; TIGR01033; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 253 Probable transcriptional regulatory FT protein TM_0466. FT /FTId=PRO_0000175917. SQ SEQUENCE 253 AA; 28463 MW; 42B3E9F03311C5DB CRC64; MSGHNKWANI KHRKMAQDAK KSKIFTKLIR EIIVAAREGG GNIETNPRLR AAVERARAEN MPKENIERAI KRGTGELEGV DYQEVIYEGY APGGVAVYIR ALTDNKNRTA QELRHLFNKY GGSLAESGSV SWIFERKGVI EISRDKVKDL EELMMIAIDA GAEDIKDAED PIQIITAPEN LSEVKSKLEE AGYEVEAKVT FIPKNTVKVT GKDAEKVLEF LNALEDMDDV QEVYSNFEMD DKEMEEILSR LEG // ID Y859_THEMA Reviewed; 116 AA. AC Q9WZW3; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=UPF0092 membrane protein TM_0859; GN OrderedLocusNames=TM_0859; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0092 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35941.1; -; Genomic_DNA. DR PIR; D72325; D72325. DR RefSeq; NP_228668.1; NC_000853.1. DR RefSeq; WP_004080747.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZW3; -. DR STRING; 243274.TM0859; -. DR EnsemblBacteria; AAD35941; AAD35941; TM_0859. DR GeneID; 898532; -. DR KEGG; tma:TM0859; -. DR PATRIC; 23936646; VBITheMar51294_0872. DR eggNOG; ENOG4107Z7W; Bacteria. DR eggNOG; COG1862; LUCA. DR InParanoid; Q9WZW3; -. DR KO; K03210; -. DR OMA; KTMPHRT; -. DR OrthoDB; EOG6RNQKV; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR003849; Preprotein_translocase_YajC. DR Pfam; PF02699; YajC; 1. DR PRINTS; PR01853; YAJCTRNLCASE. DR SMART; SM01323; YajC; 1. DR TIGRFAMs; TIGR00739; yajC; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 116 UPF0092 membrane protein TM_0859. FT /FTId=PRO_0000097035. FT TRANSMEM 25 45 Helical. {ECO:0000255}. SQ SEQUENCE 116 AA; 12843 MW; E2836793CA744EA3 CRC64; MPEIIYAAAP GASNGTTTTA TGGGWGSLLF MLIFFIAIFY FMIILPQRRR EKQFQQMISQ MKRGDTVVTI GGIVGKVIDI KKDTVKIKTA NSTELEITKR AISTVIKERS QENQEG // ID Y964_THEMA Reviewed; 402 AA. AC Q9X059; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=UPF0272 protein TM_0964 {ECO:0000255|HAMAP-Rule:MF_01074}; GN OrderedLocusNames=TM_0964; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0272 family. {ECO:0000255|HAMAP- CC Rule:MF_01074}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36043.1; -; Genomic_DNA. DR PIR; A72312; A72312. DR RefSeq; NP_228772.1; NC_000853.1. DR RefSeq; WP_004080598.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X059; -. DR STRING; 243274.TM0964; -. DR EnsemblBacteria; AAD36043; AAD36043; TM_0964. DR GeneID; 898701; -. DR KEGG; tma:TM0964; -. DR PATRIC; 23936859; VBITheMar51294_0978. DR eggNOG; ENOG4108086; Bacteria. DR eggNOG; COG1641; LUCA. DR InParanoid; Q9X059; -. DR KO; K09121; -. DR OMA; TMKKGRP; -. DR OrthoDB; EOG6FRCSF; -. DR Proteomes; UP000008183; Chromosome. DR HAMAP; MF_01074; UPF0272; 1. DR InterPro; IPR002822; UPF0272. DR Pfam; PF01969; DUF111; 1. DR TIGRFAMs; TIGR00299; TIGR00299; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 402 UPF0272 protein TM_0964. FT /FTId=PRO_0000146856. SQ SEQUENCE 402 AA; 45064 MW; B712DE541A0E30A3 CRC64; MRILYLDPFS GISGDMFLGL LVDLGVDPEK IKSRLEKLNV EFDLVVKKVN KKGVTATKVD VVFPRKEHHE DHIVSDHDHH HHHGRHLSEI VEVLSRLEDP LKEKAIRMFE ALAEAESKIH GLSKEKVHFH EVGAMDAVIE IAGAVVGLEL LEVEKVFCGT VNTGSGFVMT EHGRYPVPAP ATAELLKGIP IYMDQKVRAE LVTPTGAVIL KILVDEFRTP ILRVEKVGYG AGTMDLEIPN VLRGYLGYIE PSERTGDVLI ETNVDDMNPQ LFGHLMERLF EAGAKDVFFT PIYMKKNRPA VKVSVLCHES KKDEILKLLF KESTSIGARV FYPEKVEATR TLKTVKTEYG EIPVKIASFD SEIVNISPEY EACKKVAQEK GIPLKEVYRA VYKSVSEVRN DV // ID Y983_THEMA Reviewed; 79 AA. AC Q9X078; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=UPF0033 protein TM_0983; GN OrderedLocusNames=TM_0983; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP STRUCTURE BY NMR. RX PubMed=11854485; DOI=10.1073/pnas.042684599; RA Yee A., Chang X., Pineda-Lucena A., Wu B., Semesi A., Le B., RA Ramelot T., Lee G.M., Bhattacharyya S., Gutierrez P., Denisov A., RA Lee C.-H., Cort J.R., Kozlov G., Liao J., Finak G., Chen L., RA Wishart D., Lee W., McIntosh L.P., Gehring K., Kennedy M.A., RA Edwards A.M., Arrowsmith C.H.; RT "An NMR approach to structural proteomics."; RL Proc. Natl. Acad. Sci. U.S.A. 99:1825-1830(2002). CC -!- SIMILARITY: Belongs to the UPF0033 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36062.1; -; Genomic_DNA. DR PIR; D72310; D72310. DR RefSeq; NP_228791.1; NC_000853.1. DR RefSeq; WP_004080581.1; NZ_CP011107.1. DR PDB; 1JDQ; NMR; -; A=1-79. DR PDBsum; 1JDQ; -. DR ProteinModelPortal; Q9X078; -. DR SMR; Q9X078; 1-79. DR STRING; 243274.TM0983; -. DR EnsemblBacteria; AAD36062; AAD36062; TM_0983. DR GeneID; 898729; -. DR KEGG; tma:TM0983; -. DR PATRIC; 23936895; VBITheMar51294_0996. DR eggNOG; ENOG41084XP; Bacteria. DR eggNOG; COG0425; LUCA. DR InParanoid; Q9X078; -. DR OMA; SEWRILI; -. DR OrthoDB; EOG6W9XFB; -. DR EvolutionaryTrace; Q9X078; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.30.110.40; -; 1. DR InterPro; IPR001455; TusA-like. DR Pfam; PF01206; TusA; 1. DR SUPFAM; SSF64307; SSF64307; 1. DR PROSITE; PS01148; UPF0033; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 79 UPF0033 protein TM_0983. FT /FTId=PRO_0000159075. FT STRAND 8 11 {ECO:0000244|PDB:1JDQ}. FT HELIX 19 29 {ECO:0000244|PDB:1JDQ}. FT STRAND 36 43 {ECO:0000244|PDB:1JDQ}. FT HELIX 46 56 {ECO:0000244|PDB:1JDQ}. FT STRAND 61 66 {ECO:0000244|PDB:1JDQ}. FT STRAND 68 70 {ECO:0000244|PDB:1JDQ}. FT STRAND 72 77 {ECO:0000244|PDB:1JDQ}. SQ SEQUENCE 79 AA; 9168 MW; 4762FE620FB122EB CRC64; MAKYQVTKTL DVRGEVCPVP DVETKRALQN MKPGEILEVW IDYPMSKERI PETVKKLGHE VLEIEEVGPS EWKIYIKVK // ID Y984_THEMA Reviewed; 1536 AA. AC Q9X079; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=UPF0192 protein TM_0984; DE Flags: Precursor; GN OrderedLocusNames=TM_0984; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0192 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36063.1; -; Genomic_DNA. DR PIR; E72310; E72310. DR RefSeq; NP_228792.1; NC_000853.1. DR RefSeq; WP_010865234.1; NC_000853.1. DR ProteinModelPortal; Q9X079; -. DR STRING; 243274.TM0984; -. DR EnsemblBacteria; AAD36063; AAD36063; TM_0984. DR GeneID; 898730; -. DR KEGG; tma:TM0984; -. DR PATRIC; 23936897; VBITheMar51294_0997. DR eggNOG; ENOG4107S85; Bacteria. DR eggNOG; COG2373; LUCA. DR InParanoid; Q9X079; -. DR KO; K06894; -. DR OMA; YVWRATA; -. DR OrthoDB; EOG6X3W1C; -. DR BioCyc; TMAR243274:GC6P-1014-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro. DR Gene3D; 1.50.10.20; -; 1. DR InterPro; IPR002890; A2M_N. DR InterPro; IPR011625; A2M_N_2. DR InterPro; IPR001599; Macroglobln_a2. DR InterPro; IPR019565; MacrogloblnA2_thiol-ester-bond. DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase. DR Pfam; PF00207; A2M; 1. DR Pfam; PF01835; A2M_N; 1. DR Pfam; PF07703; A2M_N_2; 1. DR Pfam; PF10569; Thiol-ester_cl; 1. DR SMART; SM01360; A2M; 1. DR SMART; SM01359; A2M_N_2; 1. DR SUPFAM; SSF48239; SSF48239; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 20 {ECO:0000255}. FT CHAIN 21 1536 UPF0192 protein TM_0984. FT /FTId=PRO_0000036245. SQ SEQUENCE 1536 AA; 175956 MW; 71D493908F0CC1F4 CRC64; MGMKRLIFLV FLLISFSLFG GYAYFSRYPV LHPDEGLSFV ISDLENITLN VWKISEEDFL KAVFDPESFN FSLLEITRPI YSKKFSSEEW KEFSFPLKDR GFYFATLVSN EGTVFRRVID RSLFIVTDLE AIYFSDSEKL RLHVFDSDGD FVEGAEVLLF EDSKLIDRVF TGKDGVVSIT KHFDTFYIRY GDSRFFGGVY FSGGGLEREK LFFVTDRPIY KPSDTVHFRG QIFSFEEGLY KAFEKTKVTV SIFDTKKNEV YRSEFETDEL GGFSGSMKLP DTASVGLYKV NVDHGGRRYY EYFLVEEYRK PEYKVEIETD KDVYISGEVV NYLVRVKYFN GQPVAKAQVA YYVRAFPEEG SGYLVYRGTD FTDEEGNLRL GVKTEEGFQG SYRLEVIVTD ESQRQIEETR SVKVYADNVL ISPLDRYVST SPGKQVRVKV KVTDLSGNPL NGLLTTSSED STSTVAVENG EAIVTFTPKE PKSYRIELSF GKANTHFYVY AYCGAGTSSE FVINPATNTV KPGDELSVQI LAPGKVMGVL GIVSNRVYDT IPVSFTGSVN LRVRIPKDIP EKNLFISFVG LDDNGRIYKL ERLNVLLDTN FTTMKILFDK DQYEPGEMAQ ITIESNVDRV CLFLVDEAIY AMVGAEPPVL ENFLYPYMNY PRTRGGFPHY WRLYVSRNSF RNKLASLPEE KTFADFKQNA LPSKLNVREY FPDTALWIPS LKLHNGTARV SFKVPDSITS FRATAYGFSK DRFSQTESEM VVSKKFYLMP HLPSFLRESD VIKISATVFN RTSKTLPVQL TVELPENIEL LEGSSSRHFL MEANSSHTET WTVKAVSASE GSFVKFVAVG EDLNDAVSMR LPVERFAFER EFYRIMLLDG KETLEIPGQF ISSRIRFLDS IVPLVEDSLK RLIDFPYGCV EQTMSRFFPA VVAASAGIEV ENLEEIIQRG LFKLYSYQHN DGGWGWFRFG ESDDFMTCYV MEGLYFTMKA GYDVAESVLQ RGIEYLRKHP SAYGSYVLDL YGVNHEPFKP ESEADLVFLS LSSKEALKQL MNYVVQDEQK AYLNVYSNNP LISEIQLNSV FLRALAKWKE FPELERKVTN YLLLKKDSAF WTSTKDTSFV ILALLEAMPE YASTTLKVIN SENTFELKPG EERSLVPGSL TVSGKGIVEV EVVYIEVPKE AVSEGLEIKR EFYKRYELLI EENKMIVDAF VPIGRGYVPR SIHPVEKEQT EELYILPYKY WKKTIEYRGV PLEINGAEVK IKGETYTFFR IETFNGLILV FFRNEALIYD TEKNTITRYL DVTDAGFMRS GPVFLMKGFV LVGDEKIPVP EDVTGLSCTM DEILLRGENK TYWYRNGEFV DLPFVARRVF FWDGKKLVAE NIRFSGSSKT LRNRVFEVVF DVGDVKIELG DIIKTVVRVK GDGNYLIVED FIPSCAQVLS NYREKGIEEN KFSYSWYSSW NAWYSGREIR TDRVALFARY LYGNSFDYVW RATAEGVFHL LPARVYPMYS RGLYAHTDPD VLFIGADFID GRDDQP // ID Y986_THEMA Reviewed; 318 AA. AC Q9X081; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein TM_0986; GN OrderedLocusNames=TM_0986; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: To E.coli YfaT and P.aeruginosa PA4490. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36065.1; -; Genomic_DNA. DR PIR; G72310; G72310. DR RefSeq; NP_228794.1; NC_000853.1. DR RefSeq; WP_004080576.1; NZ_CP011107.1. DR STRING; 243274.TM0986; -. DR EnsemblBacteria; AAD36065; AAD36065; TM_0986. DR GeneID; 896809; -. DR KEGG; tma:TM0986; -. DR KEGG; tmi:THEMA_09420; -. DR KEGG; tmw:THMA_1008; -. DR PATRIC; 23936901; VBITheMar51294_0999. DR eggNOG; ENOG4108QJJ; Bacteria. DR eggNOG; COG3234; LUCA. DR InParanoid; Q9X081; -. DR KO; K09934; -. DR OMA; DVEKYNY; -. DR OrthoDB; EOG63FW15; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.90.1720.10; -; 2. DR InterPro; IPR009558; DUF1175. DR InterPro; IPR000064; NLP_P60_dom. DR Pfam; PF06672; DUF1175; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 318 Uncharacterized protein TM_0986. FT /FTId=PRO_0000216217. SQ SEQUENCE 318 AA; 36705 MW; 7041AB7510531380 CRC64; MKRYLILLIV TGVLLWNVVE VLRFRVEFSG GTFVLKNVQD IFVPLEVRGA KVECSKNFVL EENGVLIKQV RPGETVTLHF ESGGIFRVKK ELKIEARASE EDSDGDGYPD SLELDSEDSE RFRNWFVWIA LSAFKNDPLL WPKEERDCSG FVRYCAREAL KKHTGSWFSL SGYNGPVWED VEKYNYPNLP LVGTKMFRIE KGAYRGVEDF SNFAVARILV ECSMEFVTKS VSEALPGDIA VFFHPEDVEM PYHLMIFVGN LNLADHEGWF VYHTGPIGEN PGELRFVRYS ELVNYDPSWA PLEINPYFLG FYRFRFLK // ID YIDC_THEMA Reviewed; 445 AA. AC Q9X1H2; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=Membrane protein insertase YidC {ECO:0000255|HAMAP-Rule:MF_01810}; DE AltName: Full=Foldase YidC {ECO:0000255|HAMAP-Rule:MF_01810}; DE AltName: Full=Membrane integrase YidC {ECO:0000255|HAMAP-Rule:MF_01810}; DE AltName: Full=Membrane protein YidC {ECO:0000255|HAMAP-Rule:MF_01810}; GN Name=yidC {ECO:0000255|HAMAP-Rule:MF_01810}; GN OrderedLocusNames=TM_1461; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Required for the insertion and/or proper folding and/or CC complex formation of integral membrane proteins into the membrane. CC Involved in integration of membrane proteins that insert both CC dependently and independently of the Sec translocase complex, as CC well as at least some lipoproteins. Aids folding of multispanning CC membrane proteins. {ECO:0000255|HAMAP-Rule:MF_01810}. CC -!- SUBUNIT: Interacts with the Sec translocase complex via SecD. CC Specifically interacts with transmembrane segments of nascent CC integral membrane proteins during membrane integration. CC {ECO:0000255|HAMAP-Rule:MF_01810}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01810}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01810}. CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01810}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36529.1; -; Genomic_DNA. DR PIR; F72251; F72251. DR RefSeq; NP_229260.1; NC_000853.1. DR RefSeq; WP_010865347.1; NC_000853.1. DR STRING; 243274.TM1461; -. DR DNASU; 898017; -. DR EnsemblBacteria; AAD36529; AAD36529; TM_1461. DR GeneID; 898017; -. DR KEGG; tma:TM1461; -. DR PATRIC; 23937874; VBITheMar51294_1475. DR eggNOG; ENOG4105DHW; Bacteria. DR eggNOG; COG0706; LUCA. DR InParanoid; Q9X1H2; -. DR KO; K03217; -. DR OMA; KSMIKMR; -. DR OrthoDB; EOG6X6RF2; -. DR BioCyc; TMAR243274:GC6P-1499-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051205; P:protein insertion into membrane; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR HAMAP; MF_01810; YidC_type1; 1. DR InterPro; IPR019998; Membr_insert_YidC. DR InterPro; IPR028055; Membr_insert_YidC/Oxa1_C. DR InterPro; IPR001708; Membrane_insert_OXA1/ALB3/YidC. DR PANTHER; PTHR12428; PTHR12428; 1. DR Pfam; PF02096; 60KD_IMP; 1. DR TIGRFAMs; TIGR03592; yidC_oxa1_cterm; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Chaperone; Complete proteome; KW Membrane; Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 445 Membrane protein insertase YidC. FT /FTId=PRO_0000124760. FT TRANSMEM 6 26 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. FT TRANSMEM 248 268 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. FT TRANSMEM 313 333 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. FT TRANSMEM 352 372 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. FT TRANSMEM 388 408 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. SQ SEQUENCE 445 AA; 51421 MW; 465A3CCAF62579F2 CRC64; MVLRKVVAIL LAILPIFLFA VEPIKVVRSE KEIVVLTRFE EYHFDLEKGI LKDFYTLVDG RKHVFTYGND GFDVLDEGTP LTVIEEPIVT GVGKVSEGFS DEVSIVYNYG YVKKIFTIKN NENYTFFVDI ESSKPVDVTV PRVSVDTSTD RYLENYFASF NPKTRTLVLL KHDEGLLFEG TLKVNGQKRF IVFMGPNKRT LIKKAFPEDY DVLIKALVNI PGFNKWYDSV FYGLVWFFWW LKDLTKNFGW AIMLFTLIVR LILYPLYHAQ TKSLINMRKL QPQIEAIKKK YKDPTKQQEA LLKLYREAGV NPASGCLMLL IQLPIFMLLW SVIRYYVEEF AYSGSFLIWK DLSAGGFSNN WLFLVITIVA SYYTTLLTSQ DARTAWQGII MSVIFPFLFV GLPSGLFLYY ATNTLIQLAV TYYTYKRYKI KGLTTRELLG LPKKA // ID Y763_THEMA Reviewed; 106 AA. AC Q9WZM2; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=UPF0145 protein TM_0763; GN OrderedLocusNames=TM_0763; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0145 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35845.1; -; Genomic_DNA. DR PIR; A72336; A72336. DR RefSeq; NP_228572.1; NC_000853.1. DR RefSeq; WP_004080935.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZM2; -. DR STRING; 243274.TM0763; -. DR EnsemblBacteria; AAD35845; AAD35845; TM_0763. DR GeneID; 898431; -. DR KEGG; tma:TM0763; -. DR PATRIC; 23936448; VBITheMar51294_0776. DR eggNOG; ENOG4105K8R; Bacteria. DR eggNOG; COG0393; LUCA. DR InParanoid; Q9WZM2; -. DR OMA; TEVCAYG; -. DR OrthoDB; EOG6TN47M; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.30.110.70; -; 1. DR HAMAP; MF_00338; UPF0145; 1. DR InterPro; IPR002765; UPF0145. DR Pfam; PF01906; YbjQ_1; 1. DR SUPFAM; SSF117782; SSF117782; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 106 UPF0145 protein TM_0763. FT /FTId=PRO_0000138485. SQ SEQUENCE 106 AA; 11383 MW; CA7EBC7EFE7D0D0B CRC64; MIITTTEQVP GYRVKEILGV VSGNVVMSKH LGRDIAAAFK TLAGGEIKGY TEMLTEARNI ALERMMKEAE KLGADAVIGF RYSSSTIMSG AAEILAYGTA VKLEKI // ID Y929_THEMA Reviewed; 397 AA. AC P56727; P46803; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 1. DT 13-APR-2016, entry version 82. DE RecName: Full=Uncharacterized protein TM_0929; GN OrderedLocusNames=TM_0929; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=8168477; RA Darimont B., Sterner R.; RT "Sequence, assembly and evolution of a primordial ferredoxin from RT Thermotoga maritima."; RL EMBO J. 13:1772-1781(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SEQUENCE CAUTION: CC Sequence=AAA65436.1; Type=Frameshift; Positions=276, 300, 320; Note=The frameshift in position 320 separates TM_0929 and TM_0928.; Evidence={ECO:0000305}; CC Sequence=CAA57668.1; Type=Frameshift; Positions=276, 300, 320; Note=The frameshift in position 320 separates TM_0929 and TM_0928.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U24145; AAA65436.1; ALT_FRAME; Genomic_DNA. DR EMBL; X82178; CAA57668.1; ALT_FRAME; Genomic_DNA. DR EMBL; AE000512; AAD36010.1; -; Genomic_DNA. DR PIR; A72315; A72315. DR RefSeq; NP_228737.1; NC_000853.1. DR RefSeq; WP_004080633.1; NZ_CP011107.1. DR STRING; 243274.TM0929; -. DR EnsemblBacteria; AAD36010; AAD36010; TM_0929. DR GeneID; 898603; -. DR KEGG; tma:TM0929; -. DR PATRIC; 23936789; VBITheMar51294_0943. DR eggNOG; ENOG4105EZM; Bacteria. DR eggNOG; COG3864; LUCA. DR InParanoid; P56727; -. DR OMA; IWDLAMD; -. DR OrthoDB; EOG6MD91P; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR025154; Put_metallopeptidase_dom. DR InterPro; IPR018698; VWA-like_dom. DR Pfam; PF09967; DUF2201; 1. DR Pfam; PF13203; DUF2201_N; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 397 Uncharacterized protein TM_0929. FT /FTId=PRO_0000216216. SQ SEQUENCE 397 AA; 45822 MW; 15F6A8397030D933 CRC64; MKGEETLKKA LLNIGKESPF YYYVLLGVKL VPSKNTRNLK LSFSTTGDVM LLYNPEAIGK KPLRMVQALL IHEVMHIVLQ HFRIKPKDER DRKIWDLAMD AAINQYIPEL AAFGVPLDVL VKEGHTTDND TLFVLPPEWM MFENAEMYHK WILEEMERLG RYDVEVVAEF RDNVDDHSGL FEEDVPVEMI LDLTKDRTKK AFNLFGNTLP SGVRREVSLS LENPELDWKT LLRRFFGVSI KADRYTTPLR PNRRYDHLPG WRNEYLPRIA AVVDTSGSIV EKELNQFISE LEKISNIAGE ELWLVQVDKS VTSAMKYRSG KWKDLEIVGG GSTDLQPAID YSERVLRSEG TVVFTDGHTD VPIARRRILF VLSRYHNEEF LKEARKMYGR DAVVVLS // ID YA00_THEMA Reviewed; 132 AA. AC Q9X095; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 74. DE RecName: Full=UPF0332 protein TM_1000; GN OrderedLocusNames=TM_1000; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0332 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36082.1; -; Genomic_DNA. DR PIR; B72307; B72307. DR RefSeq; NP_228808.1; NC_000853.1. DR RefSeq; WP_004080552.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X095; -. DR STRING; 243274.TM1000; -. DR EnsemblBacteria; AAD36082; AAD36082; TM_1000. DR GeneID; 898710; -. DR KEGG; tma:TM1000; -. DR PATRIC; 23936929; VBITheMar51294_1013. DR eggNOG; ENOG41060KZ; Bacteria. DR eggNOG; COG1895; LUCA. DR InParanoid; Q9X095; -. DR KO; K09132; -. DR OMA; YYAMFYA; -. DR OrthoDB; EOG60656T; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR007842; HEPN_dom. DR Pfam; PF05168; HEPN; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 132 UPF0332 protein TM_1000. FT /FTId=PRO_0000159642. SQ SEQUENCE 132 AA; 15650 MW; 7D872D60B8D3FAB1 CRC64; MNEKEKIIEY WRRRARECLD DAKLLLKNER LHSAVNRIYY ALFYQVSALL LAKGLSFSKH SGVLAAFNRE FVKTGKVNKE LGKFYNRMFE HRKTGDYGEL VEFEEENVKD WIRKAEGFLD AIEKLIEDLK RA // ID Y914_THEMA Reviewed; 213 AA. AC Q9X016; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 85. DE RecName: Full=UPF0111 protein TM_0914; GN OrderedLocusNames=TM_0914; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the UPF0111 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35995.1; -; Genomic_DNA. DR PIR; A72320; A72320. DR RefSeq; NP_228722.1; NC_000853.1. DR RefSeq; WP_004080648.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X016; -. DR STRING; 243274.TM0914; -. DR EnsemblBacteria; AAD35995; AAD35995; TM_0914. DR GeneID; 898588; -. DR KEGG; tma:TM0914; -. DR PATRIC; 23936759; VBITheMar51294_0928. DR eggNOG; ENOG41080JC; Bacteria. DR eggNOG; COG1392; LUCA. DR InParanoid; Q9X016; -. DR KO; K07220; -. DR OMA; VFESETI; -. DR OrthoDB; EOG6BKJ6Z; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR002727; DUF47. DR InterPro; IPR018445; Put_Phosphate_transp_reg. DR Pfam; PF01865; PhoU_div; 1. DR TIGRFAMs; TIGR00153; TIGR00153; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 213 UPF0111 protein TM_0914. FT /FTId=PRO_0000154910. SQ SEQUENCE 213 AA; 25122 MW; 3542A02A6064C359 CRC64; MWFSGKKEQT IISLFFKHID KVEETLKCVF DLIKKYLEDT DDIESLYLRT QRLESEADRL RRKTEMEMYS GAFLPNFRGD LLGLIESVDK VANKAEYVAD LIVLQKPEVP HELKDLILSQ MEYSLKAYES LKSALKFLFE DLERVEEFVL AVEKYEHDED AVERTALRKL FEMDIERSVK LEVKELIRSI GDIADRTEDV SDRAEIILLK RRF // ID YBEY_THEMA Reviewed; 150 AA. AC Q9X1J7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE RecName: Full=Endoribonuclease YbeY {ECO:0000255|HAMAP-Rule:MF_00009}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00009}; GN Name=ybeY {ECO:0000255|HAMAP-Rule:MF_00009}; GN OrderedLocusNames=TM_1509; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP STRUCTURE BY NMR, COFACTOR, AND ZINC BINDING. RX PubMed=15965736; DOI=10.1007/s10969-005-5277-z; RA Penhoat C.H., Li Z., Atreya H.S., Kim S., Yee A., Xiao R., Murray D., RA Arrowsmith C.H., Szyperski T.; RT "NMR solution structure of Thermotoga maritima protein TM1509 reveals RT a Zn-metalloprotease-like tertiary structure."; RL J. Struct. Funct. Genomics 6:51-62(2005). CC -!- FUNCTION: Single strand-specific metallo-endoribonuclease involved CC in late-stage 70S ribosome quality control and in maturation of CC the 3' terminus of the 16S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00009}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00009, CC ECO:0000269|PubMed:15965736}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00009, CC ECO:0000269|PubMed:15965736}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00009}. CC -!- SIMILARITY: Belongs to the endoribonuclease YbeY family. CC {ECO:0000255|HAMAP-Rule:MF_00009}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36576.1; -; Genomic_DNA. DR PIR; F72244; F72244. DR RefSeq; NP_229309.1; NC_000853.1. DR RefSeq; WP_004081854.1; NZ_CP011107.1. DR PDB; 1TVI; NMR; -; A=1-150. DR PDBsum; 1TVI; -. DR ProteinModelPortal; Q9X1J7; -. DR SMR; Q9X1J7; 1-150. DR STRING; 243274.TM1509; -. DR EnsemblBacteria; AAD36576; AAD36576; TM_1509. DR GeneID; 898186; -. DR KEGG; tma:TM1509; -. DR PATRIC; 23937976; VBITheMar51294_1526. DR eggNOG; ENOG4105KGE; Bacteria. DR eggNOG; COG0319; LUCA. DR InParanoid; Q9X1J7; -. DR KO; K07042; -. DR OMA; EENAREF; -. DR OrthoDB; EOG680X6D; -. DR EvolutionaryTrace; Q9X1J7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.390.30; -; 1. DR HAMAP; MF_00009; Endoribonucl_YbeY; 1. DR InterPro; IPR023091; MetalPrtase_cat_dom_prd. DR InterPro; IPR002036; YbeY. DR InterPro; IPR020549; YbeY_CS. DR Pfam; PF02130; UPF0054; 1. DR TIGRFAMs; TIGR00043; TIGR00043; 1. DR PROSITE; PS01306; UPF0054; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Endonuclease; Hydrolase; KW Metal-binding; Nuclease; Reference proteome; Ribosome biogenesis; KW rRNA processing; Zinc. FT CHAIN 1 150 Endoribonuclease YbeY. FT /FTId=PRO_0000102553. FT METAL 102 102 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. FT METAL 106 106 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. FT METAL 112 112 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. FT STRAND 3 6 {ECO:0000244|PDB:1TVI}. FT HELIX 11 16 {ECO:0000244|PDB:1TVI}. FT HELIX 18 28 {ECO:0000244|PDB:1TVI}. FT STRAND 35 38 {ECO:0000244|PDB:1TVI}. FT HELIX 41 49 {ECO:0000244|PDB:1TVI}. FT STRAND 59 61 {ECO:0000244|PDB:1TVI}. FT STRAND 67 69 {ECO:0000244|PDB:1TVI}. FT STRAND 72 76 {ECO:0000244|PDB:1TVI}. FT HELIX 78 87 {ECO:0000244|PDB:1TVI}. FT HELIX 92 108 {ECO:0000244|PDB:1TVI}. FT HELIX 120 137 {ECO:0000244|PDB:1TVI}. SQ SEQUENCE 150 AA; 17550 MW; 5BDE227C0BE6DCC5 CRC64; MIRILGEGKG SKLLENLKEK LEEIVKKEIG DVHVNVILVS EDEIKELNQQ FRGQDRPTDV LTFPLMEEDV YGEIYVCPLI VEENAREFNN TFEKELLEVV IHGILHLAGY DHEFEDKNSK EMFEKQKKYV EEVWGEWRSN PSEDSDPGKR // ID YQGF_THEMA Reviewed; 218 AA. AC Q9X1N1; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 20-JAN-2016, entry version 85. DE RecName: Full=Putative pre-16S rRNA nuclease {ECO:0000305}; DE EC=3.1.-.-; GN OrderedLocusNames=TM_1545; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Could be a nuclease involved in processing of the 5'-end CC of pre-16S rRNA. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the YqgF nuclease family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36612.1; -; Genomic_DNA. DR PIR; E72243; E72243. DR RefSeq; NP_229345.1; NC_000853.1. DR RefSeq; WP_010865357.1; NC_000853.1. DR ProteinModelPortal; Q9X1N1; -. DR STRING; 243274.TM1545; -. DR DNASU; 897559; -. DR EnsemblBacteria; AAD36612; AAD36612; TM_1545. DR GeneID; 897559; -. DR KEGG; tma:TM1545; -. DR PATRIC; 23938052; VBITheMar51294_1563. DR eggNOG; ENOG41084RN; Bacteria. DR eggNOG; COG0816; LUCA. DR InParanoid; Q9X1N1; -. DR KO; K07447; -. DR OMA; PINNELE; -. DR OrthoDB; EOG6WMJ20; -. DR BioCyc; TMAR243274:GC6P-1586-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IEA:InterPro. DR Gene3D; 3.30.420.140; -; 1. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR005227; YqgF. DR InterPro; IPR006641; YqgF/RNaseH-like_dom. DR Pfam; PF03652; RuvX; 1. DR SMART; SM00732; YqgFc; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Nuclease; Reference proteome; KW Ribosome biogenesis. FT CHAIN 1 218 Putative pre-16S rRNA nuclease. FT /FTId=PRO_0000172162. SQ SEQUENCE 218 AA; 24916 MW; 3F2CE17C51DE32F0 CRC64; MDIQLFQGYG GKVIVAVDYG ERKCGVAFGE ILPQKSLVIP TKNLKEFIRK LKPDKIIFGL PLSMSGKYTQ QTFKTVAVAF KFSKEYETYL CDERLTTKIG ERISKRDDAV SAALIFQSFF ENSSVCEKVT DPRKKVDLAL EKVDGEVLLY EFPDPSLNIE AREVDVVTKN PVLAYFYSKN GYFVGRELWE KKYDLIISGK NCEELKKYLK ENGRLVCL // ID YIDD_THEMA Reviewed; 81 AA. AC Q9X1H3; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Putative membrane protein insertion efficiency factor {ECO:0000255|HAMAP-Rule:MF_00386}; GN OrderedLocusNames=TM_1462; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Could be involved in insertion of integral membrane CC proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00386}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00386}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_00386}. CC -!- SIMILARITY: Belongs to the UPF0161 family. {ECO:0000255|HAMAP- CC Rule:MF_00386}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36530.1; -; Genomic_DNA. DR PIR; G72251; G72251. DR RefSeq; NP_229261.1; NC_000853.1. DR RefSeq; WP_004081754.1; NZ_CP011107.1. DR STRING; 243274.TM1462; -. DR EnsemblBacteria; AAD36530; AAD36530; TM_1462. DR GeneID; 897757; -. DR KEGG; tma:TM1462; -. DR PATRIC; 23937876; VBITheMar51294_1476. DR eggNOG; ENOG4105VAS; Bacteria. DR eggNOG; COG0759; LUCA. DR InParanoid; Q9X1H3; -. DR KO; K08998; -. DR OMA; REAIEYH; -. DR OrthoDB; EOG61ZTN6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR HAMAP; MF_00386; UPF0161_YidD; 1. DR InterPro; IPR002696; Membr_insert_effic_factor. DR Pfam; PF01809; Haemolytic; 1. DR ProDom; PD004225; DUF37; 1. DR SMART; SM01234; Haemolytic; 1. DR TIGRFAMs; TIGR00278; TIGR00278; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome. FT CHAIN 1 81 Putative membrane protein insertion FT efficiency factor. FT /FTId=PRO_0000171890. SQ SEQUENCE 81 AA; 9622 MW; 844BC5E39AFAA537 CRC64; MKKLLIMLIR FYQRYISPLK PPTCRFTPTC SNYFIQALEK HGLLKGTFLG LRRILRCNPL SKGGYDPVPE EFSFKPRRRW S // ID Q9X1B1_THEMA Unreviewed; 791 AA. AC Q9X1B1; G4FFC7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 113. DE SubName: Full=ATP-dependent Clp protease {ECO:0000313|EMBL:AGL50322.1}; DE SubName: Full=ATP-dependent Clp protease, ATPase subunit {ECO:0000313|EMBL:AAD36462.1}; GN OrderedLocusNames=TM_1391 {ECO:0000313|EMBL:AAD36462.1}; GN ORFNames=Tmari_1398 {ECO:0000313|EMBL:AGL50322.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36462.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36462.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36462.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50322.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50322.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. CC {ECO:0000256|RuleBase:RU004432}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36462.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50322.1; -; Genomic_DNA. DR PIR; H72258; H72258. DR RefSeq; NP_229192.1; NC_000853.1. DR RefSeq; WP_004081598.1; NZ_CP011107.1. DR SMR; Q9X1B1; 161-344. DR STRING; 243274.TM1391; -. DR EnsemblBacteria; AAD36462; AAD36462; TM_1391. DR EnsemblBacteria; AGL50322; AGL50322; Tmari_1398. DR GeneID; 898085; -. DR KEGG; tma:TM1391; -. DR KEGG; tmi:THEMA_07360; -. DR KEGG; tmm:Tmari_1398; -. DR KEGG; tmw:THMA_1420; -. DR PATRIC; 23937728; VBITheMar51294_1403. DR eggNOG; ENOG4105C2Z; Bacteria. DR eggNOG; COG0542; LUCA. DR KO; K03696; -. DR OMA; LEEFIHQ; -. DR OrthoDB; EOG65F8SM; -. DR BioCyc; TMAR243274:GC6P-1428-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.1780.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004176; Clp_N. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR018368; ClpA/B_CS1. DR InterPro; IPR028299; ClpA/B_CS2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001943; UVR_dom. DR Pfam; PF00004; AAA; 1. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF02861; Clp_N; 2. DR Pfam; PF10431; ClpB_D2-small; 1. DR Pfam; PF02151; UVR; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 2. DR SMART; SM01086; ClpB_D2-small; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF81923; SSF81923; 1. DR PROSITE; PS00870; CLPAB_1; 1. DR PROSITE; PS00871; CLPAB_2; 1. DR PROSITE; PS50151; UVR; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00463698}; KW Chaperone {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00480820}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD36462.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00463698}; KW Protease {ECO:0000313|EMBL:AAD36462.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 418 453 UVR. {ECO:0000259|PROSITE:PS50151}. FT COILED 414 464 {ECO:0000256|SAM:Coils}. FT COILED 701 732 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 791 AA; 90251 MW; 9B1CD6DDFE6515EF CRC64; MFNLEEYTEK AQKVMMSIQD IMTRYRQNQL SSEHILLAIL EEGNNVGVEL LKELNVDINR LKDEVEVFIG KYGVRVPEGA SVSQIFITPD ARHVIEKARE EARRMGDSKI GTEHLILGMV LSPDSTAFRI LSRYGVTPER VYEAIRKIRS TGKTDEAENV EALARFTVDL TQLAREKKLM PVVDREKEIR RVIQILSRRT KNNPVLIGDP GVGKTAVVEG LAQRIVEGKV PLFLRNVRVL KLDMGRLVAG TRFRGDFEER LKRLLDELKR KKGEVILFID EVHTVVGAGA AEGALDAANI MKPELTTGEI QIIGATTVEE YRKYIEKDRA LERRFQPVMV EEPTVEQTIE ILKGLRKVFE EHHHVKITDD ALEAAAKLSA RYITNRFLPD KAVDLIDEAA AYVRLESSYP SEELLKLEEE IKNLEDKIND AVVKGEYEEA AKLKVELQKL KNEYEEKRKK QEKVEPVVDE NVVAKIVEQW TGIPVSRIME SEREKLLKLE EFIHQRLVNQ EEAVKIVART IRRARVGIKN PRRPIGVFLF LGPTGVGKTE LARTLADVLF GSEDAMIRLD MSEYMEKHSV ARLIGAPPGY VGYEEGGQLT EAVRKRPYSV ILLDEIEKAH PDVFNILLQV FEDGRLTDGK GNTVDFRNTI IIMTSNIGSE KILEMSENGV RIEIEKELRN TFKPEFLNRI DAIVYFKPLT MEEVKKIVEI MVRQLQEILK EKNISIELTE RAKEYLAEAG YVPSLGARPL RRIIELELES MIADKILEGE IKEGDRVLVD ADEYGLKIER R // ID Q9X0D6_THEMA Unreviewed; 285 AA. AC Q9X0D6; G4FEV2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36123.1}; GN OrderedLocusNames=TM_1046 {ECO:0000313|EMBL:AAD36123.1}; GN ORFNames=Tmari_1050 {ECO:0000313|EMBL:AGL49974.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36123.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36123.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36123.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49974.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49974.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36123.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49974.1; -; Genomic_DNA. DR PIR; H72300; H72300. DR RefSeq; NP_228852.1; NC_000853.1. DR RefSeq; WP_004080469.1; NZ_CP011107.1. DR STRING; 243274.TM1046; -. DR ESTHER; thema-q9x0d6; 6_AlphaBeta_hydrolase. DR EnsemblBacteria; AAD36123; AAD36123; TM_1046. DR EnsemblBacteria; AGL49974; AGL49974; Tmari_1050. DR GeneID; 897227; -. DR KEGG; tma:TM1046; -. DR KEGG; tmi:THEMA_09130; -. DR KEGG; tmm:Tmari_1050; -. DR KEGG; tmw:THMA_1068; -. DR PATRIC; 23937021; VBITheMar51294_1059. DR eggNOG; ENOG4108YS5; Bacteria. DR eggNOG; ENOG4111KJ6; LUCA. DR OMA; HIPYLMW; -. DR OrthoDB; EOG6HF5W8; -. DR BioCyc; TMAR243274:GC6P-1075-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.1820; -; 2. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR022742; Hydrolase_4. DR Pfam; PF12146; Hydrolase_4; 1. DR SUPFAM; SSF53474; SSF53474; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 285 AA; 33647 MW; D28B99088E26541A CRC64; MRLITFDASY DPIAEESKTV RVYVFEPEKI ERNLIFLHGI GNGNIPYLLW FGEKFREYNI KTWFLILPYH EKRAPENWSG GEPFYHSSPS FCVKRFDEAV QDVIDLVDVV KRDNDKPISL MGFSFGGMIT TIALAREKRI EKGVICCSGG DWRWINWYSP YTERLRELYR KNGNEYGCRS EKDCIKNRRN APEIIKSFNS IEDIRKKPPV GCYFYDPASF APFVDQKVLF FWALFDHVIP YQSYACLHKL LKNKKTVYLP SGHKGSYFFR RYIAKRVVRF LIDDE // ID Q9X200_THEMA Unreviewed; 86 AA. AC Q9X200; G4FG59; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 88. DE SubName: Full=Flagellar biosynthesis-related protein {ECO:0000313|EMBL:AAD36739.1}; GN OrderedLocusNames=TM_1672 {ECO:0000313|EMBL:AAD36739.1}; GN ORFNames=Tmari_1680 {ECO:0000313|EMBL:AGL50604.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36739.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36739.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36739.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50604.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50604.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36739.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50604.1; -; Genomic_DNA. DR PIR; F72225; F72225. DR RefSeq; NP_229472.1; NC_000853.1. DR RefSeq; WP_004082188.1; NZ_CP011107.1. DR STRING; 243274.TM1672; -. DR EnsemblBacteria; AAD36739; AAD36739; TM_1672. DR EnsemblBacteria; AGL50604; AGL50604; Tmari_1680. DR GeneID; 897118; -. DR KEGG; tma:TM1672; -. DR KEGG; tmi:THEMA_05880; -. DR KEGG; tmm:Tmari_1680; -. DR KEGG; tmw:THMA_1714; -. DR PATRIC; 23938318; VBITheMar51294_1689. DR eggNOG; ENOG41084WQ; Bacteria. DR eggNOG; COG2257; LUCA. DR KO; K04061; -. DR OMA; HEVPIYE; -. DR OrthoDB; EOG6DVJXQ; -. DR BioCyc; TMAR243274:GC6P-1720-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR Gene3D; 3.40.1690.10; -; 1. DR InterPro; IPR004683; T3SS_FlhB-rel. DR InterPro; IPR006135; T3SS_substrate_exporter. DR InterPro; IPR029025; T3SS_substrate_exporter_C. DR PANTHER; PTHR30531; PTHR30531; 1. DR Pfam; PF01312; Bac_export_2; 1. DR SUPFAM; SSF160544; SSF160544; 1. DR TIGRFAMs; TIGR00789; flhB_rel; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AAD36739.1}; KW Cilium {ECO:0000313|EMBL:AAD36739.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD36739.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 86 AA; 9962 MW; 42881EBC0394F3F7 CRC64; MRTDEIKKAV ALKYDPTRTS APEVVAKGVG EVAERIIEMA RRHGIPIEER PDIIDDLLRL DLFSEIPEEM YLVIAEIYAF LKRYDK // ID Q9WXN6_THEMA Unreviewed; 280 AA. AC Q9WXN6; G4FGU6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 96. DE SubName: Full=Beta-glucoside ABC transport system, permease protein 2 {ECO:0000313|EMBL:AGL48952.1}; DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35123.1}; GN OrderedLocusNames=TM_0029 {ECO:0000313|EMBL:AAD35123.1}; GN ORFNames=Tmari_0026 {ECO:0000313|EMBL:AGL48952.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35123.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35123.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35123.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48952.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48952.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032, CC ECO:0000256|SAAS:SAAS00537635}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35123.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48952.1; -; Genomic_DNA. DR PIR; G72428; G72428. DR RefSeq; NP_227845.1; NC_000853.1. DR RefSeq; WP_004082483.1; NZ_CP011107.1. DR STRING; 243274.TM0029; -. DR TCDB; 3.A.1.5.16; the atp-binding cassette (abc) superfamily. DR DNASU; 896849; -. DR EnsemblBacteria; AAD35123; AAD35123; TM_0029. DR EnsemblBacteria; AGL48952; AGL48952; Tmari_0026. DR GeneID; 896849; -. DR KEGG; tma:TM0029; -. DR KEGG; tmi:THEMA_04655; -. DR KEGG; tmm:Tmari_0026; -. DR KEGG; tmw:THMA_0025; -. DR PATRIC; 23934898; VBITheMar51294_0027. DR eggNOG; ENOG4108QCB; Bacteria. DR eggNOG; COG1173; LUCA. DR KO; K02034; -. DR OMA; DSYASEV; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-29-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR025966; OppC_N. DR Pfam; PF00528; BPD_transp_1; 1. DR Pfam; PF12911; OppC_N; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00496716}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496716, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496724}. FT TRANSMEM 15 36 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 78 101 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 113 133 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 139 157 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 188 208 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 214 237 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 244 269 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 74 266 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 280 AA; 31206 MW; 160A43F2A3F66190 CRC64; MFRTMIRPLF KNKKFIIGFS IFLFFLFLGI FGPMFYRVDP TEMTWDYEQP PSSAHPLGTD TYGRDVLAQL LHGIRSSLYI GFLAAIISLV IGTIIGSFSA VKRGIVDDVL MGITNIVLTT PSILIAILIA SYLKVRSVEM VAVILGLFQW PWFARAIRAQ LMSVMSREYV YLSVMAGYSD LRLVIEDLIP TIATYAFMSF VLFINGGIMG EAGLSLIGLG PTQGISLGIM LQWAVLMEAV RRGLWWWFVP PGLAIVAVTA SLLVISTAMD EVFNPRLREE // ID Q9WZT5_THEMA Unreviewed; 319 AA. AC Q9WZT5; G4FCZ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 104. DE SubName: Full=Sugar kinase, pfkB family {ECO:0000313|EMBL:AAD35910.1}; DE SubName: Full=Tagatose-6-phosphate kinase / 1-phosphofructokinase {ECO:0000313|EMBL:AGL49755.1}; DE EC=2.7.1.144 {ECO:0000313|EMBL:AGL49755.1}; DE EC=2.7.1.56 {ECO:0000313|EMBL:AGL49755.1}; GN OrderedLocusNames=TM_0828 {ECO:0000313|EMBL:AAD35910.1}; GN ORFNames=Tmari_0830 {ECO:0000313|EMBL:AGL49755.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35910.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35910.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35910.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49755.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49755.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. CC {ECO:0000256|SAAS:SAAS00549292}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35910.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49755.1; -; Genomic_DNA. DR PIR; H72327; H72327. DR RefSeq; NP_228637.1; NC_000853.1. DR RefSeq; WP_004080817.1; NC_023151.1. DR PDB; 2AJR; X-ray; 2.46 A; A/B=1-319. DR PDBsum; 2AJR; -. DR STRING; 243274.TM0828; -. DR EnsemblBacteria; AAD35910; AAD35910; TM_0828. DR EnsemblBacteria; AGL49755; AGL49755; Tmari_0830. DR GeneID; 898498; -. DR KEGG; tma:TM0828; -. DR KEGG; tmi:THEMA_00500; -. DR KEGG; tmm:Tmari_0830; -. DR PATRIC; 23936582; VBITheMar51294_0841. DR eggNOG; ENOG4105DE4; Bacteria. DR eggNOG; COG1105; LUCA. DR KO; K00882; -. DR OMA; ANAQERM; -. DR OrthoDB; EOG61KBKF; -. DR BioCyc; TMAR243274:GC6P-857-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009024; F:tagatose-6-phosphate kinase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR017583; Tagatose/fructose_Pkinase. DR Pfam; PF00294; PfkB; 1. DR PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR PROSITE; PS00583; PFKB_KINASES_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2AJR}; KW ATP-binding {ECO:0000256|SAAS:SAAS00434118}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|SAAS:SAAS00446051, ECO:0000313|EMBL:AAD35910.1}; KW Magnesium {ECO:0000213|PDB:2AJR}; KW Metal-binding {ECO:0000213|PDB:2AJR}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00434118}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00446051, KW ECO:0000313|EMBL:AAD35910.1}. FT DOMAIN 31 297 PfkB. {ECO:0000259|Pfam:PF00294}. FT METAL 255 255 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:2AJR}. FT METAL 292 292 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:2AJR}. FT METAL 295 295 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:2AJR}. FT METAL 297 297 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:2AJR}. SQ SEQUENCE 319 AA; 35868 MW; 4EA409B9E6662E7E CRC64; MVLTVTLNPA LDREIFIEDF QVNRLYRIND LSKTQMSPGG KGINVSIALS KLGVPSVATG FVGGYMGKIL VEELRKISKL ITTNFVYVEG ETRENIEIID EKNKTITAIN FPGPDVTDMD VNHFLRRYKM TLSKVDCVVI SGSIPPGVNE GICNELVRLA RERGVFVFVE QTPRLLERIY EGPEFPNVVK PDLRGNHASF LGVDLKTFDD YVKLAEKLAE KSQVSVVSYE VKNDIVATRE GVWLIRSKEE IDTSHLLGAG DAYVAGMVYY FIKHGANFLE MAKFGFASAL AATRRKEKYM PDLEAIKKEY DHFTVERVK // ID Q9WY19_THEMA Unreviewed; 88 AA. AC Q9WY19; G4FH89; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 123. DE RecName: Full=Acyl carrier protein {ECO:0000256|HAMAP-Rule:MF_01217, ECO:0000256|RuleBase:RU003545}; DE Short=ACP {ECO:0000256|HAMAP-Rule:MF_01217}; GN Name=acpP {ECO:0000256|HAMAP-Rule:MF_01217}; GN OrderedLocusNames=TM_0175 {ECO:0000313|EMBL:AAD35268.1}; GN ORFNames=Tmari_0173 {ECO:0000313|EMBL:AGL49099.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35268.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35268.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35268.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49099.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49099.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01217, CC ECO:0000256|RuleBase:RU003545, ECO:0000256|SAAS:SAAS00510058}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_01217, ECO:0000256|RuleBase:RU003545, CC ECO:0000256|SAAS:SAAS00569451}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01217}. CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific CC serine of apo-ACP by AcpS. This modification is essential for CC activity because fatty acids are bound in thioester linkage to the CC sulfhydryl of the prosthetic group. {ECO:0000256|HAMAP- CC Rule:MF_01217}. CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific CC serine of apo-ACP by acpS. {ECO:0000256|RuleBase:RU003545}. CC -!- SIMILARITY: Contains 1 acyl carrier domain. {ECO:0000256|HAMAP- CC Rule:MF_01217, ECO:0000256|RuleBase:RU003545}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35268.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49099.1; -; Genomic_DNA. DR PIR; E72409; E72409. DR RefSeq; NP_227990.1; NC_000853.1. DR RefSeq; WP_004082810.1; NZ_CP011107.1. DR PDB; 1VKU; X-ray; 2.00 A; A=1-88. DR PDBsum; 1VKU; -. DR STRING; 243274.TM0175; -. DR EnsemblBacteria; AAD35268; AAD35268; TM_0175. DR EnsemblBacteria; AGL49099; AGL49099; Tmari_0173. DR GeneID; 897015; -. DR KEGG; tma:TM0175; -. DR KEGG; tmi:THEMA_03925; -. DR KEGG; tmm:Tmari_0173; -. DR KEGG; tmw:THMA_0171; -. DR PATRIC; 23935198; VBITheMar51294_0176. DR eggNOG; COG0236; LUCA. DR KO; K02078; -. DR OMA; QMGKEDI; -. DR OrthoDB; EOG6MWNJM; -. DR BioCyc; TMAR243274:GC6P-176-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000036; F:ACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1200.10; -; 1. DR HAMAP; MF_01217; Acyl_carrier; 1. DR InterPro; IPR003231; Acyl_carrier. DR InterPro; IPR009081; PP-bd_ACP. DR InterPro; IPR006162; Ppantetheine_attach_site. DR Pfam; PF00550; PP-binding; 1. DR ProDom; PD000887; PD000887; 1. DR SUPFAM; SSF47336; SSF47336; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VKU}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01217}; KW Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01217, KW ECO:0000256|SAAS:SAAS00510070}; KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01217, KW ECO:0000256|SAAS:SAAS00510070}; KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01217, KW ECO:0000256|SAAS:SAAS00510070}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01217, KW ECO:0000256|SAAS:SAAS00510070}; KW Phosphopantetheine {ECO:0000256|HAMAP-Rule:MF_01217, KW ECO:0000256|RuleBase:RU003545}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01217}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 6 75 Acyl carrier. FT {ECO:0000259|PROSITE:PS50075}. FT MOD_RES 38 38 O-(pantetheine 4'-phosphoryl)serine. FT {ECO:0000256|HAMAP-Rule:MF_01217}. SQ SEQUENCE 88 AA; 10285 MW; DF44279D407CA06B CRC64; MERKKLIAKF VEIASEKMGK DLETVDEENT FKELGFDSID VIDLVMFFED EFALRIEDEE ISKIRKVKDL IDIVIKKLEE IDDEVSEG // ID Q9X180_THEMA Unreviewed; 755 AA. AC Q9X180; G4FF95; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 128. DE SubName: Full=Sensor histidine kinase {ECO:0000313|EMBL:AAD36429.1}; GN OrderedLocusNames=TM_1359 {ECO:0000313|EMBL:AAD36429.1}; GN ORFNames=Tmari_1366 {ECO:0000313|EMBL:AGL50290.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36429.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36429.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36429.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50290.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50290.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. {ECO:0000256|SAAS:SAAS00146860}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36429.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50290.1; -; Genomic_DNA. DR PIR; H72262; H72262. DR RefSeq; NP_229160.1; NC_000853.1. DR RefSeq; WP_004081555.1; NZ_CP011107.1. DR PDB; 3A0R; X-ray; 3.80 A; A=408-755. DR PDB; 3A0S; X-ray; 1.47 A; A=424-518. DR PDB; 3A0T; X-ray; 1.91 A; A=605-755. DR PDB; 3A0V; X-ray; 1.70 A; A=424-518. DR PDB; 3A0W; X-ray; 1.69 A; A/B=605-755. DR PDB; 3A0X; X-ray; 1.89 A; A=605-755. DR PDB; 3A0Y; X-ray; 1.57 A; A/B=605-755. DR PDB; 3A0Z; X-ray; 1.75 A; A/B=605-755. DR PDBsum; 3A0R; -. DR PDBsum; 3A0S; -. DR PDBsum; 3A0T; -. DR PDBsum; 3A0V; -. DR PDBsum; 3A0W; -. DR PDBsum; 3A0X; -. DR PDBsum; 3A0Y; -. DR PDBsum; 3A0Z; -. DR DIP; DIP-48290N; -. DR STRING; 243274.TM1359; -. DR EnsemblBacteria; AAD36429; AAD36429; TM_1359. DR EnsemblBacteria; AGL50290; AGL50290; Tmari_1366. DR GeneID; 898121; -. DR KEGG; tma:TM1359; -. DR KEGG; tmi:THEMA_07545; -. DR KEGG; tmm:Tmari_1366; -. DR KEGG; tmw:THMA_1384; -. DR PATRIC; 23937656; VBITheMar51294_1371. DR eggNOG; ENOG4105ES5; Bacteria. DR eggNOG; COG0642; LUCA. DR eggNOG; COG2202; LUCA. DR eggNOG; COG2203; LUCA. DR KO; K02486; -. DR OMA; QYLREES; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; TMAR243274:GC6P-1392-MONOMER; -. DR BRENDA; 2.7.13.3; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.450.40; -; 2. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003018; GAF. DR InterPro; IPR029016; GAF_dom-like. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR000014; PAS. DR InterPro; IPR013767; PAS_fold. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF00989; PAS; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00065; GAF; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SMART; SM00091; PAS; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55781; SSF55781; 2. DR SUPFAM; SSF55785; SSF55785; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR TIGRFAMs; TIGR00229; sensory_box; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50112; PAS; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3A0R, ECO:0000213|PDB:3A0S, KW ECO:0000213|PDB:3A0T, ECO:0000213|PDB:3A0V}; KW ATP-binding {ECO:0000256|SAAS:SAAS00441253}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|SAAS:SAAS00529081, ECO:0000313|EMBL:AAD36429.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00441253}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00529081, KW ECO:0000313|EMBL:AAD36429.1}. FT DOMAIN 412 457 PAS (PER-ARNT-SIM). FT {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 544 752 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. FT NP_BIND 708 710 ADP. {ECO:0000213|PDB:3A0T}. FT NP_BIND 714 718 ADP. {ECO:0000213|PDB:3A0T}. FT COILED 152 190 {ECO:0000256|SAM:Coils}. FT BINDING 661 661 ADP. {ECO:0000213|PDB:3A0T}. FT BINDING 689 689 ADP. {ECO:0000213|PDB:3A0T}. SQ SEQUENCE 755 AA; 88729 MW; 61D11F4FDC4D0E9E CRC64; MVPERLKQIK GIRILESEDE IPQEGFTCRF GKHTVVANDE ESFEIVRLYK RLTVYELLLS LVDSICVHPK EEALRFSLKK VREFLDAEEV YLIEGDASYS SKGEKLSIDE IKKKHPGASV REWRNKLHLV VVREGAFDEE EEVLCTKLLE FIGNVSEKLW RLKEEVQKLK KSYEEQLKVS EIQKEHIKKM RIIYYVSQAM RSVYDPNNLY RVILLSLVSE RGFNFDRAVL LKKDEGTGSL MVVSAVGGDT LQEHEELKRY LRKRTLRYTD LVQFLREEAL TFSFETKFNE KIRGKRFYYR EHPIFERVVL RKSIVRTSRE TLEKIRYEIE DVISILENDE FIVFPLVGRW DTLGVVVVDN KFSKKEVTDL DLDVLKLFSE SAGLALENAY NYENLRKKTL DLQRQNELVE HLRNFSESIL ESLETAIITL SKDGRITEWN KKAEQLFGLK KENVLGRRLK DLPDFEEIGS VAESVFENKE PVFLNFYKFG ERYFNIRFSP FRNAKTQLLE GVIITIDDVT ELYKYEEERK RRERLSILGE MTARVAHEIR NPITIIGGFI MRMKKHLDDP ETLKKYINII TNELSRLETI VKEILEYSKE RQVLEFTEFN LNELIREVYV LFEEKIRKMN IDFCFETDNE DLRVEADRTR IKQVLINLVQ NAIEATGENG KIKITSEDMY TKVRVSVWNS GPPIPEELKE KIFSPFFTTK TQGTGLGLSI CRKIIEDEHG GKIWTENREN GVVFIFEIPK TPEKR // ID Q9X175_THEMA Unreviewed; 321 AA. AC Q9X175; G4FF90; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 99. DE SubName: Full=Inosine-5-monophosphate dehydrogenase {ECO:0000313|EMBL:AGL50285.1}; DE EC=1.1.1.205 {ECO:0000313|EMBL:AGL50285.1}; DE SubName: Full=Inosine-5-monophosphate dehydrogenase-related protein {ECO:0000313|EMBL:AAD36425.1}; GN OrderedLocusNames=TM_1354 {ECO:0000313|EMBL:AAD36425.1}; GN ORFNames=Tmari_1361 {ECO:0000313|EMBL:AGL50285.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36425.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36425.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36425.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50285.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50285.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36425.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50285.1; -; Genomic_DNA. DR PIR; B72265; B72265. DR RefSeq; NP_229155.1; NC_000853.1. DR RefSeq; WP_004081550.1; NZ_CP011107.1. DR STRING; 243274.TM1354; -. DR EnsemblBacteria; AAD36425; AAD36425; TM_1354. DR EnsemblBacteria; AGL50285; AGL50285; Tmari_1361. DR GeneID; 898126; -. DR KEGG; tma:TM1354; -. DR KEGG; tmi:THEMA_07570; -. DR KEGG; tmm:Tmari_1361; -. DR KEGG; tmw:THMA_1379; -. DR PATRIC; 23937646; VBITheMar51294_1366. DR eggNOG; ENOG4107RUD; Bacteria. DR eggNOG; COG2172; LUCA. DR OMA; YLHDERR; -. DR OrthoDB; EOG6FZ4DM; -. DR BioCyc; TMAR243274:GC6P-1387-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR003594; HATPase_C. DR Pfam; PF00571; CBS; 2. DR Pfam; PF13581; HATPase_c_2; 1. DR SMART; SM00116; CBS; 2. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS51371; CBS; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50285.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 22 80 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 85 141 CBS. {ECO:0000259|PROSITE:PS51371}. SQ SEQUENCE 321 AA; 36231 MW; 9F149CDCA2A24892 CRC64; MSVSIIDRLQ AIFQDVRVSE FMNPDVIYVT PDKTLLHVKE IMRIKRISGV PVVDDKKRVV GIVSLEDIIK ALEGSYIKDS VEKRMTKNVV CLKETDTLQD AVKTFEKYGY GRFPVVDDEG KLVGIVTKHD IIYFLLAKLG IMYLHDKRME EVLEKGTSLI TGEVLEKGKA DFVFHIDYFD VNMIGIGASK LKRFLLERGV DEELARRIAI ATYEAEANVV IHSESDGYIY CFIDNEKITV RVEDRGKGIE NLELAMREGY STAPDHIREL GFGAGMGLPN MKRYSDKMVI ISEVGKGVIV EMVFFRRDRG EDKGDSGKTG A // ID G4FEX6_THEMA Unreviewed; 253 AA. AC G4FEX6; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 11-MAY-2016, entry version 44. DE SubName: Full=Carboxylesterase {ECO:0000313|EMBL:AGL49948.1}; DE EC=3.1.1.1 {ECO:0000313|EMBL:AGL49948.1}; DE SubName: Full=Esterase {ECO:0000313|EMBL:AAD36099.1}; GN OrderedLocusNames=TM_1022 {ECO:0000313|EMBL:AAD36099.1}; GN ORFNames=Tmari_1024 {ECO:0000313|EMBL:AGL49948.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AGL49948.1, ECO:0000313|Proteomes:UP000013901}; RN [1] {ECO:0000313|EMBL:AAD36099.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36099.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49948.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49948.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36099.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49948.1; -; Genomic_DNA. DR PIR; E72302; E72302. DR RefSeq; NP_228828.1; NC_000853.1. DR RefSeq; WP_004080508.1; NZ_CP011107.1. DR STRING; 243274.TM1022; -. DR ESTHER; thema-ESTA; CarbLipBact_2. DR EnsemblBacteria; AAD36099; AAD36099; TM_1022. DR EnsemblBacteria; AGL49948; AGL49948; Tmari_1024. DR GeneID; 897048; -. DR KEGG; tma:TM1022; -. DR KEGG; tmi:THEMA_09250; -. DR KEGG; tmm:Tmari_1024; -. DR KEGG; tmw:THMA_1043; -. DR eggNOG; ENOG4108DVB; Bacteria. DR eggNOG; COG1647; LUCA. DR KO; K03928; -. DR OMA; SKGYTCH; -. DR BioCyc; TMAR243274:GC6P-1051-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0016298; F:lipase activity; IBA:GO_Central. DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR012354; Esterase_lipase. DR InterPro; IPR022742; Hydrolase_4. DR Pfam; PF12146; Hydrolase_4; 1. DR PIRSF; PIRSF017388; Esterase_lipase; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49948.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 111 Helical. {ECO:0000256|SAM:Phobius}. FT ACT_SITE 98 98 Nucleophile. FT {ECO:0000256|PIRSR:PIRSR017388-1}. FT ACT_SITE 201 201 Charge relay system. FT {ECO:0000256|PIRSR:PIRSR017388-1}. FT ACT_SITE 231 231 Charge relay system. FT {ECO:0000256|PIRSR:PIRSR017388-1}. SQ SEQUENCE 253 AA; 28750 MW; 32E9C94B87F2BFC3 CRC64; MNFPRCKTVK KSLPIFLEGG NEGVLFIHGY TGSPHDFEYM AKEVNRAGFT VSVPRLPGHG TCGEDFLTTT ARDWLRRAFD AYYDLKAICD RVYVVGLSMG GVIALILASQ MNPPKLVTLA AATHVFDKRI VLTPILKLFT KKMPCENTEK YEDPDIEYLR KEYWSYNWPK QAAELYKLMK LARKSVSKIT SATLVVAAKN DNMVPMKAAE FIYNNIRSEK RKLLVFEKSG HVLSNDVEKE DVTRAVIEWL KGE // ID Q9X0Z1_THEMA Unreviewed; 274 AA. AC Q9X0Z1; G4FE84; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 93. DE SubName: Full=Phosphate ABC transporter, periplasmic phosphate-binding protein {ECO:0000313|EMBL:AAD36338.1}; DE SubName: Full=Phosphate ABC transporter, periplasmic phosphate-binding protein PstS {ECO:0000313|EMBL:AGL50193.1}; GN OrderedLocusNames=TM_1264 {ECO:0000313|EMBL:AAD36338.1}; GN ORFNames=Tmari_1269 {ECO:0000313|EMBL:AGL50193.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36338.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36338.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36338.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50193.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50193.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36338.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50193.1; -; Genomic_DNA. DR PIR; C72276; C72276. DR RefSeq; NP_229069.1; NC_000853.1. DR RefSeq; WP_004079990.1; NZ_CP011107.1. DR STRING; 243274.TM1264; -. DR EnsemblBacteria; AAD36338; AAD36338; TM_1264. DR EnsemblBacteria; AGL50193; AGL50193; Tmari_1269. DR GeneID; 898219; -. DR KEGG; tma:TM1264; -. DR KEGG; tmi:THEMA_08015; -. DR KEGG; tmm:Tmari_1269; -. DR KEGG; tmw:THMA_1289; -. DR PATRIC; 23937468; VBITheMar51294_1280. DR eggNOG; ENOG4107TR4; Bacteria. DR eggNOG; COG0226; LUCA. DR KO; K02040; -. DR OMA; REVFFEK; -. DR OrthoDB; EOG6BS8T4; -. DR BioCyc; TMAR243274:GC6P-1295-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0042301; F:phosphate ion binding; IBA:GO_Central. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0016036; P:cellular response to phosphate starvation; IBA:GO_Central. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GOC. DR GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central. DR InterPro; IPR024370; PBP_domain. DR InterPro; IPR011862; Phos-bd. DR Pfam; PF12849; PBP_like_2; 1. DR TIGRFAMs; TIGR02136; ptsS_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 19 256 PBP_domain. {ECO:0000259|Pfam:PF12849}. SQ SEQUENCE 274 AA; 30556 MW; 167269FAF14CB396 CRC64; MKRFVVLLLS LVSVFLVAET LVIKGSNTVF PIAQLWIEEF KKLHPDLQVT LEGAGSSTGI AALFNGTTDI ANSSRWLKPS EIERMNKEGK YFIPFLIAFD GIAIIVNKDL GIDDISIETL KKIYTGEIQY WSQVNPNLPK QRIVVYSRNT ASGTYETFEN KVLGGARMAP YVRMVESTQL EVESVSKNPY AIAYVGVGYV TDDVKVLKVN GIYPTKENIL KGKYPIARPL FMFVDATNGF PEMGSLVFEY IMFAFSKKGQ ELVEKAGYIA AYGQ // ID Q9X1W8_THEMA Unreviewed; 787 AA. AC Q9X1W8; G4FG22; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 128. DE RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}; DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}; DE AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973}; GN Name=lon {ECO:0000256|HAMAP-Rule:MF_01973}; GN OrderedLocusNames=TM_1633 {ECO:0000313|EMBL:AAD36700.1}; GN ORFNames=Tmari_1642 {ECO:0000313|EMBL:AGL50566.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36700.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36700.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36700.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50566.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50566.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: ATP-dependent serine protease that mediates the CC selective degradation of mutant and abnormal proteins as well as CC certain short-lived regulatory proteins. Required for cellular CC homeostasis and for survival from DNA damage and developmental CC changes induced by stress. Degrades polypeptides processively to CC yield small peptide fragments that are 5 to 10 amino acids long. CC Binds to DNA in a double-stranded, site-specific manner. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00338846}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, CC ECO:0000256|SAAS:SAAS00004348}. CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, CC ECO:0000256|SAAS:SAAS00536021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, CC ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00004358}. CC -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}. CC -!- SIMILARITY: Belongs to the peptidase S16 family. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, CC ECO:0000256|SAAS:SAAS00536024}. CC -!- SIMILARITY: Contains 1 Lon N-terminal domain. {ECO:0000256|HAMAP- CC Rule:MF_01973}. CC -!- SIMILARITY: Contains 1 Lon proteolytic domain. {ECO:0000256|HAMAP- CC Rule:MF_01973}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36700.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50566.1; -; Genomic_DNA. DR PIR; A72230; A72230. DR RefSeq; NP_229433.1; NC_000853.1. DR RefSeq; WP_004082110.1; NZ_CP011107.1. DR SMR; Q9X1W8; 611-785. DR STRING; 243274.TM1633; -. DR MEROPS; S16.001; -. DR EnsemblBacteria; AAD36700; AAD36700; TM_1633. DR EnsemblBacteria; AGL50566; AGL50566; Tmari_1642. DR GeneID; 896846; -. DR KEGG; tma:TM1633; -. DR KEGG; tmi:THEMA_06080; -. DR KEGG; tmm:Tmari_1642; -. DR KEGG; tmw:THMA_1674; -. DR PATRIC; 23938240; VBITheMar51294_1652. DR eggNOG; ENOG4105C6P; Bacteria. DR eggNOG; COG0466; LUCA. DR KO; K01338; -. DR OMA; VVFPYMM; -. DR OrthoDB; EOG6XHC23; -. DR BioCyc; TMAR243274:GC6P-1679-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0033554; P:cellular response to stress; IEA:UniProtKB-HAMAP. DR GO; GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01973; lon_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR027543; Lon_bac. DR InterPro; IPR004815; Lon_bac/euk-typ. DR InterPro; IPR027065; Lon_Prtase. DR InterPro; IPR003111; LON_substr-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008269; Pept_S16_C. DR InterPro; IPR008268; Peptidase_S16_AS. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10046; PTHR10046; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF05362; Lon_C; 1. DR Pfam; PF02190; LON_substr_bdg; 1. DR PIRSF; PIRSF001174; Lon_proteas; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00464; LON; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00763; lon; 1. DR PROSITE; PS01046; LON_SER; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-2, KW ECO:0000256|SAAS:SAAS00417290}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00417288}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00417291}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-2, KW ECO:0000256|SAAS:SAAS00417290}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00417291}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Serine protease {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00417291}; KW Stress response {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|SAAS:SAAS00417292}. FT DOMAIN 31 225 LON. {ECO:0000259|SMART:SM00464}. FT DOMAIN 369 514 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 377 384 ATP. {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-2}. FT COILED 213 250 {ECO:0000256|SAM:Coils}. FT ACT_SITE 693 693 {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1}. FT ACT_SITE 736 736 {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1}. SQ SEQUENCE 787 AA; 89266 MW; 6B10BA690D1A5562 CRC64; MSKKSKDTEK SFKILEKYAS QQEKELEIPD SLPCIPLRNG MGVFPNTVVP FYVGRTGSLI ALEEAMEKYN RLLLVVNQKD PSVEIPEPED LYKVGTVVKV LQIMKLPDDT FKVLVEGLER AQIEEFVSTD PFFLTKIKIL KVKYRKTKKL EALMRSVKDK AVRYFNLTHR FPQETLVTLK EMQDPDKLAD FVASILPVPL ETKQELLETV HPLERLEKIL SILVKEIEIL EIEEEIEKKV KDRIEKTQRE YVLREKLRAI KEELGVEEEL EIKELYEKVE KGDYPDYVKE KAYKEIQRLE KMSPYSAEAT VVRTYLDWLL NLPWNVATED RLDIKEARKI LDKNHYGLGE VKERILEYLV ARKFSKNLKA PILCLVGPPG VGKTSLGRTI AEAMGRKFGR MSLGGLRDEA EIKGHRRTYV GALPGRIIQI IRRLGTKNPV ILLDEVDKMG ISFQGDPASA LLEVLDPEQN KDFVDHYLEV PFDLSQVLFI TTANVLHTIP PALRDRMEII EIPGYSDPEK YHIARDYIIP KIARSYGLSK VMFTPGAIKK IIREYTKEAG VRNLERVIEK VIRKSLVKGE KKSFKITTKD VEELLGPPVF REEEILEEDT VGAVTGLAWT PVGGSVLIVE SLLLPGRGNL ILTGNMGDVM KESARIALSV VRKMCGEECR EVFEKNDIHI HVPEGAVPKD GPSAGITITV ALYSAVTGKK VRRDVAMTGE ITLRGKILPV GGIKEKLLAA KRAGIKKVIL PSRNRPDVEK IPKEYLNGME IVYCSEIQEV LKEAIVR // ID Q9X1G1_THEMA Unreviewed; 140 AA. AC Q9X1G1; G4FFI4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 96. DE SubName: Full=Tetratricopeptide repeat (TPR) family protein {ECO:0000313|EMBL:AGL50379.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36517.1}; GN OrderedLocusNames=TM_1449 {ECO:0000313|EMBL:AAD36517.1}; GN ORFNames=Tmari_1455 {ECO:0000313|EMBL:AGL50379.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36517.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36517.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36517.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50379.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50379.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36517.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50379.1; -; Genomic_DNA. DR PIR; E72253; E72253. DR RefSeq; NP_229248.1; NC_000853.1. DR RefSeq; WP_004081726.1; NZ_CP011107.1. DR STRING; 243274.TM1449; -. DR EnsemblBacteria; AAD36517; AAD36517; TM_1449. DR EnsemblBacteria; AGL50379; AGL50379; Tmari_1455. DR GeneID; 898027; -. DR KEGG; tma:TM1449; -. DR KEGG; tmi:THEMA_07070; -. DR KEGG; tmm:Tmari_1455; -. DR KEGG; tmw:THMA_1479; -. DR PATRIC; 23937850; VBITheMar51294_1463. DR eggNOG; ENOG41062R4; Bacteria. DR eggNOG; COG0457; LUCA. DR OMA; ARAIECY; -. DR OrthoDB; EOG676Z0H; -. DR BioCyc; TMAR243274:GC6P-1487-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF13414; TPR_11; 1. DR SMART; SM00028; TPR; 2. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50005; TPR; 2. DR PROSITE; PS50293; TPR_REGION; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 35 102 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 140 AA; 16171 MW; F433D43346929821 CRC64; MVSSEFEEAY RELEEGKLES ALEKFLKIAE KEQSVEVWVN IGNIYRRMNL LAKAIESYKR ALEIDQKNPV VLFNLGSAYY QMGKFFEALK LLEKAEEQGL TDPRVKIVKA LCKIKLNLPD PMEGLDEDQK RIVKDLMKNG // ID Q9X0W4_THEMA Unreviewed; 355 AA. AC Q9X0W4; G4FEB0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=Radical SAM, Pyruvate-formate lyase-activating enzyme like protein {ECO:0000313|EMBL:AGL50167.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36312.1}; GN OrderedLocusNames=TM_1237 {ECO:0000313|EMBL:AAD36312.1}; GN ORFNames=Tmari_1243 {ECO:0000313|EMBL:AGL50167.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36312.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36312.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36312.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50167.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50167.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|PIRSR:PIRSR004869-50}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|PIRSR:PIRSR004869-50}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36312.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50167.1; -; Genomic_DNA. DR PIR; F72279; F72279. DR RefSeq; NP_229042.1; NC_000853.1. DR RefSeq; WP_004080040.1; NZ_CP011107.1. DR STRING; 243274.TM1237; -. DR EnsemblBacteria; AAD36312; AAD36312; TM_1237. DR EnsemblBacteria; AGL50167; AGL50167; Tmari_1243. DR GeneID; 898247; -. DR KEGG; tma:TM1237; -. DR KEGG; tmi:THEMA_08150; -. DR KEGG; tmm:Tmari_1243; -. DR KEGG; tmw:THMA_1262; -. DR PATRIC; 23937414; VBITheMar51294_1254. DR eggNOG; COG1180; LUCA. DR KO; K04069; -. DR OMA; PLPTNCV; -. DR OrthoDB; EOG6QK4PP; -. DR BioCyc; TMAR243274:GC6P-1267-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004869; PflX_prd; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|PIRSR:PIRSR004869-50}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR004869-50}; KW Lyase {ECO:0000313|EMBL:AGL50167.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR004869-50}; KW Pyruvate {ECO:0000313|EMBL:AGL50167.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR004869-50}. FT DOMAIN 128 299 Radical_SAM. {ECO:0000259|Pfam:PF04055}. FT METAL 133 133 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. FT METAL 137 137 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. FT METAL 140 140 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. SQ SEQUENCE 355 AA; 40139 MW; FA27C779C4B4B8FE CRC64; MGVCRICGLS LDEISDSIGV CLECLRKGNL DFARKAHRKW REEIGLPVER WAREEGKVCF LCVNSCVIPE GKTGFCGVLR NEGGRLSYIT GSHRKAFLHW YYDPHPTNCV ALPICPEREH RGFYNFAVFF AGCNLDCLFC QNIDHKYMVK DGRISEGKIV DIDELVEIAM KPRVSCVCFF GGDPTPWTVF ALEFAVKLGN RRRICWETNG LAHPRIMERM ARVSLESGGI VKIDWKAFSP EVYEALTGVD GKSAVRRIME NVQLVSSMGK GREIPLLVIS VLVIPHYIDE KEIEGIAGFI SSVDPEIPLV LLAFAPQHLM SDLPTTRKHH MERVKQKALE KGLKRVFVEN VWLLS // ID Q9WZG0_THEMA Unreviewed; 217 AA. AC Q9WZG0; G4FDC8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=Ray-related protein {ECO:0000313|EMBL:AAD35778.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL49621.1}; GN OrderedLocusNames=TM_0696 {ECO:0000313|EMBL:AAD35778.1}; GN ORFNames=Tmari_0696 {ECO:0000313|EMBL:AGL49621.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35778.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35778.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35778.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49621.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49621.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35778.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49621.1; -; Genomic_DNA. DR PIR; F72345; F72345. DR RefSeq; NP_228505.1; NC_000853.1. DR RefSeq; WP_004081057.1; NZ_CP011107.1. DR STRING; 243274.TM0696; -. DR DNASU; 898363; -. DR EnsemblBacteria; AAD35778; AAD35778; TM_0696. DR EnsemblBacteria; AGL49621; AGL49621; Tmari_0696. DR GeneID; 898363; -. DR KEGG; tma:TM0696; -. DR KEGG; tmi:THEMA_01185; -. DR KEGG; tmm:Tmari_0696; -. DR KEGG; tmw:THMA_0711; -. DR PATRIC; 23936310; VBITheMar51294_0708. DR eggNOG; ENOG4105IAB; Bacteria. DR eggNOG; COG2930; LUCA. DR OMA; IGAESTD; -. DR OrthoDB; EOG6P338T; -. DR BioCyc; TMAR243274:GC6P-722-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0032587; C:ruffle membrane; IBA:GO_Central. DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central. DR GO; GO:1900027; P:regulation of ruffle assembly; IBA:GO_Central. DR InterPro; IPR007461; Ysc84_actin-binding. DR Pfam; PF04366; Ysc84; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 217 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972323. FT DOMAIN 96 211 Ysc84. {ECO:0000259|Pfam:PF04366}. SQ SEQUENCE 217 AA; 24048 MW; 303BA7D4DCE3AC29 CRC64; MKQFLVALTI LTSSLFSFAS ALDIIDESFL ALKEFLDQPD SGAFLSLLER ARGIFIVPKY LKLGWVLGGQ YGQGVLLKRD PETNTWYGPL FVKMYGLSFG PQIGFQSVSL IAVIMENVDA FAEGNITLGG SLSVAAGPLG RRLSADYNLD ASVYSYSIAR GFYAGFSLEG AKIDVDLDLT REYYNVYRIE PEEILRREVS GRAEKIVNLL NEKLTEE // ID Q9X0N2_THEMA Unreviewed; 399 AA. AC Q9X0N2; G4FEJ9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 115. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108}; DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108}; GN OrderedLocusNames=TM_1148 {ECO:0000313|EMBL:AAD36224.1}; GN ORFNames=Tmari_1155 {ECO:0000313|EMBL:AGL50079.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36224.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36224.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36224.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50079.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50079.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) CC + NADPH. {ECO:0000256|PIRNR:PIRNR000108}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRNR:PIRNR000108, CC ECO:0000256|PIRSR:PIRSR000108-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRNR:PIRNR000108, CC ECO:0000256|PIRSR:PIRSR000108-3}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000256|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-3}; CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. {ECO:0000256|PIRNR:PIRNR000108}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36224.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50079.1; -; Genomic_DNA. DR PIR; H72288; H72288. DR RefSeq; NP_228954.1; NC_000853.1. DR RefSeq; WP_004080233.1; NZ_CP011107.1. DR PDB; 1ZOR; X-ray; 2.24 A; A/B=1-399. DR PDBsum; 1ZOR; -. DR STRING; 243274.TM1148; -. DR EnsemblBacteria; AAD36224; AAD36224; TM_1148. DR EnsemblBacteria; AGL50079; AGL50079; Tmari_1155. DR GeneID; 898338; -. DR KEGG; tma:TM1148; -. DR KEGG; tmi:THEMA_08600; -. DR KEGG; tmm:Tmari_1155; -. DR KEGG; tmw:THMA_1172; -. DR PATRIC; 23937233; VBITheMar51294_1165. DR eggNOG; ENOG4105D5N; Bacteria. DR eggNOG; COG0538; LUCA. DR KO; K00031; -. DR OMA; VMGMYNF; -. DR OrthoDB; EOG628F3X; -. DR BioCyc; TMAR243274:GC6P-1177-MONOMER; -. DR BRENDA; 1.1.1.42; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006102; P:isocitrate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; -; 1. DR InterPro; IPR004790; Isocitrate_DH_NADP. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR PANTHER; PTHR11822; PTHR11822; 1. DR Pfam; PF00180; Iso_dh; 1. DR PIRSF; PIRSF000108; IDH_NADP; 1. DR SMART; SM01329; Iso_dh; 1. DR TIGRFAMs; TIGR00127; nadp_idh_euk; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1ZOR}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Magnesium {ECO:0000256|PIRNR:PIRNR000108, KW ECO:0000256|PIRSR:PIRSR000108-3}; KW Manganese {ECO:0000256|PIRNR:PIRNR000108, KW ECO:0000256|PIRSR:PIRSR000108-3}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000108, KW ECO:0000256|PIRSR:PIRSR000108-3}; KW NADP {ECO:0000256|PIRNR:PIRNR000108}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000108, KW ECO:0000313|EMBL:AGL50079.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}. FT REGION 94 100 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000108-2}. FT METAL 247 247 Magnesium or manganese. FT {ECO:0000256|PIRSR:PIRSR000108-3}. FT METAL 270 270 Magnesium or manganese. FT {ECO:0000256|PIRSR:PIRSR000108-3}. FT BINDING 77 77 Substrate. FT {ECO:0000256|PIRSR:PIRSR000108-2}. FT BINDING 109 109 Substrate. FT {ECO:0000256|PIRSR:PIRSR000108-2}. FT BINDING 132 132 Substrate. FT {ECO:0000256|PIRSR:PIRSR000108-2}. FT SITE 139 139 Critical for catalysis. FT {ECO:0000256|PIRSR:PIRSR000108-1}. FT SITE 208 208 Critical for catalysis. FT {ECO:0000256|PIRSR:PIRSR000108-1}. SQ SEQUENCE 399 AA; 45403 MW; 21828AFA6AE10034 CRC64; MEKVKVKNPI VELDGDEMAR VMWKMIKEKL ILPYLDIQLV YFDLGIKKRD ETDDQITIEA AKAIKKYGVG VKCATITPDA ERVKEYNLKK AWKSPNATIR AYLDGTVFRK PIMVKNVPPL VKRWKKPIII GRHAYGDIYN AVEAKVEGPA EVELVVRNKE NKTLLVHKFE GNGVVMAMHN LEKSIRSFAQ SCINYAISEK VDIWFATKDT ISKVYHAYFK DIFQEEVDKR KEELEKAGVN YRYMLIDDAA AQILRSEGGM LWACMNYEGD IMSDMIASGF GSLGLMTSVL VSPDGVYEFE AAHGTVRRHY YRYLKGEKTS TNPTASIFAW TGAIRKRGEL DGTPEVCEFA DKLEKAVINT IESGVITKDL QPFTEPPIDK YVTLEEFIDE VKKNLEKLL // ID Q9WZG3_THEMA Unreviewed; 97 AA. AC Q9WZG3; G4FDC5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 81. DE SubName: Full=Flagellar biosynthesis protein FliZ {ECO:0000313|EMBL:AGL49624.1}; DE SubName: Full=Flagellar biosynthesis protein FliZ, putative {ECO:0000313|EMBL:AAD35781.1}; GN OrderedLocusNames=TM_0699 {ECO:0000313|EMBL:AAD35781.1}; GN ORFNames=Tmari_0699 {ECO:0000313|EMBL:AGL49624.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35781.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35781.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35781.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49624.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49624.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35781.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49624.1; -; Genomic_DNA. DR PIR; A72346; A72346. DR RefSeq; NP_228508.1; NC_000853.1. DR RefSeq; WP_004081050.1; NZ_CP011107.1. DR STRING; 243274.TM0699; -. DR EnsemblBacteria; AAD35781; AAD35781; TM_0699. DR EnsemblBacteria; AGL49624; AGL49624; Tmari_0699. DR GeneID; 898366; -. DR KEGG; tma:TM0699; -. DR KEGG; tmi:THEMA_01170; -. DR KEGG; tmm:Tmari_0699; -. DR KEGG; tmw:THMA_0714; -. DR PATRIC; 23936316; VBITheMar51294_0711. DR eggNOG; ENOG4106HCJ; Bacteria. DR eggNOG; ENOG410Y2UT; LUCA. DR KO; K02418; -. DR OMA; RVIERCY; -. DR OrthoDB; EOG6N949X; -. DR BioCyc; TMAR243274:GC6P-725-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:InterPro. DR InterPro; IPR022781; Flagellar_biosynth_FliO. DR Pfam; PF04347; FliO; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AAD35781.1}; KW Cilium {ECO:0000313|EMBL:AAD35781.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35781.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 97 AA; 11282 MW; CADF68471812DFB6 CRC64; MSGILQFLLA FGIVLFFLLL VYYFVKRGTF IQKGSSISVL ERHYLDRKTF IAIVRVIDEY LVILVTDSGA TVIKKLEDYE EKSFSSMFFK KLGRKIK // ID Q9WYR6_THEMA Unreviewed; 159 AA. AC Q9WYR6; G4FE35; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Acetyl xylan esterase {ECO:0000313|EMBL:AGL49357.1}; DE EC=3.1.1.41 {ECO:0000313|EMBL:AGL49357.1}; DE SubName: Full=Acetyl xylan esterase-related protein {ECO:0000313|EMBL:AAD35520.1}; GN OrderedLocusNames=TM_0435 {ECO:0000313|EMBL:AAD35520.1}; GN ORFNames=Tmari_0432 {ECO:0000313|EMBL:AGL49357.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35520.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35520.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35520.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49357.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49357.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35520.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49357.1; -; Genomic_DNA. DR PIR; F72376; F72376. DR RefSeq; NP_228245.1; NC_000853.1. DR RefSeq; WP_004081531.1; NC_000853.1. DR SMR; Q9WYR6; 2-158. DR STRING; 243274.TM0435; -. DR EnsemblBacteria; AAD35520; AAD35520; TM_0435. DR EnsemblBacteria; AGL49357; AGL49357; Tmari_0432. DR GeneID; 897449; -. DR KEGG; tma:TM0435; -. DR KEGG; tmi:THEMA_02550; -. DR KEGG; tmm:Tmari_0432; -. DR PATRIC; 23935755; VBITheMar51294_0441. DR eggNOG; COG3458; LUCA. DR KO; K01060; -. DR OrthoDB; EOG6CZQPN; -. DR BioCyc; TMAR243274:GC6P-450-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0047739; F:cephalosporin-C deacetylase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR008391; AXE1_dom. DR Pfam; PF05448; AXE1; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49357.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 158 AXE1. {ECO:0000259|Pfam:PF05448}. SQ SEQUENCE 159 AA; 18722 MW; 131FC65BB64A0CD4 CRC64; MALFDMPLEK LRSYLPERYE EGDFDQFWRK TLEESKGFPL DPVFERVDYL LENVEVYDVT FSGYKGQRIK AWLILPVVRK EEKLPCVVQF IGYRGGRGFP FDWLFWSSAG YANFVMDTRG QGTSRTKGDT PDYCEEPLNP QFPGFMTRGI LDPKTYYYI // ID Q9WYL1_THEMA Unreviewed; 443 AA. AC Q9WYL1; G4FHU0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 112. DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:AAD35465.1}; GN OrderedLocusNames=TM_0379 {ECO:0000313|EMBL:AAD35465.1}; GN ORFNames=Tmari_0377 {ECO:0000313|EMBL:AGL49302.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35465.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35465.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35465.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49302.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49302.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35465.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49302.1; -; Genomic_DNA. DR PIR; D72383; D72383. DR RefSeq; NP_228190.1; NC_000853.1. DR RefSeq; WP_004083195.1; NZ_CP011107.1. DR STRING; 243274.TM0379; -. DR EnsemblBacteria; AAD35465; AAD35465; TM_0379. DR EnsemblBacteria; AGL49302; AGL49302; Tmari_0377. DR GeneID; 897354; -. DR KEGG; tma:TM0379; -. DR KEGG; tmi:THEMA_02825; -. DR KEGG; tmm:Tmari_0377; -. DR KEGG; tmw:THMA_0386; -. DR PATRIC; 23935639; VBITheMar51294_0384. DR eggNOG; ENOG4107QYY; Bacteria. DR eggNOG; COG0446; LUCA. DR OMA; MATHPYL; -. DR OrthoDB; EOG6QVRCJ; -. DR BioCyc; TMAR243274:GC6P-393-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR SUPFAM; SSF51905; SSF51905; 1. DR SUPFAM; SSF55424; SSF55424; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 299 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. FT DOMAIN 330 429 Pyr_redox_dim. FT {ECO:0000259|Pfam:PF02852}. SQ SEQUENCE 443 AA; 47598 MW; 954E69313CAC1F74 CRC64; MRYDVVVVGG GPAGLVAAFT TKRFFGDKKI LVVKKTEKEM VPCGIPYIFH TLGSVENDYM GIEDRFKGAG IDLLIDEVVD GNPDEKKLFT KSGKEISYDK LIIATGSSPN IPKIPGVDLK GVFTVPKEAD YLKLLHEKVK DANDVVIIGG GFIGVEVADE IKKSGKNVTL VEIMDSLLPV SFDPDFGELA RKELESDNVK VLTGRKVTEI LGTEKVEGVK LDSGETIPAD VVVLATGYKP NSELARKLGL KVTELGFIET DEYMRTSKPD IFAAGDCVQH KDFLTGKPSR LMLASAAVFD ARIAASNLYG LKVIRTNKGS LNAYSTVIGS KAFGSVGITE RIAKEEGFEV VVGKAEAPDR HPGKFEDTSK LVVKLIFSED SKILLGAQVC GGKSVGEIVN LISLGIQKGI TANDLFTMQI GTHPLLTSAP TVYPLAKAAE MVL // ID Q9X0X4_THEMA Unreviewed; 431 AA. AC Q9X0X4; G4FEA1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 103. DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}; DE Short=ATase {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}; DE EC=2.4.2.14 {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}; DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}; GN Name=purF {ECO:0000256|HAMAP-Rule:MF_01931}; GN OrderedLocusNames=TM_1247 {ECO:0000313|EMBL:AAD36322.1}; GN ORFNames=Tmari_1252 {ECO:0000313|EMBL:AGL50176.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36322.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36322.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36322.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50176.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50176.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from CC phosphoribosylpyrophosphate (PRPP) and glutamine. CC {ECO:0000256|HAMAP-Rule:MF_01931}. CC -!- CATALYTIC ACTIVITY: 5-phospho-beta-D-ribosylamine + diphosphate + CC L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate CC + H(2)O. {ECO:0000256|HAMAP-Rule:MF_01931, CC ECO:0000256|PIRNR:PIRNR000485}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01931}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01931}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01931, CC ECO:0000256|PIRSR:PIRSR000485-3}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-3}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D- CC ribose 1-diphosphate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_01931, CC ECO:0000256|PIRNR:PIRNR000485}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000256|HAMAP-Rule:MF_01931}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC purine/pyrimidine phosphoribosyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36322.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50176.1; -; Genomic_DNA. DR PIR; A72277; A72277. DR RefSeq; NP_229052.1; NC_000853.1. DR RefSeq; WP_004080018.1; NZ_CP011107.1. DR STRING; 243274.TM1247; -. DR EnsemblBacteria; AAD36322; AAD36322; TM_1247. DR EnsemblBacteria; AGL50176; AGL50176; Tmari_1252. DR GeneID; 898236; -. DR KEGG; tma:TM1247; -. DR KEGG; tmi:THEMA_08100; -. DR KEGG; tmm:Tmari_1252; -. DR KEGG; tmw:THMA_1272; -. DR PATRIC; 23937434; VBITheMar51294_1263. DR eggNOG; ENOG4105CBA; Bacteria. DR eggNOG; COG0034; LUCA. DR KO; K00764; -. DR OMA; IRHFGVK; -. DR OrthoDB; EOG6KT2Q1; -. DR BioCyc; TMAR243274:GC6P-1278-MONOMER; -. DR UniPathway; UPA00074; UER00124. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_01931; PurF; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005854; PurF. DR Pfam; PF13537; GATase_7; 1. DR Pfam; PF00156; Pribosyltran; 1. DR PIRSF; PIRSF000485; Amd_phspho_trans; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR01134; purF; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01931}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931, KW ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:AAD36322.1}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01931}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01931}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01931}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01931}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01931, KW ECO:0000256|PIRNR:PIRNR000485}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01931, KW ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:AAD36322.1}. FT DOMAIN 2 212 Glutamine amidotransferase type-2. FT {ECO:0000259|PROSITE:PS51278}. FT ACT_SITE 2 2 For GATase activity. FT {ECO:0000256|PIRSR:PIRSR000485-1}. FT ACT_SITE 2 2 Nucleophile. {ECO:0000256|HAMAP- FT Rule:MF_01931}. FT METAL 227 227 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01931, FT ECO:0000256|PIRSR:PIRSR000485-3}. FT METAL 274 274 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01931}. FT METAL 334 334 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01931}. FT METAL 335 335 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01931}. FT METAL 371 371 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01931, FT ECO:0000256|PIRSR:PIRSR000485-3}. FT METAL 420 420 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01931, FT ECO:0000256|PIRSR:PIRSR000485-3}. FT METAL 423 423 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01931, FT ECO:0000256|PIRSR:PIRSR000485-3}. SQ SEQUENCE 431 AA; 47564 MW; 7FB872CC8AC29508 CRC64; MCGIAGVWNV KDAFSVLHDV LLGLQHRGQE SVGVVVDGFK TIKGKGLVDT VLTEDRWEDA EKGIGHVRYS TAGSLEDIQP IVAFTRKGRL AIAHNGNIPN GEKWIEMLKE KGAVFQSSLD SEVFLHLISM SEGDLKESIV KALKKVPLAY SLLILHEEFL AAARDPYGVR PLFYGKYGDG IVVASEDAAL KAIGVEDIEE VPSGTVVFFS NKGTETVRFS KKEKRFCSFE FIYFARPDSH FLDQSVHIAR YRMGEELYRE NPIEADVVVP VLDSGLSGAM GFSSASGIPL DIGLMRNRYV GRSFIMPVDR EKIVKKKLVP IEDVVSGKRV VVIDDSIVRG TTMGIIVKIL REAGAKEVHV GIHSPPVRFP CFYGIDTARK KELVAGERAV EEVKKIVNAD SLFYLSLEGL KRAIGRSELC VACFSGEYLH E // ID Q9X1M9_THEMA Unreviewed; 249 AA. AC Q9X1M9; G4FFT1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Flagellar basal-body rod protein FlgF {ECO:0000313|EMBL:AAD36610.1}; GN OrderedLocusNames=TM_1543 {ECO:0000313|EMBL:AAD36610.1}; GN ORFNames=Tmari_1551 {ECO:0000313|EMBL:AGL50475.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36610.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36610.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36610.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50475.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50475.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body CC {ECO:0000256|RuleBase:RU362116}. CC -!- SIMILARITY: Belongs to the flagella basal body rod proteins CC family. {ECO:0000256|RuleBase:RU362116}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36610.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50475.1; -; Genomic_DNA. DR PIR; C72243; C72243. DR RefSeq; NP_229343.1; NC_000853.1. DR RefSeq; WP_004081931.1; NZ_CP011107.1. DR STRING; 243274.TM1543; -. DR EnsemblBacteria; AAD36610; AAD36610; TM_1543. DR EnsemblBacteria; AGL50475; AGL50475; Tmari_1551. DR GeneID; 897348; -. DR KEGG; tma:TM1543; -. DR KEGG; tmi:THEMA_06570; -. DR KEGG; tmm:Tmari_1551; -. DR KEGG; tmw:THMA_1577; -. DR PATRIC; 23938046; VBITheMar51294_1561. DR eggNOG; ENOG4105KTQ; Bacteria. DR eggNOG; COG4786; LUCA. DR KO; K02391; -. DR KO; K02392; -. DR OMA; HERIRIP; -. DR OrthoDB; EOG6M6JKX; -. DR BioCyc; TMAR243274:GC6P-1583-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030694; C:bacterial-type flagellum basal body, rod; IEA:InterPro. DR GO; GO:0009424; C:bacterial-type flagellum hook; IBA:GO_Central. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IBA:GO_Central. DR InterPro; IPR020013; Flagellar_FlgE/F/G. DR InterPro; IPR010930; Flg_bb/hook_C_dom. DR InterPro; IPR012836; FlgF. DR Pfam; PF06429; Flg_bbr_C; 1. DR TIGRFAMs; TIGR03506; FlgEFG_subfam; 1. DR TIGRFAMs; TIGR02490; flgF; 1. PE 3: Inferred from homology; KW Bacterial flagellum {ECO:0000256|RuleBase:RU362116}; KW Cell projection {ECO:0000313|EMBL:AAD36610.1}; KW Cilium {ECO:0000313|EMBL:AAD36610.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD36610.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 178 243 Flg_bbr_C. {ECO:0000259|Pfam:PF06429}. SQ SEQUENCE 249 AA; 28243 MW; 42E681A22582BF56 CRC64; MTRGIYNAAM GMLVDMAKLD RIANDLANVD TAGYKQDREA FRAYLRREVF RQEPNPVESR TKKVPIGPLE YATVLDEVRT DLSQGPVEET DVPYHLAING EGFFRIEFNG GEYYTRNGEF TVNSEGYIVT NYGGYLLDEN GERVRFFDDF TVDEEGYVRD AYGNIVTRIG VYNLENPEKF GNTLFTGENP SPSENFRIMQ GYVEKSNVDA LKAMVDMISA MRHYELSQRA VTVNDELNGK LINSLASLK // ID Q9X1Y5_THEMA Unreviewed; 553 AA. AC Q9X1Y5; G4FG41; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=Exopolysaccharide biosynthesis protein related to N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase {ECO:0000313|EMBL:AGL50585.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36719.1}; GN OrderedLocusNames=TM_1652 {ECO:0000313|EMBL:AAD36719.1}; GN ORFNames=Tmari_1661 {ECO:0000313|EMBL:AGL50585.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36719.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36719.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36719.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50585.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50585.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36719.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50585.1; -; Genomic_DNA. DR PIR; A72228; A72228. DR RefSeq; NP_229452.1; NC_000853.1. DR RefSeq; WP_004082158.1; NZ_CP011107.1. DR STRING; 243274.TM1652; -. DR EnsemblBacteria; AAD36719; AAD36719; TM_1652. DR EnsemblBacteria; AGL50585; AGL50585; Tmari_1661. DR GeneID; 897915; -. DR KEGG; tma:TM1652; -. DR KEGG; tmi:THEMA_05985; -. DR KEGG; tmm:Tmari_1661; -. DR KEGG; tmw:THMA_1693; -. DR PATRIC; 23938278; VBITheMar51294_1671. DR eggNOG; ENOG41083CR; Bacteria. DR eggNOG; ENOG410ZXBD; LUCA. DR OMA; VTKFPIG; -. DR OrthoDB; EOG6038SP; -. DR BioCyc; TMAR243274:GC6P-1698-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR018711; NAGPA. DR Pfam; PF09992; NAGPA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 401 543 NAGPA. {ECO:0000259|Pfam:PF09992}. SQ SEQUENCE 553 AA; 61271 MW; DA5F5C9625BAC6A0 CRC64; MKQIILVLLI FASVVFGSYL ISGGKAFPLR TVFSEGIYYV CAEDLAPAGV GYIHSNGYHY IVYDNHVLFI KEHETIFDFV EKLSPPLFVD GLLFVPIDAL KKVMEGYQMY TKGEKVLIYD SLPIVLSAAK EKNGVTITYT GTIVPDMVSV EKSMGRVRIN LSPVVVSLPN VSEDIKVELE KNGLSFIVDV GNFYPDVEYS IGDGKLLFRF LLVEGFFGRL EVADGVVFER KIEEFDEGEK TVVNYLIMDP EKVTIKPVVS ENGFGTIERL DEMVKRVGGI AGINGNYFDP VTKFPIGLVV IDGKPYSAMF SGRPVFAITE DNEVFIGRVI VDVTLMVKDV LFLVKGINTL GEGEVLVYTK EFSKEIPKKD DKIYFVVKDS KVSQIGYKSH AEDSEYVVSI SKKYEEYLSD LKEGDEVYIS LQPNIPLRIK QAVEGGPLLI QNGAPIPDAW EEKARYGGGI AYAKAPRTVI ATKDGKLWFL VFEGYNHITR GLTYDELVDF LVSRGFEDAM CVDGGSSSVM AVAGSLFGRT ENSTAAIPVG IVVWEKKKTE VGK // ID Q9X1S2_THEMA Unreviewed; 206 AA. AC Q9X1S2; G4FFX4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36653.1}; GN OrderedLocusNames=TM_1586 {ECO:0000313|EMBL:AAD36653.1}; GN ORFNames=Tmari_1594 {ECO:0000313|EMBL:AGL50518.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36653.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36653.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36653.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50518.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50518.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36653.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50518.1; -; Genomic_DNA. DR PIR; B72236; B72236. DR RefSeq; NP_229386.1; NC_000853.1. DR RefSeq; WP_004082018.1; NZ_CP011107.1. DR PDB; 1VKW; X-ray; 2.00 A; A=1-206. DR PDBsum; 1VKW; -. DR STRING; 243274.TM1586; -. DR DNASU; 897434; -. DR EnsemblBacteria; AAD36653; AAD36653; TM_1586. DR EnsemblBacteria; AGL50518; AGL50518; Tmari_1594. DR GeneID; 897434; -. DR KEGG; tma:TM1586; -. DR KEGG; tmi:THEMA_06350; -. DR KEGG; tmm:Tmari_1594; -. DR KEGG; tmw:THMA_1621; -. DR PATRIC; 23938136; VBITheMar51294_1605. DR eggNOG; ENOG4107IG3; Bacteria. DR eggNOG; COG0778; LUCA. DR OMA; NAGYIME; -. DR OrthoDB; EOG68DD44; -. DR BioCyc; TMAR243274:GC6P-1627-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.109.10; -; 1. DR InterPro; IPR000415; Nitroreductase-like. DR InterPro; IPR029478; TM1586_NiRdase. DR Pfam; PF14512; TM1586_NiRdase; 1. DR SUPFAM; SSF55469; SSF55469; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VKW}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 182 TM1586_NiRdase. FT {ECO:0000259|Pfam:PF14512}. FT DISULFID 162 201 {ECO:0000213|PDB:1VKW}. SQ SEQUENCE 206 AA; 24067 MW; 5FD13CBE83C6A5E6 CRC64; MNIFEAIENR HSVRDFLERK MPERVKDDIE NLLVKFITKK LDWKINLSSF PSYIYAKAEK HFDELVEYGF QGEQIVLFLT AQGFGTCWMA RSPHPDVPYI IVFGYPRTRN FTRKRRPITS FLENDLEELP PEIVKIVEMT ILAPSALNRQ PWKIKYTGGE LCISSERPVD LGIALSHAYL TAREIFKREP VIQKRGEDTY CLILNP // ID Q9X1V9_THEMA Unreviewed; 785 AA. AC Q9X1V9; G4FG13; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 110. DE SubName: Full=Beta-mannosidase {ECO:0000313|EMBL:AGL50557.1}; DE EC=3.2.1.25 {ECO:0000313|EMBL:AGL50557.1}; DE SubName: Full=Beta-mannosidase, putative {ECO:0000313|EMBL:AAD36691.1}; GN OrderedLocusNames=TM_1624 {ECO:0000313|EMBL:AAD36691.1}; GN ORFNames=Tmari_1633 {ECO:0000313|EMBL:AGL50557.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36691.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36691.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36691.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50557.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50557.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. CC {ECO:0000256|SAAS:SAAS00568376}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36691.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50557.1; -; Genomic_DNA. DR PIR; H72228; H72228. DR RefSeq; NP_229424.1; NC_000853.1. DR RefSeq; WP_004082096.1; NZ_CP011107.1. DR STRING; 243274.TM1624; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR EnsemblBacteria; AAD36691; AAD36691; TM_1624. DR EnsemblBacteria; AGL50557; AGL50557; Tmari_1633. DR GeneID; 897929; -. DR KEGG; tma:TM1624; -. DR KEGG; tmi:THEMA_06125; -. DR KEGG; tmm:Tmari_1633; -. DR KEGG; tmw:THMA_1665; -. DR PATRIC; 23938222; VBITheMar51294_1643. DR eggNOG; ENOG4105CNT; Bacteria. DR eggNOG; COG3250; LUCA. DR KO; K01192; -. DR OMA; ALATNWF; -. DR OrthoDB; EOG6VHZ94; -. DR BioCyc; TMAR243274:GC6P-1670-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004567; F:beta-mannosidase activity; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 2.60.40.320; -; 1. DR Gene3D; 3.20.20.80; -; 2. DR InterPro; IPR008979; Galactose-bd-like. DR InterPro; IPR013812; Glyco_hydro_2/20_Ig-like. DR InterPro; IPR006102; Glyco_hydro_2_Ig-like. DR InterPro; IPR006104; Glyco_hydro_2_N. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF00703; Glyco_hydro_2; 1. DR Pfam; PF02837; Glyco_hydro_2_N; 1. DR SUPFAM; SSF49303; SSF49303; 1. DR SUPFAM; SSF49785; SSF49785; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000313|EMBL:AGL50557.1}; KW Hydrolase {ECO:0000313|EMBL:AGL50557.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 59 124 Glyco_hydro_2_N. FT {ECO:0000259|Pfam:PF02837}. FT DOMAIN 231 286 Glyco_hydro_2. FT {ECO:0000259|Pfam:PF00703}. SQ SEQUENCE 785 AA; 92373 MW; 7515D43B3E620DF4 CRC64; MKRIDLNGFW SVRDNEGRFS FEGTVPGVVQ ADLVRKGLLP HPYVGMNEDL FKEIEDREWI YEREFEFKED VKEGERVDLV FEGVDTLSDV YLNGVYLGST EDMFIEYRFD VTNVLKEKNH LKVYIKSPIR VPKTLEQNYG VLGGPEDPIR GYIRKAQYSY GWDWGARIVT SGIWKPVYLE VYRARLQDST AYLLELEGKD ALVRVNGFVH GEGNLIVEVY VNGEKIGEFP VLEKNGEKLF DGVFHLKDVK LWYPWNVGKP YLYDFVFVLK DLNGEIYREE KKIGLRRVRI VQEPDEEGKT FIFEINGEKV FAKGANWIPS ENILTWLKEE DYEKLVKMAR SANMNMLRVW GGGIYEREIF YRLCDELGIM VWQDFMYACL EYPDHLPWFR KLANEEARKI VRKLRYHPSI VLWCGNNENN WGFDEWGNMA RKVDGINLGN RLYLFDFPEI CAEEDPSTPY WPSSPYGGEK ANSEKEGDRH VWYVWSGWMN YENYEKDTGR FISEFGFQGA PHPETIEFFS KPEEREIFHP VMLKHNKQVE GQERLIRFIF GNFGKCKDFD SFVYLSQLNQ AEAIKFGVEH WRSRKYKTAG ALFWQFNDSW PVFSWSAVDY FKRPKALYYY ARRFFAEVLP VLKKRDNKIE LLVVSDLRET KEVSLRLAAY EKKGEKVFEK TYRTVLPADG VSLVDRVELP DDLFFFVEAE VDGVKYRNYR VFRKWRDLEL PDPEISLEDM GELIELTAQR PAFGVKILSD EVPEDDFLFL EPGRSITLKK PDGVRGVKSL FDYLR // ID Q9WY42_THEMA Unreviewed; 440 AA. AC Q9WY42; G4FHB3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 110. DE RecName: Full=DNA repair protein radA {ECO:0000256|RuleBase:RU003555}; GN OrderedLocusNames=TM_0199 {ECO:0000313|EMBL:AAD35291.1}; GN ORFNames=Tmari_0197 {ECO:0000313|EMBL:AGL49123.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35291.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35291.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35291.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49123.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49123.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: DNA-dependent ATPase involved in processing of CC recombination intermediates, plays a role in repairing DNA breaks. CC Stimulates the branch migration of RecA-mediated strand transfer CC reactions, allowing the 3' invading strand to extend heteroduplex CC DNA faster. Binds ssDNA in the presence of ADP but not other CC nucleotides, has ATPase activity that is stimulated by ssDNA and CC various branched DNA structures, but inhibited by SSB. Does not CC have RecA's homology-searching function. CC {ECO:0000256|RuleBase:RU003555}. CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily. CC {ECO:0000256|RuleBase:RU003555}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35291.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49123.1; -; Genomic_DNA. DR PIR; A72405; A72405. DR RefSeq; NP_228014.1; NC_000853.1. DR RefSeq; WP_004082860.1; NZ_CP011107.1. DR STRING; 243274.TM0199; -. DR MEROPS; S16.A04; -. DR DNASU; 897069; -. DR EnsemblBacteria; AAD35291; AAD35291; TM_0199. DR EnsemblBacteria; AGL49123; AGL49123; Tmari_0197. DR GeneID; 897069; -. DR KEGG; tma:TM0199; -. DR KEGG; tmi:THEMA_03735; -. DR KEGG; tmm:Tmari_0197; -. DR KEGG; tmw:THMA_0206; -. DR PATRIC; 23935270; VBITheMar51294_0201. DR eggNOG; ENOG4105DNJ; Bacteria. DR eggNOG; COG1066; LUCA. DR KO; K04485; -. DR OMA; FEGERGH; -. DR OrthoDB; EOG6DRPHC; -. DR BioCyc; TMAR243274:GC6P-212-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 2.20.28.10; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR004504; DNA_repair_RadA. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020588; RecA_ATP-bd. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR004039; Rubredoxin-type_fold. DR PRINTS; PR01874; DNAREPAIRADA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR TIGRFAMs; TIGR00416; sms; 1. DR PROSITE; PS50162; RECA_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU003555}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA damage {ECO:0000256|RuleBase:RU003555}; KW DNA repair {ECO:0000256|RuleBase:RU003555}; KW DNA-binding {ECO:0000256|RuleBase:RU003555}; KW Metal-binding {ECO:0000256|RuleBase:RU003555}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU003555}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000256|RuleBase:RU003555}; KW Zinc-finger {ECO:0000256|RuleBase:RU003555}. FT DOMAIN 55 204 RECA_2. {ECO:0000259|PROSITE:PS50162}. SQ SEQUENCE 440 AA; 48262 MW; 6407D771BF1DB574 CRC64; MKKFVCSNCG YVSPKWFGRC PQCGEYDTAE EVQRRKNREG SPSLFLNLED AGEISLERLS TGFSELDRAF RGGIVPGQVI LLSGEPGIGK STIALQIAER FAERGLVVYV SGEESPQQLK LRADRLLLKR KKDILLTLEN DIDEIISSLQ NKRVSFMVVD SIQTVFSSDL GSSPGSISQV KNVTMKTIDF AKRRGVPVLL VGHVTKEGEI AGPKLVEHMV DTVAYFEGDR RTGLRLLKIT KNRFGPSDEV AVFELKENGF VQVENPSFTE GDADLPGNVL TCVFEGTKPF VVQIQALVSK NRTFSPKRVC KGVDVNRVML LIAVISKYLK LPIETHDVYV NVVGGLRVTD PAADLAIALS IVSSYLEVSL HNTAAVGEIG LDGRVRKVYN INRRLNSLKS SGRIIVPPIE EEQKGVFEVR DLKEAVSIIG GEILGTPGAD // ID Q9X053_THEMA Unreviewed; 323 AA. AC Q9X053; G4FF32; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Ribose ABC transport system, periplasmic ribose-binding protein RbsB {ECO:0000313|EMBL:AGL49885.1}; DE SubName: Full=Ribose ABC transporter, periplasmic ribose-binding protein {ECO:0000313|EMBL:AAD36037.1}; GN OrderedLocusNames=TM_0958 {ECO:0000313|EMBL:AAD36037.1}; GN ORFNames=Tmari_0960 {ECO:0000313|EMBL:AGL49885.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36037.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36037.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36037.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49885.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49885.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36037.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49885.1; -; Genomic_DNA. DR PIR; C72311; C72311. DR RefSeq; NP_228766.1; NC_000853.1. DR RefSeq; WP_004080604.1; NZ_CP011107.1. DR PDB; 2FN8; X-ray; 2.15 A; A=30-323. DR PDB; 2FN9; X-ray; 1.40 A; A/B=30-310. DR PDBsum; 2FN8; -. DR PDBsum; 2FN9; -. DR STRING; 243274.TM0958; -. DR TCDB; 3.A.1.2.19; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36037; AAD36037; TM_0958. DR EnsemblBacteria; AGL49885; AGL49885; Tmari_0960. DR GeneID; 898695; -. DR KEGG; tma:TM0958; -. DR KEGG; tmi:THEMA_09555; -. DR KEGG; tmm:Tmari_0960; -. DR KEGG; tmw:THMA_0981; -. DR PATRIC; 23936847; VBITheMar51294_0972. DR eggNOG; ENOG4105E9V; Bacteria. DR eggNOG; COG1879; LUCA. DR KO; K10439; -. DR OMA; MENILQS; -. DR OrthoDB; EOG61P6T8; -. DR BioCyc; TMAR243274:GC6P-988-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015749; P:monosaccharide transport; IBA:GOC. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR025997; SBP_2_dom. DR Pfam; PF13407; Peripla_BP_4; 1. DR SUPFAM; SSF53822; SSF53822; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2FN8, ECO:0000213|PDB:2FN9}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 323 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007217057. FT DOMAIN 34 293 Peripla_BP_4. {ECO:0000259|Pfam:PF13407}. SQ SEQUENCE 323 AA; 35865 MW; 0DC70073B8A8A350 CRC64; MKKSLFVVLV LVGLLLVSFT GLAQEQQKPK GKMAIVISTL NNPWFVVLAE TAKQRAEQLG YEATIFDSQN DTAKESAHFD AIIAAGYDAI IFNPTDADGS IANVKRAKEA GIPVFCVDRG INARGLAVAQ IYSDNYYGGV LMGEYFVKFL KEKYPDAKEI PYAELLGILS AQPTWDRSNG FHSVVDQYPE FKMVAQQSAE FDRDTAYKVT EQILQAHPEI KAIWCGNDAM ALGAMKACEA AGRTDIYIFG FDGAEDVINA IKEGKQIVAT IMQFPKLMAR LAVEWADQYL RGERSFPEIV PVTVELVTRE NIDKYTAYGR KEE // ID Q9WXT8_THEMA Unreviewed; 858 AA. AC Q9WXT8; G4FGZ8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 96. DE SubName: Full=Flagellar hook-associated protein 1 {ECO:0000313|EMBL:AAD35177.1}; DE SubName: Full=Flagellar hook-associated protein FlgK {ECO:0000313|EMBL:AGL49006.1}; GN OrderedLocusNames=TM_0083 {ECO:0000313|EMBL:AAD35177.1}; GN ORFNames=Tmari_0080 {ECO:0000313|EMBL:AGL49006.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35177.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35177.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35177.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49006.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49006.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the flagella basal body rod proteins CC family. {ECO:0000256|SAAS:SAAS00560878}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35177.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49006.1; -; Genomic_DNA. DR PIR; E72419; E72419. DR RefSeq; NP_227899.1; NC_000853.1. DR RefSeq; WP_004082609.1; NZ_CP011107.1. DR STRING; 243274.TM0083; -. DR EnsemblBacteria; AAD35177; AAD35177; TM_0083. DR EnsemblBacteria; AGL49006; AGL49006; Tmari_0080. DR GeneID; 896910; -. DR KEGG; tma:TM0083; -. DR KEGG; tmi:THEMA_04390; -. DR KEGG; tmm:Tmari_0080; -. DR KEGG; tmw:THMA_0079; -. DR PATRIC; 23935006; VBITheMar51294_0081. DR eggNOG; ENOG4105E1Q; Bacteria. DR eggNOG; COG1256; LUCA. DR KO; K02396; -. DR OMA; QYRQVNN; -. DR OrthoDB; EOG6NWBMH; -. DR BioCyc; TMAR243274:GC6P-83-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009424; C:bacterial-type flagellum hook; IEA:InterPro. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR InterPro; IPR001444; Flag_bb_rod_N. DR InterPro; IPR010810; Flagellin_hook_IN_motif. DR InterPro; IPR010930; Flg_bb/hook_C_dom. DR InterPro; IPR002371; FlgK. DR Pfam; PF07196; Flagellin_IN; 1. DR Pfam; PF00460; Flg_bb_rod; 1. DR Pfam; PF06429; Flg_bbr_C; 1. DR PRINTS; PR01005; FLGHOOKAP1. DR TIGRFAMs; TIGR02492; flgK_ends; 1. PE 3: Inferred from homology; KW Cell projection {ECO:0000313|EMBL:AAD35177.1}; KW Cilium {ECO:0000313|EMBL:AAD35177.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35177.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 10 39 Flg_bb_rod. {ECO:0000259|Pfam:PF00460}. FT DOMAIN 805 856 Flg_bbr_C. {ECO:0000259|Pfam:PF06429}. FT COILED 150 177 {ECO:0000256|SAM:Coils}. FT COILED 796 823 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 858 AA; 95453 MW; F4E3A479F0250BAF CRC64; MPDMSMFGIL NTALTGIHAH KLAMNIVGHN IANASTPGYS RQRPVIEANP PIPLTTLTQP SFPLQMGTGA RVKTIVRLRD AFLDVQYRQV NNRYNYWDTV LSNLHFIEQL LAEPGEDGIR SLVDNFWNAF KEVMSDPSST ASKAEVVSRA QQMVSQIKDL YGRLEQLRED IDAEIVQRVS EINQMIKRLA DLNNKIRTSM MLNSPPNDLL DERDRILDEL SNLANINYTE AEDGQITLRI GNQIVLNGST YRELRALERP YGKGYHELFV GNSQLILSDG KLKALIDLRD SSIVKYMRKL DEFVLFITDS LNLVHRDGFE SNGVTTNLNF FKKIEAFSDD PSIFRIKGNR KLEMGPYHTV TGLHSANSQA EIEGRRFNSN DVVLSFDGGS SNVLNISAGT TIGDLVGSWN LLGTSLKVGT HAGGYRLYLE DSTGSLRNRL FLSLGDSLSQ MGFDTETKGY ITIKESDLSG LSSGVYNINV EYILEDGTRQ TETISVDLSS GVNLSNIEAS INSSSHLRAQ IYADPSTGEN MLVIVPDEQL NFDPSAVKVL SDDDFFTESN AFVRNYEVLK YKDTLENIFY GQTGFDPTRP FTITINSTDI EIDPAVDTLE TLVEKINEKN TGVLADLTPH HSLVFRASSL YDFDLRMMEI KGPQGFFEAV GFVDPDGDPT TFDWNTSFTL VSKSDDFTTL SERFKVADIL TFDRAPYDEP LNIVNQFEVS SSLATNPANL AVDVGYALEN SDWNATSIKP SGGANPELLE TIQNLYTRKM LSNGKESFYE FFGGVVSELG VEAETASNLK NNTEILRQEI DNAREEVKGV SLDEEMANMI EYQHAFSAAA KVITAVDQMI QTVINMVG // ID Q9X0U5_THEMA Unreviewed; 328 AA. AC Q9X0U5; G4FEC8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 99. DE SubName: Full=Putative regulator of mannoside utilization, LacI family {ECO:0000313|EMBL:AGL50149.1}; DE SubName: Full=Transcriptional regulator, LacI family {ECO:0000313|EMBL:AAD36293.1}; GN OrderedLocusNames=TM_1218 {ECO:0000313|EMBL:AAD36293.1}; GN ORFNames=Tmari_1225 {ECO:0000313|EMBL:AGL50149.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36293.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36293.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36293.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50149.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50149.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains HTH lacI-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00590899}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36293.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50149.1; -; Genomic_DNA. DR PIR; H72281; H72281. DR RefSeq; NP_229023.1; NC_000853.1. DR RefSeq; WP_004080078.1; NZ_CP011107.1. DR STRING; 243274.TM1218; -. DR EnsemblBacteria; AAD36293; AAD36293; TM_1218. DR EnsemblBacteria; AGL50149; AGL50149; Tmari_1225. DR GeneID; 898266; -. DR KEGG; tma:TM1218; -. DR KEGG; tmi:THEMA_08240; -. DR KEGG; tmm:Tmari_1225; -. DR KEGG; tmw:THMA_1244; -. DR PATRIC; 23937378; VBITheMar51294_1236. DR eggNOG; ENOG4105ETE; Bacteria. DR eggNOG; COG1609; LUCA. DR KO; K02529; -. DR OMA; PAHYSIA; -. DR OrthoDB; EOG6SJJMM; -. DR BioCyc; TMAR243274:GC6P-1248-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR000843; Tscrpt_reg_HTH_LacI. DR Pfam; PF00356; LacI; 1. DR PRINTS; PR00036; HTHLACI. DR SMART; SM00354; HTH_LACI; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF53822; SSF53822; 1. DR PROSITE; PS00356; HTH_LACI_1; 1. DR PROSITE; PS50932; HTH_LACI_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00590989}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00590865}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00590865}. FT DOMAIN 2 56 HTH lacI-type DNA-binding. FT {ECO:0000259|PROSITE:PS50932}. SQ SEQUENCE 328 AA; 36966 MW; B3B82652EE47262D CRC64; MASIKDVAKL AGVSIATVSR VINGYNNVSE ETRKKVIDAI RKLNYHPVYA VKGAVLKRTI GVLVPNFGGF HYNEILTGIE KEAIKRDFTL MISTTLHRTS VELERLEVFF AKRVDGIIVC SSKKDEEQLE RLIKSAIPVV VVDREEPEIR LDNVGIDNYA AGRMCAKYLL EKGHRKVLLL KGRKDIYSFS DRERGFIDYS TRHGIDVKVT PCGYFAEHGY HAVERYLKKH GRDFTAIFAI NDLSAFGALK ALHDLGVLVP DEVSVMGFDD DPISSYTIPP LTTVRQPREE MGRVAFEILY ERLSGKKGVA RRVVLPVEIV ERESVKQL // ID Q9X0R6_THEMA Unreviewed; 643 AA. AC Q9X0R6; G4FEG2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=PleD-related protein {ECO:0000313|EMBL:AAD36259.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL50115.1}; GN OrderedLocusNames=TM_1184 {ECO:0000313|EMBL:AAD36259.1}; GN ORFNames=Tmari_1191 {ECO:0000313|EMBL:AGL50115.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36259.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36259.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36259.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50115.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50115.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains GGDEF domain. CC {ECO:0000256|SAAS:SAAS00496774}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36259.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50115.1; -; Genomic_DNA. DR PIR; F72284; F72284. DR RefSeq; NP_228989.1; NC_000853.1. DR RefSeq; WP_004080164.1; NZ_CP011107.1. DR STRING; 243274.TM1184; -. DR EnsemblBacteria; AAD36259; AAD36259; TM_1184. DR EnsemblBacteria; AGL50115; AGL50115; Tmari_1191. DR GeneID; 898301; -. DR KEGG; tma:TM1184; -. DR KEGG; tmi:THEMA_08415; -. DR KEGG; tmm:Tmari_1191; -. DR KEGG; tmw:THMA_1209; -. DR PATRIC; 23937308; VBITheMar51294_1202. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; COG2199; LUCA. DR eggNOG; COG2202; LUCA. DR OMA; YGISVFP; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1213-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR InterPro; IPR000014; PAS. DR Pfam; PF00990; GGDEF; 1. DR Pfam; PF13426; PAS_9; 2. DR SMART; SM00267; GGDEF; 1. DR SMART; SM00091; PAS; 2. DR SUPFAM; SSF55073; SSF55073; 1. DR SUPFAM; SSF55785; SSF55785; 2. DR TIGRFAMs; TIGR00254; GGDEF; 1. DR TIGRFAMs; TIGR00229; sensory_box; 2. DR PROSITE; PS50887; GGDEF; 1. DR PROSITE; PS50112; PAS; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 5 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 62 84 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 90 113 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 122 182 PAS (PER-ARNT-SIM). FT {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 241 295 PAS (PER-ARNT-SIM). FT {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 513 643 GGDEF. {ECO:0000259|PROSITE:PS50887}. SQ SEQUENCE 643 AA; 74520 MW; 9B8B57A48B47FB5F CRC64; MKKLIWPVLL VGTAFLIIYS FLIGTPLEIH LATRWEIALP RVLFLLGSFL LNTLFSLTGS YVVLFGSVSL FLGALMNLLE FFFVYPPLFY AVKLIFYVAG SLLLLIGIFR VFLKLKRFTL MFRGLFEENN DMVIYYDPSG KIVDVNPAAE RFLGYTRIEL LGKTIEEISK PAEEKVLFQI LNFSQNGIKT LEREFLSKDG RTILCECKLV PVYEGKKIAM IQEIARPIDD IRKIEDQIRK ERKRFLTYFN NIPVLSVILR EDGTVEDVNE AGCKLLGVNR EQLLNKNWFD MFHESFPHET FERSFKEKMV HEGRIDGRVI RWVFIPLEEN RVMVTGLDIT ELKENLTSLE SDKKFYQLLL DLSKSLLSLG WNDFVFKQYL SPLGEVFGSK SVALYEKKNG NFVLTASLNG SFEEILSRIP EDIDCENEML GIPLEYETET FAVLLIGCGK TDERLFEMAR LLKNYLELIY WKLKGEERIL WLAERDSLTG VYNREAFENR LAYLINLSKR YNRKLSFVFI DLDDFKRIND SKGHLVGDRV LKEFVNRLTS LLRKSDVVGR LGGDEFGIVL PETDRTGAEI LMKRIEEHFR EPVLVDGELF SVNFSYGISV FPEDGESVKE LLKVADERMY MNKFSKKRGR ENV // ID Q9WYX2_THEMA Unreviewed; 313 AA. AC Q9WYX2; G4FDW8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=Dipeptide transport system permease protein DppC {ECO:0000313|EMBL:AGL49424.1}; DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35587.1}; GN OrderedLocusNames=TM_0502 {ECO:0000313|EMBL:AAD35587.1}; GN ORFNames=Tmari_0499 {ECO:0000313|EMBL:AGL49424.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35587.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35587.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35587.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49424.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49424.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032, CC ECO:0000256|SAAS:SAAS00537635}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35587.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49424.1; -; Genomic_DNA. DR PIR; E72371; E72371. DR RefSeq; NP_228312.1; NC_000853.1. DR RefSeq; WP_004081440.1; NZ_CP011107.1. DR STRING; 243274.TM0502; -. DR DNASU; 897543; -. DR EnsemblBacteria; AAD35587; AAD35587; TM_0502. DR EnsemblBacteria; AGL49424; AGL49424; Tmari_0499. DR GeneID; 897543; -. DR KEGG; tma:TM0502; -. DR KEGG; tmi:THEMA_02160; -. DR KEGG; tmm:Tmari_0499; -. DR KEGG; tmw:THMA_0515; -. DR PATRIC; 23935909; VBITheMar51294_0509. DR eggNOG; ENOG4105C2T; Bacteria. DR eggNOG; COG1173; LUCA. DR KO; K02034; -. DR OMA; IAGRDIY; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-526-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0016151; F:nickel cation binding; IBA:GO_Central. DR GO; GO:0015099; F:nickel cation transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0035444; P:nickel cation transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR025966; OppC_N. DR Pfam; PF00528; BPD_transp_1; 1. DR Pfam; PF12911; OppC_N; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00496716}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496716, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496724}. FT TRANSMEM 20 39 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 114 138 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 150 168 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 174 190 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 237 258 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 279 299 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 112 300 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 313 AA; 34746 MW; F75DC1D75E8EFCC7 CRC64; MNQEFKRIMK RFFRDPSAII GFSLVLFFVV IAILAPVIAP PIHPLTRAKL PDPYLMPVVS WNQSPQPPTT KEDALAKNPN REPIRCVDYH PFGVIGGRDI LYGIVWGTRT AFKIGLIVTL ARLLIGVFIG SISGYFGGWI DEVLMRITDI FLSIPFLIAA VVLTTVLGTG LDKVMIAMIV FGWMGAARLI RGNILQVREE QFVLAAKAIG VPDFLIILKH VLPNTIFPVL IWASMNMGSL VITAAVLSFL GLGAPQGYAD WGSILSYSRD WMMEIGKHWY ALVYPGTAMV LFVLGWNLLG DALRDAFDPR LKF // ID Q9WZK1_THEMA Unreviewed; 209 AA. AC Q9WZK1; G4FD81; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 98. DE SubName: Full=Serine/threonine protein phosphatase {ECO:0000313|EMBL:AAD35823.1}; GN OrderedLocusNames=TM_0742 {ECO:0000313|EMBL:AAD35823.1}; GN ORFNames=Tmari_0743 {ECO:0000313|EMBL:AGL49668.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35823.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35823.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35823.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49668.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49668.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35823.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49668.1; -; Genomic_DNA. DR PIR; A72340; A72340. DR RefSeq; NP_228551.1; NC_000853.1. DR RefSeq; WP_004080979.1; NZ_CP011107.1. DR STRING; 243274.TM0742; -. DR DNASU; 898409; -. DR EnsemblBacteria; AAD35823; AAD35823; TM_0742. DR EnsemblBacteria; AGL49668; AGL49668; Tmari_0743. DR GeneID; 898409; -. DR KEGG; tma:TM0742; -. DR KEGG; tmi:THEMA_00945; -. DR KEGG; tmm:Tmari_0743; -. DR KEGG; tmw:THMA_0760; -. DR PATRIC; 23936404; VBITheMar51294_0755. DR eggNOG; ENOG410807P; Bacteria. DR eggNOG; COG0639; LUCA. DR KO; K07313; -. DR OMA; CHAGIRP; -. DR OrthoDB; EOG6VHZ8B; -. DR BioCyc; TMAR243274:GC6P-768-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR SUPFAM; SSF56300; SSF56300; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 175 Metallophos. {ECO:0000259|Pfam:PF00149}. SQ SEQUENCE 209 AA; 24236 MW; C7C246F5682B4960 CRC64; MTYAVGDIHG CFYALKSLLE KLPLSEEDEL IFMGDYVDRG PNSREVIEFL IELSKHHRCI FLRGNHEEML LNCVKNGSDC DLWFFNGARS TVESFGGVEE IKKFLPFFEN TVYHYEKENY VFVHGGVRPG VSLEDQDPFD LVWIRDEFIY SENPLPGKIV VFGHTPFEEP FVSRDKIGID TGCVYGGRLT ALRVEDRKFF QVECANRRW // ID Q9WY90_THEMA Unreviewed; 191 AA. AC Q9WY90; G4FHG2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 99. DE RecName: Full=Electron transport complex subunit A {ECO:0000256|HAMAP-Rule:MF_00459}; GN OrderedLocusNames=TM_0248 {ECO:0000313|EMBL:AAD35339.1}; GN ORFNames=Tmari_0246 {ECO:0000313|EMBL:AGL49172.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35339.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35339.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35339.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49172.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49172.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000256|HAMAP-Rule:MF_00459}. CC -!- SUBUNIT: Composed of six subunits. {ECO:0000256|HAMAP- CC Rule:MF_00459}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00459}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00459}. CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000256|HAMAP- CC Rule:MF_00459, ECO:0000256|SAAS:SAAS00573673}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35339.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49172.1; -; Genomic_DNA. DR PIR; A72399; A72399. DR RefSeq; NP_228062.1; NC_000853.1. DR RefSeq; WP_004082952.1; NZ_CP011107.1. DR STRING; 243274.TM0248; -. DR EnsemblBacteria; AAD35339; AAD35339; TM_0248. DR EnsemblBacteria; AGL49172; AGL49172; Tmari_0246. DR GeneID; 897155; -. DR KEGG; tma:TM0248; -. DR KEGG; tmi:THEMA_03485; -. DR KEGG; tmm:Tmari_0246; -. DR KEGG; tmw:THMA_0255; -. DR PATRIC; 23935371; VBITheMar51294_0251. DR eggNOG; ENOG4105DGN; Bacteria. DR eggNOG; COG4657; LUCA. DR KO; K03617; -. DR OMA; FTEMVIN; -. DR OrthoDB; EOG6GBMG7; -. DR BioCyc; TMAR243274:GC6P-261-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR HAMAP; MF_00459; RsxA_RnfA; 1. DR InterPro; IPR011293; Elect_transpt_RnfA/RsxA. DR InterPro; IPR003667; Rnf-Nqr. DR Pfam; PF02508; Rnf-Nqr; 1. DR PIRSF; PIRSF006102; NQR_DE; 1. DR TIGRFAMs; TIGR01943; rnfA; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00459}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00459}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00459}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00459, KW ECO:0000256|SAAS:SAAS00465084}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00459, KW ECO:0000256|SAAS:SAAS00465084}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00459, KW ECO:0000256|SAAS:SAAS00465084}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00459}. FT TRANSMEM 4 24 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00459}. FT TRANSMEM 38 58 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00459}. FT TRANSMEM 69 89 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00459}. FT TRANSMEM 100 120 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00459}. FT TRANSMEM 132 152 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00459}. FT TRANSMEM 169 189 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00459}. SQ SEQUENCE 191 AA; 20865 MW; 063DD1A948D8C8FD CRC64; MKVFLLFFSA IFVNNFVLAR FLGICPFLGV SKRLETATGM GIAVTFVMTV SAAISWFLDK LLISTGLEFL RTIVFILVIA SFVQFVELFL KKTSPDLYEA LGIFLPLITT NCAILGMVLL NSLMKLNFVE AVFHALGSGL GFALALVIFA GIREKMDLYD LPEPFKGTAI ALITAGLLSL AFMGFQGMVK L // ID Q9X2F0_THEMA Unreviewed; 105 AA. AC Q9X2F0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36893.1}; GN OrderedLocusNames=TM_1830 {ECO:0000313|EMBL:AAD36893.1}; GN ORFNames=Tmari_1839 {ECO:0000313|EMBL:AGL50763.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36893.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36893.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36893.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50763.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50763.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains GGDEF domain. CC {ECO:0000256|SAAS:SAAS00496774}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36893.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50763.1; -; Genomic_DNA. DR PIR; B72205; B72205. DR RefSeq; NP_229627.1; NC_000853.1. DR RefSeq; WP_010865413.1; NZ_CP011107.1. DR STRING; 243274.TM1830; -. DR EnsemblBacteria; AAD36893; AAD36893; TM_1830. DR EnsemblBacteria; AGL50763; AGL50763; Tmari_1839. DR GeneID; 897692; -. DR KEGG; tma:TM1830; -. DR KEGG; tmm:Tmari_1839; -. DR KEGG; tmw:THMA_1874; -. DR PATRIC; 23938647; VBITheMar51294_1850. DR eggNOG; ENOG41073J1; Bacteria. DR eggNOG; ENOG41102Q8; LUCA. DR OMA; DTANTFT; -. DR OrthoDB; EOG61044X; -. DR BioCyc; TMAR243274:GC6P-1881-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR Pfam; PF00990; GGDEF; 1. DR SMART; SM00267; GGDEF; 1. DR SUPFAM; SSF55073; SSF55073; 1. DR TIGRFAMs; TIGR00254; GGDEF; 1. DR PROSITE; PS50887; GGDEF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 105 GGDEF. {ECO:0000259|PROSITE:PS50887}. SQ SEQUENCE 105 AA; 11681 MW; 94A9AA9CA6749A13 CRC64; MEGGLRATKN PIPFRGLGGG QVIARWGGEE FLILCPETKL NEAVSLAERI RTKIEKEVFE NGLNVTVSIG VCEMKDHETI DDLLKEADDN LYLAKQRGKN RVIGR // ID Q9X1M7_THEMA Unreviewed; 286 AA. AC Q9X1M7; G4FFS9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Flagellar basal-body P-ring formation protein FlgA {ECO:0000313|EMBL:AGL50473.1}; DE SubName: Full=Flagellar protein FlgA, putative {ECO:0000313|EMBL:AAD36608.1}; GN OrderedLocusNames=TM_1541 {ECO:0000313|EMBL:AAD36608.1}; GN ORFNames=Tmari_1549 {ECO:0000313|EMBL:AGL50473.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36608.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36608.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36608.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:3FRN} RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 19-286. RA Patskovsky Y., Bonanno J.B., Romero R., Gilmore M., Hu S., Bain K., RA Koss J., Sauder J.M., Burley S.K., Almo S.C.; RT "CRYSTAL STRUCTURE OF flagellar protein FlgA FROM Thermotoga RT maritima."; RL Submitted (JAN-2009) to the PDB data bank. RN [3] {ECO:0000313|EMBL:AGL50473.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50473.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36608.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50473.1; -; Genomic_DNA. DR PIR; A72243; A72243. DR RefSeq; NP_229341.1; NC_000853.1. DR RefSeq; WP_004081926.1; NZ_CP011107.1. DR PDB; 3FRN; X-ray; 2.05 A; A=19-286. DR PDBsum; 3FRN; -. DR STRING; 243274.TM1541; -. DR EnsemblBacteria; AAD36608; AAD36608; TM_1541. DR EnsemblBacteria; AGL50473; AGL50473; Tmari_1549. DR GeneID; 897628; -. DR KEGG; tma:TM1541; -. DR KEGG; tmi:THEMA_06580; -. DR KEGG; tmm:Tmari_1549; -. DR KEGG; tmw:THMA_1575; -. DR PATRIC; 23938042; VBITheMar51294_1559. DR eggNOG; ENOG4106BEP; Bacteria. DR eggNOG; COG1261; LUCA. DR KO; K02386; -. DR OMA; AMNVESR; -. DR OrthoDB; EOG6KHFZD; -. DR BioCyc; TMAR243274:GC6P-1581-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR Gene3D; 3.90.1210.10; -; 1. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR017585; Flag_basal_body_FlgA_C. DR InterPro; IPR013974; SAF. DR Pfam; PF13144; ChapFlgA; 1. DR SMART; SM00858; SAF; 1. DR SUPFAM; SSF51269; SSF51269; 1. DR TIGRFAMs; TIGR03170; flgA_cterm; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3FRN}; KW Cell projection {ECO:0000313|EMBL:AAD36608.1}; KW Cilium {ECO:0000313|EMBL:AAD36608.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD36608.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 158 220 SAF. {ECO:0000259|SMART:SM00858}. SQ SEQUENCE 286 AA; 32617 MW; 4ECA2DC8AD9F8564 CRC64; MKVLLILIVL ISSFLFSETL TLKETLLASP GVLFLDDITI EKVESEKNLM ILLPGLEYLV TRDLLRTKFP EYDFTGPENV RITVEGYSSL KNAVFEEIGK KAEAKDFEAF VVKTFGTLPE KFEPQTIRVT KISKNLFSVF LRFPDTYVTL NMLLRKERNV VVLKRNINVG DVIKEEDVRL EKRNVFEIYG EPFFDVSEVV GKISRRYLKE GTVLTADMVK DPPDVVKGQV VPAYVDMGSI KVTTFVEVLE NGYLGETVRA MNVESRKYVF GRVERGPVLR ILEVVE // ID Q9X0Q1_THEMA Unreviewed; 237 AA. AC Q9X0Q1; G4FEH7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 111. DE SubName: Full=3-oxoacyl-(Acyl carrier protein) reductase {ECO:0000313|EMBL:AAD36244.1}; DE SubName: Full=3-oxoacyl-[acyl-carrier protein] reductase {ECO:0000313|EMBL:AGL50100.1}; DE EC=1.1.1.100 {ECO:0000313|EMBL:AGL50100.1}; GN OrderedLocusNames=TM_1169 {ECO:0000313|EMBL:AAD36244.1}; GN ORFNames=Tmari_1176 {ECO:0000313|EMBL:AGL50100.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36244.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36244.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36244.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50100.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50100.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36244.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50100.1; -; Genomic_DNA. DR PIR; D72285; D72285. DR RefSeq; NP_228974.1; NC_000853.1. DR RefSeq; WP_004080200.1; NZ_CP011107.1. DR PDB; 1O5I; X-ray; 2.50 A; A/B/C/D=1-237. DR PDBsum; 1O5I; -. DR STRING; 243274.TM1169; -. DR EnsemblBacteria; AAD36244; AAD36244; TM_1169. DR EnsemblBacteria; AGL50100; AGL50100; Tmari_1176. DR GeneID; 898317; -. DR KEGG; tma:TM1169; -. DR KEGG; tmi:THEMA_08490; -. DR KEGG; tmm:Tmari_1176; -. DR KEGG; tmw:THMA_1194; -. DR PATRIC; 23937278; VBITheMar51294_1187. DR eggNOG; ENOG4105RGH; Bacteria. DR eggNOG; COG1028; LUCA. DR KO; K00059; -. DR OMA; VESQIPM; -. DR OrthoDB; EOG6N3CR8; -. DR BioCyc; TMAR243274:GC6P-1198-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR002347; SDR_fam. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O5I}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW NAD {ECO:0000213|PDB:1O5I}; Nucleotide-binding {ECO:0000213|PDB:1O5I}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50100.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT NP_BIND 16 19 NAD. {ECO:0000213|PDB:1O5I}. FT BINDING 56 56 NAD; via amide nitrogen. FT {ECO:0000213|PDB:1O5I}. FT BINDING 77 77 NAD; via carbonyl oxygen. FT {ECO:0000213|PDB:1O5I}. FT BINDING 145 145 NAD. {ECO:0000213|PDB:1O5I}. FT DISULFID 37 54 {ECO:0000213|PDB:1O5I}. SQ SEQUENCE 237 AA; 26192 MW; B04776C05364CED7 CRC64; MELGIRDKGV LVLAASRGIG RAVADVLSQE GAEVTICARN EELLKRSGHR YVVCDLRKDL DLLFEKVKEV DILVLNAGGP KAGFFDELTN EDFKEAIDSL FLNMIKIVRN YLPAMKEKGW GRIVAITSFS VISPIENLYT SNSARMALTG FLKTLSFEVA PYGITVNCVA PGWTETERVK ELLSEEKKKQ VESQIPMRRM AKPEEIASVV AFLCSEKASY LTGQTIVVDG GLSKFPL // ID Q9X0N7_THEMA Unreviewed; 301 AA. AC Q9X0N7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=Dipeptide transport system permease protein DppC {ECO:0000313|EMBL:AGL50084.1}; DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD36229.1}; GN OrderedLocusNames=TM_1153 {ECO:0000313|EMBL:AAD36229.1}; GN ORFNames=Tmari_1160 {ECO:0000313|EMBL:AGL50084.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36229.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36229.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36229.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50084.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50084.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032, CC ECO:0000256|SAAS:SAAS00537635}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36229.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50084.1; -; Genomic_DNA. DR PIR; E72289; E72289. DR RefSeq; NP_228959.1; NC_000853.1. DR RefSeq; WP_010865273.1; NZ_CP011107.1. DR STRING; 243274.TM1153; -. DR DNASU; 898333; -. DR EnsemblBacteria; AAD36229; AAD36229; TM_1153. DR EnsemblBacteria; AGL50084; AGL50084; Tmari_1160. DR GeneID; 898333; -. DR KEGG; tma:TM1153; -. DR KEGG; tmi:THEMA_08575; -. DR KEGG; tmm:Tmari_1160; -. DR KEGG; tmw:THMA_1177; -. DR PATRIC; 23937243; VBITheMar51294_1170. DR eggNOG; ENOG4105C2T; Bacteria. DR eggNOG; COG1173; LUCA. DR KO; K02034; -. DR OMA; WGFDLSN; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1182-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR025966; OppC_N. DR Pfam; PF00528; BPD_transp_1; 1. DR Pfam; PF12911; OppC_N; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00496716}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496716, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496724}. FT TRANSMEM 34 57 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 97 123 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 143 170 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 263 284 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 95 285 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 301 AA; 33094 MW; D3375287DB588BD9 CRC64; MWYYYEKREA RSKVVVSERI FRPVFKLFRR RTGVLAFVGM IILLFYIFLA IFAPVLAPYD PTVRVGRSLQ PPSEKHLFGT DNLGRDIFSR VIYGSRIALM VAFLAVVIAS AIGIPLGLIS GYVGGIFDRV LTLVMDAVYS FPGLILAIAV AAVLGPGMMN IAVSIAVVYA PTYFRVVRNQ VTSVKNELYV EAARALGAKD WEILVKYVLP NVFPSIVVVL SMNLADAIMT EAGLSFLGLG IAPPTPDWGF DLSNGQRFIL SRAWWGVLFP GLAIITSVLG FSMFSEGLSE ILNPNIGERS K // ID Q9WZ88_THEMA Unreviewed; 397 AA. AC Q9WZ88; G4FDK3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=Putative teichuronic acid biosynthesis glycosyl transferase TuaC {ECO:0000313|EMBL:AGL49544.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35704.1}; GN OrderedLocusNames=TM_0619 {ECO:0000313|EMBL:AAD35704.1}; GN ORFNames=Tmari_0619 {ECO:0000313|EMBL:AGL49544.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35704.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35704.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35704.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49544.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49544.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35704.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49544.1; -; Genomic_DNA. DR PIR; C72354; C72354. DR RefSeq; NP_228429.1; NC_000853.1. DR RefSeq; WP_004081194.1; NZ_CP011107.1. DR STRING; 243274.TM0619; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAD35704; AAD35704; TM_0619. DR EnsemblBacteria; AGL49544; AGL49544; Tmari_0619. DR GeneID; 897705; -. DR KEGG; tma:TM0619; -. DR KEGG; tmi:THEMA_01570; -. DR KEGG; tmm:Tmari_0619; -. DR KEGG; tmw:THMA_0635; -. DR PATRIC; 23936149; VBITheMar51294_0628. DR eggNOG; ENOG4107W7V; Bacteria. DR eggNOG; COG0438; LUCA. DR OMA; RFREACL; -. DR OrthoDB; EOG6038VM; -. DR BioCyc; TMAR243274:GC6P-644-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49544.1}. SQ SEQUENCE 397 AA; 45202 MW; E1702DC0FD8E3B4C CRC64; MKVLIITNLF PLNNNSNSGI FVVQRLRHYK SFNVNLDTIS LGHHNSKIAS LLEKLLRGHS NKKTLEEVEN VKFYPVSIEI NLLRLIKYGL LRNYFTVLCK EYKKMIEEAF NLNEYDLIHA HGMYSVPAGL TAKILAEKYR KPFIVTLHGS DVNLFMPHRK EIYVSILESA SATIFVSKAL LEKAKSLGFS GKNAVVIPNG YDETIFKPMD KEAVRKELGI HREGYKYVGF VGNLIPIKRA DKLGEIFHLI AKEIPETFFI IVGDGPLRKK IEKETKGLNI IFTGRLPQKD VAKYMNAMDV MVLPSRNEGW PCVILEAQAC GTCVIGSSNR GIPEAIGFPE YVVEEGDQFE ERFARRVVEV LNEGYDVNRI LERAKGFTWR NIVEKEIDVH KRVVLKS // ID Q9X009_THEMA Unreviewed; 378 AA. AC Q9X009; G4FCR9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 115. DE SubName: Full=Flagellar biosynthesis protein FlhF {ECO:0000313|EMBL:AAD35988.1}; GN OrderedLocusNames=TM_0907 {ECO:0000313|EMBL:AAD35988.1}; GN ORFNames=Tmari_0909 {ECO:0000313|EMBL:AGL49834.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35988.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35988.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35988.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49834.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49834.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35988.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49834.1; -; Genomic_DNA. DR PIR; B72319; B72319. DR RefSeq; NP_228715.1; NC_000853.1. DR RefSeq; WP_004080660.1; NZ_CP011107.1. DR STRING; 243274.TM0907; -. DR EnsemblBacteria; AAD35988; AAD35988; TM_0907. DR EnsemblBacteria; AGL49834; AGL49834; Tmari_0909. DR GeneID; 898581; -. DR KEGG; tma:TM0907; -. DR KEGG; tmi:THEMA_00100; -. DR KEGG; tmm:Tmari_0909; -. DR KEGG; tmw:THMA_0929; -. DR PATRIC; 23936745; VBITheMar51294_0921. DR eggNOG; ENOG4105FZW; Bacteria. DR eggNOG; COG1419; LUCA. DR KO; K02404; -. DR OMA; LITADIF; -. DR OrthoDB; EOG618QQ6; -. DR BioCyc; TMAR243274:GC6P-937-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:InterPro. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR020006; FlhF. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000897; SRP54_GTPase_dom. DR PANTHER; PTHR11564:SF3; PTHR11564:SF3; 1. DR Pfam; PF00448; SRP54; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03499; FlhF; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AAD35988.1}; KW Cilium {ECO:0000313|EMBL:AAD35988.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35988.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 171 317 AAA. {ECO:0000259|SMART:SM00382}. FT DOMAIN 172 363 SRP54. {ECO:0000259|SMART:SM00962}. SQ SEQUENCE 378 AA; 42958 MW; 989B318A35345F5D CRC64; MKIKKYVAES IREAMIMIRR ELGENAVILS SRRIKKGGFF GIGGKTYFEV TAAVEEERKK EENTSYRLQE ILVKNRQSSN DNIKGEFDEI KRTINEIKQM LVTEKRQTLP EGLSKILYGM EKQEILPEIR YKLIDFLKMK FGDLDPNSNE TFKILSEQFV NLVKTNAPDF KNAKVLFVGT TGVGKTTSLA KLAARFKIDE KKRVAILTLD TYRIAAAEQL KIYADIMDIP MKIAYTPKEA EYEMMALKDY DIVLVDTAGR SHQNDLQMSE LRALSEAVKP NITFLVLSMN YKLDDMKRIV ERFSAVKPTH IILTKMDETS VYGTFVNISE ITGLPIAFVT NGQRVPDDIF EANPVELARI VAGEVLNHAR SSGTSEKE // ID Q9X222_THEMA Unreviewed; 240 AA. AC Q9X222; G4FG83; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 85. DE SubName: Full=Leader peptidase (Prepilin peptidase) {ECO:0000313|EMBL:AGL50628.1}; DE EC=3.4.23.43 {ECO:0000313|EMBL:AGL50628.1}; DE SubName: Full=Type IV prepilin peptidase {ECO:0000313|EMBL:AAD36763.1}; GN OrderedLocusNames=TM_1696 {ECO:0000313|EMBL:AAD36763.1}; GN ORFNames=Tmari_1704 {ECO:0000313|EMBL:AGL50628.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36763.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36763.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36763.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50628.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50628.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36763.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50628.1; -; Genomic_DNA. DR PIR; B72220; B72220. DR RefSeq; NP_229496.1; NC_000853.1. DR RefSeq; WP_004082212.1; NZ_CP011107.1. DR STRING; 243274.TM1696; -. DR DNASU; 897287; -. DR EnsemblBacteria; AAD36763; AAD36763; TM_1696. DR EnsemblBacteria; AGL50628; AGL50628; Tmari_1704. DR GeneID; 897287; -. DR KEGG; tma:TM1696; -. DR KEGG; tmi:THEMA_05760; -. DR KEGG; tmm:Tmari_1704; -. DR KEGG; tmw:THMA_1738; -. DR PATRIC; 23938366; VBITheMar51294_1713. DR eggNOG; ENOG4105EHH; Bacteria. DR eggNOG; COG1989; LUCA. DR KO; K02654; -. DR OMA; ITDILYM; -. DR OrthoDB; EOG6F55M8; -. DR BioCyc; TMAR243274:GC6P-1744-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR InterPro; IPR010627; Pept_A24A_N. DR InterPro; IPR000045; Prepilin_IV_endopep_pep. DR Pfam; PF06750; DiS_P_DiS; 1. DR Pfam; PF01478; Peptidase_A24; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50628.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 22 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 97 115 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 121 139 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 146 164 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 176 205 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 217 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 9 88 DiS_P_DiS. {ECO:0000259|Pfam:PF06750}. FT DOMAIN 104 204 Peptidase_A24. FT {ECO:0000259|Pfam:PF01478}. SQ SEQUENCE 240 AA; 27002 MW; A83BD08E953B4A21 CRC64; MWYLLTFAIG TIVGSFLNVV IYRSTKEDLK LWDPPHSFCP NCKRKIEWYD NIPVISYILL RGKCRHCGWR IPIRYPIVEI STGTLFLMNR VLIKDPLLFV SSCVIASALI AISLIDLETY LIPDYLNFTV LIFSFVVALR TSFLEHLISF LIVTIMFLIL KAMYRDGLGA GDVILAMGIG FLLSPVPSIF AILIASISGI LYALIKGKGK MDIKTRIPFG PFLALGGYTL FLISYGMGWL // ID Q9WZ41_THEMA Unreviewed; 459 AA. AC Q9WZ41; G4FDP9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 121. DE SubName: Full=Heat shock serine protease, periplasmic {ECO:0000313|EMBL:AAD35656.1}; DE SubName: Full=HtrA protease/chaperone protein {ECO:0000313|EMBL:AGL49494.1}; GN OrderedLocusNames=TM_0571 {ECO:0000313|EMBL:AAD35656.1}; GN ORFNames=Tmari_0569 {ECO:0000313|EMBL:AGL49494.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35656.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35656.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35656.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49494.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49494.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35656.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49494.1; -; Genomic_DNA. DR PIR; F72359; F72359. DR RefSeq; NP_228381.1; NC_000853.1. DR RefSeq; WP_004081291.1; NZ_CP011107.1. DR PDB; 1L1J; X-ray; 2.80 A; A/B=24-262. DR PDBsum; 1L1J; -. DR STRING; 243274.TM0571; -. DR MEROPS; S01.491; -. DR EnsemblBacteria; AAD35656; AAD35656; TM_0571. DR EnsemblBacteria; AGL49494; AGL49494; Tmari_0569. DR GeneID; 897635; -. DR KEGG; tma:TM0571; -. DR KEGG; tmi:THEMA_01815; -. DR KEGG; tmm:Tmari_0569; -. DR KEGG; tmw:THMA_0585; -. DR PATRIC; 23936051; VBITheMar51294_0580. DR eggNOG; ENOG4105C0H; Bacteria. DR eggNOG; COG0265; LUCA. DR OMA; ITIKRAR; -. DR OrthoDB; EOG61ZTDN; -. DR BioCyc; TMAR243274:GC6P-595-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 2.30.42.10; -; 2. DR InterPro; IPR001478; PDZ. DR InterPro; IPR011782; Pept_S1C_Do. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001940; Peptidase_S1C. DR Pfam; PF13180; PDZ_2; 1. DR PRINTS; PR00834; PROTEASES2C. DR SMART; SM00228; PDZ; 2. DR SUPFAM; SSF50156; SSF50156; 2. DR SUPFAM; SSF50494; SSF50494; 1. DR TIGRFAMs; TIGR02037; degP_htrA_DO; 1. DR PROSITE; PS50106; PDZ; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1L1J}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD35656.1}; KW Protease {ECO:0000313|EMBL:AAD35656.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}; KW Stress response {ECO:0000313|EMBL:AAD35656.1}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 459 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007217056. FT DOMAIN 264 323 PDZ (DHR). {ECO:0000259|PROSITE:PS50106}. SQ SEQUENCE 459 AA; 49924 MW; B78FF003A8189F75 CRC64; MKKFFLTIAV ALILTSVFPY VNPDYESPIV NVVEACAPAV VKIDVVKTVK TSFFDPYFEQ FFKKWFGELP PGFERQVASL GSGFIFDPEG YILTNYHVVG GADNITVTML DGSKYDAEYI GGDEELDIAV IKIKASDKKF PYLEFGDSDK VKIGEWAIAI GNPLGFQHTV TVGVVSATNR RIPKPDGSGY YVGLIQTDAA INPGNSGGPL LNIHGEVIGI NTAIVNPQEA VNLGFAIPIN TVKKFLDTIL TQKKVEKAYL GVTVMTLTEE TAKALGLEST SGALITSVQK GSPAEKAGLK EGDVILKVDD QDVRSHEELV SIIHTYKPGD TAVLTIERKG KIMKVQVTFG SSSEEEKTTT GEEKIDALGI TVSNITPADR ETYSIPEEIN GVIVKESTGK FGLQKGDVIT TVYVNGKRYD INSVGDLKKV TSIVKNGDYI ALYIYRNGAK VFVSFIYQR // ID Q9X115_THEMA Unreviewed; 95 AA. AC Q9X115; G4FE60; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 99. DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:AAD36363.1}; GN OrderedLocusNames=TM_1289 {ECO:0000313|EMBL:AAD36363.1}; GN ORFNames=Tmari_1297 {ECO:0000313|EMBL:AGL50221.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36363.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36363.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36363.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50221.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50221.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36363.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50221.1; -; Genomic_DNA. DR PIR; H72271; H72271. DR RefSeq; NP_229093.1; NC_000853.1. DR RefSeq; WP_004079944.1; NZ_CP011107.1. DR STRING; 243274.TM1289; -. DR DNASU; 898194; -. DR EnsemblBacteria; AAD36363; AAD36363; TM_1289. DR EnsemblBacteria; AGL50221; AGL50221; Tmari_1297. DR GeneID; 898194; -. DR KEGG; tma:TM1289; -. DR KEGG; tmi:THEMA_07890; -. DR KEGG; tmm:Tmari_1297; -. DR KEGG; tmw:THMA_1315; -. DR PATRIC; 23937518; VBITheMar51294_1305. DR eggNOG; ENOG410642X; Bacteria. DR eggNOG; COG1145; LUCA. DR OMA; INNEICT; -. DR OrthoDB; EOG6SNF03; -. DR BioCyc; TMAR243274:GC6P-1320-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF13187; Fer4_9; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 28 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 29 58 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 95 AA; 10304 MW; AFEDB05FF25A34E7 CRC64; MPWVNSKCVG CGNCVKVCPV EGAIRIENGK AVIDNYKCIR CGKCFDACPV GAIRPNYENP ALRGMGRGFG RGLGRGFGRG MGRGYGRGRG RWDEF // ID Q9WZA6_THEMA Unreviewed; 992 AA. AC Q9WZA6; G4FDI5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 85. DE SubName: Full=Capsule polysaccharide export protein {ECO:0000313|EMBL:AGL49564.1}; DE SubName: Full=Polysaccharide export protein, putative {ECO:0000313|EMBL:AAD35722.1}; GN OrderedLocusNames=TM_0638 {ECO:0000313|EMBL:AAD35722.1}; GN ORFNames=Tmari_0639 {ECO:0000313|EMBL:AGL49564.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35722.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35722.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35722.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49564.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49564.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35722.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49564.1; -; Genomic_DNA. DR PIR; E72350; E72350. DR RefSeq; NP_228447.1; NC_000853.1. DR RefSeq; WP_004081159.1; NZ_CP011107.1. DR STRING; 243274.TM0638; -. DR EnsemblBacteria; AAD35722; AAD35722; TM_0638. DR EnsemblBacteria; AGL49564; AGL49564; Tmari_0639. DR GeneID; 897736; -. DR KEGG; tma:TM0638; -. DR KEGG; tmi:THEMA_01470; -. DR KEGG; tmm:Tmari_0639; -. DR KEGG; tmw:THMA_0654; -. DR PATRIC; 23936189; VBITheMar51294_0648. DR eggNOG; ENOG41082Z1; Bacteria. DR eggNOG; COG1596; LUCA. DR KO; K01991; -. DR OMA; TENFAYV; -. DR OrthoDB; EOG6FZ4B4; -. DR BioCyc; TMAR243274:GC6P-663-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0015159; F:polysaccharide transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003715; Poly_export. DR InterPro; IPR019554; Soluble_ligand-bd. DR Pfam; PF02563; Poly_export; 1. DR Pfam; PF10531; SLBB; 6. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 179 225 SLBB. {ECO:0000259|Pfam:PF10531}. FT DOMAIN 256 293 SLBB. {ECO:0000259|Pfam:PF10531}. FT DOMAIN 336 387 SLBB. {ECO:0000259|Pfam:PF10531}. FT DOMAIN 414 457 SLBB. {ECO:0000259|Pfam:PF10531}. FT DOMAIN 804 848 SLBB. {ECO:0000259|Pfam:PF10531}. FT DOMAIN 882 933 SLBB. {ECO:0000259|Pfam:PF10531}. SQ SEQUENCE 992 AA; 109624 MW; 19291DDF29721BF3 CRC64; MKRALIFLFL LIAVFSLSYT IRKGDVLRIE VVGYPDLTRS CAVDIEGAIT FPYVGRVKVE GLSVDQVTDL LKERLSRSFS EPEVIVSLQQ IAPRNVYVSG VVNRVVNMGI EDLSVSELLS LLSVDLSSVD LSKVKVLRDG KVFELDLSSL LWGEAPEKDV MLQENDQVIL PEKSYTEFVK IVGAVSKPGI YPYRREMTLL DAVAAAGGTT QESSGKIIVL SKDETVEVSE KDIYQKNLLL KPGDTVHVQK IDERFAYVVG AVARPGMYTF SREESLTLKN LIAKAGGVSV DKRFIEKALI TRGGETLEYD PDVLDENVEI EVGDVVEIKK FEKTEVYVSG YVSRPGVYEI SPKENVTLEK LLSMAGGIKG TLEEVDSIVV TRDGSVITLS PNNLDFSVKP GDVVNVKEFV PKKAYVLGYV RNPGLYTFGK NEAFTLRNLI AKAGGFVDEG QVVSVKVAGK EYSPDEIVKE DILLEDGVFV YVERYTDRFV YMVGDNVSRN GKMSFEKEEP FTLSTALKKY GIEDFSLIKS LSLLRNGREM TFDPEKILTE DVPLEKGDTI LVRTVQTKRV YFTGDVYGYV DFAKDEDITL EKALARFGKV QRKYIAGLKV IMDGRVQKFD ELVDVPLEDG AVVELNLKES IRVYVDGFVR APQMVVFEPD ETPVLDRAIV KAGGYREDTL FEAGNITVLR DGHEITVPKE QTSSFELEDG DLVFVKYREK THVYVFGEGI TNTLVTFEDE ETPTLRSVLG KVGGVKSTGS ERIVVVKPDG EKEEVDYEEV IKTGGPVLES GSVVFVPLET ENFAYVVGEV ARPGAYELKG DVTLLKLIAQ AGGLSNWALR TKVILRRGEK EFTYDFTSIE EVQNVKVEPG DVVYVPPVET NYVYVLGNVK NPGIVKVDRY STVFDVVMRA GGFTEKAAAS RIFLFRGGPQ GEVTVCDLSG VLSGKGGGVN LNVSPGDVVF VPDNPLIQVT EALSIVNTIF STIRNVKDVM GW // ID Q9WZA1_THEMA Unreviewed; 136 AA. AC Q9WZA1; G4FDJ0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Flagellar protein FlgJ [peptidoglycan hydrolase] {ECO:0000313|EMBL:AGL49559.1}; DE EC=3.2.1.- {ECO:0000313|EMBL:AGL49559.1}; DE SubName: Full=Flagellar-related protein {ECO:0000313|EMBL:AAD35717.1}; GN OrderedLocusNames=TM_0633 {ECO:0000313|EMBL:AAD35717.1}; GN ORFNames=Tmari_0634 {ECO:0000313|EMBL:AGL49559.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35717.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35717.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35717.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49559.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49559.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35717.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49559.1; -; Genomic_DNA. DR PIR; F72353; F72353. DR RefSeq; NP_228442.1; NC_000853.1. DR RefSeq; WP_004081166.1; NZ_CP011107.1. DR PDB; 4QDN; X-ray; 1.70 A; A=1-136. DR PDBsum; 4QDN; -. DR STRING; 243274.TM0633; -. DR CAZy; GH73; Glycoside Hydrolase Family 73. DR EnsemblBacteria; AAD35717; AAD35717; TM_0633. DR EnsemblBacteria; AGL49559; AGL49559; Tmari_0634. DR GeneID; 897729; -. DR KEGG; tma:TM0633; -. DR KEGG; tmi:THEMA_01495; -. DR KEGG; tmm:Tmari_0634; -. DR KEGG; tmw:THMA_0649; -. DR PATRIC; 23936179; VBITheMar51294_0643. DR eggNOG; ENOG4107XZS; Bacteria. DR eggNOG; COG1705; LUCA. DR KO; K02395; -. DR OMA; SPENSMI; -. DR OrthoDB; EOG6KQ6M6; -. DR BioCyc; TMAR243274:GC6P-658-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0004040; F:amidase activity; IEA:InterPro. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom. DR Pfam; PF01832; Glucosaminidase; 1. DR SMART; SM00047; LYZ2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4QDN}; KW Cell projection {ECO:0000313|EMBL:AAD35717.1}; KW Cilium {ECO:0000313|EMBL:AAD35717.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35717.1}; KW Glycosidase {ECO:0000313|EMBL:AGL49559.1}; KW Hydrolase {ECO:0000313|EMBL:AGL49559.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 136 AA; 15826 MW; 462AFE611152E23C CRC64; MKERFLERFS ESAFLLERLT GIDGKILLAQ SALETGWGRH TVGNNLFGIK KLSWLEGGVR AETKEFDGVK TIDTFQSFVS PENSMIAYLI LIKECYNRAW ECRKEPEKYF RLLQRYGYAT DPMYAEKCLD VYNCVE // ID Q9X097_THEMA Unreviewed; 184 AA. AC Q9X097; G4FEZ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36084.1}; GN OrderedLocusNames=TM_1002 {ECO:0000313|EMBL:AAD36084.1}; GN ORFNames=Tmari_1006 {ECO:0000313|EMBL:AGL49931.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36084.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36084.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36084.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49931.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49931.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36084.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49931.1; -; Genomic_DNA. DR PIR; D72307; D72307. DR RefSeq; NP_228810.1; NC_000853.1. DR RefSeq; WP_004080548.1; NZ_CP011107.1. DR SMR; Q9X097; 49-182. DR STRING; 243274.TM1002; -. DR EnsemblBacteria; AAD36084; AAD36084; TM_1002. DR EnsemblBacteria; AGL49931; AGL49931; Tmari_1006. DR GeneID; 896839; -. DR KEGG; tma:TM1002; -. DR KEGG; tmi:THEMA_09345; -. DR KEGG; tmm:Tmari_1006; -. DR KEGG; tmw:THMA_1024; -. DR PATRIC; 23936933; VBITheMar51294_1015. DR eggNOG; ENOG4105E37; Bacteria. DR eggNOG; COG2461; LUCA. DR OMA; VVWSSMN; -. DR OrthoDB; EOG63NMG2; -. DR BioCyc; TMAR243274:GC6P-1032-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR000014; PAS. DR SUPFAM; SSF55785; SSF55785; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 184 AA; 21441 MW; 45E4B071056AC6EE CRC64; MSKPSSFRER VADEIDPVVS PETYEKLPDE IKRVAGMLTP DTEYSLVRDN DIKIESGYLS LEELNAIFKT LPFDITFVDK HGRVRFFSGG HRIFHRAPTV LGRPVQFCHP PRSVHIVNKI LKAFKEGRKE PAEFWINMGD RKIHIRYFQV LDKEGNYLGT LEVVQDITRI KELEGEKRLL DWEN // ID Q9X2J0_THEMA Unreviewed; 249 AA. AC Q9X2J0; G4FGR9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 93. DE SubName: Full=Elongator protein 3/MiaB/NifB {ECO:0000313|EMBL:AGL50816.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36939.1}; GN OrderedLocusNames=TM_1877 {ECO:0000313|EMBL:AAD36939.1}; GN ORFNames=Tmari_1892 {ECO:0000313|EMBL:AGL50816.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36939.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36939.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36939.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50816.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50816.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36939.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50816.1; -; Genomic_DNA. DR PIR; H72200; H72200. DR RefSeq; NP_229673.1; NC_000853.1. DR RefSeq; WP_004082428.1; NZ_CP011107.1. DR STRING; 243274.TM1877; -. DR EnsemblBacteria; AAD36939; AAD36939; TM_1877. DR EnsemblBacteria; AGL50816; AGL50816; Tmari_1892. DR GeneID; 897795; -. DR KEGG; tma:TM1877; -. DR KEGG; tmi:THEMA_04785; -. DR KEGG; tmm:Tmari_1892; -. DR KEGG; tmw:THMA_1927; -. DR PATRIC; 23938743; VBITheMar51294_1898. DR eggNOG; ENOG4108UC2; Bacteria. DR eggNOG; COG1856; LUCA. DR KO; K09711; -. DR OMA; NFHIGFP; -. DR OrthoDB; EOG62NX42; -. DR BioCyc; TMAR243274:GC6P-1928-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 13 224 Radical_SAM. {ECO:0000259|Pfam:PF04055}. SQ SEQUENCE 249 AA; 27680 MW; C18FBF37FC7F7FCB CRC64; MTVDPSHTIP VSVTGAFCSL NCPHCGAHYL RHMISVDEIP ALVKKGYRSF LISGGMLPDG SIPFEKYYEH LKELKESHGL LYNFHVGFQK SKVAKELADV VSMDFFGDET VLKSIYGLAL TPQEILDIAH FYENVVFHIT VGITGGKITH EEKALEILSQ ETDTVVLNVF IPTPGTKFGK SFPPDLQEVV KLFEKARKLF KRVILGCMQP RGEYRKKLQS ELKDLVDVIT KPVGGTGEFK GCCAFIGRG // ID Q9WZY8_THEMA Unreviewed; 643 AA. AC Q9WZY8; G4FCT9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=Multimodular transpeptidase-transglycosylase {ECO:0000313|EMBL:AGL49813.1}; DE EC=2.4.1.129 {ECO:0000313|EMBL:AGL49813.1}; DE EC=3.4.-.- {ECO:0000313|EMBL:AGL49813.1}; DE SubName: Full=Penicillin-binding protein, class 1A {ECO:0000313|EMBL:AAD35967.1}; GN OrderedLocusNames=TM_0886 {ECO:0000313|EMBL:AAD35967.1}; GN ORFNames=Tmari_0888 {ECO:0000313|EMBL:AGL49813.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35967.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35967.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35967.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49813.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49813.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35967.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49813.1; -; Genomic_DNA. DR PIR; G72320; G72320. DR RefSeq; NP_228694.1; NC_000853.1. DR RefSeq; WP_004080706.1; NZ_CP011107.1. DR STRING; 243274.TM0886; -. DR CAZy; GT51; Glycosyltransferase Family 51. DR EnsemblBacteria; AAD35967; AAD35967; TM_0886. DR EnsemblBacteria; AGL49813; AGL49813; Tmari_0888. DR GeneID; 898560; -. DR KEGG; tma:TM0886; -. DR KEGG; tmi:THEMA_00205; -. DR KEGG; tmm:Tmari_0888; -. DR KEGG; tmw:THMA_0908; -. DR PATRIC; 23936703; VBITheMar51294_0900. DR eggNOG; ENOG4105BZ4; Bacteria. DR eggNOG; COG0744; LUCA. DR OMA; ALNPYMQ; -. DR OrthoDB; EOG6CGCKC; -. DR BioCyc; TMAR243274:GC6P-916-MONOMER; -. DR BRENDA; 2.4.1.129; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0008658; F:penicillin binding; IEA:InterPro. DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR001264; Glyco_trans_51. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR001460; PCN-bd_Tpept. DR Pfam; PF00912; Transgly; 1. DR Pfam; PF00905; Transpeptidase; 1. DR SUPFAM; SSF53955; SSF53955; 1. DR SUPFAM; SSF56601; SSF56601; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000313|EMBL:AGL49813.1}; KW Hydrolase {ECO:0000313|EMBL:AGL49813.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49813.1}. FT DOMAIN 55 219 Transgly. {ECO:0000259|Pfam:PF00912}. FT DOMAIN 323 553 Transpeptidase. FT {ECO:0000259|Pfam:PF00905}. SQ SEQUENCE 643 AA; 73672 MW; 152291C19EBB717F CRC64; MKKFLLSFFI ASLLTFFLLW GLYFFFTKDL PPPEEKLVPT IRLFYSDGTP LLVSRNIWID LSDIPEKFVE ILLTSEDEEF YKHPGFDLMG FLRALIMDIK TLSFSQGGST ITQQLARTLY LSMDKSIVRK LKEIFISFWL ERIRTKDEIL EMYINSVYMG NGIYGFQTAS KLYFGKDLSD LSVPEMCVLV ALIKSPENFN PLKDPETSRK RAKIVLDRLL TEKRISTQEY ENYSAELSKL EFHTQQMNVD EELFWRVVRE AQDLGFSLNE LRYGYRVYLT LDKELQKKVY NTVEDDKTAF VGVKVKTGEI VAYRGVGLQY GTGWRQIGSA IKPLYYYYAV LKGRNPSDLL LDLPLKIGEW EPENFDKTFK GTVSLKEALV DSRNIPSVLL YSYLQPESVR SFITEVLKLR ARYPDDLTAS LGTVETAPEE IVKVYSAIFN GGVVLEPYII DKIEDRNGKI IYRGYPKVLS VVPSFVRSAQ EASEILKSIL KEVVERGTGV RVKIPGKEIA GKTGTAEKNA WFVGGDDEYI FAVVKDGENL LGGRDCAPVW KEIVSSWEKF EGDLRYKRLD KPGIPLIDDR TIEYLDYAKL VELVNGSKLP VSVLVKVLQL MDYNHQIEFL SKLNSVDPIL SLEIWKKFLM EGG // ID Q9WZE1_THEMA Unreviewed; 224 AA. AC Q9WZE1; G4FDF1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 77. DE RecName: Full=Basal-body rod modification protein FlgD {ECO:0000256|RuleBase:RU362076}; GN OrderedLocusNames=TM_0673 {ECO:0000313|EMBL:AAD35757.1}; GN ORFNames=Tmari_0673 {ECO:0000313|EMBL:AGL49598.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35757.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35757.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35757.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49598.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49598.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Required for flagellar hook formation. May act as a CC scaffolding protein. {ECO:0000256|RuleBase:RU362076}. CC -!- SIMILARITY: Belongs to the FlgD family. CC {ECO:0000256|RuleBase:RU362076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35757.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49598.1; -; Genomic_DNA. DR PIR; H72346; H72346. DR RefSeq; NP_228482.1; NC_000853.1. DR RefSeq; WP_004081097.1; NZ_CP011107.1. DR STRING; 243274.TM0673; -. DR EnsemblBacteria; AAD35757; AAD35757; TM_0673. DR EnsemblBacteria; AGL49598; AGL49598; Tmari_0673. DR GeneID; 898341; -. DR KEGG; tma:TM0673; -. DR KEGG; tmi:THEMA_01300; -. DR KEGG; tmm:Tmari_0673; -. DR KEGG; tmw:THMA_0688; -. DR PATRIC; 23936260; VBITheMar51294_0683. DR eggNOG; ENOG4105W00; Bacteria. DR eggNOG; COG1843; LUCA. DR KO; K02389; -. DR OMA; QMTSYAN; -. DR OrthoDB; EOG6BKJ7S; -. DR BioCyc; TMAR243274:GC6P-698-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009424; C:bacterial-type flagellum hook; IBA:GO_Central. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW. DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IBA:GO_Central. DR InterPro; IPR005648; FlgD. DR InterPro; IPR025965; FlgD_Ig. DR Pfam; PF03963; FlgD; 1. DR Pfam; PF13860; FlgD_ig; 1. PE 3: Inferred from homology; KW Bacterial flagellum biogenesis {ECO:0000256|RuleBase:RU362076}; KW Cell projection {ECO:0000313|EMBL:AGL49598.1}; KW Cilium {ECO:0000313|EMBL:AGL49598.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AGL49598.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 102 175 FlgD_ig. {ECO:0000259|Pfam:PF13860}. SQ SEQUENCE 224 AA; 24355 MW; D8FCDE694556A8AA CRC64; MIYDMSGIYL SSLTGIRNNS SSSSNSLDKE AFLRLLLQEL EMQDPLEPME TKDMISQLSQ LTSLEQITNL TSAVKDFVEA QTSVSPAQLA SLIGKYVVVR NNTVNLVGGQ SDSIIFNVDE DAHVVVQILD ENGKLVRTED LGTVQVGVHA WQWDGRDDNG ISVEDGSYTY RVYKLTSSGL EEIGGMEGGV VEAVQIKDGK GFVLVNGSLY PVDSILEISQ EGDA // ID Q9WZ10_THEMA Unreviewed; 272 AA. AC Q9WZ10; G4FDT1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 79. DE SubName: Full=Fumarate hydratase class I, aerobic L(+)-tartrate dehydratase alpha subunit {ECO:0000313|EMBL:AGL49462.1}; DE EC=4.2.1.2 {ECO:0000313|EMBL:AGL49462.1}; DE EC=4.2.1.32 {ECO:0000313|EMBL:AGL49462.1}; DE SubName: Full=Fumarate hydratase, N-terminal subunit {ECO:0000313|EMBL:AAD35625.1}; GN OrderedLocusNames=TM_0540 {ECO:0000313|EMBL:AAD35625.1}; GN ORFNames=Tmari_0537 {ECO:0000313|EMBL:AGL49462.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35625.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35625.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35625.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49462.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49462.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35625.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49462.1; -; Genomic_DNA. DR PIR; A72364; A72364. DR RefSeq; NP_228350.1; NC_000853.1. DR RefSeq; WP_004081365.1; NZ_CP011107.1. DR STRING; 243274.TM0540; -. DR DNASU; 897594; -. DR EnsemblBacteria; AAD35625; AAD35625; TM_0540. DR EnsemblBacteria; AGL49462; AGL49462; Tmari_0537. DR GeneID; 897594; -. DR KEGG; tma:TM0540; -. DR KEGG; tmi:THEMA_01975; -. DR KEGG; tmm:Tmari_0537; -. DR KEGG; tmw:THMA_0553; -. DR PATRIC; 23935987; VBITheMar51294_0548. DR eggNOG; ENOG4108JSW; Bacteria. DR eggNOG; COG1951; LUCA. DR KO; K01677; -. DR OMA; IQCWANR; -. DR OrthoDB; EOG6TXR10; -. DR BioCyc; TMAR243274:GC6P-564-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0008730; F:L(+)-tartrate dehydratase activity; IEA:UniProtKB-EC. DR InterPro; IPR004646; Fe-S_hydro-lyase_TtdA-typ_cat. DR Pfam; PF05681; Fumerase; 1. DR TIGRFAMs; TIGR00722; ttdA_fumA_fumB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000313|EMBL:AGL49462.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 11 268 Fumerase. {ECO:0000259|Pfam:PF05681}. SQ SEQUENCE 272 AA; 30554 MW; 726E783AF762840D CRC64; MINKHVISEK IKKAIVEANI KINPEVEEII ERYEGPFSDI IKENYRVSKE EKLPLCQDTG IVEFFVFIGH EVKLEEPIEE TLNRAVGEVY SEYPFRYSVV SDPLFERINT GTNTPAIVHI FQVKGKSLEI RFLVKGGGSE NLTVLRMMTP TSDVEKVKEF VIEHIKEHGA KACPPLHVGI GIGGTADKAL LLSKLALTKS FKERNKDPKY AGLEKELEKE LNFLGIGFQG LGKGITVYSV HIEHFPTHIA TLPVAVSVDC YLCRRGKVTF ED // ID Q9WZS7_THEMA Unreviewed; 395 AA. AC Q9WZS7; G4FD04; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=NADH-dependent butanol dehydrogenase A {ECO:0000313|EMBL:AGL49746.1}; DE EC=1.1.1.- {ECO:0000313|EMBL:AGL49746.1}; DE SubName: Full=NADH-dependent butanol dehydrogenase, putative {ECO:0000313|EMBL:AAD35902.1}; GN OrderedLocusNames=TM_0820 {ECO:0000313|EMBL:AAD35902.1}; GN ORFNames=Tmari_0821 {ECO:0000313|EMBL:AGL49746.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35902.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35902.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35902.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49746.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49746.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35902.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49746.1; -; Genomic_DNA. DR PIR; G72329; G72329. DR RefSeq; NP_228629.1; NC_000853.1. DR RefSeq; WP_004080839.1; NZ_CP011107.1. DR PDB; 1VLJ; X-ray; 1.78 A; A/B=1-395. DR PDBsum; 1VLJ; -. DR STRING; 243274.TM0820; -. DR EnsemblBacteria; AAD35902; AAD35902; TM_0820. DR EnsemblBacteria; AGL49746; AGL49746; Tmari_0821. DR GeneID; 898489; -. DR KEGG; tma:TM0820; -. DR KEGG; tmi:THEMA_00545; -. DR KEGG; tmm:Tmari_0821; -. DR KEGG; tmw:THMA_0840; -. DR PATRIC; 23936562; VBITheMar51294_0832. DR eggNOG; ENOG4107QW4; Bacteria. DR eggNOG; COG1979; LUCA. DR OMA; AVQPKFA; -. DR OrthoDB; EOG676Z4N; -. DR BioCyc; TMAR243274:GC6P-848-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR InterPro; IPR001670; ADH_Fe. DR InterPro; IPR018211; ADH_Fe_CS. DR Pfam; PF00465; Fe-ADH; 1. DR PROSITE; PS00913; ADH_IRON_1; 1. DR PROSITE; PS00060; ADH_IRON_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VLJ}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000213|PDB:1VLJ}; Metal-binding {ECO:0000213|PDB:1VLJ}; KW NADP {ECO:0000213|PDB:1VLJ}; KW Nucleotide-binding {ECO:0000213|PDB:1VLJ}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49746.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 9 361 Fe-ADH. {ECO:0000259|Pfam:PF00465}. FT NP_BIND 40 42 NADP. {ECO:0000213|PDB:1VLJ}. FT NP_BIND 99 103 NADP. {ECO:0000213|PDB:1VLJ}. FT NP_BIND 148 150 NADP. {ECO:0000213|PDB:1VLJ}. FT NP_BIND 180 183 NADP. {ECO:0000213|PDB:1VLJ}. FT METAL 195 195 Iron. {ECO:0000213|PDB:1VLJ}. FT METAL 199 199 Iron; via tele nitrogen. FT {ECO:0000213|PDB:1VLJ}. FT METAL 268 268 Iron; via tele nitrogen. FT {ECO:0000213|PDB:1VLJ}. FT METAL 282 282 Iron; via tele nitrogen. FT {ECO:0000213|PDB:1VLJ}. FT BINDING 71 71 NADP; via carbonyl oxygen. FT {ECO:0000213|PDB:1VLJ}. FT BINDING 139 139 NADP. {ECO:0000213|PDB:1VLJ}. FT BINDING 143 143 NADP; via carbonyl oxygen. FT {ECO:0000213|PDB:1VLJ}. FT BINDING 161 161 NADP. {ECO:0000213|PDB:1VLJ}. SQ SEQUENCE 395 AA; 43355 MW; 6053E21CD1DF374A CRC64; MENFVFHNPT KIVFGRGTIP KIGEEIKNAG IRKVLFLYGG GSIKKNGVYD QVVDSLKKHG IEWVEVSGVK PNPVLSKVHE AVEVAKKEKV EAVLGVGGGS VVDSAKAVAA GALYEGDIWD AFIGKYQIEK ALPIFDVLTI SATGTEMNGN AVITNEKTKE KYGVSSKALY PKVSIIDPSV QFTLPKEQTV YGAVDAISHI LEYYFDGSSP EISNEIAEGT IRTIMKMTER LIEKPDDYEA RANLAWSATI ALNGTMAVGR RGGEWACHRI EHSLSALYDI AHGAGLAIVF PAWMKYVYRK NPAQFERFAK KIFGFEGEGE ELILKGIEAF KNWLKKVGAP VSLKDAGIPE EDIDKIVDNV MLLVEKNLKP KGASLGRIMV LEREDVREIL KLAAK // ID Q9WZJ2_THEMA Unreviewed; 136 AA. AC Q9WZJ2; G4FD90; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Serine-protein kinase rsbW {ECO:0000313|EMBL:AGL49659.1}; DE EC=2.7.11.1 {ECO:0000313|EMBL:AGL49659.1}; DE SubName: Full=Sigma-B regulator, putative {ECO:0000313|EMBL:AAD35814.1}; GN OrderedLocusNames=TM_0733 {ECO:0000313|EMBL:AAD35814.1}; GN ORFNames=Tmari_0734 {ECO:0000313|EMBL:AGL49659.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35814.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35814.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35814.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49659.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49659.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35814.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49659.1; -; Genomic_DNA. DR PIR; H72338; H72338. DR RefSeq; NP_228542.1; NC_000853.1. DR RefSeq; WP_004080993.1; NZ_CP011107.1. DR STRING; 243274.TM0733; -. DR EnsemblBacteria; AAD35814; AAD35814; TM_0733. DR EnsemblBacteria; AGL49659; AGL49659; Tmari_0734. DR GeneID; 898400; -. DR KEGG; tma:TM0733; -. DR KEGG; tmi:THEMA_00990; -. DR KEGG; tmm:Tmari_0734; -. DR KEGG; tmw:THMA_0751; -. DR PATRIC; 23936386; VBITheMar51294_0746. DR eggNOG; ENOG4105S6H; Bacteria. DR eggNOG; COG2172; LUCA. DR KO; K04757; -. DR OMA; DFGPKVD; -. DR OrthoDB; EOG6S7XW5; -. DR BioCyc; TMAR243274:GC6P-759-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003594; HATPase_C. DR Pfam; PF13581; HATPase_c_2; 1. DR SUPFAM; SSF55874; SSF55874; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000313|EMBL:AGL49659.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49659.1}. FT DOMAIN 12 128 HATPase_c. {ECO:0000259|Pfam:PF13581}. SQ SEQUENCE 136 AA; 15724 MW; 15AB5A035DF9A75D CRC64; MIDTVSVVLF SKKSHIKIAR SVLRDFLQMH ESSDSLIVDM EIVLGEILAN VIKHTYKNDE TKRIIVSYTL KDEVFHMLVR DFGPPVDPTR LKPMPPDLEN PREGGYGFYI ISRVTDEFRV RPLRNGNLTV VKKKLR // ID Q9X1N0_THEMA Unreviewed; 336 AA. AC Q9X1N0; G4FFT2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=Rod shape-determining protein MreB {ECO:0000313|EMBL:AAD36611.1}; GN OrderedLocusNames=TM_1544 {ECO:0000313|EMBL:AAD36611.1}; GN ORFNames=Tmari_1552 {ECO:0000313|EMBL:AGL50476.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36611.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36611.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36611.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50476.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50476.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36611.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50476.1; -; Genomic_DNA. DR PIR; D72243; D72243. DR RefSeq; NP_229344.1; NC_000853.1. DR RefSeq; WP_004081933.1; NZ_CP011107.1. DR SMR; Q9X1N0; 5-330. DR STRING; 243274.TM1544; -. DR EnsemblBacteria; AAD36611; AAD36611; TM_1544. DR EnsemblBacteria; AGL50476; AGL50476; Tmari_1552. DR GeneID; 897974; -. DR KEGG; tma:TM1544; -. DR KEGG; tmi:THEMA_06565; -. DR KEGG; tmm:Tmari_1552; -. DR KEGG; tmw:THMA_1578; -. DR PATRIC; 23938048; VBITheMar51294_1562. DR eggNOG; ENOG4105DFF; Bacteria. DR eggNOG; COG1077; LUCA. DR KO; K03569; -. DR OMA; AIVRYMR; -. DR OrthoDB; EOG66QM00; -. DR BioCyc; TMAR243274:GC6P-1584-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro. DR InterPro; IPR004753; MreB_Mrl. DR Pfam; PF06723; MreB_Mbl; 1. DR PRINTS; PR01652; SHAPEPROTEIN. DR TIGRFAMs; TIGR00904; mreB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 336 AA; 36193 MW; D67D94C8B96FBE9B CRC64; MPRGDIGIDL GTASIIVYKR GEGIVLHEPS VVAISEKTGE IVAIGEEAKK MLGKTPEGLK AIRPMKDGVI ADYRMIEAII RNFLKKIIGR FSFVKPSLII GVPTKITEVE KRAVFEAGLN AGARRVHIVS EPIAAAIGAG IDVMASEGNM VVDIGGGTTD IAVISLGGTV VGESVRMAGD AMDEAIVKFI RKKYGLIIGE STAEEIKKRI GKTHPAFENY EIEIKGRDVV TGLPRTDRVS SEDVREAIEP IIFALLTKLK NVLERTPPEL SADIINNGIR LTGGGALLRG LDRTIYDEIH VKTIVADDPI TCVARGTGIL LEDEKLLKTV CETYSR // ID Q9WYE0_THEMA Unreviewed; 316 AA. AC Q9WYE0; G4FHL8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 124. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35392.1}; DE SubName: Full=Xyloglucan ABC transport system, ATP-binding protein 2 {ECO:0000313|EMBL:AGL49228.1}; GN OrderedLocusNames=TM_0304 {ECO:0000313|EMBL:AAD35392.1}; GN ORFNames=Tmari_0302 {ECO:0000313|EMBL:AGL49228.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35392.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35392.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35392.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49228.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49228.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35392.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49228.1; -; Genomic_DNA. DR PIR; E72393; E72393. DR RefSeq; NP_228116.1; NC_000853.1. DR RefSeq; WP_004083029.1; NZ_CP011107.1. DR STRING; 243274.TM0304; -. DR TCDB; 3.A.1.5.30; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35392; AAD35392; TM_0304. DR EnsemblBacteria; AGL49228; AGL49228; Tmari_0302. DR GeneID; 897234; -. DR KEGG; tma:TM0304; -. DR KEGG; tmi:THEMA_03205; -. DR KEGG; tmm:Tmari_0302; -. DR KEGG; tmw:THMA_0311; -. DR PATRIC; 23935487; VBITheMar51294_0309. DR eggNOG; ENOG4105GTU; Bacteria. DR eggNOG; COG4608; LUCA. DR KO; K02032; -. DR OMA; GPDKGCQ; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-317-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35392.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35392.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 3 251 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 316 AA; 35861 MW; F5CB85B2B2E99A70 CRC64; MRVSVRNLTK IFRVGSIFSL KKLVAIDNVS FEIGSGEIFS LAGESGCGKT TTAKILLGLE EPTNGEVLYD GIKLKDFVEN EMHFLKKVQT VQQNPFSTFN PFRKVEDYLF KTVLRFKMAN TKDEALRLIE EKLSVVGLNF DEIKGRYPSE FSGGQLQRIS IARALLTNPS FLVADEPVSM IDASLRISIV NLFRDLKERF GISILYITHD LSTAYYVADK LAIMFRGSIV EMGRAQDILD TPFHPYTKLL KSSIPVPDPE YEWDENINLS STEREEFFAK GCKFASRCPE VMSICRESVP PDFDVNGRVV KCWLYK // ID Q9WZW8_THEMA Unreviewed; 280 AA. AC Q9WZW8; G4FCW0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 99. DE SubName: Full=Ribonuclease Z {ECO:0000313|EMBL:AGL49791.1}; DE EC=3.1.26.11 {ECO:0000313|EMBL:AGL49791.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35946.1}; GN OrderedLocusNames=TM_0864 {ECO:0000313|EMBL:AAD35946.1}; GN ORFNames=Tmari_0866 {ECO:0000313|EMBL:AGL49791.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35946.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35946.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35946.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49791.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49791.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35946.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49791.1; -; Genomic_DNA. DR PIR; C72322; C72322. DR RefSeq; NP_228673.1; NC_000853.1. DR RefSeq; WP_004080741.1; NZ_CP011107.1. DR PDB; 1WW1; X-ray; 2.60 A; A/B=1-280. DR PDB; 2E7Y; X-ray; 1.97 A; A/B=1-280. DR PDBsum; 1WW1; -. DR PDBsum; 2E7Y; -. DR STRING; 243274.TM0864; -. DR DNASU; 898537; -. DR EnsemblBacteria; AAD35946; AAD35946; TM_0864. DR EnsemblBacteria; AGL49791; AGL49791; Tmari_0866. DR GeneID; 898537; -. DR KEGG; tma:TM0864; -. DR KEGG; tmi:THEMA_00315; -. DR KEGG; tmm:Tmari_0866; -. DR KEGG; tmw:THMA_0886; -. DR PATRIC; 23936656; VBITheMar51294_0877. DR eggNOG; ENOG4107QRW; Bacteria. DR eggNOG; COG1234; LUCA. DR KO; K00784; -. DR OMA; NTRNNAM; -. DR OrthoDB; EOG61P6TK; -. DR BioCyc; TMAR243274:GC6P-894-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0034414; P:tRNA 3'-trailer cleavage, endonucleolytic; IBA:GOC. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR013470; RNase_Z_THEMA. DR Pfam; PF12706; Lactamase_B_2; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR02650; RNase_Z_T_toga; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1WW1, ECO:0000213|PDB:2E7Y}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49791.1}; KW Metal-binding {ECO:0000213|PDB:1WW1, ECO:0000213|PDB:2E7Y}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000213|PDB:1WW1, ECO:0000213|PDB:2E7Y}. FT DOMAIN 21 245 Lactamase_B. {ECO:0000259|Pfam:PF12706}. FT METAL 48 48 Zinc 1; via tele nitrogen. FT {ECO:0000213|PDB:2E7Y}. FT METAL 50 50 Zinc 1; via pros nitrogen. FT {ECO:0000213|PDB:2E7Y}. FT METAL 52 52 Zinc 2. {ECO:0000213|PDB:2E7Y}. FT METAL 53 53 Zinc 2; via tele nitrogen. FT {ECO:0000213|PDB:2E7Y}. FT METAL 134 134 Zinc 1; via tele nitrogen. FT {ECO:0000213|PDB:2E7Y}. FT METAL 190 190 Zinc 1. {ECO:0000213|PDB:2E7Y}. FT METAL 190 190 Zinc 2. {ECO:0000213|PDB:2E7Y}. FT METAL 244 244 Zinc 2; via tele nitrogen. FT {ECO:0000213|PDB:2E7Y}. SQ SEQUENCE 280 AA; 32658 MW; C4FE9C50C3EE9BA5 CRC64; MNIIGFSKAL FSTWIYYSPE RILFDAGEGV STTLGSKVYA FKYVFLTHGH VDHIAGLWGV VNIRNNGMGD REKPLDVFYP EGNRAVEEYT EFIKRANPDL RFSFNVHPLK EGERVFLRNA GGFKRYVQPF RTKHVSSEVS FGYHIFEVRR KLKKEFQGLD SKEISRLVKE KGRDFVTEEY HKKVLTISGD SLALDPEEIR GTELLIHECT FLDARDRRYK NHAAIDEVME SVKAAGVKKV ILYHISTRYI RQLKSVIKKY REEMPDVEIL YMDPRKVFEM // ID Q9WYD3_THEMA Unreviewed; 257 AA. AC Q9WYD3; G4FHL1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 102. DE SubName: Full=3-oxoacyl-[acyl-carrier protein] reductase {ECO:0000313|EMBL:AGL49221.1}; DE EC=1.1.1.100 {ECO:0000313|EMBL:AGL49221.1}; DE SubName: Full=Oxidoreductase, short chain dehydrogenase/reductase family {ECO:0000313|EMBL:AAD35385.1}; GN OrderedLocusNames=TM_0297 {ECO:0000313|EMBL:AAD35385.1}; GN ORFNames=Tmari_0295 {ECO:0000313|EMBL:AGL49221.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35385.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35385.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35385.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49221.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49221.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35385.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49221.1; -; Genomic_DNA. DR PIR; A72395; A72395. DR RefSeq; NP_228109.1; NC_000853.1. DR RefSeq; WP_004083016.1; NZ_CP011107.1. DR STRING; 243274.TM0297; -. DR DNASU; 897222; -. DR EnsemblBacteria; AAD35385; AAD35385; TM_0297. DR EnsemblBacteria; AGL49221; AGL49221; Tmari_0295. DR GeneID; 897222; -. DR KEGG; tma:TM0297; -. DR KEGG; tmm:Tmari_0295; -. DR KEGG; tmw:THMA_0304; -. DR PATRIC; 23935473; VBITheMar51294_0302. DR eggNOG; ENOG4105CHR; Bacteria. DR eggNOG; ENOG410XNW1; LUCA. DR OMA; GVTCKAY; -. DR OrthoDB; EOG6N3CR8; -. DR BioCyc; TMAR243274:GC6P-310-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24322; PTHR24322; 2. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49221.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 257 AA; 27886 MW; 724484FF3EDF5EAC CRC64; MNILEKLFSL KRKVALVTGG GQGIGKAIAQ ALAAAGAAVL IMDINEETAR RTVEEIKEKG GEADFYVGDV TKEEDCFGAV KKALDRWGKL DIGVNNAGIG DWCEAENYPV EKWKKVIDVN LVGVFLSAKA EFHAMKERKY GKIINIASMS GHIVNKPQKQ TAYNASKAGV IHLTRSLAAE WAPYGIRVNS ISPGYIRTPL IESPNVKDLV PLWLDMIPLG RLGEVDDLIG AAIFLASPAS DYMTGHDLVI DGGYTVW // ID Q9WZB2_THEMA Unreviewed; 640 AA. AC Q9WZB2; G4FDI0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 91. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35728.1}; GN OrderedLocusNames=TM_0644 {ECO:0000313|EMBL:AAD35728.1}; GN ORFNames=Tmari_0644 {ECO:0000313|EMBL:AGL49569.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35728.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35728.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35728.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49569.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49569.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35728.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49569.1; -; Genomic_DNA. DR PIR; C72351; C72351. DR RefSeq; NP_228453.1; NC_000853.1. DR RefSeq; WP_004081154.1; NZ_CP011107.1. DR STRING; 243274.TM0644; -. DR EnsemblBacteria; AAD35728; AAD35728; TM_0644. DR EnsemblBacteria; AGL49569; AGL49569; Tmari_0644. DR GeneID; 897748; -. DR KEGG; tma:TM0644; -. DR KEGG; tmi:THEMA_01445; -. DR KEGG; tmm:Tmari_0644; -. DR KEGG; tmw:THMA_0659; -. DR PATRIC; 23936202; VBITheMar51294_0654. DR eggNOG; ENOG4107SYR; Bacteria. DR eggNOG; COG0489; LUCA. DR eggNOG; COG3206; LUCA. DR OMA; MINIQIE; -. DR OrthoDB; EOG69D3H6; -. DR BioCyc; TMAR243274:GC6P-669-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR032807; GNVR. DR InterPro; IPR003856; LipoPS_biosynth. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13807; GNVR; 1. DR Pfam; PF02706; Wzz; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 39 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 442 462 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 5 172 Wzz. {ECO:0000259|Pfam:PF02706}. FT DOMAIN 384 461 GNVR. {ECO:0000259|Pfam:PF13807}. FT COILED 182 223 {ECO:0000256|SAM:Coils}. FT COILED 233 267 {ECO:0000256|SAM:Coils}. FT COILED 309 333 {ECO:0000256|SAM:Coils}. FT COILED 367 401 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 640 AA; 72679 MW; 38961ADA8448BDFC CRC64; MEERELTLSD ILLMFKRRSK LFWLVLVLTV FATGIYLFLA TPQYEAYARV KVSTQKGMRL GLSIEGLLGG LSSLLGGGGS QEDEIQIMLS RRNIIAVIDE LDLVHKLLDE KDIEKAKKNG LTEDDLKLSL YSYMVEKLIT VEPVKNSSIL EVKVTWHEPK LAAEIANKIV ENYTKISENI AKSQLGAKMD FLEEQIPKVE QELKEAESKL KVFKEQNRIY SVEAQTQVLI DRYASLLQKM EEARIAMEAT QKQSEFFSKE LKDLDIEIEQ IKDSITFDPI ISQLKSNMIN IQIELAGLME RYTETNPAVV QKKAELQETQ KQLEIELKRL LTSQVKKTGN PVYEEALSSL IKAESEKILY QSQYEAFKKL YEDMEKELSK LPELEQKLIE LERDYKVKET IYTTLLQAKY ESLISEAAIT ANANVIDWAV PPLEPSKPNK KLTLAIGGVL GIFLGILAVF FAEFSDRRIK SESEAEYLLG LEKIVARVPL TQNEEVMEKA LGIPAVKSGK VTFITALEDG AGVSTLAKHM AKLLSKKEKV LLLTEEKVEG TFDRKDVFDL LKNPDVLEEL KERYDKIIVD APSLKRTPDF LPIAEKSDTV YIVIRLEHTL SEDLKTLHTL KKIDGFILNG LTKKNSTYVE // ID Q9X218_THEMA Unreviewed; 384 AA. AC Q9X218; G4FG79; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 109. DE SubName: Full=Aminotransferase, class V {ECO:0000313|EMBL:AAD36759.1}; DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:AGL50624.1}; DE EC=2.8.1.7 {ECO:0000313|EMBL:AGL50624.1}; GN OrderedLocusNames=TM_1692 {ECO:0000313|EMBL:AAD36759.1}; GN ORFNames=Tmari_1700 {ECO:0000313|EMBL:AGL50624.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36759.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36759.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36759.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50624.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50624.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|SAAS:SAAS00549899}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36759.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50624.1; -; Genomic_DNA. DR PIR; F72223; F72223. DR RefSeq; NP_229492.1; NC_000853.1. DR RefSeq; WP_004082208.1; NZ_CP011107.1. DR PDB; 1ECX; X-ray; 2.70 A; A/B=1-384. DR PDB; 1EG5; X-ray; 2.00 A; A/B=1-384. DR PDBsum; 1ECX; -. DR PDBsum; 1EG5; -. DR STRING; 243274.TM1692; -. DR EnsemblBacteria; AAD36759; AAD36759; TM_1692. DR EnsemblBacteria; AGL50624; AGL50624; Tmari_1700. DR GeneID; 897893; -. DR KEGG; tma:TM1692; -. DR KEGG; tmi:THEMA_05780; -. DR KEGG; tmm:Tmari_1700; -. DR KEGG; tmw:THMA_1734; -. DR PATRIC; 23938358; VBITheMar51294_1709. DR eggNOG; ENOG4105C3J; Bacteria. DR eggNOG; COG1104; LUCA. DR KO; K04487; -. DR OMA; YKKRGRM; -. DR OrthoDB; EOG62RSBK; -. DR BioCyc; TMAR243274:GC6P-1740-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR016454; Cysteine_dSase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF005572; NifS; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1ECX, ECO:0000213|PDB:1EG5}; KW Aminotransferase {ECO:0000313|EMBL:AAD36759.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Pyridoxal phosphate {ECO:0000256|SAAS:SAAS00435198}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD36759.1}. FT DOMAIN 3 365 Aminotran_5. {ECO:0000259|Pfam:PF00266}. FT COILED 248 271 {ECO:0000256|SAM:Coils}. FT SITE 99 99 Important for catalytic activity. FT {ECO:0000213|PDB:1ECX}. FT SITE 177 177 Important for catalytic activity. FT {ECO:0000213|PDB:1ECX}. FT SITE 203 203 Important for catalytic activity. FT {ECO:0000213|PDB:1ECX}. FT MOD_RES 203 203 N6-(pyridoxal phosphate)lysine. FT {ECO:0000213|PDB:1EG5}. SQ SEQUENCE 384 AA; 42799 MW; 7763BD94B83355E9 CRC64; MRVYFDNNAT TRVDDRVLEE MIVFYREKYG NPNSAHGMGI EANLHMEKAR EKVAKVLGVS PSEIFFTSCA TESINWILKT VAETFEKRKR TIITTPIEHK AVLETMKYLS MKGFKVKYVP VDSRGVVKLE ELEKLVDEDT FLVSIMAANN EVGTIQPVED VTRIVKKKNK ETLVHVDAVQ TIGKIPFSLE KLEVDYASFS AHKFHGPKGV GITYIRKGVP IRPLIHGGGQ ERGLRSGTQN VPGIVGAARA MEIAVEELSE AAKHMEKLRS KLVSGLMNLG AHIITPLEIS LPNTLSVSFP NIRGSTLQNL LSGYGIYVST SSACTSKDER LSHVLDAMGV DRRIAQGAIR ISLCKYNTEE EVDYFLKKIE EILSFLDLTG NNRR // ID Q9X0Y4_THEMA Unreviewed; 611 AA. AC Q9X0Y4; G4FE91; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36331.1}; GN OrderedLocusNames=TM_1257 {ECO:0000313|EMBL:AAD36331.1}; GN ORFNames=Tmari_1262 {ECO:0000313|EMBL:AGL50186.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36331.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36331.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36331.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50186.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50186.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36331.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50186.1; -; Genomic_DNA. DR PIR; D72275; D72275. DR RefSeq; NP_229062.1; NC_000853.1. DR RefSeq; WP_004080005.1; NZ_CP011107.1. DR STRING; 243274.TM1257; -. DR EnsemblBacteria; AAD36331; AAD36331; TM_1257. DR EnsemblBacteria; AGL50186; AGL50186; Tmari_1262. DR GeneID; 898226; -. DR KEGG; tma:TM1257; -. DR KEGG; tmm:Tmari_1262; -. DR KEGG; tmw:THMA_1282; -. DR PATRIC; 23937454; VBITheMar51294_1273. DR eggNOG; ENOG41061U6; Bacteria. DR eggNOG; COG0433; LUCA. DR KO; K06915; -. DR OMA; EFPFPAW; -. DR OrthoDB; EOG6D8B61; -. DR BioCyc; TMAR243274:GC6P-1288-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR018538; HerA_barrel_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF09378; HAS-barrel; 1. DR SUPFAM; SSF52540; SSF52540; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 6 109 HAS-barrel. {ECO:0000259|Pfam:PF09378}. SQ SEQUENCE 611 AA; 70010 MW; 7FB042D4E49097AB CRC64; MSGRKIGVVT GIFQSSPYEF FVRMTAEKPG EAYKVFAQIE DVVKVEYLTG YGTVVTYGMI VDIQNRWDGD LRNGYEEEVA LEKLKPAYPI YIAKVKVTRS FLKEGNKLLE DAPEIPPNIG SPVFLVGDEE IDIALGFDEL KRKNVALPVG LLKNGRPAYL DLRYILGDNG AHINVSGQSG VAAKTSYTTF LVKSMIETSS KNDGDLMREL REARYIIFNV KGESLLFLDR ISKEWYSERE KWDEMYRVLG IEPKPFENVA FYAPSREKGA YIPDVNKRLI GVNVYGWDVF DIVEMNLLEL MFDPDEMTRN QNFQLAVWSL QEHLSQRMEE MYQEFLKEGY IVDRKKLPSE ALREVVMKKG EVVDLPLDLD SLIKDLGEGG RTREYLLGEH VQKQTIGMLI RRLKAAQKMD FDRLWVKPPL KVEPWQTNYR IDWNVPGRVT VIDISKLRER AQAFVVGAIL SEVMREKERN SGFTQPVFIF LDELNKYAPR HGGGALANIF RDVAERGRSF RVILIGAEQT ASEVDYRVIT QAATVVVGRQ KGAELIKPEY SHLTEHYKRK AALLRQGEVI IDQPFLNLPL TVKFPLPAWC TREGGWHNPE GKTWEEEEFI I // ID Q9X1E7_THEMA Unreviewed; 403 AA. AC Q9X1E7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 100. DE SubName: Full=Oxidoreductase, putative {ECO:0000313|EMBL:AAD36503.1}; DE SubName: Full=Sarcosine oxidase alpha subunit {ECO:0000313|EMBL:AGL50363.1}; DE EC=1.5.3.1 {ECO:0000313|EMBL:AGL50363.1}; GN OrderedLocusNames=TM_1433 {ECO:0000313|EMBL:AAD36503.1}; GN ORFNames=Tmari_1439 {ECO:0000313|EMBL:AGL50363.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36503.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36503.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36503.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50363.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50363.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36503.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50363.1; -; Genomic_DNA. DR PIR; F72254; F72254. DR RefSeq; NP_229233.1; NC_000853.1. DR RefSeq; WP_008195104.1; NZ_CP011107.1. DR STRING; 243274.TM1433; -. DR EnsemblBacteria; AAD36503; AAD36503; TM_1433. DR EnsemblBacteria; AGL50363; AGL50363; Tmari_1439. DR GeneID; 898042; -. DR KEGG; tma:TM1433; -. DR KEGG; tmi:THEMA_07150; -. DR KEGG; tmm:Tmari_1439; -. DR KEGG; tmw:THMA_1463; -. DR PATRIC; 23937814; VBITheMar51294_1445. DR eggNOG; ENOG4105P5G; Bacteria. DR eggNOG; COG0446; LUCA. DR OMA; IMPGKEI; -. DR OrthoDB; EOG6KT2M0; -. DR BioCyc; TMAR243274:GC6P-1471-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-EC. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00469; PNDRDTASEII. DR SUPFAM; SSF51905; SSF51905; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50363.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 296 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. SQ SEQUENCE 403 AA; 44862 MW; 07AE02B348CBDFBD CRC64; MRVDVMVIGA GAAGMAAALK AKEEGAEVLL VERDERTGGI LNQCIHNGFG LHYFRQELTG PEYAERFQEK MEKMGIRALT NAYVKRVEDR RVILVTEQGI EEVEVGALVY ATGARERPFG SLMIPGDRPS GIFTAGVAQR LINIENRLPG KRALILGSGD IGLIMARRLT LEGMEVVGVV ERLPYAGGLL RNVIQCLEDY NIPLYLSSTV VEVRGRERLE EVVVAKVDEQ FRPIPRTERV FKVDTLVLSV GLIPQVELIE NLVVKNPTSR GVGVSNIGQT SRDWIFSAGN CTVIFDLVDY VSYEGETAGR YAAKFVKGEI PREKIPVRPG KNVMVVHPIW YTPAEPLTLY LRVKKPMEKG RLVVGRFARE FEDLVPSEML RVKISDRDLE GLDEIVVSVE EVN // ID Q9WZ59_THEMA Unreviewed; 557 AA. AC Q9WZ59; G4FDM9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=Cell division protein FtsI [Peptidoglycan synthetase] {ECO:0000313|EMBL:AGL49514.1}; DE EC=2.4.1.129 {ECO:0000313|EMBL:AGL49514.1}; DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:AAD35675.1}; GN OrderedLocusNames=TM_0590 {ECO:0000313|EMBL:AAD35675.1}; GN ORFNames=Tmari_0589 {ECO:0000313|EMBL:AGL49514.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35675.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35675.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35675.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49514.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49514.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35675.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49514.1; -; Genomic_DNA. DR PIR; G72356; G72356. DR RefSeq; NP_228400.1; NC_000853.1. DR RefSeq; WP_004081264.1; NZ_CP011107.1. DR STRING; 243274.TM0590; -. DR EnsemblBacteria; AAD35675; AAD35675; TM_0590. DR EnsemblBacteria; AGL49514; AGL49514; Tmari_0589. DR GeneID; 897662; -. DR KEGG; tma:TM0590; -. DR KEGG; tmi:THEMA_01710; -. DR KEGG; tmm:Tmari_0589; -. DR KEGG; tmw:THMA_0606; -. DR PATRIC; 23936095; VBITheMar51294_0601. DR eggNOG; ENOG4105CJN; Bacteria. DR eggNOG; COG0768; LUCA. DR KO; K05515; -. DR OMA; QIDEKIW; -. DR OrthoDB; EOG6N0HHV; -. DR BioCyc; TMAR243274:GC6P-615-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008658; F:penicillin binding; IEA:InterPro. DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR005311; PBP_dimer. DR InterPro; IPR001460; PCN-bd_Tpept. DR Pfam; PF03717; PBP_dimer; 1. DR Pfam; PF00905; Transpeptidase; 1. DR SUPFAM; SSF56519; SSF56519; 1. DR SUPFAM; SSF56601; SSF56601; 1. PE 4: Predicted; KW Cell cycle {ECO:0000313|EMBL:AGL49514.1}; KW Cell division {ECO:0000313|EMBL:AGL49514.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000313|EMBL:AGL49514.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49514.1}. FT DOMAIN 127 174 PBP_dimer. {ECO:0000259|Pfam:PF03717}. FT DOMAIN 209 537 Transpeptidase. FT {ECO:0000259|Pfam:PF00905}. SQ SEQUENCE 557 AA; 61900 MW; DCBF394417124A80 CRC64; MKNRLILILM ALSFVLIIMK AFQVQILEHE KHKKYIDLLQ TRLVKIPAPR GKIISSDGKV LAKDEVVYVL DPWLNSIDEL KKTGLFTPEE ILSLVKGESI VIDKARADVI SKAGMRVVMD YRRKYEPLAP HVVGYVNADR AGVYGVESVY DEFLTGTDGV KMVFVEPSGA ISSEVLRSPP KPGEDVTLTI DTRIQKVAEE SLEKIGNPGS VILSDVRTGE ILALASFPEY NPQDFYEGFT KREWERFARN SPSPLINRAI SSAYSPGSSI KILWAVAALL NGVDPEEKIN CRGVFEYRNS RGEVVARYRD WKEEGHGFTD LRKAIRVSCN VYFYQLGLKL GVDKMVEVAK KLSIFEKTGI DLPGEKSGTL PSPEWKMSKI GEPWYPGDTI LMSIGQGYLT ATPIELLKLV SLVANEGIFY RPHVVKRIGS KAVKPEIETQ VQIDEKIWNF IKDAMVDVTS FKGNEKEDPG TAYHVFGDFP YRVAGKTGTA EAGSGAPHSW FVGFAPAENP EVAIVVMVEH GGYGSGAASQ IARRVLEEYF KLKESAQETP VSSRSRD // ID Q9WZN9_THEMA Unreviewed; 334 AA. AC Q9WZN9; G4FD41; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Glycosidase, PH1107-related protein {ECO:0000313|EMBL:AGL49708.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35864.1}; GN OrderedLocusNames=TM_0782 {ECO:0000313|EMBL:AAD35864.1}; GN ORFNames=Tmari_0783 {ECO:0000313|EMBL:AGL49708.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35864.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35864.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35864.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49708.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49708.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35864.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49708.1; -; Genomic_DNA. DR PIR; G72332; G72332. DR RefSeq; NP_228591.1; NC_000853.1. DR RefSeq; WP_004080903.1; NZ_CP011107.1. DR STRING; 243274.TM0782; -. DR EnsemblBacteria; AAD35864; AAD35864; TM_0782. DR EnsemblBacteria; AGL49708; AGL49708; Tmari_0783. DR GeneID; 898450; -. DR KEGG; tma:TM0782; -. DR KEGG; tmi:THEMA_00740; -. DR KEGG; tmm:Tmari_0783; -. DR KEGG; tmw:THMA_0801; -. DR PATRIC; 23936486; VBITheMar51294_0795. DR eggNOG; ENOG41064R8; Bacteria. DR eggNOG; COG2152; LUCA. DR OMA; LFHRPHM; -. DR OrthoDB; EOG6M9DSP; -. DR BioCyc; TMAR243274:GC6P-809-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. DR Gene3D; 2.115.10.20; -; 1. DR InterPro; IPR023296; Glyco_hydro_beta-prop. DR InterPro; IPR007184; Mannoside_phosphorylase. DR Pfam; PF04041; Glyco_hydro_130; 1. DR PIRSF; PIRSF016202; PH1107; 1. DR SUPFAM; SSF75005; SSF75005; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000313|EMBL:AGL49708.1}; KW Hydrolase {ECO:0000313|EMBL:AGL49708.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 334 AA; 38254 MW; 93CD79683EFEA9FE CRC64; MVEELLGKAL ARKRSLRKDE TIDVFNRVTY FFPKDFVITN YPRNPVAVFN PGAVLVGKAL HVFPRLIFDY YKYVSSIGHF IVNIDDLLNG EVKKPLEMEV VFWPRDIQEF LGCEDPRVFF RNSRFELLYT AKGYKDWSQE GKPHTDFLAY AVLDEDLNLI EKRYISIKST LGEYVPVSMK DSSFVESKVI LTRLTVGDAK VCWRGRLEGS YIDLYSLDPV FFPEEWETKV GWSTNTVEVK EGYLVGWHAV LKDLTYKNGL ALVDGRGRLL GTTNYVLSPK GVIEEYGDRI RVIFGCGLVV YGGRVIWIGG VSDWAIGVFE TSEREIMNLM KEAT // ID Q9WZD1_THEMA Unreviewed; 522 AA. AC Q9WZD1; G4FDG1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35747.1}; GN OrderedLocusNames=TM_0663 {ECO:0000313|EMBL:AAD35747.1}; GN ORFNames=Tmari_0663 {ECO:0000313|EMBL:AGL49588.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35747.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35747.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35747.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49588.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49588.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35747.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49588.1; -; Genomic_DNA. DR PIR; D72349; D72349. DR RefSeq; NP_228472.1; NC_000853.1. DR RefSeq; WP_004081110.1; NZ_CP011107.1. DR STRING; 243274.TM0663; -. DR DNASU; 897777; -. DR EnsemblBacteria; AAD35747; AAD35747; TM_0663. DR EnsemblBacteria; AGL49588; AGL49588; Tmari_0663. DR GeneID; 897777; -. DR KEGG; tma:TM0663; -. DR KEGG; tmm:Tmari_0663; -. DR KEGG; tmw:THMA_0678; -. DR PATRIC; 23936240; VBITheMar51294_0673. DR eggNOG; ENOG41085DD; Bacteria. DR eggNOG; COG0595; LUCA. DR KO; K12574; -. DR OMA; VDHSIYG; -. DR OrthoDB; EOG6FRCZ8; -. DR BioCyc; TMAR243274:GC6P-688-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.60.15.10; -; 2. DR InterPro; IPR001279; Metallo-B-lactamas. DR SUPFAM; SSF56281; SSF56281; 4. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 522 AA; 60668 MW; D7A5E16AA88F79CC CRC64; MRIEIFDGHR NIGGNKIRVV DSENDGFLLD FGLNFSRWGE FFEEFLNPRT GKILHDLLKL KMVPRLNIYR DDLFDGKFED PVNHAFLFLS HAHADHTGMV GLIDEKIPLL MTGETFAVMR ASVYTSNSNV LTQLGGKKRR KVNDKDLENG IREDLTVSPG NSKNAEKLTR RVSFPKNIEF NDDLTVVDVN SLWKNELFVE PVYHSVIGAA GLAARVDDLW LAYTGDFRTG PETAEEERYW LDTLGEKRLA LSLRTSRFFE NLKDKRPLVL IVEGTRVTRE ENIENTEKDV FENAMRVFRG TKNLILVDFP IRHLERLFTF LKVCMENDRR LVLMPKDYAY LLEMERVEPL WKLTDEERSF VRVYHPGKVT YINLEKDALL RAREEGILLS PEEINLHPEK HTMVAGYWDF PHILDLDERV LNGAVYIHST SEAYTEEQEI DAKRFMNWLR YFNIIPFGIR EVNGNIVFTK EFHASGHVSP QGLEKILNEL NPDYIVPVHT LNPGWFVERW GERVLLENVI VL // ID Q9WZ81_THEMA Unreviewed; 39 AA. AC Q9WZ81; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 109. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35697.1}; DE SubName: Full=WD40 repeat-containing protein {ECO:0000313|EMBL:AGL49537.1}; GN OrderedLocusNames=TM_0612 {ECO:0000313|EMBL:AAD35697.1}; GN ORFNames=Tmari_0612 {ECO:0000313|EMBL:AGL49537.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35697.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35697.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35697.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49537.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49537.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35697.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49537.1; -; Genomic_DNA. DR PIR; H72355; H72355. DR RefSeq; NP_228422.1; NC_000853.1. DR RefSeq; WP_010865162.1; NZ_CP011107.1. DR STRING; 243274.TM0612; -. DR EnsemblBacteria; AAD35697; AAD35697; TM_0612. DR EnsemblBacteria; AGL49537; AGL49537; Tmari_0612. DR GeneID; 897695; -. DR KEGG; tma:TM0612; -. DR KEGG; tmi:THEMA_01605; -. DR KEGG; tmm:Tmari_0612; -. DR KEGG; tmw:THMA_0628; -. DR PATRIC; 23936137; VBITheMar51294_0622. DR OrthoDB; EOG6WX4WJ; -. DR BioCyc; TMAR243274:GC6P-637-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.130.10.10; -; 1. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR017986; WD40_repeat_dom. DR Pfam; PF00400; WD40; 1. DR SMART; SM00320; WD40; 1. DR SUPFAM; SSF50978; SSF50978; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Repeat {ECO:0000256|RuleBase:RU003532}; KW WD repeat {ECO:0000256|RuleBase:RU000362}. FT DOMAIN 5 39 WD_REPEATS_REGION. FT {ECO:0000259|PROSITE:PS50294}. SQ SEQUENCE 39 AA; 4404 MW; 4539E2AD33E55729 CRC64; MIKTLKEHTK IVRSVTFSPN GKYLAVGDIC GTVEIWRVL // ID Q9X271_THEMA Unreviewed; 324 AA. AC Q9X271; G4FGD5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 128. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36814.1}; DE SubName: Full=Oligopeptide transport ATP-binding protein OppD {ECO:0000313|EMBL:AGL50681.1}; GN OrderedLocusNames=TM_1749 {ECO:0000313|EMBL:AAD36814.1}; GN ORFNames=Tmari_1757 {ECO:0000313|EMBL:AGL50681.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36814.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36814.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36814.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50681.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50681.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36814.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50681.1; -; Genomic_DNA. DR PIR; H72215; H72215. DR RefSeq; NP_229547.1; NC_000853.1. DR RefSeq; WP_004082281.1; NZ_CP011107.1. DR STRING; 243274.TM1749; -. DR TCDB; 3.A.1.5.15; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36814; AAD36814; TM_1749. DR EnsemblBacteria; AGL50681; AGL50681; Tmari_1757. DR GeneID; 897864; -. DR KEGG; tma:TM1749; -. DR KEGG; tmi:THEMA_05490; -. DR KEGG; tmm:Tmari_1757; -. DR KEGG; tmw:THMA_1791; -. DR PATRIC; 23938474; VBITheMar51294_1767. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR KO; K02031; -. DR OMA; QINEAYR; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1797-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36814.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36814.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 5 255 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 324 AA; 36331 MW; 773591BD27DAF3AE CRC64; MMELLNVNNL KVEFHRVEGI VKAVDGISYK LNKGESLGIV GESGSGKSVS VLSLLRLINR NGRIVDGEAI FLGKDLLKLN KEELRNIRGK DISIIFQNPM TSLNPIIRVG IQVMEPIIWH RLMKNEEARE RAIELLERVG IPESPKRFLN YPFQFSGGMR QRVMIAMALA CHPKLLIADE PTTALDVTIQ AQIMELLQEL KEEYGMSVIF ITHDLSVATN FCDRIITMYA GKIVEEAPVE EILKTPLHPY TKGLLNSTLE IGSRGKKLVP IPGNPPNPTK HPSGCKFHPR CSFAMEICQR EEPPLVNISE NHRVACHLIK GESK // ID Q9X1Q1_THEMA Unreviewed; 433 AA. AC Q9X1Q1; G4FFV3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 126. DE RecName: Full=Signal recognition particle protein {ECO:0000256|HAMAP-Rule:MF_00306}; DE AltName: Full=Fifty-four homolog {ECO:0000256|HAMAP-Rule:MF_00306}; GN Name=ffh {ECO:0000256|HAMAP-Rule:MF_00306}; GN OrderedLocusNames=TM_1565 {ECO:0000313|EMBL:AAD36632.1}; GN ORFNames=Tmari_1573 {ECO:0000313|EMBL:AGL50497.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36632.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36632.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36632.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50497.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50497.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Binds to the hydrophobic CC signal sequence of the ribosome-nascent chain (RNC) as it emerges CC from the ribosomes. The SRP-RNC complex is then targeted to the CC cytoplasmic membrane where it interacts with the SRP receptor CC FtsY. {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. CC {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}. CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. CC {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- DOMAIN: Composed of three domains: the N-terminal N domain, which CC is responsible for interactions with the ribosome, the central G CC domain, which binds GTP, and the C-terminal M domain, which binds CC the RNA and the signal sequence of the RNC. {ECO:0000256|HAMAP- CC Rule:MF_00306}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00306}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36632.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50497.1; -; Genomic_DNA. DR PIR; F72236; F72236. DR RefSeq; NP_229365.1; NC_000853.1. DR RefSeq; WP_004081977.1; NZ_CP011107.1. DR SMR; Q9X1Q1; 362-423. DR STRING; 243274.TM1565; -. DR EnsemblBacteria; AAD36632; AAD36632; TM_1565. DR EnsemblBacteria; AGL50497; AGL50497; Tmari_1573. DR GeneID; 897963; -. DR KEGG; tma:TM1565; -. DR KEGG; tmi:THEMA_06455; -. DR KEGG; tmm:Tmari_1573; -. DR KEGG; tmw:THMA_1600; -. DR PATRIC; 23938092; VBITheMar51294_1583. DR eggNOG; ENOG4105CB9; Bacteria. DR eggNOG; COG0541; LUCA. DR KO; K03106; -. DR OMA; MLPGMGQ; -. DR OrthoDB; EOG62K1ZH; -. DR BioCyc; TMAR243274:GC6P-1606-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW. DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 1.10.260.30; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00306; SRP54; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004125; Signal_recog_particle_SRP54_M. DR InterPro; IPR022941; SRP54. DR InterPro; IPR000897; SRP54_GTPase_dom. DR InterPro; IPR004780; SRP_Ffh. DR PANTHER; PTHR11564:SF7; PTHR11564:SF7; 1. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR Pfam; PF02978; SRP_SPB; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SMART; SM00963; SRP54_N; 1. DR SUPFAM; SSF47446; SSF47446; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00959; ffh; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00306}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00306}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_00306}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00306}; KW Signal recognition particle {ECO:0000256|HAMAP-Rule:MF_00306}. FT DOMAIN 266 279 SRP54. {ECO:0000259|PROSITE:PS00300}. FT NP_BIND 106 113 GTP. {ECO:0000256|HAMAP-Rule:MF_00306}. FT NP_BIND 187 191 GTP. {ECO:0000256|HAMAP-Rule:MF_00306}. FT NP_BIND 245 248 GTP. {ECO:0000256|HAMAP-Rule:MF_00306}. SQ SEQUENCE 433 AA; 48701 MW; B907E982F4D29357 CRC64; MFENLQEKLS RVFKNLSGRG KITEKNVKDA IREVKLSLLE ADVNYKVVKE FVDHVLQKAL GEEVLRSLTP DQQFIKIVRD ELVRIMGEKN EPLRLVHRPA PIMMVGLQGS GKTTTCAKLA KLLKKEGRNP LLVAADLYRP AAVDQLVKLG NQIGVNVVHD YNKTPVEIVK EAVDVAESTG KDVLIVDTAG RLHIDEEMMK ELEEIKKILN PDEILLVVDA MMGQDAVNTA KVFDERLDLT GFVVTKMDGD ARGGVILSIK YVTGKPVKFI GTSEKLDGLE PFHPDRIANR ILGMGDVLSL IEKVEKELDQ EKMKKSAEKF LKAEFTLEDF KEQLQEMKKL GPLSSILEML PGAPKVDVEM SEKELKKIEA IINSMTIEER RNPGIINASR KRRIARGSGT TVQDVNKLLK SYEQMKALMK RMKKGRFKIP FGF // ID Q9WZE2_THEMA Unreviewed; 67 AA. AC Q9WZE2; G4FDE9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 75. DE SubName: Full=Flagellar protein FlbD {ECO:0000313|EMBL:AGL49600.1}; DE SubName: Full=Flagellar protein, putative {ECO:0000313|EMBL:AAD35758.1}; GN OrderedLocusNames=TM_0675 {ECO:0000313|EMBL:AAD35758.1}; GN ORFNames=Tmari_0675 {ECO:0000313|EMBL:AGL49600.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35758.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35758.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35758.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49600.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49600.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35758.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49600.1; -; Genomic_DNA. DR PIR; A72347; A72347. DR RefSeq; NP_228483.1; NC_000853.1. DR RefSeq; WP_004081092.1; NZ_CP011107.1. DR STRING; 243274.TM0675; -. DR EnsemblBacteria; AAD35758; AAD35758; TM_0675. DR EnsemblBacteria; AGL49600; AGL49600; Tmari_0675. DR GeneID; 898343; -. DR KEGG; tma:TM0675; -. DR KEGG; tmi:THEMA_01290; -. DR KEGG; tmm:Tmari_0675; -. DR KEGG; tmw:THMA_0690; -. DR PATRIC; 23936266; VBITheMar51294_0686. DR eggNOG; ENOG41068WV; Bacteria. DR eggNOG; COG1582; LUCA. DR KO; K02385; -. DR OMA; MIKVTTR; -. DR OrthoDB; EOG68H8F3; -. DR BioCyc; TMAR243274:GC6P-700-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR InterPro; IPR009384; FlbD. DR Pfam; PF06289; FlbD; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AAD35758.1}; KW Cilium {ECO:0000313|EMBL:AAD35758.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35758.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 67 AA; 8043 MW; 8D148E6BDC2E9DDF CRC64; MIRLTRIDGR WFFLNADLIE TVEALPDTTI TLINGKKYIV KESAEEVVQR VIEYKRKIFS WWKEQGR // ID Q9X1L9_THEMA Unreviewed; 92 AA. AC Q9X1L9; G4FFS1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 100. DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:AAD36600.1}; DE SubName: Full=Ferredoxin-like protein {ECO:0000313|EMBL:AGL50465.1}; GN OrderedLocusNames=TM_1533 {ECO:0000313|EMBL:AAD36600.1}; GN ORFNames=Tmari_1541 {ECO:0000313|EMBL:AGL50465.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36600.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36600.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36600.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50465.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50465.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36600.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50465.1; -; Genomic_DNA. DR PIR; A72242; A72242. DR RefSeq; NP_229333.1; NC_000853.1. DR RefSeq; WP_004081910.1; NZ_CP011107.1. DR STRING; 243274.TM1533; -. DR EnsemblBacteria; AAD36600; AAD36600; TM_1533. DR EnsemblBacteria; AGL50465; AGL50465; Tmari_1541. DR GeneID; 897627; -. DR KEGG; tma:TM1533; -. DR KEGG; tmi:THEMA_06620; -. DR KEGG; tmm:Tmari_1541; -. DR KEGG; tmw:THMA_1567; -. DR PATRIC; 23938026; VBITheMar51294_1551. DR eggNOG; ENOG4105WQV; Bacteria. DR eggNOG; COG2440; LUCA. DR KO; K03855; -. DR OMA; ECGSCRI; -. DR OrthoDB; EOG6XSZQF; -. DR BioCyc; TMAR243274:GC6P-1573-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR007859; ETFD_OxRdtase/FixX. DR InterPro; IPR012206; Fd_FixX. DR Pfam; PF05187; ETF_QO; 1. DR PIRSF; PIRSF036548; Fdx_FixX; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 19 51 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 52 81 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 92 AA; 10717 MW; F515B0F992B7E4C1 CRC64; MRIEDKLYLN RYRTDEENPH LKIKDESICA EKCSDRPCVS CCPADVYEWT ESGMEVKFEG CLECGTCRIV CPFGNIEWNY PRGNYGVLYK FG // ID Q9X2H1_THEMA Unreviewed; 328 AA. AC Q9X2H1; G4FGP8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 101. DE SubName: Full=Transcriptional regulator, LacI family {ECO:0000313|EMBL:AAD36918.1}; GN OrderedLocusNames=TM_1856 {ECO:0000313|EMBL:AAD36918.1}; GN ORFNames=Tmari_1871 {ECO:0000313|EMBL:AGL50795.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36918.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36918.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36918.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50795.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50795.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains HTH lacI-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00590899}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36918.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50795.1; -; Genomic_DNA. DR PIR; A72204; A72204. DR RefSeq; NP_229652.1; NC_000853.1. DR RefSeq; WP_004082407.1; NZ_CP011107.1. DR STRING; 243274.TM1856; -. DR EnsemblBacteria; AAD36918; AAD36918; TM_1856. DR EnsemblBacteria; AGL50795; AGL50795; Tmari_1871. DR GeneID; 897806; -. DR KEGG; tma:TM1856; -. DR KEGG; tmi:THEMA_04890; -. DR KEGG; tmm:Tmari_1871; -. DR KEGG; tmw:THMA_1906; -. DR PATRIC; 23938701; VBITheMar51294_1877. DR eggNOG; ENOG4108M8T; Bacteria. DR eggNOG; COG1609; LUCA. DR KO; K02529; -. DR OMA; MEHLYGL; -. DR OrthoDB; EOG6SJJMM; -. DR BioCyc; TMAR243274:GC6P-1907-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR000843; Tscrpt_reg_HTH_LacI. DR Pfam; PF00356; LacI; 1. DR PRINTS; PR00036; HTHLACI. DR SMART; SM00354; HTH_LACI; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF53822; SSF53822; 1. DR PROSITE; PS00356; HTH_LACI_1; 1. DR PROSITE; PS50932; HTH_LACI_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00590989}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00590865}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00590865}. FT DOMAIN 2 56 HTH lacI-type DNA-binding. FT {ECO:0000259|PROSITE:PS50932}. SQ SEQUENCE 328 AA; 36974 MW; 20EC4EE815FF2245 CRC64; MPTIEDVAKL AGVSIATVSR VINGSGYVSE KTRYKVWKAI EELGYKPEIS AKLLASKGKL FNIYVFASKR ILSPLQNNGI LGEFYGVIIR AIEENCGRLG MNVELKMLEN FSESNGADGY IFIGGDLSEK TLKEIKSRKK PFVLVDHYIP GERVDCVISD GYDGAVYATN YLISKGFKRI VHVHGPLHPY GFKMRYDGYK DAMEKAGLMP RFYECDDTEE GTRKVIDIML NSYGTPEAIF TSNDSIAFWV IKRLKEHNIK VPDDVSVIGF DDIVDAENFD PPLTTLRVFK YEMGCLACKR LHELLTGINP HPVRILVFTQ FVKRKSTK // ID Q9WZE9_THEMA Unreviewed; 205 AA. AC Q9WZE9; G4FDE1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Membrane metalloprotease {ECO:0000313|EMBL:AGL49608.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35765.1}; GN OrderedLocusNames=TM_0683 {ECO:0000313|EMBL:AAD35765.1}; GN ORFNames=Tmari_0683 {ECO:0000313|EMBL:AGL49608.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35765.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35765.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35765.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49608.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49608.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35765.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49608.1; -; Genomic_DNA. DR PIR; H72347; H72347. DR RefSeq; NP_228492.1; NC_000853.1. DR RefSeq; WP_004081080.1; NZ_CP011107.1. DR STRING; 243274.TM0683; -. DR EnsemblBacteria; AAD35765; AAD35765; TM_0683. DR EnsemblBacteria; AGL49608; AGL49608; Tmari_0683. DR GeneID; 898350; -. DR KEGG; tma:TM0683; -. DR KEGG; tmi:THEMA_01250; -. DR KEGG; tmm:Tmari_0683; -. DR KEGG; tmw:THMA_0698; -. DR PATRIC; 23936284; VBITheMar51294_0695. DR eggNOG; ENOG4108Z4T; Bacteria. DR eggNOG; COG1994; LUCA. DR OMA; WFSKMER; -. DR OrthoDB; EOG6WHNQN; -. DR BioCyc; TMAR243274:GC6P-709-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49608.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metalloprotease {ECO:0000313|EMBL:AGL49608.1}; KW Protease {ECO:0000313|EMBL:AGL49608.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 115 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 165 185 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 205 AA; 23609 MW; A5A22D826840402B CRC64; MVNMRIIVPT LGNILTGFLA VLIVATPREY IKGFVAYKLG DTTPKQAGRL SLNPFVHLDP LGTISFILFE FGWTRSVPIR YWKLKNKKKD LLKISLLGPA VSFILFFLCG LIASHLPEED FWWFLMVKAA KYNLTYALFS LFPIPPLDGS KILASLLPDR YMEWLVKYEV YGVLFMIALL VLWIIPLVMN PFVRFIDGFV WMIVR // ID Q9X0R1_THEMA Unreviewed; 137 AA. AC Q9X0R1; G4FEG7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 84. DE RecName: Full=Flagellar protein FliS {ECO:0000256|PIRNR:PIRNR039090}; GN OrderedLocusNames=TM_1179 {ECO:0000313|EMBL:AAD36254.1}; GN ORFNames=Tmari_1186 {ECO:0000313|EMBL:AGL50110.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36254.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36254.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36254.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50110.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50110.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000256|PIRNR:PIRNR039090}. CC -!- SIMILARITY: Belongs to the FliS family. CC {ECO:0000256|PIRNR:PIRNR039090}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36254.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50110.1; -; Genomic_DNA. DR PIR; F72286; F72286. DR RefSeq; NP_228984.1; NC_000853.1. DR RefSeq; WP_004080180.1; NZ_CP011107.1. DR STRING; 243274.TM1179; -. DR EnsemblBacteria; AAD36254; AAD36254; TM_1179. DR EnsemblBacteria; AGL50110; AGL50110; Tmari_1186. DR GeneID; 898307; -. DR KEGG; tma:TM1179; -. DR KEGG; tmi:THEMA_08440; -. DR KEGG; tmm:Tmari_1186; -. DR KEGG; tmw:THMA_1204; -. DR PATRIC; 23937298; VBITheMar51294_1197. DR eggNOG; ENOG4105MQ3; Bacteria. DR eggNOG; COG1516; LUCA. DR KO; K02422; -. DR OMA; AQSRYAI; -. DR OrthoDB; EOG6N687W; -. DR BioCyc; TMAR243274:GC6P-1208-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:InterPro. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW. DR Gene3D; 1.20.120.340; -; 1. DR InterPro; IPR003713; FliS. DR Pfam; PF02561; FliS; 1. DR PIRSF; PIRSF039090; Flis; 1. DR SUPFAM; SSF101116; SSF101116; 1. DR TIGRFAMs; TIGR00208; fliS; 1. PE 3: Inferred from homology; KW Bacterial flagellum biogenesis {ECO:0000256|PIRNR:PIRNR039090}; KW Cell projection {ECO:0000313|EMBL:AAD36254.1}; KW Cilium {ECO:0000313|EMBL:AAD36254.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR039090}; KW Flagellum {ECO:0000313|EMBL:AAD36254.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 137 AA; 15696 MW; 5C32FA748CCD4C6B CRC64; MKENTYLEKM VMTASPAKLV QMLYEKAVEV LKEAENLLAD KKFVEFNEKV TRAQDIITEL NLSLDMEKGG TIAQNLRALY NYMFQRLVEG NVKKDVEKIR EVRGMLEELL EVWKEAMKKA GNVTPPEKKQ GGLNLMG // ID Q9X1L0_THEMA Unreviewed; 236 AA. AC Q9X1L0; G4FFQ9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=Diaminopimelate epimerase {ECO:0000256|SAAS:SAAS00316707}; DE EC=5.1.1.7 {ECO:0000256|SAAS:SAAS00316689}; GN OrderedLocusNames=TM_1522 {ECO:0000313|EMBL:AAD36589.1}; GN ORFNames=Tmari_1530 {ECO:0000313|EMBL:AGL50454.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36589.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36589.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36589.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50454.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50454.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6- CC diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso- CC DAP), a precursor of L-lysine and an essential component of the CC bacterial peptidoglycan. {ECO:0000256|SAAS:SAAS00351434}. CC -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso- CC diaminoheptanedioate. {ECO:0000256|SAAS:SAAS00316693}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step CC 1/1. {ECO:0000256|SAAS:SAAS00316687}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00316708}. CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family. CC {ECO:0000256|SAAS:SAAS00583234}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36589.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50454.1; -; Genomic_DNA. DR PIR; C72246; C72246. DR RefSeq; NP_229322.1; NC_000853.1. DR RefSeq; WP_004081881.1; NZ_CP011107.1. DR STRING; 243274.TM1522; -. DR DNASU; 897985; -. DR EnsemblBacteria; AAD36589; AAD36589; TM_1522. DR EnsemblBacteria; AGL50454; AGL50454; Tmari_1530. DR GeneID; 897985; -. DR KEGG; tma:TM1522; -. DR KEGG; tmi:THEMA_06690; -. DR KEGG; tmm:Tmari_1530; -. DR KEGG; tmw:THMA_1554; -. DR PATRIC; 23938002; VBITheMar51294_1539. DR eggNOG; ENOG410812M; Bacteria. DR eggNOG; COG0253; LUCA. DR KO; K01778; -. DR OMA; AKYCASG; -. DR OrthoDB; EOG6ND0M5; -. DR BioCyc; TMAR243274:GC6P-1562-MONOMER; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway. DR InterPro; IPR018510; DAP_epimerase_AS. DR InterPro; IPR001653; DAP_epimerase_DapF. DR PANTHER; PTHR31689; PTHR31689; 1. DR Pfam; PF01678; DAP_epimerase; 2. DR TIGRFAMs; TIGR00652; DapF; 1. DR PROSITE; PS01326; DAP_EPIMERASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS00429562}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00429534}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00429665}; KW Isomerase {ECO:0000256|SAAS:SAAS00475366, KW ECO:0000313|EMBL:AGL50454.1}; KW Lysine biosynthesis {ECO:0000256|SAAS:SAAS00429562}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 236 AA; 26874 MW; A14E28EF7AEAE201 CRC64; MCYSANGNTF LIVDNTQKRI PEEKKPDFVR ENVGDLDGVI FVELVDGKYF MDYYNRDGSM AAFCGNGARA FSQYLIDRGW IKEKEFTFLS RAGEIKVIVD DSIWVRMPGV SEKKEMKVDG YEGYFVVVGV PHFVMEVKGI DELDVEKLGR DLRYKTGANV DFYEVLPDRL KVRTYERGVE RETKACGTGV TSVFVVYRDK TGAKEVKIQV PGGTLFLKEE NGEIFLRGDV KRCSEE // ID Q9WYY9_THEMA Unreviewed; 309 AA. AC Q9WYY9; G4FDV2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 85. DE SubName: Full=GAF domain-containing protein {ECO:0000313|EMBL:AGL49440.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35604.1}; GN OrderedLocusNames=TM_0519 {ECO:0000313|EMBL:AAD35604.1}; GN ORFNames=Tmari_0515 {ECO:0000313|EMBL:AGL49440.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35604.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35604.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35604.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49440.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49440.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35604.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49440.1; -; Genomic_DNA. DR PIR; E72365; E72365. DR RefSeq; NP_228329.1; NC_000853.1. DR RefSeq; WP_004081407.1; NZ_CP011107.1. DR STRING; 243274.TM0519; -. DR EnsemblBacteria; AAD35604; AAD35604; TM_0519. DR EnsemblBacteria; AGL49440; AGL49440; Tmari_0515. DR GeneID; 897570; -. DR KEGG; tma:TM0519; -. DR KEGG; tmi:THEMA_02080; -. DR KEGG; tmm:Tmari_0515; -. DR KEGG; tmw:THMA_0531; -. DR PATRIC; 23935943; VBITheMar51294_0526. DR eggNOG; ENOG4108ZGC; Bacteria. DR eggNOG; COG1956; LUCA. DR KO; K07170; -. DR OMA; SKETNYL; -. DR OrthoDB; EOG6QP15Z; -. DR BioCyc; TMAR243274:GC6P-543-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.30.450.40; -; 1. DR InterPro; IPR003018; GAF. DR InterPro; IPR029016; GAF_dom-like. DR Pfam; PF01590; GAF; 1. DR SMART; SM00065; GAF; 1. DR SUPFAM; SSF55781; SSF55781; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 180 309 GAF. {ECO:0000259|SMART:SM00065}. SQ SEQUENCE 309 AA; 36182 MW; 7ACE8E89CA2D2524 CRC64; MRSIVQNKVE ECLEILKWDK TKWIDFWREL RRKFGPIVPN YERKLELNDE KIEKILREIE RRELDRFKWD WLDVSRNKKI ECAESLSERE DFLDLKREDF SVFLMSLLGL SDWVVVDGEK EKIVVMDVFS LWRKGLLREL SLATLHAVIE FRKGKEIGNY GGKKEYFDSL LKEIEKILKR GKEALGDLCE FLRNHVSYYD WVGFYFVEDG KLKLGPFVGE PTEHVEIPFG VGICGQAAER EETFVVQDVS KETNYLSCSP KTKAEIVVPI FKDGKIIGEL DIDSYSPSPF SEEDRAFLEK VCELVSKVV // ID Q9WXP1_THEMA Unreviewed; 357 AA. AC Q9WXP1; G4FGV1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 100. DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:AGL48957.1}; DE SubName: Full=Iron-sulfur cluster-binding protein {ECO:0000313|EMBL:AAD35128.1}; GN OrderedLocusNames=TM_0034 {ECO:0000313|EMBL:AAD35128.1}; GN ORFNames=Tmari_0031 {ECO:0000313|EMBL:AGL48957.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35128.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35128.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35128.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48957.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48957.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35128.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48957.1; -; Genomic_DNA. DR PIR; G72424; G72424. DR RefSeq; NP_227850.1; NC_000853.1. DR RefSeq; WP_004082494.1; NZ_CP011107.1. DR STRING; 243274.TM0034; -. DR EnsemblBacteria; AAD35128; AAD35128; TM_0034. DR EnsemblBacteria; AGL48957; AGL48957; Tmari_0031. DR GeneID; 896855; -. DR KEGG; tma:TM0034; -. DR KEGG; tmi:THEMA_04630; -. DR KEGG; tmm:Tmari_0031; -. DR KEGG; tmw:THMA_0030; -. DR PATRIC; 23934908; VBITheMar51294_0032. DR eggNOG; ENOG4105E44; Bacteria. DR eggNOG; COG2768; LUCA. DR KO; K07138; -. DR OMA; GCGRCIG; -. DR OrthoDB; EOG6FFS38; -. DR BioCyc; TMAR243274:GC6P-34-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR007160; DUF362. DR Pfam; PF04015; DUF362; 1. DR Pfam; PF00037; Fer4; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|RuleBase:RU003429}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|RuleBase:RU003429}; KW Iron-sulfur {ECO:0000256|RuleBase:RU003429}; KW Metal-binding {ECO:0000256|RuleBase:RU003429}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 186 215 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 216 243 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 357 AA; 38995 MW; 6A22F68149293BCE CRC64; MPAKVYFTDM TTNPNMNMLQ KLELLLKKVE LEKIIEKDKF VAVKLHFGEY GNLAFIRPQY VKIIVDQIKK LGGKPFLTDA NTLYTGHRSN AVDHLINAYL NGFTYEVTGA PVIIADGLRG SDEIKVKIDG NYVKEAKIGA AIALADAIVA VTHFKGHEAT GFGGTIKNVG MGSASRAGKM EQHSESKPYV VEEKCVACGT CAKFCPVGAI TVTKVAKIDY EKCIGCGQCI AMCSYGAMSP KWDSSTDSLS KKMAEYAKAV LKDKKAVFIS FIMNISPDCD CWNMNKPPVA PDIGIAVSTD PVALDQACID LVLQKTGKDP FLEVHPDVTW KTQLEYAEEI GLGTREYELV KVACDLK // ID Q9WY41_THEMA Unreviewed; 820 AA. AC Q9WY41; G4FHB2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 113. DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:AGL49122.1}; DE SubName: Full=ATP-dependent Clp protease, ATPase subunit {ECO:0000313|EMBL:AAD35290.1}; GN OrderedLocusNames=TM_0198 {ECO:0000313|EMBL:AAD35290.1}; GN ORFNames=Tmari_0196 {ECO:0000313|EMBL:AGL49122.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35290.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35290.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35290.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49122.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49122.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. CC {ECO:0000256|RuleBase:RU004432}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35290.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49122.1; -; Genomic_DNA. DR PIR; H72404; H72404. DR RefSeq; NP_228013.1; NC_000853.1. DR RefSeq; WP_004082850.1; NZ_CP011107.1. DR SMR; Q9WY41; 163-355. DR STRING; 243274.TM0198; -. DR EnsemblBacteria; AAD35290; AAD35290; TM_0198. DR EnsemblBacteria; AGL49122; AGL49122; Tmari_0196. DR GeneID; 897068; -. DR KEGG; tma:TM0198; -. DR KEGG; tmi:THEMA_03740; -. DR KEGG; tmm:Tmari_0196; -. DR KEGG; tmw:THMA_0205; -. DR PATRIC; 23935268; VBITheMar51294_0200. DR eggNOG; ENOG4105C2Z; Bacteria. DR eggNOG; COG0542; LUCA. DR KO; K03696; -. DR OMA; HIREEIN; -. DR OrthoDB; EOG65F8SM; -. DR BioCyc; TMAR243274:GC6P-211-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.1780.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004176; Clp_N. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR018368; ClpA/B_CS1. DR InterPro; IPR028299; ClpA/B_CS2. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00004; AAA; 1. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF02861; Clp_N; 2. DR Pfam; PF10431; ClpB_D2-small; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 2. DR SMART; SM01086; ClpB_D2-small; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF81923; SSF81923; 1. DR PROSITE; PS00870; CLPAB_1; 1. DR PROSITE; PS00871; CLPAB_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00463698, ECO:0000313|EMBL:AGL49122.1}; KW Chaperone {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00480820}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD35290.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00463698, ECO:0000313|EMBL:AGL49122.1}; KW Protease {ECO:0000313|EMBL:AAD35290.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Repeat {ECO:0000256|SAAS:SAAS00417491}. FT DOMAIN 203 346 AAA. {ECO:0000259|SMART:SM00382}. FT DOMAIN 540 711 AAA. {ECO:0000259|SMART:SM00382}. FT DOMAIN 719 808 ClpB_D2-small. FT {ECO:0000259|SMART:SM01086}. FT COILED 435 462 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 820 AA; 93593 MW; 9DC3AD88F7A78E35 CRC64; MFDKFSEKTA QIFVTAQEEA KELGHSYVGT EHLLLAILKV DRSPAVELLE EMGASYSKVR SEIISMVGMG MRGFVPSPQM TPRAKRVTEL AYEEAKILGS DKINPEHLLL GILREGEGIA IHILRKLGVD IATLRREIID IYSYSSNKNL EYEEEEDYTY RSVKQLEGFG VNLTELAAKK ELDPVIGREE EIERVMQVLV RRKKNNPVLI GDPGVGKTAI VEGLAQRIVA GDVPEILKNK VIFSLDVAAL VAGTKYRGEF EKRMKKLLQI VTKDKNIILF IDEIHTIVGA GSAEGAIDAA NILKPALARG EISCIGATTP DEYRRYIEKD AALERRFQKI YVKEPTEEET LEILKGLKRK YEAHHKVIYT DKALEAAVYL SKRYITDHYL PDKAIDVIDE AGARARLKVF VLPPELKDMK LELERIRSDK ELAVLNQDYE KAAQLKEEEM ELEAEYRKRY AEWRRRAETA VVKVDVDDVA EVVSSWTGVP LRKIEETEVE KLLNLEEALH QRIVAQDEAI KAVARAIRRA RSGLKDPRRP IGVFLFLGPT GVGKTELAKA LAEYLFGDER ALIRFDMSEY MERFSVSRLI GAPPGYVGYE EGGTLTEKVR RRPFSVILFD EIEKAHPDVF NILLQIMDDG RLTDSQGREV DFRNTIIIMT SNIGSSYINK SKRTLGFVGD NNEEKEFEKI KDLVLEEVKR TFRPEFLNRI DETIIFHPLK KEHIEQIIDI LLRDLRKRLS EKNMKLVLTK SAKEFLVEKG FDPVYGARPL KRAIQRYVED PLSEEILRGK FNEGDTIVCR ARKDALRFTR KGEKKEKVVQ // ID Q9S5X6_THEMA Unreviewed; 326 AA. AC Q9S5X6; G4FEF2; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 11-MAY-2016, entry version 122. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36269.1}; DE SubName: Full=Xylobiose ABC transport system, ATP-binding protein 1 {ECO:0000313|EMBL:AGL50125.1}; GN OrderedLocusNames=TM_1194 {ECO:0000313|EMBL:AAD36269.1}; GN ORFNames=Tmari_1201 {ECO:0000313|EMBL:AGL50125.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36269.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36269.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36269.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50125.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50125.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36269.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50125.1; -; Genomic_DNA. DR PIR; G72283; G72283. DR RefSeq; NP_228999.1; NC_000853.1. DR RefSeq; WP_004080134.1; NZ_CP011107.1. DR STRING; 243274.TM1194; -. DR EnsemblBacteria; AAD36269; AAD36269; TM_1194. DR EnsemblBacteria; AGL50125; AGL50125; Tmari_1201. DR GeneID; 898290; -. DR KEGG; tma:TM1194; -. DR KEGG; tmi:THEMA_08360; -. DR KEGG; tmm:Tmari_1201; -. DR KEGG; tmw:THMA_1220; -. DR PATRIC; 23937330; VBITheMar51294_1212. DR KO; K02031; -. DR OMA; TTRMAIM; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1224-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36269.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36269.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 13 261 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 326 AA; 36399 MW; 0767A30901F9E6D1 CRC64; METLISGKNL KAYYVLDLWG SKKVVKAVDN VSLDILPNEI YGIAGESGCG KSTLLKALLA LLDPPLRLMD GELLYNIEGR PTNVTLLKSE TIRKLRWSFI SYIPQGSMHV LNPVKRVRDT FIEILSSHVK KQTKEFLDLA VQHLKDLGLP ERVLNMFPHQ LSGGMRQRVT IALATVLKPR VIFADEPTTA LDVVAQRAVM QLIRKIQNDL KNTVVLVTHD MGVHAQITTR MAIMYAGKIV EEGPTLEIFK NPLHPYTRYL IQSLPAIGDK KLRSGIPGSP PSLVAPPPGC RFHPRCPHAS QRCREEEPLL KEIKPGHKVA CFLMEG // ID Q9WXT7_THEMA Unreviewed; 304 AA. AC Q9WXT7; G4FGZ7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 97. DE SubName: Full=Flagellar hook-associated protein 3 {ECO:0000313|EMBL:AAD35176.1}; DE SubName: Full=Flagellar hook-associated protein FlgL {ECO:0000313|EMBL:AGL49005.1}; GN OrderedLocusNames=TM_0082 {ECO:0000313|EMBL:AAD35176.1}; GN ORFNames=Tmari_0079 {ECO:0000313|EMBL:AGL49005.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35176.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35176.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35176.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49005.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49005.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the bacterial flagellin family. CC {ECO:0000256|SAAS:SAAS00588699}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35176.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49005.1; -; Genomic_DNA. DR PIR; D72419; D72419. DR RefSeq; NP_227898.1; NC_000853.1. DR RefSeq; WP_004082608.1; NZ_CP011107.1. DR STRING; 243274.TM0082; -. DR EnsemblBacteria; AAD35176; AAD35176; TM_0082. DR EnsemblBacteria; AGL49005; AGL49005; Tmari_0079. DR GeneID; 896909; -. DR KEGG; tma:TM0082; -. DR KEGG; tmi:THEMA_04395; -. DR KEGG; tmm:Tmari_0079; -. DR KEGG; tmw:THMA_0078; -. DR PATRIC; 23935004; VBITheMar51294_0080. DR eggNOG; ENOG4105DTJ; Bacteria. DR eggNOG; COG1344; LUCA. DR KO; K02397; -. DR OMA; EYIFSGY; -. DR OrthoDB; EOG6X9MHB; -. DR BioCyc; TMAR243274:GC6P-82-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009424; C:bacterial-type flagellum hook; IEA:InterPro. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR Gene3D; 1.20.1330.10; -; 1. DR InterPro; IPR013384; Flagell_FlgL. DR InterPro; IPR001029; Flagellin_D0/D1. DR Pfam; PF00669; Flagellin_N; 1. DR TIGRFAMs; TIGR02550; flagell_flgL; 1. PE 3: Inferred from homology; KW Bacterial flagellum {ECO:0000256|SAAS:SAAS00482835}; KW Cell projection {ECO:0000313|EMBL:AAD35176.1}; KW Cilium {ECO:0000313|EMBL:AAD35176.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35176.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 6 138 Flagellin_D0/D1. FT {ECO:0000259|Pfam:PF00669}. SQ SEQUENCE 304 AA; 34334 MW; 5295A61508D50649 CRC64; MRVTNKMISD RVLFNIQTSL KRIAKLHDQL SSGYKVRYPS DDAVVAKRAS DILTRKRELE QFQRSVDHVQ TYVNAYDSAL QTVSSITQRL RELLVRAANG TLSKAEREAI AEEIDKIKEN LVEVANTRIG NEYIFSGYDV FSQPVENENG IWKISTLPAS NKSRSILVLG HSIDYGVTAS EVFELDSGKN VFQMLEEVSA TLRSNLNETQ ISERVSNVFL KELSSFEERI TKTIGKVGGV SRFIDMVNSR VQDLDFFFTE YLSKERDADI TELVTDLAMQ QSVLEAALKS ASRVLQATLV DFVR // ID Q9WZL3_THEMA Unreviewed; 358 AA. AC Q9WZL3; G4FD69; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 120. DE SubName: Full=Nitrite reductase probable [NAD(P)H] subunit {ECO:0000313|EMBL:AGL49680.1}; DE EC=1.7.1.4 {ECO:0000313|EMBL:AGL49680.1}; DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AAD35836.1}; GN OrderedLocusNames=TM_0754 {ECO:0000313|EMBL:AAD35836.1}; GN ORFNames=Tmari_0755 {ECO:0000313|EMBL:AGL49680.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35836.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35836.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35836.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49680.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49680.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35836.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49680.1; -; Genomic_DNA. DR PIR; H72337; H72337. DR RefSeq; NP_228563.1; NC_000853.1. DR RefSeq; WP_004080954.1; NZ_CP011107.1. DR SMR; Q9WZL3; 2-350. DR STRING; 243274.TM0754; -. DR EnsemblBacteria; AAD35836; AAD35836; TM_0754. DR EnsemblBacteria; AGL49680; AGL49680; Tmari_0755. DR GeneID; 898422; -. DR KEGG; tma:TM0754; -. DR KEGG; tmi:THEMA_00880; -. DR KEGG; tmm:Tmari_0755; -. DR KEGG; tmw:THMA_0773; -. DR PATRIC; 23936430; VBITheMar51294_0767. DR eggNOG; ENOG4108I5Y; Bacteria. DR eggNOG; COG0446; LUCA. DR KO; K00362; -. DR KO; K00540; -. DR OMA; IVGNGPG; -. DR OrthoDB; EOG6QVRCJ; -. DR BioCyc; TMAR243274:GC6P-781-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-EC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00469; PNDRDTASEII. DR SUPFAM; SSF51905; SSF51905; 1. DR SUPFAM; SSF55424; SSF55424; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49680.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 279 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. SQ SEQUENCE 358 AA; 40200 MW; D1410E7557525074 CRC64; MKVVIVGNGP GGVELAKQLS EEHEVTIVER ETVPYYTKPM LSHYVAGLAE EKSLFPYPID WYEKKGIKLL LGTTAKRIDA EKKVLETDRG TLEYDVLVLA TGAKPRTLKI PGWERMYTLR TIEDAKRLKG AVEREKDLLI IGGGFIGLEI AGNLSKQGIK VKVVEKMTRL MGLDEELTER IKGELEKHGV EFYLGRDVER IENDVLVTDK EEIPARVILC SIGIVPEVSL AKESGLDVNR GILVDKTFRT SKPDIYAIGD CAEHEGIICG TAKAAMAHAK VLANTLKGIP DEYDFHFRSS YFKFGDFPIA IVGELTDRGE WIDSETKSFY RDEKIVGVVV LSDVRKAREW EERLRSTR // ID Q9WZE5_THEMA Unreviewed; 169 AA. AC Q9WZE5; G4FDE6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 79. DE SubName: Full=Flagellar protein, putative {ECO:0000313|EMBL:AAD35761.1}; GN OrderedLocusNames=TM_0678 {ECO:0000313|EMBL:AAD35761.1}; GN ORFNames=Tmari_0678 {ECO:0000313|EMBL:AGL49603.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35761.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35761.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35761.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49603.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49603.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35761.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49603.1; -; Genomic_DNA. DR PIR; D72347; D72347. DR RefSeq; NP_228486.1; NC_000853.1. DR RefSeq; WP_004081086.1; NZ_CP011107.1. DR STRING; 243274.TM0678; -. DR EnsemblBacteria; AAD35761; AAD35761; TM_0678. DR EnsemblBacteria; AGL49603; AGL49603; Tmari_0678. DR GeneID; 898346; -. DR KEGG; tma:TM0678; -. DR KEGG; tmi:THEMA_01275; -. DR KEGG; tmm:Tmari_0678; -. DR KEGG; tmw:THMA_0693; -. DR PATRIC; 23936272; VBITheMar51294_0689. DR eggNOG; ENOG4105HRX; Bacteria. DR eggNOG; COG1580; LUCA. DR KO; K02415; -. DR OMA; NDEIMDA; -. DR OrthoDB; EOG67DPPD; -. DR BioCyc; TMAR243274:GC6P-703-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR GO; GO:0006935; P:chemotaxis; IEA:InterPro. DR InterPro; IPR005503; FliL. DR Pfam; PF03748; FliL; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AAD35761.1}; KW Cilium {ECO:0000313|EMBL:AAD35761.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35761.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 42 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 169 AA; 18687 MW; C8B15D4B14961FAD CRC64; MAEEERREEE QPKRRMGASL ITSIVVPLVV SVAVYFLLPM FLGSNQGKQG ENVPSTPVRI KAVLIQQGEN QTFLLKGGRD VVVIDSLSFS VGSDACRAAI AERKDEIMDA LMMIFLSKDK SELSTVPGLE LLKRQIRDAV NTITGFVGDK EKYGVLDVYL YIKAFATTE // ID Q9WZU7_THEMA Unreviewed; 304 AA. AC Q9WZU7; G4FCY1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Formiminotransferase-cyclodeaminase/formiminotetrahydrofolate cyclodeaminase, putative {ECO:0000313|EMBL:AAD35925.1}; DE SubName: Full=Glutamate formiminotransferase / Glutamate formyltransferase {ECO:0000313|EMBL:AGL49770.1}; DE EC=2.1.2.5 {ECO:0000313|EMBL:AGL49770.1}; GN OrderedLocusNames=TM_0843 {ECO:0000313|EMBL:AAD35925.1}; GN ORFNames=Tmari_0845 {ECO:0000313|EMBL:AGL49770.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35925.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35925.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35925.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49770.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49770.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35925.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49770.1; -; Genomic_DNA. DR PIR; D72326; D72326. DR RefSeq; NP_228652.1; NC_000853.1. DR RefSeq; WP_004080786.1; NZ_CP011107.1. DR STRING; 243274.TM0843; -. DR EnsemblBacteria; AAD35925; AAD35925; TM_0843. DR EnsemblBacteria; AGL49770; AGL49770; Tmari_0845. DR GeneID; 898514; -. DR KEGG; tma:TM0843; -. DR KEGG; tmi:THEMA_00425; -. DR KEGG; tmm:Tmari_0845; -. DR KEGG; tmw:THMA_0864; -. DR PATRIC; 23936612; VBITheMar51294_0856. DR eggNOG; ENOG4105CCS; Bacteria. DR eggNOG; COG3643; LUCA. DR KO; K00603; -. DR OMA; EPENLIN; -. DR OrthoDB; EOG6TXQW2; -. DR BioCyc; TMAR243274:GC6P-872-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005542; F:folic acid binding; IEA:InterPro. DR GO; GO:0030409; F:glutamate formimidoyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.30.70.670; -; 1. DR Gene3D; 3.30.990.10; -; 1. DR InterPro; IPR013802; Formiminotransferase_C. DR InterPro; IPR004227; Formiminotransferase_cat. DR InterPro; IPR012886; Formiminotransferase_N. DR InterPro; IPR022384; FormiminoTrfase_subdom. DR Pfam; PF02971; FTCD; 1. DR Pfam; PF07837; FTCD_N; 1. DR SMART; SM01221; FTCD; 1. DR SMART; SM01222; FTCD_N; 1. DR SUPFAM; SSF55116; SSF55116; 2. DR TIGRFAMs; TIGR02024; FtcD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35925.1}. SQ SEQUENCE 304 AA; 34411 MW; 362716127A78C20C CRC64; MKLIESVPNF SEGRRKEVVE KIVAEAKKYD RVWVLDWSMD ADHNRSVITL VGEPENLINA LFDMTKKAAE LIDLRNHTGQ HPRMGAADVI PLVPLYNTTM EECVEYSKIL GRRIGEELGI PVYLYEKSAT RPERQNLADI RKGEFEGFFE KIKDPLWKPD FGPDRVHPTA GVTAVGAREF LIAFNVNLGT RDVKIAEKIA RAIRFSSGGL RYVKAIGVDL KGRGVVQVSI NITNHKKTPL YRVFELIKME AERYGVPVLG SEIVGLFPLE SLLKTVSYYL RTDLNAKKVI ESNLLEILVR ESEK // ID Q9WZ47_THEMA Unreviewed; 255 AA. AC Q9WZ47; G4FDP2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 99. DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|HAMAP-Rule:MF_01925}; DE Short=P5C reductase {ECO:0000256|HAMAP-Rule:MF_01925}; DE Short=P5CR {ECO:0000256|HAMAP-Rule:MF_01925}; DE EC=1.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01925}; DE AltName: Full=PCA reductase {ECO:0000256|HAMAP-Rule:MF_01925}; GN Name=proC {ECO:0000256|HAMAP-Rule:MF_01925}; GN OrderedLocusNames=TM_0578 {ECO:0000313|EMBL:AAD35663.1}; GN ORFNames=Tmari_0576 {ECO:0000313|EMBL:AGL49501.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35663.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35663.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35663.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49501.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49501.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate CC (PCA) to L-proline. {ECO:0000256|HAMAP-Rule:MF_01925}. CC -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5- CC carboxylate + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_01925}. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC proline from L-glutamate 5-semialdehyde: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01925}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925}. CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase CC family. {ECO:0000256|HAMAP-Rule:MF_01925}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35663.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49501.1; -; Genomic_DNA. DR PIR; E72360; E72360. DR RefSeq; NP_228388.1; NC_000853.1. DR RefSeq; WP_004081281.1; NZ_CP011107.1. DR STRING; 243274.TM0578; -. DR EnsemblBacteria; AAD35663; AAD35663; TM_0578. DR EnsemblBacteria; AGL49501; AGL49501; Tmari_0576. DR GeneID; 897646; -. DR KEGG; tma:TM0578; -. DR KEGG; tmi:THEMA_01780; -. DR KEGG; tmm:Tmari_0576; -. DR KEGG; tmw:THMA_0592; -. DR PATRIC; 23936065; VBITheMar51294_0587. DR eggNOG; ENOG4105II7; Bacteria. DR eggNOG; COG0345; LUCA. DR KO; K00286; -. DR OMA; QYRTSPK; -. DR OrthoDB; EOG6JB16S; -. DR BioCyc; TMAR243274:GC6P-602-MONOMER; -. DR UniPathway; UPA00098; UER00361. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.3730.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01925; P5C_reductase; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR029036; P5CR_dimer. DR InterPro; IPR028939; ProC_N. DR InterPro; IPR000304; Pyrroline-COOH_reductase. DR PANTHER; PTHR11645; PTHR11645; 1. DR Pfam; PF03807; F420_oxidored; 1. DR Pfam; PF14748; P5CR_dimer; 1. DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00112; proC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01925}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925, KW ECO:0000313|EMBL:AGL49501.1}; KW Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 86 F420_oxidored. FT {ECO:0000259|Pfam:PF03807}. FT DOMAIN 148 252 P5CR_dimer. {ECO:0000259|Pfam:PF14748}. SQ SEQUENCE 255 AA; 27830 MW; 02A5FDD5E531013B CRC64; MTIGIVGVGN MGSIFAEKFS KEAERILLVE KDSEKLSRFN APPYEIADLE KVREADLIVL AVKPQDAPIV LSALKGFDGI LLSIVAGLKI EEIRKYGIHK VARIMPNVAV RVGEGVLATA FSADMSLEER ELVKSLLEKL GFVVEIEEKL FSAVTALTGS GPAFIFVVVE AFLDAALKMG IPLDTAKELV YRLFKGSAEL LTETGEHPAL WKHRVSSPAG TTIEGLITME RFAVRSGVIE SLISSYRRAL ELEEK // ID Q9WY87_THEMA Unreviewed; 318 AA. AC Q9WY87; G4FHF9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=Electron transport complex subunit D {ECO:0000256|HAMAP-Rule:MF_00462}; GN OrderedLocusNames=TM_0245 {ECO:0000313|EMBL:AAD35336.1}; GN ORFNames=Tmari_0243 {ECO:0000313|EMBL:AGL49169.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35336.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35336.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35336.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49169.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49169.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000256|HAMAP-Rule:MF_00462}. CC -!- SUBUNIT: Composed of six subunits. {ECO:0000256|HAMAP- CC Rule:MF_00462}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00462}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00462}. CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000256|HAMAP- CC Rule:MF_00462, ECO:0000256|SAAS:SAAS00571749}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35336.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49169.1; -; Genomic_DNA. DR PIR; F72398; F72398. DR RefSeq; NP_228059.1; NC_000853.1. DR RefSeq; WP_004082949.1; NZ_CP011107.1. DR STRING; 243274.TM0245; -. DR EnsemblBacteria; AAD35336; AAD35336; TM_0245. DR EnsemblBacteria; AGL49169; AGL49169; Tmari_0243. DR GeneID; 897147; -. DR KEGG; tma:TM0245; -. DR KEGG; tmi:THEMA_03500; -. DR KEGG; tmm:Tmari_0243; -. DR KEGG; tmw:THMA_0252; -. DR PATRIC; 23935365; VBITheMar51294_0248. DR eggNOG; ENOG4105D6A; Bacteria. DR eggNOG; COG4658; LUCA. DR KO; K03614; -. DR OMA; YLIRTWG; -. DR OrthoDB; EOG65BDMX; -. DR BioCyc; TMAR243274:GC6P-258-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR HAMAP; MF_00462; RsxD_RnfD; 1. DR InterPro; IPR011303; Elect_transpt_RnfD/RsxD. DR InterPro; IPR004338; NADH_Q_Rdtase_NQR2_RnfD. DR PANTHER; PTHR30578:SF0; PTHR30578:SF0; 1. DR Pfam; PF03116; NQR2_RnfD_RnfE; 1. DR TIGRFAMs; TIGR01946; rnfD; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00462}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00462}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00462}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00462, KW ECO:0000256|SAAS:SAAS00462498}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00462, KW ECO:0000256|SAAS:SAAS00462498}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00462, KW ECO:0000256|SAAS:SAAS00462498}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00462}. FT TRANSMEM 20 42 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 44 66 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 92 112 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 129 149 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 182 202 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 209 229 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 237 257 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 267 287 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00462}. SQ SEQUENCE 318 AA; 34688 MW; DD2D0E2D511BBE60 CRC64; MKLISAYAPH LREEDDVRKI MLDVLIALSP AVIGAAYFFG WYALFLCIAG AVIGELFDIF VMRYLRGVKD FVPDGSGAVT GLLLAMNVST RLPFWAFLLG LVFALGIGKH VFGGLGQNIF NPALVGRAFL LISFPTYMTT WVVPGAGFWK SPADVVTAAT PLALFKEHGV FTPYWDLFIG KVGGSLGETS ALLLIIGFIY LLLRKRVKIF IPVSYIGTVL VFSSIAYLMN PRYGDPLFHL LSGGLMLGAL FMATDMVTSP ITAKGQVIFG IGCGVLTMAI RLFGAYPEGV SFSILFMNAL VPLIDRYTRP RIFGEVKK // ID Q9WXW7_THEMA Unreviewed; 317 AA. AC Q9WXW7; G4FH27; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 91. DE SubName: Full=Monosaccharide-transporting ATPase {ECO:0000313|EMBL:AGL49035.1}; DE EC=3.6.3.17 {ECO:0000313|EMBL:AGL49035.1}; DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35206.1}; GN OrderedLocusNames=TM_0112 {ECO:0000313|EMBL:AAD35206.1}; GN ORFNames=Tmari_0109 {ECO:0000313|EMBL:AGL49035.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35206.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35206.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35206.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49035.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49035.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|SAAS:SAAS00582814}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35206.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49035.1; -; Genomic_DNA. DR PIR; G72416; G72416. DR RefSeq; NP_227928.1; NC_000853.1. DR RefSeq; WP_004082684.1; NZ_CP011107.1. DR STRING; 243274.TM0112; -. DR TCDB; 3.A.1.2.18; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35206; AAD35206; TM_0112. DR EnsemblBacteria; AGL49035; AGL49035; Tmari_0109. DR GeneID; 896939; -. DR KEGG; tma:TM0112; -. DR KEGG; tmi:THEMA_04245; -. DR KEGG; tmm:Tmari_0109; -. DR KEGG; tmw:THMA_0108; -. DR PATRIC; 23935064; VBITheMar51294_0110. DR eggNOG; ENOG4105CNN; Bacteria. DR eggNOG; COG1172; LUCA. DR KO; K10440; -. DR OMA; KYLLYMY; -. DR OrthoDB; EOG61P6T8; -. DR BioCyc; TMAR243274:GC6P-112-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015407; F:monosaccharide-transporting ATPase activity; IEA:UniProtKB-EC. DR GO; GO:0015749; P:monosaccharide transport; IBA:GOC. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00476327}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49035.1}; KW Membrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAAS:SAAS00476327, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00476193}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 114 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 121 143 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 163 181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 212 233 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 266 285 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 291 310 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 317 AA; 33475 MW; 2AA573D3E60AAAAD CRC64; MASKFKKRTF RELGPLVALV SLAVFTAILN PRFLTAFNLQ ALGRQIAIFG LLAIGETFVI ISGGGAIDLS PGSMVALTGV MVAWLMTHGV PVWISVILIL LFSIGAGAWH GLFVTKLRVP AFIITLGTLT IARGMAAVIT KGWPIIGLPS SFLKIGQGEF LKIPIPVWIL LAVALVADFF LRKTVYGKHL RASGGNEVAA RFSGVNVDRV RMIAFMVSGF LAGVVGIIIA ARLSQGQPGV GSMYELYAIA STVIGGTSLT GGEGSVLGAI VGASIISLLW NALVLLNVST YWHNVVIGIV IVVAVTLDIL RRRLASK // ID Q9WY62_THEMA Unreviewed; 236 AA. AC Q9WY62; G4FHD3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=Flagellar assembly protein FliH {ECO:0000313|EMBL:AGL49143.1}; DE SubName: Full=Flagellar export/assembly protein {ECO:0000313|EMBL:AAD35311.1}; GN OrderedLocusNames=TM_0219 {ECO:0000313|EMBL:AAD35311.1}; GN ORFNames=Tmari_0217 {ECO:0000313|EMBL:AGL49143.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35311.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35311.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35311.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49143.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49143.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35311.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49143.1; -; Genomic_DNA. DR PIR; E72404; E72404. DR RefSeq; NP_228034.1; NC_000853.1. DR RefSeq; WP_004082901.1; NZ_CP011107.1. DR STRING; 243274.TM0219; -. DR EnsemblBacteria; AAD35311; AAD35311; TM_0219. DR EnsemblBacteria; AGL49143; AGL49143; Tmari_0217. DR GeneID; 897110; -. DR KEGG; tma:TM0219; -. DR KEGG; tmi:THEMA_03630; -. DR KEGG; tmm:Tmari_0217; -. DR KEGG; tmw:THMA_0226; -. DR PATRIC; 23935310; VBITheMar51294_0221. DR eggNOG; ENOG41062YF; Bacteria. DR eggNOG; COG1317; LUCA. DR KO; K02411; -. DR OMA; ANESKMQ; -. DR OrthoDB; EOG6091GR; -. DR BioCyc; TMAR243274:GC6P-232-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR InterPro; IPR018035; Flagellar_FliH/T3SS_HrpE. DR Pfam; PF02108; FliH; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AAD35311.1}; KW Cilium {ECO:0000313|EMBL:AAD35311.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35311.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 95 212 FliH. {ECO:0000259|Pfam:PF02108}. FT COILED 15 56 {ECO:0000256|SAM:Coils}. FT COILED 62 96 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 236 AA; 27454 MW; B3EE6BC7743A4988 CRC64; MLLRKDEVFY IDLPRKIEKE EKVKEEKTKE NAAEEIQRIE KMREKILSEA QEEARKIIEG ARKDAEEILS NASSEAEALK LEAKKVLEEA KTMKNDFQKY ILALKEKIQK QVNQRIEEIL PELLDILRIL FKKILEKEMD ESTVERKLRS ALSKVVGIKN VKIRINPEDA KKLDLSEVSK ETLIPDPNVE RGGVIVETDF GILDKTFSHQ WELVEDIFEE VVGFEGHPER AEKEVE // ID Q9X0N5_THEMA Unreviewed; 325 AA. AC Q9X0N5; G4FEJ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 124. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36227.1}; DE SubName: Full=Oligopeptide transport ATP-binding protein OppF {ECO:0000313|EMBL:AGL50082.1}; GN OrderedLocusNames=TM_1151 {ECO:0000313|EMBL:AAD36227.1}; GN ORFNames=Tmari_1158 {ECO:0000313|EMBL:AGL50082.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36227.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36227.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36227.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50082.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50082.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36227.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50082.1; -; Genomic_DNA. DR PIR; C72289; C72289. DR RefSeq; NP_228957.1; NC_000853.1. DR RefSeq; WP_004080230.1; NZ_CP011107.1. DR STRING; 243274.TM1151; -. DR EnsemblBacteria; AAD36227; AAD36227; TM_1151. DR EnsemblBacteria; AGL50082; AGL50082; Tmari_1158. DR GeneID; 898335; -. DR KEGG; tma:TM1151; -. DR KEGG; tmm:Tmari_1158; -. DR KEGG; tmw:THMA_1175; -. DR PATRIC; 23937239; VBITheMar51294_1168. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR KO; K02032; -. DR OMA; RSSRKEM; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1180-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36227.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36227.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 4 260 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 325 AA; 37194 MW; 1B005B8E25AA1DA9 CRC64; MALIEVQNLK KYFPVKQGPI DVLLRKPRKF VKAVDGVNFQ IDEGKSLGLV GESGSGKTTT GRVILRLEEP TDGKIIFDGR DITKLSKEEM RKLRKEMQII FQDPMASLNP YMRVGKAIEH ALEIHGIGDR SSRKEMVLEM LRRVNLEPAE DIYRRYPREL SGGQRQRVVI ARALILKPRL VVADEAVAML DVSVRSQLLR LLQELRKEFN LTMLFITHDL ATTKYVCDEI AVMYLGKIVE IGDFEDIYLN PKHPYTQALI SAVPEPSLKK KKKFIPEGET PNPIDVPSGC RFHPRCPYRM DICMKEEPQL KAVEENHKVA CHLYN // ID Q9WY75_THEMA Unreviewed; 364 AA. AC Q9WY75; G4FHE7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 89. DE SubName: Full=Cell division protein FtsW {ECO:0000313|EMBL:AGL49157.1}; DE SubName: Full=Cell division protein, rodA/ftsW/spoVE family {ECO:0000313|EMBL:AAD35324.1}; GN OrderedLocusNames=TM_0233 {ECO:0000313|EMBL:AAD35324.1}; GN ORFNames=Tmari_0231 {ECO:0000313|EMBL:AGL49157.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35324.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35324.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35324.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49157.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49157.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the SEDS family. CC {ECO:0000256|SAAS:SAAS00587907}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35324.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49157.1; -; Genomic_DNA. DR PIR; C72402; C72402. DR RefSeq; NP_228047.1; NC_000853.1. DR RefSeq; WP_004082928.1; NZ_CP011107.1. DR STRING; 243274.TM0233; -. DR EnsemblBacteria; AAD35324; AAD35324; TM_0233. DR EnsemblBacteria; AGL49157; AGL49157; Tmari_0231. DR GeneID; 897132; -. DR KEGG; tma:TM0233; -. DR KEGG; tmi:THEMA_03560; -. DR KEGG; tmm:Tmari_0231; -. DR KEGG; tmw:THMA_0240; -. DR PATRIC; 23935341; VBITheMar51294_0236. DR eggNOG; ENOG4105CNI; Bacteria. DR eggNOG; COG0772; LUCA. DR KO; K03588; -. DR OMA; GLLIRCS; -. DR OrthoDB; EOG68M4JQ; -. DR BioCyc; TMAR243274:GC6P-246-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:InterPro. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS. DR InterPro; IPR001182; Cell_cycle_FtsW/RodA. DR PANTHER; PTHR30474; PTHR30474; 1. DR Pfam; PF01098; FTSW_RODA_SPOVE; 1. DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000313|EMBL:AAD35324.1}; KW Cell division {ECO:0000313|EMBL:AAD35324.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00481328, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00481328, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00481328, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 159 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 198 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 269 289 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 301 327 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 339 359 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 364 AA; 40598 MW; 6A97EB466CE443A9 CRC64; MNEKSLVFFV IVLLCVGFIS LSSFEIVRDY VKPVRDTAHV VLNHLMKLAV AIAFFVVFLY TDHRLLFSKQ IIIGGYVLSL VLLTVVLFLP SSERGAHRWI DLGSFSFQPS ELVKIYILLF LAWYVEKNSL FMKKFFRGFL KPILLVSPLL FLVLIEPDFS TFVLLVFMVI LTLYAAETRG IYVLSFFLVI ISLFISMYKT GVLEHFMKNY QMERLISYLR GNVSEQVVEA VNAIRNGGTL GKGLVLGEEK LFVPVVTSDF VLAIVGEELG FIGLGVVLFS FYGLVHSLVK VATKMHTVPS VRTFISGFAI LIMLQVMTNV GVISGILPVT GVTLPLVSYG GSSLLSIMIG FGIVGNMILE SERE // ID Q9X298_THEMA Unreviewed; 344 AA. AC Q9X298; G4FGG4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000256|HAMAP-Rule:MF_00945}; GN Name=nusA {ECO:0000256|HAMAP-Rule:MF_00945}; GN OrderedLocusNames=TM_1777 {ECO:0000313|EMBL:AAD36840.1}; GN ORFNames=Tmari_1787 {ECO:0000313|EMBL:AGL50711.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36840.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36840.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36840.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50711.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50711.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Participates in both transcription termination and CC antitermination. {ECO:0000256|HAMAP-Rule:MF_00945}. CC -!- SUBUNIT: Monomer. Binds directly to the core enzyme of the DNA- CC dependent RNA polymerase and to nascent RNA. {ECO:0000256|HAMAP- CC Rule:MF_00945}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00945}. CC -!- SIMILARITY: Belongs to the NusA family. {ECO:0000256|HAMAP- CC Rule:MF_00945}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000256|HAMAP- CC Rule:MF_00945}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000256|HAMAP- CC Rule:MF_00945}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36840.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50711.1; -; Genomic_DNA. DR PIR; H72213; H72213. DR RefSeq; NP_229574.1; NC_000853.1. DR RefSeq; WP_004082323.1; NZ_CP011107.1. DR PDB; 1HH2; X-ray; 2.10 A; P=1-344. DR PDB; 1L2F; X-ray; 2.50 A; A=1-344. DR PDBsum; 1HH2; -. DR PDBsum; 1L2F; -. DR STRING; 243274.TM1777; -. DR EnsemblBacteria; AAD36840; AAD36840; TM_1777. DR EnsemblBacteria; AGL50711; AGL50711; Tmari_1787. DR GeneID; 897087; -. DR KEGG; tma:TM1777; -. DR KEGG; tmi:THEMA_05320; -. DR KEGG; tmm:Tmari_1787; -. DR KEGG; tmw:THMA_1821; -. DR PATRIC; 23938536; VBITheMar51294_1797. DR eggNOG; ENOG4105CHV; Bacteria. DR eggNOG; COG0195; LUCA. DR KO; K02600; -. DR OMA; RAMIVEQ; -. DR OrthoDB; EOG6NSGHW; -. DR BioCyc; TMAR243274:GC6P-1826-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0031564; P:transcription antitermination; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.1480.10; -; 1. DR Gene3D; 3.30.300.20; -; 2. DR HAMAP; MF_00945_B; NusA_B; 1. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR025249; KH_dom_NusA-like. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR009019; KH_prok-type. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR030842; NusA_bac. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR InterPro; IPR013735; TF_NusA_N. DR InterPro; IPR010213; Tscrpt_termination_fac_NusA. DR Pfam; PF13184; KH_5; 1. DR Pfam; PF08529; NusA_N; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54814; SSF54814; 2. DR SUPFAM; SSF69705; SSF69705; 1. DR TIGRFAMs; TIGR01953; NusA; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1HH2, ECO:0000213|PDB:1L2F}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00945}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00945}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00945}; KW Transcription antitermination {ECO:0000256|HAMAP-Rule:MF_00945}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00945}; KW Transcription termination {ECO:0000256|HAMAP-Rule:MF_00945}. FT DOMAIN 302 344 KH. {ECO:0000259|PROSITE:PS50084}. SQ SEQUENCE 344 AA; 37920 MW; D87A6C9A42DB4D0D CRC64; MNIGLLEALD QLEEEKGISK EEVIPILEKA LVSAYRKNFG NSKNVEVVID RNTGNIKVYQ LLEVVEEVED PATQISLEEA KKIDPLAEVG SIVKKELNVK NFGRIAAQTA KQVLIQRIRE LEKEKQFEKY SELKGTVTTA EVIRVMGEWA DIRIGKLETR LPKKEWIPGE EIKAGDLVKV YIIDVVKTTK GPKILVSRRV PEFVIGLMKL EIPEVENGIV EIKAIAREPG VRTKVAVASN DPNVDPIGAC IGEGGSRIAA ILKELKGEKL DVLKWSDDPK QLIANALAPA TVIEVEILDK ENKAARVLVP PTQLSLAIGK GGQNARLAAK LTGWKIDIKP IMNL // ID Q9X0F4_THEMA Unreviewed; 332 AA. AC Q9X0F4; G4FET4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 125. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36139.1}; DE SubName: Full=Putative rhamnose ABC transporter, ATP-binding component {ECO:0000313|EMBL:AGL49992.1}; GN OrderedLocusNames=TM_1064 {ECO:0000313|EMBL:AAD36139.1}; GN ORFNames=Tmari_1068 {ECO:0000313|EMBL:AGL49992.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36139.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36139.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36139.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49992.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49992.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36139.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49992.1; -; Genomic_DNA. DR PIR; C72300; C72300. DR RefSeq; NP_228870.1; NC_000853.1. DR RefSeq; WP_004080423.1; NZ_CP011107.1. DR STRING; 243274.TM1064; -. DR TCDB; 3.A.1.5.12; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36139; AAD36139; TM_1064. DR EnsemblBacteria; AGL49992; AGL49992; Tmari_1068. DR GeneID; 897636; -. DR KEGG; tma:TM1064; -. DR KEGG; tmi:THEMA_09040; -. DR KEGG; tmm:Tmari_1068; -. DR KEGG; tmw:THMA_1086; -. DR PATRIC; 23937057; VBITheMar51294_1077. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR KO; K02031; -. DR OMA; ALCAEPS; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1093-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36139.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36139.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 5 259 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 332 AA; 37241 MW; 95A78280D4DEF702 CRC64; MSTLLQIKNL RTYFFTDEGV VKAVDGVSFE IEEGRTLGVV GESGCGKSVT ARSIIKLLST AGRIVSGEIL YNMDGQMVDL VKFSKEEIRK VRGRHIAMIF QEPMAAFSPV YTIGDQITEG MIYHFGITKQ EARERAVELL RRVGIPKPEK MIDSYPFEYS GGMRQRAMIA MALSCNPRLL IADEPTTALD VTIQAQVLDL LKDLQQEYKM AIMMITHNMG VVAEMADHVV VMYLGRVVES APVEELFYNP KHPYTSLLLR SIPVVGKRVE RLEVIEGDVP DPRNMPKGCR FHPRCPYMMK GICDEREPVE VEVGPEHRVS CFLYGGEKDG AS // ID Q9WZC4_THEMA Unreviewed; 176 AA. AC Q9WZC4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Transcriptional regulator, MerR family, near polyamine transporter {ECO:0000313|EMBL:AGL49581.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35740.1}; GN OrderedLocusNames=TM_0656 {ECO:0000313|EMBL:AAD35740.1}; GN ORFNames=Tmari_0656 {ECO:0000313|EMBL:AGL49581.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35740.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35740.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35740.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49581.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49581.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35740.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49581.1; -; Genomic_DNA. DR PIR; E72348; E72348. DR RefSeq; NP_228465.1; NC_000853.1. DR RefSeq; WP_010865177.1; NZ_CP011107.1. DR STRING; 243274.TM0656; -. DR EnsemblBacteria; AAD35740; AAD35740; TM_0656. DR EnsemblBacteria; AGL49581; AGL49581; Tmari_0656. DR GeneID; 897765; -. DR KEGG; tma:TM0656; -. DR KEGG; tmi:THEMA_01385; -. DR KEGG; tmm:Tmari_0656; -. DR KEGG; tmw:THMA_0671; -. DR PATRIC; 23936226; VBITheMar51294_0666. DR eggNOG; ENOG4105NN9; Bacteria. DR eggNOG; COG1396; LUCA. DR OMA; SMKLIHN; -. DR OrthoDB; EOG615VS0; -. DR BioCyc; TMAR243274:GC6P-681-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR013096; Cupin_2. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF07883; Cupin_2; 1. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF51182; SSF51182; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 61 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 176 AA; 20434 MW; 3BA5457E3A9B2F6D CRC64; MRIGEKLRKL RLSRGLTQEE LAERTDLSRS FISQLESDKT SPSIDTLERI LEALGTDLKH FFSDVEEERI VFKKEERVPV YDEPEGVKSE ILMSGVEDKE IDPILVTLEP GAQTEEESYH EGSEFGFVIQ GRIDLYLDGK RYRLKEGDCF YYKADKKHYV KNPGKKKAVL LWIMID // ID Q9WZ08_THEMA Unreviewed; 284 AA. AC Q9WZ08; G4FDT3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 91. DE SubName: Full=Cation efflux system protein {ECO:0000313|EMBL:AAD35623.1}; DE SubName: Full=Cobalt-zinc-cadmium resistance protein CzcD {ECO:0000313|EMBL:AGL49460.1}; GN OrderedLocusNames=TM_0538 {ECO:0000313|EMBL:AAD35623.1}; GN ORFNames=Tmari_0535 {ECO:0000313|EMBL:AGL49460.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35623.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35623.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35623.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49460.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49460.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF) CC transporter (TC 2.A.4) family. {ECO:0000256|SAAS:SAAS00536237}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35623.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49460.1; -; Genomic_DNA. DR PIR; G72363; G72363. DR RefSeq; NP_228348.1; NC_000853.1. DR RefSeq; WP_004081367.1; NZ_CP011107.1. DR STRING; 243274.TM0538; -. DR EnsemblBacteria; AAD35623; AAD35623; TM_0538. DR EnsemblBacteria; AGL49460; AGL49460; Tmari_0535. DR GeneID; 897592; -. DR KEGG; tma:TM0538; -. DR KEGG; tmi:THEMA_01985; -. DR KEGG; tmm:Tmari_0535; -. DR KEGG; tmw:THMA_0551; -. DR PATRIC; 23935983; VBITheMar51294_0546. DR eggNOG; ENOG4105PGM; Bacteria. DR eggNOG; COG1230; LUCA. DR KO; K16264; -. DR OMA; IQMEYQH; -. DR OrthoDB; EOG6VF39C; -. DR BioCyc; TMAR243274:GC6P-562-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0061088; P:regulation of sequestering of zinc ion; IBA:GO_Central. DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central. DR GO; GO:0071577; P:zinc II ion transmembrane transport; IBA:GOC. DR Gene3D; 1.20.1510.10; -; 1. DR Gene3D; 3.30.70.1350; -; 1. DR InterPro; IPR002524; Cation_efflux. DR InterPro; IPR027470; Cation_efflux_CTD. DR InterPro; IPR027469; Cation_efflux_TMD. DR PANTHER; PTHR11562; PTHR11562; 1. DR Pfam; PF01545; Cation_efflux; 1. DR Pfam; PF16916; ZT_dimer; 1. DR TIGRFAMs; TIGR01297; CDF; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00272934}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00272934, KW ECO:0000256|SAAS:SAAS00417858, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00417858, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00417858, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00417883}. FT TRANSMEM 7 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 72 91 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 127 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 139 159 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 205 273 ZT_dimer. {ECO:0000259|Pfam:PF16916}. FT COILED 239 266 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 284 AA; 32205 MW; 97DD44CBD770C016 CRC64; MKKKLLFSIW LNAIITLSEV VGGLISGSLA LLGDSLHNFS DTMSLLGSFI AMKISEKPKN KKYTFGYRRS EIIVAFLNSV SIFVVSTLVV IEAVKRLLSP ATVHTSVLLL VSSIGLAANF FSVILLHTHS KESMNVRSAY LHLIADTLSS ILVVLGAVFM RVWKIYWLDP VLAFVIALYM FKEAYEIVKE SLEILMEASP NLDFEKIKEE IEKIEGVRNA HHFHAWRVGE KEIHFECHVE VDNMELKDAQ KIIDEIEKRL KKYGITHTTV QLECERCSKE MICS // ID G4FEF4_THEMA Unreviewed; 552 AA. AC G4FEF4; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 11-MAY-2016, entry version 44. DE SubName: Full=Alpha-galactosidase {ECO:0000313|EMBL:AGL50123.1}; DE EC=3.2.1.22 {ECO:0000313|EMBL:AGL50123.1}; GN OrderedLocusNames=TM_1192 {ECO:0000313|EMBL:AAD36267.1}; GN ORFNames=Tmari_1199 {ECO:0000313|EMBL:AGL50123.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AGL50123.1, ECO:0000313|Proteomes:UP000013901}; RN [1] {ECO:0000313|EMBL:AAD36267.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36267.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50123.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50123.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36267.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50123.1; -; Genomic_DNA. DR PIR; E72283; E72283. DR RefSeq; NP_228997.1; NC_000853.1. DR RefSeq; WP_004080136.1; NZ_CP011107.1. DR SMR; G4FEF4; 1-525. DR STRING; 243274.TM1192; -. DR CAZy; GH36; Glycoside Hydrolase Family 36. DR EnsemblBacteria; AAD36267; AAD36267; TM_1192. DR EnsemblBacteria; AGL50123; AGL50123; Tmari_1199. DR GeneID; 898292; -. DR KEGG; tma:TM1192; -. DR KEGG; tmi:THEMA_08370; -. DR KEGG; tmm:Tmari_1199; -. DR KEGG; tmw:THMA_1218; -. DR eggNOG; ENOG4107R49; Bacteria. DR eggNOG; COG3345; LUCA. DR KO; K07407; -. DR OMA; ILGCGAP; -. DR BioCyc; TMAR243274:GC6P-1222-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011013; Gal_mutarotase_SF_dom. DR InterPro; IPR002252; Glyco_hydro_36. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF02065; Melibiase; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR SUPFAM; SSF74650; SSF74650; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|SAAS:SAAS00448502, KW ECO:0000313|EMBL:AGL50123.1}; KW Hydrolase {ECO:0000256|SAAS:SAAS00448502, KW ECO:0000313|EMBL:AGL50123.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 552 AA; 63657 MW; 91C6E6EFA24EA9D5 CRC64; MEIFGKTFRE GRFVLKEKNF TVEFAVEKIH LGWKISGRVK GSPGRLEVLR TKAPEKVLVN NWQSWGPCRV VDAFSFKPPE IDPNWRYTAS VVPDVLERNL QSDYFVAEEG KVYGFLSSKI AHPFFAVEDG ELVAYLEYFD VEFDDFVPLE PLVVLEDPNT PLLLEKYAEL VGMENNARVP KHTPTGWCSW YHYFLDLTWE ETLKNLKLAK NFPFEVFQID DAYEKDIGDW LVTRGDFPSV EEMAKVIAEN GFIPGIWTAP FSVSETSDVF NEHPDWVVKE NGEPKMAYRN WNKKIYALDL SKDEVLNWLF DLFSSLRKMG YRYFKIDFLF AGAVPGERKK NITPIQAFRK GIETIRKAVG EDSFILGCGS PLLPAVGCVD GMRIGPDTAP FWGEHIEDNG APAARWALRN AITRYFMHDR FWLNDPDCLI LREEKTDLTQ KEKELYSYTC GVLDNMIIES DDLSLVRDHG KKVLKETLEL LGGRPRVQNI MSEDLRYEIV SSGTLSGNVK IVVDLNSREY HLEKEGKSSL KKRVVKREDG RNFYFYEEGE RE // ID Q9X1C7_THEMA Unreviewed; 398 AA. AC Q9X1C7; G4FFE3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36478.1}; GN OrderedLocusNames=TM_1407 {ECO:0000313|EMBL:AAD36478.1}; GN ORFNames=Tmari_1414 {ECO:0000313|EMBL:AGL50338.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36478.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36478.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36478.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50338.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50338.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36478.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50338.1; -; Genomic_DNA. DR PIR; H72257; H72257. DR RefSeq; NP_229208.1; NC_000853.1. DR RefSeq; WP_004081637.1; NZ_CP011107.1. DR STRING; 243274.TM1407; -. DR EnsemblBacteria; AAD36478; AAD36478; TM_1407. DR EnsemblBacteria; AGL50338; AGL50338; Tmari_1414. DR GeneID; 898069; -. DR KEGG; tma:TM1407; -. DR KEGG; tmi:THEMA_07280; -. DR KEGG; tmm:Tmari_1414; -. DR KEGG; tmw:THMA_1436; -. DR PATRIC; 23937760; VBITheMar51294_1419. DR eggNOG; ENOG4108MS8; Bacteria. DR eggNOG; ENOG4110RYV; LUCA. DR OMA; FYWIPLL; -. DR OrthoDB; EOG6JTC8T; -. DR BioCyc; TMAR243274:GC6P-1444-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR029016; GAF_dom-like. DR SUPFAM; SSF55781; SSF55781; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 67 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 79 100 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 108 142 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 398 AA; 46485 MW; 9E1DA03D0D2F813D CRC64; MKPRKKSWFV EVLISYGIVF LFDYLYKTDV FKESFLNFYW IPLLIFCVRY DLVVHVFSSI LFFTFIVVSK FLSEEGLNFS SDFALANSIM LVISTVLSLI NEVRVKNMER LSLELAYRNE DVSRLEEEVR KLKKQINSLE QKLFYESTGI SSLLIELREI FTEDFEKFAQ RFVEIVSEYF DVKRMYVYRY KDGFLRLAAG IGRPELGFSL KKGVSLVVDK ALQEGVGRIL DVVDQVKSSN EPWLAVRIGD GENILGVITV EETATDNLEL VEEYLTALAT WIHIVMRKLE FEKYEKYRLK DGTFPADFYE TEKNRLKVLE AQHGIPFIEV CVRIKREELG KLLKILRRND LATKMSEDGE YLLLKLLFPL CDEIGFNIIK KRLESEISEV EIVDCESH // ID Q9WYY2_THEMA Unreviewed; 144 AA. AC Q9WYY2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Flagellar protein FliJ {ECO:0000313|EMBL:AGL49433.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35597.1}; GN OrderedLocusNames=TM_0512 {ECO:0000313|EMBL:AAD35597.1}; GN ORFNames=Tmari_0508 {ECO:0000313|EMBL:AGL49433.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35597.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35597.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35597.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49433.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49433.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35597.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49433.1; -; Genomic_DNA. DR PIR; F72368; F72368. DR RefSeq; NP_228322.1; NC_000853.1. DR RefSeq; WP_010865139.1; NZ_CP011107.1. DR STRING; 243274.TM0512; -. DR EnsemblBacteria; AAD35597; AAD35597; TM_0512. DR EnsemblBacteria; AGL49433; AGL49433; Tmari_0508. DR GeneID; 897556; -. DR KEGG; tma:TM0512; -. DR KEGG; tmi:THEMA_02115; -. DR KEGG; tmm:Tmari_0508; -. DR KEGG; tmw:THMA_0524; -. DR PATRIC; 23935929; VBITheMar51294_0519. DR eggNOG; ENOG4107B6F; Bacteria. DR eggNOG; ENOG410Y6QT; LUCA. DR KO; K02413; -. DR OMA; FASMSYL; -. DR OrthoDB; EOG6C8N03; -. DR BioCyc; TMAR243274:GC6P-536-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:InterPro. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR InterPro; IPR012823; Flagell_FliJ. DR Pfam; PF02050; FliJ; 1. DR TIGRFAMs; TIGR02473; flagell_FliJ; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AGL49433.1}; KW Cilium {ECO:0000313|EMBL:AGL49433.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AGL49433.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 15 52 {ECO:0000256|SAM:Coils}. FT COILED 64 98 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 144 AA; 18258 MW; D21CAB59F26FE1E7 CRC64; MPFRFRLQRI YDVRRKEEET LKNDLSKINE KVENTQRIIQ QLSAEKKRIE SNFLHKKVLR KEDLLNMEMQ MMFYEEEIKK KQSELSELMK EQEETRRKLF EKMKERKILE KLKERKMREY LYEENLKERK TMDEIAERKF WWES // ID Q9X1L1_THEMA Unreviewed; 327 AA. AC Q9X1L1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 99. DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:AAD36590.1}; DE EC=1.2.1.11 {ECO:0000313|EMBL:AGL50455.1}; GN OrderedLocusNames=TM_1523 {ECO:0000313|EMBL:AAD36590.1}; GN ORFNames=Tmari_1531 {ECO:0000313|EMBL:AGL50455.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36590.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36590.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36590.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50455.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50455.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase CC family. {ECO:0000256|RuleBase:RU004041, CC ECO:0000256|SAAS:SAAS00558004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36590.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50455.1; -; Genomic_DNA. DR PIR; D72246; D72246. DR RefSeq; NP_229323.1; NC_000853.1. DR RefSeq; WP_010865353.1; NC_000853.1. DR STRING; 243274.TM1523; -. DR EnsemblBacteria; AAD36590; AAD36590; TM_1523. DR EnsemblBacteria; AGL50455; AGL50455; Tmari_1531. DR GeneID; 897641; -. DR KEGG; tma:TM1523; -. DR KEGG; tmm:Tmari_1531; -. DR PATRIC; 23938004; VBITheMar51294_1540. DR eggNOG; ENOG4105CM3; Bacteria. DR eggNOG; COG0136; LUCA. DR KO; K00133; -. DR OMA; KWHKGII; -. DR OrthoDB; EOG6JB158; -. DR BioCyc; TMAR243274:GC6P-1563-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR005986; Asp_semialdehyde_DH_beta. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01296; asd_B; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50455.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 120 Semialdhyde_dh. FT {ECO:0000259|SMART:SM00859}. FT ACT_SITE 129 129 Acyl-thioester intermediate. FT {ECO:0000256|PIRSR:PIRSR000148-1}. FT ACT_SITE 237 237 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR000148-1}. SQ SEQUENCE 327 AA; 36621 MW; 91B21868679AFF1B CRC64; MKVKVGVVGA TGEVGRTMVK VLEEFNVPVT ELRLFASERS VGKEIEFKGE KFKVELLTEE SMKWKCDYFL FSAGASVSRK FAPIAAENGV TVIDNSSAFR MEKEIPLVVP EVNAYLLKGY TGIIANPNCS TIQMILSIYK LHEVYGIEEI FVSTYQSVSG AGHKGIEELL AQERGENVMK VFPKPIHRNV IPLIGDIQEN LFSQEEMKMV NETRKILNDY SIRVYPTTVR VPVLYGHSEA IMVRLKKPYE SLEKVREVIA SGEDVVVTDD LITPVDVAGK NETYVCRLRA TDERSILFWN VADNIRVGAA TNAVRILLKH AEMNGKV // ID Q9WYD4_THEMA Unreviewed; 317 AA. AC Q9WYD4; G4FHL2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=Alcohol dehydrogenase, zinc-containing {ECO:0000313|EMBL:AAD35386.1}; DE SubName: Full=Threonine dehydrogenase-related Zn-dependent dehydrogenase {ECO:0000313|EMBL:AGL49222.1}; GN OrderedLocusNames=TM_0298 {ECO:0000313|EMBL:AAD35386.1}; GN ORFNames=Tmari_0296 {ECO:0000313|EMBL:AGL49222.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35386.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35386.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35386.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49222.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49222.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35386.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49222.1; -; Genomic_DNA. DR PIR; B72395; B72395. DR RefSeq; NP_228110.1; NC_000853.1. DR RefSeq; WP_004083017.1; NZ_CP011107.1. DR STRING; 243274.TM0298; -. DR EnsemblBacteria; AAD35386; AAD35386; TM_0298. DR EnsemblBacteria; AGL49222; AGL49222; Tmari_0296. DR GeneID; 897223; -. DR KEGG; tma:TM0298; -. DR KEGG; tmi:THEMA_03235; -. DR KEGG; tmm:Tmari_0296; -. DR KEGG; tmw:THMA_0305; -. DR PATRIC; 23935475; VBITheMar51294_0303. DR eggNOG; ENOG4107RK3; Bacteria. DR eggNOG; COG1063; LUCA. DR OMA; EICPFEM; -. DR OrthoDB; EOG64R669; -. DR BioCyc; TMAR243274:GC6P-311-MONOMER; -. DR BRENDA; 1.1.1.67; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 25 126 ADH_N. {ECO:0000259|Pfam:PF08240}. SQ SEQUENCE 317 AA; 34870 MW; 18C937C6DAF319A6 CRC64; MKVLLIEKPG VASVVEKEIP VPGEDQTLVK VLACGICGTD YKIFSGGTNA NYPVVPGHEI VGVVERSGVF EKGQMVVIDP NRSCGKCDYC RKGMSQFCEN LQATGVTEPG GFAEYVLVEN SQVYPVRNVP AERAVFAEPL SCVLEGVKMV KHGFYDRILV VGAGSIGVIF GLIFKKIFPG AEIVLAEKDE KRAEYVVQTF GLKVDEPKGE YDLTVECSGT VEGFKTCFEH TGKGGMLLQF SVISKDKMVE ISPFEIYRKE MKILGSYLNP FTMKEAVKII ESGEFPFEKL VTDRLDLEGV KEYLSSHKKA LMKGIFS // ID Q9X0S2_THEMA Unreviewed; 649 AA. AC Q9X0S2; G4FEF1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Beta-galactosidase {ECO:0000256|PIRNR:PIRNR001084}; DE Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084}; DE EC=3.2.1.23 {ECO:0000256|PIRNR:PIRNR001084}; GN OrderedLocusNames=TM_1195 {ECO:0000313|EMBL:AAD36270.1}; GN ORFNames=Tmari_1202 {ECO:0000313|EMBL:AGL50126.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36270.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36270.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36270.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50126.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50126.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D- CC galactose residues in beta-D-galactosides. CC {ECO:0000256|PIRNR:PIRNR001084}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. CC {ECO:0000256|PIRNR:PIRNR001084}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36270.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50126.1; -; Genomic_DNA. DR PIR; H72283; H72283. DR RefSeq; NP_229000.1; NC_000853.1. DR RefSeq; WP_004080133.1; NZ_CP011107.1. DR SMR; Q9X0S2; 1-646. DR STRING; 243274.TM1195; -. DR CAZy; GH42; Glycoside Hydrolase Family 42. DR DNASU; 898289; -. DR EnsemblBacteria; AAD36270; AAD36270; TM_1195. DR EnsemblBacteria; AGL50126; AGL50126; Tmari_1202. DR GeneID; 898289; -. DR KEGG; tma:TM1195; -. DR KEGG; tmi:THEMA_08355; -. DR KEGG; tmm:Tmari_1202; -. DR KEGG; tmw:THMA_1221; -. DR PATRIC; 23937332; VBITheMar51294_1213. DR eggNOG; ENOG4105C4C; Bacteria. DR eggNOG; COG1874; LUCA. DR KO; K12308; -. DR OMA; MLGVCYY; -. DR OrthoDB; EOG6HMX9F; -. DR BioCyc; TMAR243274:GC6P-1225-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006073; P:cellular glucan metabolic process; IBA:GO_Central. DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro. DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR013739; Beta_galactosidase_C. DR InterPro; IPR013738; Beta_galactosidase_Trimer. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR003476; Glyco_hydro_42. DR InterPro; IPR013529; Glyco_hydro_42_N. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF02449; Glyco_hydro_42; 1. DR Pfam; PF08533; Glyco_hydro_42C; 1. DR Pfam; PF08532; Glyco_hydro_42M; 1. DR PIRSF; PIRSF001084; B-galactosidase; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR SUPFAM; SSF52317; SSF52317; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084, KW ECO:0000313|EMBL:AGL50126.1}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, KW ECO:0000313|EMBL:AGL50126.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}. FT DOMAIN 5 392 Glyco_hydro_42. FT {ECO:0000259|Pfam:PF02449}. FT DOMAIN 401 591 Glyco_hydro_42M. FT {ECO:0000259|Pfam:PF08532}. FT DOMAIN 599 646 Glyco_hydro_42C. FT {ECO:0000259|Pfam:PF08533}. FT ACT_SITE 141 141 Proton donor. FT {ECO:0000256|PIRSR:PIRSR001084-1}. FT ACT_SITE 314 314 Nucleophile. FT {ECO:0000256|PIRSR:PIRSR001084-1}. FT METAL 106 106 Zinc. {ECO:0000256|PIRSR:PIRSR001084-3}. FT METAL 150 150 Zinc. {ECO:0000256|PIRSR:PIRSR001084-3}. FT METAL 152 152 Zinc. {ECO:0000256|PIRSR:PIRSR001084-3}. FT METAL 155 155 Zinc. {ECO:0000256|PIRSR:PIRSR001084-3}. FT BINDING 102 102 Substrate. FT {ECO:0000256|PIRSR:PIRSR001084-2}. FT BINDING 140 140 Substrate. FT {ECO:0000256|PIRSR:PIRSR001084-2}. FT BINDING 322 322 Substrate. FT {ECO:0000256|PIRSR:PIRSR001084-2}. SQ SEQUENCE 649 AA; 75477 MW; 4ABEC2D73B8D9380 CRC64; MLGVCYYPEH WGTEKVEEDF RRMKELGIEY VRIGEFAWSR IESERGKFNW DWLDKTLELA EKMGLKIVLG TPTATPPKWL IDEHPEILPV DKDGRVKNFG SRRHYCFSSP VYREEVKRIV TIIVKRYGKH PAVAGWQTDN EYGCHDTVRC YCPRCKKAFQ KWLERKYEGD IKKLNEAWGT VFWSQEYRSF DEIELPNLTP ADPNPSHLLD YYRLASDQVV EFNKLQVEII REYSPGRFIT HNFMSGFTDF DHYKLSKDLD FATWDNYPLG HTLVFLRMKG ETKNPFDRVG HPDIISFSHD LYRGVGRGRF WVMEQQAGPV NWAPYNLWPA KGAVRLWTWQ AFAHGAEVVS YFRWRQAPFA QEQMHSGLLA PDSAPYPGYH EVKQVFEELK NIDINEPVES EVALVFDYET AWVFSIQPHG EGVNYIDLVF RFYSALRRLG LNVDIVPPGS SLDGYKMIVV PSLAIVKEEV LDTFKKYDGL LVLGPRSGSK TETFQIPPEM PPGLLKEIIP VEVRQVESLG DNVETLVWNG KEYPVSIWRE DVDPTITEVI ARFKDGFGAI FRKENVFYLA FWPNGDFLVD FFEALSKESG IETKRMPEGV RIQRRGEYVF SFNFTSEEVD LEIPTKVQIV LGDQKIPPYG LLIWKENER // ID Q9X1L7_THEMA Unreviewed; 338 AA. AC Q9X1L7; G4FFR9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=Electron transfer flavoprotein, alpha subunit {ECO:0000313|EMBL:AAD36598.1}; GN OrderedLocusNames=TM_1531 {ECO:0000313|EMBL:AAD36598.1}; GN ORFNames=Tmari_1539 {ECO:0000313|EMBL:AGL50463.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36598.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36598.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36598.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50463.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50463.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36598.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50463.1; -; Genomic_DNA. DR PIR; G72241; G72241. DR RefSeq; NP_229331.1; NC_000853.1. DR RefSeq; WP_004081904.1; NZ_CP011107.1. DR SMR; Q9X1L7; 209-327. DR STRING; 243274.TM1531; -. DR DNASU; 897663; -. DR EnsemblBacteria; AAD36598; AAD36598; TM_1531. DR EnsemblBacteria; AGL50463; AGL50463; Tmari_1539. DR GeneID; 897663; -. DR KEGG; tma:TM1531; -. DR KEGG; tmi:THEMA_06630; -. DR KEGG; tmm:Tmari_1539; -. DR KEGG; tmw:THMA_1565; -. DR PATRIC; 23938022; VBITheMar51294_1549. DR eggNOG; ENOG4105C10; Bacteria. DR eggNOG; COG2025; LUCA. DR KO; K03522; -. DR OMA; YGCSRPL; -. DR OrthoDB; EOG6M6JV6; -. DR BioCyc; TMAR243274:GC6P-1571-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central. DR GO; GO:0009055; F:electron carrier activity; IBA:GO_Central. DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central. DR GO; GO:0052890; F:oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor; IBA:GO_Central. DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central. DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central. DR Gene3D; 3.40.50.1220; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR014730; ETF_a/b_N. DR InterPro; IPR001308; ETF_a/FixB. DR InterPro; IPR014731; ETF_asu_C. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01012; ETF; 1. DR Pfam; PF00766; ETF_alpha; 1. DR PIRSF; PIRSF000089; Electra_flavoP_a; 1. DR SMART; SM00893; ETF; 1. DR SUPFAM; SSF52467; SSF52467; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 197 ETF. {ECO:0000259|SMART:SM00893}. SQ SEQUENCE 338 AA; 36754 MW; D6BDCDCD913033CB CRC64; MSEKKIIFVL IEHHGGKAHP VSWELIGKAR DLASKLENSE VWGVLLGEGL ESVAKEAIQR GADKVLYVKN REFNTYVNYL YKKALVDMVR KYRPEIFLIG ATLEGRELAG MVATELETGL TADCTGLDII PDKKLLAMTR PTFGGNLMAT IMCPDHRPQM ATVRPGVMKE LPPDPERTGE IIEEEYDLGT FDKLIEILET IPLQTQVNLE YAPVVVAGGK GVGGPEGFKK LKELADLLGG EVGASRAAVK AGWISPEHQV GQTGKTVRPV LYFACGISGA IQHVVGIKES EIIVAINIDE KAPIFDIADI GIVGDLHKVV PALTAKLREL LNKSGVKK // ID Q9X2G7_THEMA Unreviewed; 296 AA. AC Q9X2G7; G4FGP4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 79. DE SubName: Full=Putative glycoside hydrolase {ECO:0000313|EMBL:AGL50791.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36914.1}; GN OrderedLocusNames=TM_1852 {ECO:0000313|EMBL:AAD36914.1}; GN ORFNames=Tmari_1867 {ECO:0000313|EMBL:AGL50791.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36914.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36914.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36914.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50791.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50791.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36914.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50791.1; -; Genomic_DNA. DR PIR; E72203; E72203. DR RefSeq; NP_229648.1; NC_000853.1. DR RefSeq; WP_004082403.1; NZ_CP011107.1. DR STRING; 243274.TM1852; -. DR DNASU; 897808; -. DR EnsemblBacteria; AAD36914; AAD36914; TM_1852. DR EnsemblBacteria; AGL50791; AGL50791; Tmari_1867. DR GeneID; 897808; -. DR KEGG; tma:TM1852; -. DR KEGG; tmi:THEMA_04910; -. DR KEGG; tmm:Tmari_1867; -. DR KEGG; tmw:THMA_1902; -. DR PATRIC; 23938693; VBITheMar51294_1873. DR eggNOG; ENOG4105CKB; Bacteria. DR eggNOG; COG2152; LUCA. DR OMA; MTYTGYD; -. DR OrthoDB; EOG60CWK0; -. DR BioCyc; TMAR243274:GC6P-1903-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 2.115.10.20; -; 1. DR InterPro; IPR023296; Glyco_hydro_beta-prop. DR InterPro; IPR007184; Mannoside_phosphorylase. DR Pfam; PF04041; Glyco_hydro_130; 1. DR PIRSF; PIRSF016202; PH1107; 1. DR SUPFAM; SSF75005; SSF75005; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50791.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 296 AA; 34197 MW; 11B3960CA5C3D2C6 CRC64; MELKLERHPA NPILEPSPYF LWESRFVFNP AVVYDGELFH LLYRAQGEDM VSRIGYAVST DGIHFNKFEK PVFAPKSDDE LYGVEDPRIT KIGDEYYMVY TAYSPRGVRI AMASTKNFIT WKRYGVVIPE VDNKDAALFP EKINGKYVMF HRIPPDMWLA FSDDLVHWDN FVKIASPRPG MWDDLKIGVG APPIKTEYGW LVLYHGVQNT GTSRPIYRLG FMLLDLEDPT KVIKRSKEPI LEPEEDWEKF GGVPNVVFSD AMIEYNGYYY VYYGAADNCI ALATIPVEKV MKWCRE // ID Q9WZL5_THEMA Unreviewed; 1044 AA. AC Q9WZL5; G4FD67; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 102. DE SubName: Full=Galactosyltransferase-related protein {ECO:0000313|EMBL:AAD35838.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL49682.1}; GN OrderedLocusNames=TM_0756 {ECO:0000313|EMBL:AAD35838.1}; GN ORFNames=Tmari_0757 {ECO:0000313|EMBL:AGL49682.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35838.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35838.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35838.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49682.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49682.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35838.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49682.1; -; Genomic_DNA. DR PIR; B72338; B72338. DR RefSeq; NP_228565.1; NC_000853.1. DR RefSeq; WP_004080950.1; NZ_CP011107.1. DR STRING; 243274.TM0756; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR CAZy; GT4; Glycosyltransferase Family 4. DR DNASU; 898424; -. DR EnsemblBacteria; AAD35838; AAD35838; TM_0756. DR EnsemblBacteria; AGL49682; AGL49682; Tmari_0757. DR GeneID; 898424; -. DR KEGG; tma:TM0756; -. DR KEGG; tmi:THEMA_00870; -. DR KEGG; tmm:Tmari_0757; -. DR KEGG; tmw:THMA_0775; -. DR PATRIC; 23936434; VBITheMar51294_0769. DR eggNOG; ENOG4105EP0; Bacteria. DR eggNOG; COG0457; LUCA. DR eggNOG; COG0463; LUCA. DR eggNOG; COG0500; LUCA. DR OMA; VAHINHK; -. DR OrthoDB; EOG6Z0Q7M; -. DR BioCyc; TMAR243274:GC6P-783-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central. DR Gene3D; 1.25.40.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR025714; Methyltranfer_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR013105; TPR_2. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF00534; Glycos_transf_1; 1. DR Pfam; PF00535; Glycos_transf_2; 1. DR Pfam; PF13847; Methyltransf_31; 1. DR Pfam; PF07719; TPR_2; 1. DR SMART; SM00028; TPR; 2. DR SUPFAM; SSF48452; SSF48452; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR PROSITE; PS50005; TPR; 2. DR PROSITE; PS50293; TPR_REGION; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000313|EMBL:AAD35838.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35838.1}. FT DOMAIN 30 97 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. FT COILED 9 36 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1044 AA; 121100 MW; D7A70E0E7848E622 CRC64; MDIFEEIRKK IEQKEFSKAK EMAEKIEDEV EKYNSLGIIH YYEGKVSEAL EFFKKALDIN PVHDDALFNY SKVLFEKGEY FESWRYLTRI NNKTWEVYDM LGDTQLKQNN PAMALYYYKK AAELSNIPEM KEKYQILKDQ FKKDVKLAIF CLPGLDNFIK DIAQILSNIY DVKLVVTTDV RQIQEAYNWA DIVWLEWANE MAVEVTNKLP KDGKKILCRL HSYEALANYP EKINWKNVDK LILVAEHIER ILRDYHSEVY KQVKDKIVIV PNGLDLNRLK FKVRQPGFNI AVVAHINHKK DPAMWLQIIG MLRKIDERYT LHIAGDFQEI RYANYFKHFI KDAGLEKNVK LYGWVEDVNA FLEDKNYLLS TSIHESFGYN IAEAMAKGIK PIIHNYAGAK TQWPDDLVFN FIDEVIRIVT SRDYNSEKYR SFVEKNCSLE KQITSILSIV QLQDNNRTKN KSIHKKSTTD TENSFAKIWK EYSKIDSFTI MNDLPGKSLR SEFVSLLERF FILNKARILE VGTGTGAFSI ELALREADVT GIDIDPTSIE LAIRISKDYN VENVEFKVGD GFKLTESFKP QEFDIAFNMG VVEHFKDDDI IKMLKQMGEV AKFVVVGVPY SGSFVYKTAK ETAQKLGAWE YGFERDFLTL EPLIRRAGLI PLHEEVIGVL AEPFYLRRIN PEWVPLKIAE NLQKYFQGEK VGSWLICFAT KWPGYADEFL KLDDHKKIKF ESTQISLLTV PKPLVSIVIP VLNGANYVKR LVDNIKRIDY ENFEVVLVDD GSTDGTADLF ERLIKGEPKL REKILIIRNK ENVGTFHSRL IGVKHSQGSF VFFHDIDDLV YSKGVKKLLD DLLNFPNKKT LLTVTNALMS GEQFNGEIWC SNFYKNKEEL FVSEITSLSG KFSIIDTLIE RIPLQKAYEE LAEVLHKVGI IKMTIAEDTI LADYLLLEHF VEKMIPTFYT FLGYEVGNLQ SSSKKLLERI KQIPIQISFL MVMSQKEKLF DKATLNQLEN TVKQSAARIY GQELGQKFFE NYLEFKRRFS SILL // ID Q9WYR9_THEMA Unreviewed; 469 AA. AC Q9WYR9; G4FE32; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485}; DE EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485}; GN OrderedLocusNames=TM_0438 {ECO:0000313|EMBL:AAD35523.1}; GN ORFNames=Tmari_0435 {ECO:0000313|EMBL:AGL49360.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35523.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35523.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35523.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49360.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49360.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6- CC phosphogluconate to ribulose 5-phosphate and CO(2), with CC concomitant reduction of NADP to NADPH. CC {ECO:0000256|PIRNR:PIRNR000109}. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose CC 5-phosphate + CO(2) + NADPH. {ECO:0000256|RuleBase:RU000485}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 3/3. {ECO:0000256|RuleBase:RU000485}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. {ECO:0000256|RuleBase:RU000485}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35523.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49360.1; -; Genomic_DNA. DR PIR; A72377; A72377. DR RefSeq; NP_228248.1; NC_000853.1. DR RefSeq; WP_004081528.1; NZ_CP011107.1. DR STRING; 243274.TM0438; -. DR EnsemblBacteria; AAD35523; AAD35523; TM_0438. DR EnsemblBacteria; AGL49360; AGL49360; Tmari_0435. DR GeneID; 897453; -. DR KEGG; tma:TM0438; -. DR KEGG; tmi:THEMA_02535; -. DR KEGG; tmm:Tmari_0435; -. DR KEGG; tmw:THMA_0444; -. DR PATRIC; 23935761; VBITheMar51294_0444. DR eggNOG; ENOG4105C7Q; Bacteria. DR eggNOG; COG0362; LUCA. DR KO; K00033; -. DR OMA; EGEPCVT; -. DR OrthoDB; EOG6MSS4W; -. DR BioCyc; TMAR243274:GC6P-453-MONOMER; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 1.20.5.320; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR012284; 6PGD_dom_3. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_Gnd/GntZ. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006183; Pgluconate_DH. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000109; 6PGD; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR SMART; SM01350; 6PGD; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW NADP {ECO:0000256|RuleBase:RU000485}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000485, KW ECO:0000313|EMBL:AGL49360.1}; KW Pentose shunt {ECO:0000256|RuleBase:RU000485}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT NP_BIND 9 14 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT NP_BIND 32 34 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT NP_BIND 74 76 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT REGION 128 130 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT REGION 185 186 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT ACT_SITE 182 182 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR000109-1}. FT ACT_SITE 189 189 Proton donor. FT {ECO:0000256|PIRSR:PIRSR000109-1}. FT BINDING 102 102 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT BINDING 102 102 Substrate. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 190 190 Substrate. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 260 260 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 287 287 Substrate. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 442 442 Substrate; shared with dimeric partner. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 448 448 Substrate; shared with dimeric partner. FT {ECO:0000256|PIRSR:PIRSR000109-2}. SQ SEQUENCE 469 AA; 53019 MW; 3397E9EFDCE258F2 CRC64; MKSHIGLIGL AVMGQNLALN IARKGYKVSV YNRTAQRTEE FVKNRVTNEE IEPHYDIESF VKSLERPRKI ILMVKAGKPV DDTISQLLPH LEPGDLIIDG GNSHYMDTER RFKELSEKGI LFLGMGVSGG EYGALHGPSL MPGGSREAYN LVEEILLEIA AKTEDGPCCT YVGERSAGHF VKMVHNGIEY AIMQAIAEVY HIMRDVLSLS SEEMSSIFEE WNRGELSSFL VEITYKILRK KDEETGKPMV DVILDKAEQK GTGKWTSQAA LDLGIPTPSI NLAVVERVIS HFKDIRTRLS KLYNKRRSAT QGSEEFLRDL RNSLFFAMFM AFSQGMWLIA EASKEFGYGV SLSEVLRIWK GGCIIRAKLI DTLRRYISNE NAYLLENEEV MNLLKGKIDS LKNILKASIE NEIPVPVLSS SYNYFMSLTE ERLPANLIQA QRDFFGAHTF ERVDREGVFH INWEEGEIG // ID G4FG43_THEMA Unreviewed; 412 AA. AC G4FG43; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 11-MAY-2016, entry version 46. DE SubName: Full=Sensor histidine kinase HpkA {ECO:0000313|EMBL:AGL50587.1}; DE EC=2.7.13.3 {ECO:0000313|EMBL:AGL50587.1}; GN OrderedLocusNames=TM_1654 {ECO:0000313|EMBL:AAD36721.1}; GN ORFNames=Tmari_1663 {ECO:0000313|EMBL:AGL50587.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AGL50587.1, ECO:0000313|Proteomes:UP000013901}; RN [1] {ECO:0000313|EMBL:AAD36721.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36721.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50587.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50587.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. {ECO:0000256|SAAS:SAAS00146860}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36721.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50587.1; -; Genomic_DNA. DR PIR; C72228; C72228. DR RefSeq; NP_229454.1; NC_000853.1. DR RefSeq; WP_004082162.1; NZ_CP011107.1. DR STRING; 243274.TM1654; -. DR EnsemblBacteria; AAD36721; AAD36721; TM_1654. DR EnsemblBacteria; AGL50587; AGL50587; Tmari_1663. DR GeneID; 896859; -. DR KEGG; tma:TM1654; -. DR KEGG; tmi:THEMA_05975; -. DR KEGG; tmm:Tmari_1663; -. DR KEGG; tmw:THMA_1695; -. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; COG0642; LUCA. DR eggNOG; COG2202; LUCA. DR KO; K07636; -. DR OMA; RFILINV; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1700-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR000014; PAS. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF13426; PAS_9; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SMART; SM00091; PAS; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55785; SSF55785; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50112; PAS; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00528924}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|SAAS:SAAS00529081, ECO:0000313|EMBL:AGL50587.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00528924}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00529081, KW ECO:0000313|EMBL:AGL50587.1}. FT DOMAIN 69 104 PAS (PER-ARNT-SIM). FT {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 192 412 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. SQ SEQUENCE 412 AA; 48023 MW; 4DAAC33F9B573AAC CRC64; MSVFLFVIVA VLFVLLFLVF KKRLSEYKIL IEKLSDMLGE KGVPPLYLFE RLKKYVDNLK ETISRVEVSR DNFLTILNSL SEPIFILDRE GKITFLNEIA RELVQGRINP EGRPYYEIFE DYYINEMVEE TIKSEEPQEG TLVTYVGNEK KYFHVKVIPV ELKSGDKIFV ILFHDVTKER KLDEMRREFI ATVSHELRTP LTSIHGYAET LLEDDLENKE LVKRFLKIIE EESARMTRLI NDLLDLEKIE ESEANFEMKD VDLCEVIEYV YRIIQPIAEE NEVDLIVECE DVVVRGNKER LIQMLLNLVD NAVKYTSLKE KGEKKVWVRA YDTPDWVVVE VEDTGPGIPK EAQSRIFEKF YRVDKARSRK MGGTGLGLTI VKTIVDKHGG KIEVESEINQ GTLMRVLLPK RR // ID Q9WY64_THEMA Unreviewed; 532 AA. AC Q9WY64; G4FHD5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Flagellar M-ring protein {ECO:0000256|PIRNR:PIRNR004862}; GN OrderedLocusNames=TM_0221 {ECO:0000313|EMBL:AAD35313.1}; GN ORFNames=Tmari_0219 {ECO:0000313|EMBL:AGL49145.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35313.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35313.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35313.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49145.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49145.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: The M ring may be actively involved in energy CC transduction. {ECO:0000256|PIRNR:PIRNR004862}. CC -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body CC {ECO:0000256|PIRNR:PIRNR004862}. CC -!- SIMILARITY: Belongs to the FliF family. CC {ECO:0000256|PIRNR:PIRNR004862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35313.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49145.1; -; Genomic_DNA. DR PIR; G72404; G72404. DR RefSeq; NP_228036.1; NC_000853.1. DR RefSeq; WP_004082905.1; NZ_CP011107.1. DR STRING; 243274.TM0221; -. DR DNASU; 897114; -. DR EnsemblBacteria; AAD35313; AAD35313; TM_0221. DR EnsemblBacteria; AGL49145; AGL49145; Tmari_0219. DR GeneID; 897114; -. DR KEGG; tma:TM0221; -. DR KEGG; tmi:THEMA_03620; -. DR KEGG; tmm:Tmari_0219; -. DR KEGG; tmw:THMA_0228; -. DR PATRIC; 23935314; VBITheMar51294_0223. DR eggNOG; ENOG4105C1F; Bacteria. DR eggNOG; COG1766; LUCA. DR KO; K02409; -. DR OMA; LIRTWIV; -. DR OrthoDB; EOG6KMB3J; -. DR BioCyc; TMAR243274:GC6P-234-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009431; C:bacterial-type flagellum basal body, MS ring; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0003774; F:motor activity; IEA:InterPro. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR InterPro; IPR013556; Flag_M-ring_C. DR InterPro; IPR000067; FlgMring_FliF. DR InterPro; IPR006182; YscJ_FliF. DR Pfam; PF01514; YscJ_FliF; 1. DR Pfam; PF08345; YscJ_FliF_C; 1. DR PIRSF; PIRSF004862; FliF; 1. DR PRINTS; PR01009; FLGMRINGFLIF. DR TIGRFAMs; TIGR00206; fliF; 1. PE 3: Inferred from homology; KW Bacterial flagellum {ECO:0000256|PIRNR:PIRNR004862}; KW Cell projection {ECO:0000313|EMBL:AAD35313.1}; KW Cilium {ECO:0000313|EMBL:AAD35313.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35313.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 437 459 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 34 223 YscJ_FliF. {ECO:0000259|Pfam:PF01514}. FT DOMAIN 257 416 YscJ_FliF_C. {ECO:0000259|Pfam:PF08345}. FT COILED 468 496 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 532 AA; 60095 MW; 54B514F58C57D056 CRC64; MNIVERLRDL WKKIVDLWNS MPRERKFLVG GIGIALVIAI VLFAVVASVP HYRLLVSGLN EDEAGVIIQK LEEMNVPYKV SPGGDIYVPD SYNVYELRMK LASEGVLGSS RKGFSILSEN SFGATSFDKQ VKYQIALQEE LERSIMTIKG VKDARVHLVL PKYTYYVRGE MAEPRASVLV VLEPGAELTR EQVRGIVELV SGAVEGLKPE NVRVVDNYSR SLSDMLETDE GTFLASSKLE LKQQLEKYYE SKIKKALESV FGPGRVEVIP DISINWSKIE TEMKKYEAPA RREGLVRSQE TQVEKSQNLP PTGGPAGTDS NIPPLTYPSV TSEGTSTYER THTITNYELN EVYQKIIQNR EGEISSLSVA VIIDASSSVL QNSSDWSSVI NDLVEKGVGS ITSSASLSVA VAFLPFDRSI ERALQEELKQ IETRRRFVLY SVGIALLGFL TFMLIYLMIV QIRRIRARKL AEERRRKLEE EVKEILQEEL KEEEVSPEEK ELLELLEELE NIFSRSPSDI AEIVRLWFFE RG // ID Q9WZ00_THEMA Unreviewed; 389 AA. AC Q9WZ00; G4FDU1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 129. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35615.1}; DE SubName: Full=Oligopeptide transport ATP-binding protein OppF {ECO:0000313|EMBL:AGL49452.1}; GN OrderedLocusNames=TM_0530 {ECO:0000313|EMBL:AAD35615.1}; GN ORFNames=Tmari_0527 {ECO:0000313|EMBL:AGL49452.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35615.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35615.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35615.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49452.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49452.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35615.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49452.1; -; Genomic_DNA. DR PIR; H72366; H72366. DR RefSeq; NP_228340.1; NC_000853.1. DR RefSeq; WP_004081380.1; NZ_CP011107.1. DR STRING; 243274.TM0530; -. DR EnsemblBacteria; AAD35615; AAD35615; TM_0530. DR EnsemblBacteria; AGL49452; AGL49452; Tmari_0527. DR GeneID; 897582; -. DR KEGG; tma:TM0530; -. DR KEGG; tmi:THEMA_02025; -. DR KEGG; tmm:Tmari_0527; -. DR KEGG; tmw:THMA_0543; -. DR PATRIC; 23935967; VBITheMar51294_0538. DR eggNOG; ENOG4108JQ7; Bacteria. DR eggNOG; COG4608; LUCA. DR KO; K02032; -. DR OMA; YAEIFFK; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-554-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35615.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35615.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 15 320 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 389 AA; 44613 MW; E9F27BA9DFD43C4C CRC64; MKTIEVLSLR KYFPIRKGFL VKKIVGYVKA VDDISFSVEK GKTFALVGES GCGKTTTAKT ILRLTNPTAG RVVIDGDDTT YYFMKRRDAE NYLETTYVDI FREMREKLSP DQIVDVLEDV DKKYAEIFFK EAKESEEKFY QILLDDIDEK RMKFRRKIQI VFQDPMSSLN PRMTVGDILT EPILFHGLAK TREEAVDMAK DLLKSVGLKE YHLERYPHQF SGGQRQRIAI ARAISINPEI VILDEPTASL DVSVQAQVIN LFLKLQEEKG FTYLFISHDL GLVRFISHEV GIMYLGRIVE MGNTDEIFDN PLHPYTQALL SAVPVPDPKV ERTRKRIILR GGVPSPINRP TGCFFHPRCP YKMPVCEKEY PVMKEISPGH WVACHLHSS // ID Q9WYT4_THEMA Unreviewed; 186 AA. AC Q9WYT4; G4FE07; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=Lipoprotein signal peptidase {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00112541}; DE EC=3.4.23.36 {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00112508}; DE AltName: Full=Prolipoprotein signal peptidase {ECO:0000256|HAMAP-Rule:MF_00161}; DE AltName: Full=Signal peptidase II {ECO:0000256|HAMAP-Rule:MF_00161}; GN Name=lspA {ECO:0000256|HAMAP-Rule:MF_00161}; GN OrderedLocusNames=TM_0463 {ECO:0000313|EMBL:AAD35555.1}; GN ORFNames=Tmari_0460 {ECO:0000313|EMBL:AGL49385.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35555.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35555.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35555.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49385.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49385.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: This protein specifically catalyzes the removal of CC signal peptides from prolipoproteins. {ECO:0000256|HAMAP- CC Rule:MF_00161, ECO:0000256|RuleBase:RU000594, CC ECO:0000256|SAAS:SAAS00112518}. CC -!- CATALYTIC ACTIVITY: Release of signal peptides from bacterial CC membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|- CC (S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably CC Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, CC neutral side chains. {ECO:0000256|HAMAP-Rule:MF_00161, CC ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00112457}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal CC peptide cleavage). {ECO:0000256|HAMAP-Rule:MF_00161, CC ECO:0000256|SAAS:SAAS00112477}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00161}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00161}. CC -!- SIMILARITY: Belongs to the peptidase A8 family. CC {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|RuleBase:RU004181, CC ECO:0000256|SAAS:SAAS00581686}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35555.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49385.1; -; Genomic_DNA. DR PIR; G72373; G72373. DR RefSeq; NP_228273.1; NC_000853.1. DR RefSeq; WP_004081503.1; NC_000853.1. DR STRING; 243274.TM0463; -. DR MEROPS; A08.001; -. DR EnsemblBacteria; AAD35555; AAD35555; TM_0463. DR EnsemblBacteria; AGL49385; AGL49385; Tmari_0460. DR GeneID; 897494; -. DR KEGG; tma:TM0463; -. DR KEGG; tmi:THEMA_02375; -. DR KEGG; tmm:Tmari_0460; -. DR PATRIC; 23935823; VBITheMar51294_0470. DR eggNOG; ENOG4105M02; Bacteria. DR eggNOG; COG0597; LUCA. DR KO; K03101; -. DR OMA; ASEIHGT; -. DR OrthoDB; EOG6PGKBM; -. DR BioCyc; TMAR243274:GC6P-483-MONOMER; -. DR UniPathway; UPA00665; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00161; LspA; 1. DR InterPro; IPR001872; Peptidase_A8. DR PANTHER; PTHR33695:SF1; PTHR33695:SF1; 1. DR Pfam; PF01252; Peptidase_A8; 1. DR PRINTS; PR00781; LIPOSIGPTASE. DR TIGRFAMs; TIGR00077; lspA; 1. DR PROSITE; PS00855; SPASE_II; 1. PE 3: Inferred from homology; KW Aspartyl protease {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00473508}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00161}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00161}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00473508}; KW Lipoprotein {ECO:0000313|EMBL:AAD35555.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|SAAS:SAAS00473564}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00473508}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|SAAS:SAAS00473564}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161, KW ECO:0000256|SAAS:SAAS00473564}. FT TRANSMEM 55 75 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 81 100 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 115 135 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00161}. FT ACT_SITE 96 96 {ECO:0000256|HAMAP-Rule:MF_00161}. FT ACT_SITE 120 120 {ECO:0000256|HAMAP-Rule:MF_00161}. SQ SEQUENCE 186 AA; 20866 MW; AB303307F86D7029 CRC64; MAFVMVLTIV LDQLTKRIAS EIHGTFFIVP GFLRFVKATN RGIALGLFKN LSEQLLWTVM FVVVFLSLLP YIFKFSRLER IAMGFILGGA LGNLLDRIRF GYVLDFLNLT FLPTIFNLAD VFIIVGGALM ILGVFRGGDN ESLESRKKRR GLETGSVFEG EDTIMDLEIN DSKSDKRGQS EGQRSD // ID Q9WY40_THEMA Unreviewed; 304 AA. AC Q9WY40; G4FHB1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35289.1}; DE SubName: Full=tRNA(U54)-2-thioribothymidine synthetase {ECO:0000313|EMBL:AGL49121.1}; GN OrderedLocusNames=TM_0197 {ECO:0000313|EMBL:AAD35289.1}; GN ORFNames=Tmari_0195 {ECO:0000313|EMBL:AGL49121.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35289.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35289.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35289.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49121.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49121.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the TtcA family. CC {ECO:0000256|SAAS:SAAS00557831}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35289.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49121.1; -; Genomic_DNA. DR PIR; E72407; E72407. DR RefSeq; NP_228012.1; NC_000853.1. DR RefSeq; WP_004082849.1; NZ_CP011107.1. DR STRING; 243274.TM0197; -. DR EnsemblBacteria; AAD35289; AAD35289; TM_0197. DR EnsemblBacteria; AGL49121; AGL49121; Tmari_0195. DR GeneID; 897067; -. DR KEGG; tma:TM0197; -. DR KEGG; tmi:THEMA_03745; -. DR KEGG; tmm:Tmari_0195; -. DR KEGG; tmw:THMA_0204; -. DR PATRIC; 23935264; VBITheMar51294_0198. DR eggNOG; ENOG4107R56; Bacteria. DR eggNOG; COG0037; LUCA. DR OMA; LPKTHEK; -. DR OrthoDB; EOG693GNP; -. DR BioCyc; TMAR243274:GC6P-210-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008033; P:tRNA processing; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR012089; 2-thiocytidine_tRNA_synth_TtcA. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR011063; TilS/TtcA_N. DR InterPro; IPR020554; UPF0021_CS. DR Pfam; PF01171; ATP_bind_3; 1. DR PIRSF; PIRSF004976; ATPase_YdaO; 1. DR PROSITE; PS01263; UPF0021; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 49 171 ATP_bind_3. {ECO:0000259|Pfam:PF01171}. SQ SEQUENCE 304 AA; 34934 MW; FBDC135106A00DD5 CRC64; MKCTKCGKPA SVKLRHYNIK LCKEHFNEFI EQRVEKAIKK FKMFGRNSKI LIAVSGGKDS VSLWHMLKKL GYEVDALFIR AGKSGMVQKA QEIVEKNAEL LNTKLHIVDA TEYFGGLSTQ EISIMLRRPV CSICGVVRRY LMNKFAYENG YDVVVTGHNL NDEASVLLGN ILHWQEGYLE RQWPLLPKTH EKLVPKAKPL VLNYEEDIKL YATLNEIPHL EMACPFSVGA TSLVYKKILR ELEEEQPGIT LNFYLGFLKR KKEPKFEVEG LRECKECGYP TTAEVCSFCR LRKQVEKRKN KTPA // ID Q9X0Q3_THEMA Unreviewed; 201 AA. AC Q9X0Q3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 121. DE SubName: Full=Hcp transcriptional regulator HcpR (Crp/Fnr family) {ECO:0000313|EMBL:AGL50102.1}; DE SubName: Full=Transcriptional regulator, crp family {ECO:0000313|EMBL:AAD36246.1}; GN OrderedLocusNames=TM_1171 {ECO:0000313|EMBL:AAD36246.1}; GN ORFNames=Tmari_1178 {ECO:0000313|EMBL:AGL50102.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36246.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36246.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36246.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50102.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50102.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains HTH crp-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00433475}. CC -!- SIMILARITY: Contains cyclic nucleotide-binding domain. CC {ECO:0000256|SAAS:SAAS00443679}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36246.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50102.1; -; Genomic_DNA. DR PIR; F72285; F72285. DR RefSeq; NP_228976.1; NC_000853.1. DR RefSeq; WP_010865275.1; NZ_CP011107.1. DR PDB; 1O5L; X-ray; 2.30 A; A=1-201. DR PDBsum; 1O5L; -. DR STRING; 243274.TM1171; -. DR EnsemblBacteria; AAD36246; AAD36246; TM_1171. DR EnsemblBacteria; AGL50102; AGL50102; Tmari_1178. DR GeneID; 898315; -. DR KEGG; tma:TM1171; -. DR KEGG; tmi:THEMA_08480; -. DR KEGG; tmm:Tmari_1178; -. DR KEGG; tmw:THMA_1196; -. DR PATRIC; 23937282; VBITheMar51294_1189. DR eggNOG; ENOG4108KFT; Bacteria. DR eggNOG; COG0664; LUCA. DR OMA; IDFWGKE; -. DR OrthoDB; EOG68DD40; -. DR BioCyc; TMAR243274:GC6P-1200-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR018490; cNMP-bd-like. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR012318; HTH_CRP. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00027; cNMP_binding; 1. DR Pfam; PF13545; HTH_Crp_2; 1. DR SMART; SM00419; HTH_CRP; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF51206; SSF51206; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. DR PROSITE; PS51063; HTH_CRP_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O5L}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00433748}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00433813}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00433813}. FT DOMAIN 1 115 Cyclic nucleotide-binding. FT {ECO:0000259|PROSITE:PS50042}. FT DOMAIN 129 195 HTH crp-type DNA-binding. FT {ECO:0000259|PROSITE:PS51063}. SQ SEQUENCE 201 AA; 23395 MW; 1C9D00D0C4D1D7CF CRC64; MDLKKLLPCG KVIVFRKGEI VKHQDDPIED VLILLEGTLK TEHVSENGKT LEIDEIKPVQ IIASGFIFSS EPRFPVNVVA GENSKILSIP KEVFLDLLMK DRELLLFFLK DVSEHFRVVS EKLFFLTTKT LREKLMNFLV RHMNEKRELT LPVTLEELSR LFGCARPALS RVFQELEREG YIEKHGRRIK VLKNPFEHDR I // ID Q9X0E9_THEMA Unreviewed; 87 AA. AC Q9X0E9; G4FET9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 77. DE SubName: Full=SpoVS-related protein {ECO:0000313|EMBL:AAD36136.1}; DE SubName: Full=SpoVS-related protein, type 2 {ECO:0000313|EMBL:AGL49987.1}; GN OrderedLocusNames=TM_1059 {ECO:0000313|EMBL:AAD36136.1}; GN ORFNames=Tmari_1063 {ECO:0000313|EMBL:AGL49987.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36136.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36136.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36136.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49987.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49987.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36136.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49987.1; -; Genomic_DNA. DR PIR; F72299; F72299. DR RefSeq; NP_228865.1; NC_000853.1. DR RefSeq; WP_004080441.1; NZ_CP011107.1. DR SMR; Q9X0E9; 1-83. DR STRING; 243274.TM1059; -. DR EnsemblBacteria; AAD36136; AAD36136; TM_1059. DR EnsemblBacteria; AGL49987; AGL49987; Tmari_1063. DR GeneID; 897438; -. DR KEGG; tma:TM1059; -. DR KEGG; tmi:THEMA_09065; -. DR KEGG; tmm:Tmari_1063; -. DR KEGG; tmw:THMA_1081; -. DR PATRIC; 23937047; VBITheMar51294_1072. DR eggNOG; ENOG4105MCT; Bacteria. DR eggNOG; COG2359; LUCA. DR KO; K06416; -. DR OMA; CIPSFID; -. DR OrthoDB; EOG6ND0PF; -. DR BioCyc; TMAR243274:GC6P-1088-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR007347; SpoVS. DR Pfam; PF04232; SpoVS; 1. DR ProDom; PD061837; SpoVS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 87 AA; 9120 MW; 529E88A63A4F05E4 CRC64; MEVLKVSSKS DPNKVAGAIA GVVREHGKAE IQAIGAGAVN QAVKAIAIAR GYLAPSGIDL VFVPAFTDVE IENEKRTAIK FIVFPKS // ID Q9X0K1_THEMA Unreviewed; 387 AA. AC Q9X0K1; G4FEN1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=General secretion pathway protein D, putative {ECO:0000313|EMBL:AAD36193.1}; DE SubName: Full=Type IV pilus biogenesis protein PilQ {ECO:0000313|EMBL:AGL50047.1}; GN OrderedLocusNames=TM_1117 {ECO:0000313|EMBL:AAD36193.1}; GN ORFNames=Tmari_1123 {ECO:0000313|EMBL:AGL50047.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36193.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36193.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36193.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50047.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50047.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the GSP D family. CC {ECO:0000256|RuleBase:RU004003}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36193.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50047.1; -; Genomic_DNA. DR PIR; B72292; B72292. DR RefSeq; NP_228923.1; NC_000853.1. DR RefSeq; WP_004080304.1; NZ_CP011107.1. DR STRING; 243274.TM1117; -. DR EnsemblBacteria; AAD36193; AAD36193; TM_1117. DR EnsemblBacteria; AGL50047; AGL50047; Tmari_1123. DR GeneID; 898647; -. DR KEGG; tma:TM1117; -. DR KEGG; tmi:THEMA_08760; -. DR KEGG; tmm:Tmari_1123; -. DR KEGG; tmw:THMA_1140; -. DR PATRIC; 23937169; VBITheMar51294_1133. DR eggNOG; ENOG4105HIS; Bacteria. DR eggNOG; COG4796; LUCA. DR OMA; ITMELNE; -. DR OrthoDB; EOG6423BN; -. DR BioCyc; TMAR243274:GC6P-1146-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR001775; GspD/PilQ. DR InterPro; IPR004846; T2SS/T3SS. DR Pfam; PF00263; Secretin; 1. DR PRINTS; PR00811; BCTERIALGSPD. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 387 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972312. SQ SEQUENCE 387 AA; 42698 MW; 7D7F4533FD0738F6 CRC64; MRKLGFVLFV LITAVMTAQE EPLVSNIFQD TYILDALADI SAQTGIPIIA DTTVTGFITM ELNEVPLEQA LKMILMPGGY VFKKMDGFYL VGSPDPANPA FRYLAVTKTY KLKYITTADA QELLPAVYKS YVKFNEKNNM VTITAPEEII QEFEEDLKKI DIPIPQVKIS VIVTEVSKDY SNELGLNSLD YSFGSGQEFN ENWSATLGLV TGIIDVQTDV FGQILAQLKL LEEDQKAKIT ADPWIIVKSG EKASLFLGER QVVLLQAEGA VSRIESIDVG VSIDIQPRVM DKEELELTLS PKVSHFAGEK LGTFAVKQNE LSTTLFLKNG QTVVISGATI EDSAQTSSGV PILNKIPLIR YLFGGTTKKD SQKELYIFIK AEIQGSE // ID Q9X263_THEMA Unreviewed; 242 AA. AC Q9X263; G4FGC7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=TrmH family tRNA/rRNA methyltransferase YacO {ECO:0000313|EMBL:AGL50673.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:AGL50673.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36806.1}; GN OrderedLocusNames=TM_1741 {ECO:0000313|EMBL:AAD36806.1}; GN ORFNames=Tmari_1749 {ECO:0000313|EMBL:AGL50673.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36806.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36806.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36806.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50673.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50673.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase TrmH family. CC {ECO:0000256|SAAS:SAAS00555714}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36806.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50673.1; -; Genomic_DNA. DR PIR; D72218; D72218. DR RefSeq; NP_229539.1; NC_000853.1. DR RefSeq; WP_004082265.1; NZ_CP011107.1. DR STRING; 243274.TM1741; -. DR EnsemblBacteria; AAD36806; AAD36806; TM_1741. DR EnsemblBacteria; AGL50673; AGL50673; Tmari_1749. DR GeneID; 897868; -. DR KEGG; tma:TM1741; -. DR KEGG; tmi:THEMA_05530; -. DR KEGG; tmm:Tmari_1749; -. DR KEGG; tmw:THMA_1783; -. DR PATRIC; 23938458; VBITheMar51294_1759. DR eggNOG; ENOG4105C2N; Bacteria. DR eggNOG; COG0566; LUCA. DR KO; K03218; -. DR OMA; HAGIDFL; -. DR OrthoDB; EOG6GBMDM; -. DR BioCyc; TMAR243274:GC6P-1789-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IBA:GO_Central. DR Gene3D; 3.30.1330.30; -; 1. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR029064; L30e-like. DR InterPro; IPR004441; rRNA_MeTrfase_TrmH. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR013123; SpoU_subst-bd. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF00588; SpoU_methylase; 1. DR Pfam; PF08032; SpoU_sub_bind; 1. DR SMART; SM00967; SpoU_sub_bind; 1. DR SUPFAM; SSF55315; SSF55315; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00186; rRNA_methyl_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00477853, KW ECO:0000313|EMBL:AGL50673.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00477853, KW ECO:0000313|EMBL:AGL50673.1}. FT DOMAIN 2 78 SpoU_sub_bind. FT {ECO:0000259|SMART:SM00967}. SQ SEQUENCE 242 AA; 27096 MW; 03695F95E1921D14 CRC64; MRVYGRKILE EALRNNVPIK KVFFQKMKNP GSYFLSLVKE VEKRGIKYSF ESEERLKNLS GTKKHQGVVF DIGEYRYSSV EEILEAKTPP LIVLLDQIQD PHNLGAIVRT SVGAGANGII IPKDKSVKVT ETVVKVSAGT VFRARIAVVT NLARTIEELK EKGVWTYASD IDGTPIYEED FTFPTAFVFG NEGEGIRRLV REKCDRVVTI PMENDIDSLN VSVSVGVVLF EAVRQRRMKG AG // ID Q9WZ29_THEMA Unreviewed; 243 AA. AC Q9WZ29; G4FDR2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 103. DE SubName: Full=Putative metal-dependent phosphoesterases (PHP family) {ECO:0000313|EMBL:AGL49481.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35644.1}; GN OrderedLocusNames=TM_0559 {ECO:0000313|EMBL:AAD35644.1}; GN ORFNames=Tmari_0556 {ECO:0000313|EMBL:AGL49481.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35644.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35644.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35644.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49481.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49481.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35644.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49481.1; -; Genomic_DNA. DR PIR; F72360; F72360. DR RefSeq; NP_228369.1; NC_000853.1. DR RefSeq; WP_004081319.1; NZ_CP011107.1. DR PDB; 2ANU; X-ray; 2.40 A; A/B/C/D/E/F=1-243. DR PDBsum; 2ANU; -. DR STRING; 243274.TM0559; -. DR EnsemblBacteria; AAD35644; AAD35644; TM_0559. DR EnsemblBacteria; AGL49481; AGL49481; Tmari_0556. DR GeneID; 897617; -. DR KEGG; tma:TM0559; -. DR KEGG; tmi:THEMA_01880; -. DR KEGG; tmm:Tmari_0556; -. DR KEGG; tmw:THMA_0572; -. DR PATRIC; 23936025; VBITheMar51294_0567. DR eggNOG; ENOG4108UA1; Bacteria. DR eggNOG; COG0613; LUCA. DR KO; K07053; -. DR OMA; SVACHPY; -. DR OrthoDB; EOG6XHC2N; -. DR BioCyc; TMAR243274:GC6P-583-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; SSF89550; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2ANU}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000213|PDB:2ANU}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000213|PDB:2ANU}. FT DOMAIN 10 102 POLIIIAc. {ECO:0000259|SMART:SM00481}. FT METAL 13 13 Zinc 1; via tele nitrogen. FT {ECO:0000213|PDB:2ANU}. FT METAL 15 15 Zinc 1; via tele nitrogen. FT {ECO:0000213|PDB:2ANU}. FT METAL 20 20 Zinc 2. {ECO:0000213|PDB:2ANU}. FT METAL 45 45 Zinc 2; via tele nitrogen. FT {ECO:0000213|PDB:2ANU}. FT METAL 97 97 Zinc 1. {ECO:0000213|PDB:2ANU}. FT METAL 193 193 Zinc 1. {ECO:0000213|PDB:2ANU}. FT METAL 195 195 Zinc 2; via tele nitrogen. FT {ECO:0000213|PDB:2ANU}. SQ SEQUENCE 243 AA; 28612 MW; 523575D9276BF84A CRC64; MKTDTEWLLC DFHVHTNMSD GHLPLGEVVD LFGKHGVDVV SITDHIVDRR TLEQRKRNGE PLGAITEDKF QDYLKRLWRE QKRAWEEYGM ILIPGVEITN NTDLYHIVAV DVKEYVDPSL PVEEIVEKLK EQNALVIAAH PDRKKQDEEH LSWYLWANME RFKDTFDAWE IANRDDLFNS VGVKKYRYVA NSDFHELWHV YSWKTLVKSE KNIEAIKEAI RKNTDVAIYL MRKNRLSSLS DVI // ID Q9WZD5_THEMA Unreviewed; 256 AA. AC Q9WZD5; G4FDF7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=Putative deoxyribonuclease YcfH {ECO:0000313|EMBL:AGL49592.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35749.1}; GN OrderedLocusNames=TM_0667 {ECO:0000313|EMBL:AAD35749.1}; GN ORFNames=Tmari_0667 {ECO:0000313|EMBL:AGL49592.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35749.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35749.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35749.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49592.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49592.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35749.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49592.1; -; Genomic_DNA. DR PIR; H72349; H72349. DR RefSeq; NP_228476.1; NC_000853.1. DR RefSeq; WP_004081106.1; NZ_CP011107.1. DR PDB; 1J6O; X-ray; 1.80 A; A=1-256. DR PDBsum; 1J6O; -. DR STRING; 243274.TM0667; -. DR DrugBank; DB02325; Isopropyl Alcohol. DR EnsemblBacteria; AAD35749; AAD35749; TM_0667. DR EnsemblBacteria; AGL49592; AGL49592; Tmari_0667. DR GeneID; 897782; -. DR KEGG; tma:TM0667; -. DR KEGG; tmi:THEMA_01330; -. DR KEGG; tmm:Tmari_0667; -. DR KEGG; tmw:THMA_0682; -. DR PATRIC; 23936248; VBITheMar51294_0677. DR eggNOG; ENOG4105F8V; Bacteria. DR eggNOG; COG0084; LUCA. DR KO; K03424; -. DR OMA; LHIRDAY; -. DR OrthoDB; EOG66QM1C; -. DR BioCyc; TMAR243274:GC6P-692-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004536; F:deoxyribonuclease activity; IBA:GO_Central. DR GO; GO:0006308; P:DNA catabolic process; IBA:GO_Central. DR InterPro; IPR015991; DNase_TatD-type. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR001130; TatD_family. DR PANTHER; PTHR10060; PTHR10060; 1. DR Pfam; PF01026; TatD_DNase; 1. DR PIRSF; PIRSF005902; DNase_TatD; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR TIGRFAMs; TIGR00010; TIGR00010; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1J6O}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 256 AA; 29181 MW; FB647D78CB261985 CRC64; MVDTHAHLHF HQFDDDRNAV ISSFEENNIE FVVNVGVNLE DSKKSLDLSK TSDRIFCSVG VHPHDAKEVP EDFIEHLEKF AKDEKVVAIG ETGLDFFRNI SPAEVQKRVF VEQIELAGKL NLPLVVHIRD AYSEAYEILR TESLPEKRGV IHAFSSDYEW AKKFIDLGFL LGIGGPVTYP KNEALREVVK RVGLEYIVLE TDCPFLPPQP FRGKRNEPKY LKYVVETISQ VLGVPEAKVD EATTENARRI FLEVKE // ID Q9X270_THEMA Unreviewed; 289 AA. AC Q9X270; G4FGD4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 103. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD36813.1}; DE SubName: Full=Oligopeptide transport system permease protein OppC {ECO:0000313|EMBL:AGL50680.1}; GN OrderedLocusNames=TM_1748 {ECO:0000313|EMBL:AAD36813.1}; GN ORFNames=Tmari_1756 {ECO:0000313|EMBL:AGL50680.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36813.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36813.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36813.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50680.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50680.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032, CC ECO:0000256|SAAS:SAAS00537635}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36813.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50680.1; -; Genomic_DNA. DR PIR; G72215; G72215. DR RefSeq; NP_229546.1; NC_000853.1. DR RefSeq; WP_004082280.1; NZ_CP011107.1. DR STRING; 243274.TM1748; -. DR TCDB; 3.A.1.5.15; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36813; AAD36813; TM_1748. DR EnsemblBacteria; AGL50680; AGL50680; Tmari_1756. DR GeneID; 897182; -. DR KEGG; tma:TM1748; -. DR KEGG; tmi:THEMA_05495; -. DR KEGG; tmm:Tmari_1756; -. DR KEGG; tmw:THMA_1790; -. DR PATRIC; 23938472; VBITheMar51294_1766. DR eggNOG; ENOG4105C2T; Bacteria. DR eggNOG; COG1173; LUCA. DR KO; K02034; -. DR OMA; RFLFNAW; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1796-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR025966; OppC_N. DR Pfam; PF00528; BPD_transp_1; 1. DR Pfam; PF12911; OppC_N; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00496716}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496716, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496724}. FT TRANSMEM 26 47 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 86 109 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 121 142 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 148 168 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 207 232 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 252 275 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 86 275 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 289 AA; 31656 MW; E5676D0E844923AA CRC64; MLRKNKTESI GYWKAFWLRF KKNKMAVIGG VFVLILIALA ILAPYIAPYP YDEPHYIRAF EGPSKDFIFG TDALGRDLFS RILYSLRNAC IIGFGSQFVV LIIGGILGAV AGFKGGWIDK FIMSIVDIMF AFPTFLFNVI LVTALGRGLF TIFLAIGLTG WAGMARLVRG QVLYLKNSEF VEAAKAAGAS TFYIIRKHIL PNMIGPILVN LAFGVPGAMM TESGLAVIGM GVRPPMPSWG NLIGEGIGMM MAFPHLLIFP AVTFAFTLIS FTFLADGLRD AFNPRSEIS // ID Q9X008_THEMA Unreviewed; 275 AA. AC Q9X008; G4FCS0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Site-determining protein {ECO:0000256|PIRNR:PIRNR003092}; GN OrderedLocusNames=TM_0906 {ECO:0000313|EMBL:AAD35987.1}; GN ORFNames=Tmari_0908 {ECO:0000313|EMBL:AGL49833.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35987.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35987.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35987.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49833.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49833.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ParA family. CC {ECO:0000256|PIRNR:PIRNR003092}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35987.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49833.1; -; Genomic_DNA. DR PIR; A72319; A72319. DR RefSeq; NP_228714.1; NC_000853.1. DR RefSeq; WP_004080662.1; NZ_CP011107.1. DR STRING; 243274.TM0906; -. DR EnsemblBacteria; AAD35987; AAD35987; TM_0906. DR EnsemblBacteria; AGL49833; AGL49833; Tmari_0908. DR GeneID; 898580; -. DR KEGG; tma:TM0906; -. DR KEGG; tmi:THEMA_00105; -. DR KEGG; tmm:Tmari_0908; -. DR KEGG; tmw:THMA_0928; -. DR PATRIC; 23936743; VBITheMar51294_0920. DR eggNOG; ENOG4107R21; Bacteria. DR eggNOG; COG0455; LUCA. DR KO; K04562; -. DR OMA; MEPRSIF; -. DR OrthoDB; EOG6N680B; -. DR BioCyc; TMAR243274:GC6P-936-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR025501; MinD. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR PIRSF; PIRSF003092; MinD; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRNR:PIRNR003092, KW ECO:0000256|PIRSR:PIRSR003092-1}; KW Cell projection {ECO:0000313|EMBL:AGL49833.1}; KW Cilium {ECO:0000313|EMBL:AGL49833.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AGL49833.1}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR003092, KW ECO:0000256|PIRSR:PIRSR003092-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 16 221 CbiA. {ECO:0000259|Pfam:PF01656}. FT NP_BIND 21 28 ATP. {ECO:0000256|PIRSR:PIRSR003092-1}. SQ SEQUENCE 275 AA; 31400 MW; 9B2C502AF91FBC1A CRC64; MPDQAEHLRK NEPNIISVLS GKGGVGKSVI AVNLSLALKE KGLRVLLLDA DVGFGSVEIL LGFMAPKTLK DFFKSNVRIE DIVFETKYGV DVLSSGIDME DLILFNLGDR RRFFDEFARL LRKYDYLVID FPPGYNENLD QFYIQSDFLI LVTSPEPTSI INTYTLIKLL SVKGITPEEI FLVMNMVRNM KEGRLAADRL KRVVERFVGF TIKNYFVIKE DQVVQRSVFL QEPFVRSHSR SQPSLAIYGL REKILKEPVQ KKGFLNKIRQ MLGIG // ID Q9WXP0_THEMA Unreviewed; 395 AA. AC Q9WXP0; G4FGV0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=Phospholipase/carboxylesterase {ECO:0000313|EMBL:AGL48956.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35127.1}; GN OrderedLocusNames=TM_0033 {ECO:0000313|EMBL:AAD35127.1}; GN ORFNames=Tmari_0030 {ECO:0000313|EMBL:AGL48956.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35127.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35127.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35127.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48956.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48956.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35127.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48956.1; -; Genomic_DNA. DR PIR; F72424; F72424. DR RefSeq; NP_227849.1; NC_000853.1. DR RefSeq; WP_004082491.1; NZ_CP011107.1. DR PDB; 3DOH; X-ray; 2.60 A; A/B=16-395. DR PDB; 3DOI; X-ray; 3.00 A; A/B=16-395. DR PDBsum; 3DOH; -. DR PDBsum; 3DOI; -. DR STRING; 243274.TM0033; -. DR ESTHER; thema-TM0033; 5_AlphaBeta_hydrolase. DR EnsemblBacteria; AAD35127; AAD35127; TM_0033. DR EnsemblBacteria; AGL48956; AGL48956; Tmari_0030. DR GeneID; 896854; -. DR KEGG; tma:TM0033; -. DR KEGG; tmi:THEMA_04635; -. DR KEGG; tmm:Tmari_0030; -. DR KEGG; tmw:THMA_0029; -. DR PATRIC; 23934906; VBITheMar51294_0031. DR eggNOG; ENOG4108XDX; Bacteria. DR eggNOG; COG4099; LUCA. DR OMA; WVFHAED; -. DR OrthoDB; EOG6FV82Q; -. DR BioCyc; TMAR243274:GC6P-33-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central. DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central. DR GO; GO:0002084; P:protein depalmitoylation; IBA:GO_Central. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR003140; PLipase/COase/thioEstase. DR Pfam; PF02230; Abhydrolase_2; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3DOH, ECO:0000213|PDB:3DOI}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 395 AA; 44767 MW; 6D43EF24AEEF57C9 CRC64; MLFFIFMGIL SILFAQEDVT VKSVTLITKV FPEGEKVCAV VIEYPVEIDG QKLSPDQFSV KVKTGDTYSS RTITKVYANN SGGLSFSIFN NRGKYVVLEL STEDLHSNTI VFGPNFLNTR MKLDYIVSQL VPIFDVDGNE VEPFTSKQTD EKHLIIDDFL AFTFKDPETG VEIPYRLFVP KDVNPDRKYP LVVFLHGAGE RGTDNYLQVA GNRGAVVWAQ PRYQVVHPCF VLAPQCPPNS SWSTLFTDRE NPFNPEKPLL AVIKIIRKLL DEYNIDENRI YITGLSMGGY GTWTAIMEFP ELFAAAIPIC GGGDVSKVER IKDIPIWVFH AEDDPVVPVE NSRVLVKKLA EIGGKVRYTE YEKGFMEKHG WDPHGSWIPT YENQEAIEWL FEQSR // ID Q9WYA9_THEMA Unreviewed; 881 AA. AC Q9WYA9; G4FHI6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 111. DE SubName: Full=Pyruvate,orthophosphate dikinase {ECO:0000313|EMBL:AAD35361.1}; DE SubName: Full=Pyruvate,phosphate dikinase {ECO:0000313|EMBL:AGL49196.1}; DE EC=2.7.9.1 {ECO:0000313|EMBL:AGL49196.1}; GN OrderedLocusNames=TM_0272 {ECO:0000313|EMBL:AAD35361.1}; GN ORFNames=Tmari_0270 {ECO:0000313|EMBL:AGL49196.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35361.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35361.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35361.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49196.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49196.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR000853-3}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35361.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49196.1; -; Genomic_DNA. DR PIR; F72397; F72397. DR RefSeq; NP_228085.1; NC_000853.1. DR RefSeq; WP_004082976.1; NZ_CP011107.1. DR SMR; Q9WYA9; 3-880. DR STRING; 243274.TM0272; -. DR EnsemblBacteria; AAD35361; AAD35361; TM_0272. DR EnsemblBacteria; AGL49196; AGL49196; Tmari_0270. DR GeneID; 897187; -. DR KEGG; tma:TM0272; -. DR KEGG; tmi:THEMA_03365; -. DR KEGG; tmm:Tmari_0270; -. DR KEGG; tmw:THMA_0279; -. DR PATRIC; 23935421; VBITheMar51294_0276. DR eggNOG; ENOG4108HRN; Bacteria. DR eggNOG; COG0574; LUCA. DR KO; K01006; -. DR OMA; VRRETNP; -. DR OrthoDB; EOG6N0HGQ; -. DR BioCyc; TMAR243274:GC6P-285-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC. DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.60; -; 1. DR Gene3D; 3.30.1490.20; -; 2. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.50.30.10; -; 1. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR018274; PEP_util_AS. DR InterPro; IPR000121; PEP_util_C. DR InterPro; IPR023151; PEP_util_CS. DR InterPro; IPR002192; PPDK_PEP-bd. DR InterPro; IPR010121; Pyruvate_phosphate_dikinase. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR PANTHER; PTHR22931:SF9; PTHR22931:SF9; 1. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF02896; PEP-utilizers_C; 1. DR Pfam; PF01326; PPDK_N; 2. DR PIRSF; PIRSF000853; PPDK; 1. DR SUPFAM; SSF51621; SSF51621; 1. DR SUPFAM; SSF52009; SSF52009; 1. DR TIGRFAMs; TIGR01828; pyru_phos_dikin; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000313|EMBL:AAD35361.1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR000853-3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000853-3}; KW Pyruvate {ECO:0000313|EMBL:AAD35361.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35361.1}. FT DOMAIN 22 295 PPDK_N. {ECO:0000259|Pfam:PF01326}. FT DOMAIN 308 361 PPDK_N. {ECO:0000259|Pfam:PF01326}. FT DOMAIN 427 508 PEP-utilizers. FT {ECO:0000259|Pfam:PF00391}. FT DOMAIN 527 875 PEP-utilizers_C. FT {ECO:0000259|Pfam:PF02896}. FT COILED 296 327 {ECO:0000256|SAM:Coils}. FT ACT_SITE 460 460 Tele-phosphohistidine intermediate. FT {ECO:0000256|PIRSR:PIRSR000853-1}. FT ACT_SITE 837 837 Proton donor. FT {ECO:0000256|PIRSR:PIRSR000853-1}. FT METAL 751 751 Magnesium. FT {ECO:0000256|PIRSR:PIRSR000853-3}. FT METAL 775 775 Magnesium. FT {ECO:0000256|PIRSR:PIRSR000853-3}. FT BINDING 567 567 Substrate. FT {ECO:0000256|PIRSR:PIRSR000853-2}. FT BINDING 623 623 Substrate. FT {ECO:0000256|PIRSR:PIRSR000853-2}. FT BINDING 751 751 Substrate. FT {ECO:0000256|PIRSR:PIRSR000853-2}. FT BINDING 772 772 Substrate; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000853-2}. FT BINDING 773 773 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000853-2}. FT BINDING 774 774 Substrate. FT {ECO:0000256|PIRSR:PIRSR000853-2}. FT BINDING 775 775 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000853-2}. SQ SEQUENCE 881 AA; 98164 MW; 6E356828E7498629 CRC64; MAKKYVYFFA NGKAEGRADM KDILGGKGAN LAEMTNLGIP VPPGFTISAE VCKYYYDHGR TYPEELKEQV EEAMRRLEEV TGKKFGDPNN PLLVSVRSGA AISMPGMMDT VLNLGLNDET VKGLAKLTNN ERFAYDAYRR FLQMFGDVVL KIPHEKFEKA LEELKKEKGV KLDTELDAED LKKLVERYKQ IYKEEGKEFP QDPWKQLWLA IDAVFGSWMN ERAIKYRQIH GIKEGDLLGT AVNIVAMVFG NMGEDSGTGV AFTRDPNTGE KKPYGEFLPN AQGEDVVAGI RTPLKLEELK NRMPEVYNQL LEIMDKLEKH YRDMQDIEFT VERGKLYILQ TRNGKRTSQA AIRIAVDMVH EGLITKEEAI LRVRPEDVEQ VLHPVFDPKE KAQAKVIAKG LPASPGAATG KVVFNAKKAE ELGKAGEQVI LVRPETSPED VGGMAAAQGI LTSRGGMTSH AAVVARGMGK PAVVGAESIE VHPEEGYFKV GDVVVKEGEW ISIDGTTGEV LLGKVTTIKP QGLEGPVAEL LQWADEIRRL GVRTNADIPR DAEVARKFGA EGIGLCRTEH MFFEKDRIPK VRRMILAKTK EEREKALDEL LPLQKEDFKG LFRVMKGLPV TIRLIDPPLH EFLPQEDEQI KEVAEQMGVS FEELKNVVEN LKELNPMLGH RGCRLTITYP EIAVMQTKAI IGAAIELKKE EGIDVIPEIM IPLVGHVNEL RYLKKIIKET ADALIKEAGV ELTYKIGTMI EVPRAAVTAH QIAEEAEFFS FGTNDLTQMT FGFSRDDVGK FLPEYLEKGI LEHDPFKTLD YDGVGELVRM GKEKGRSTRP DLKVGVCGEH GGDPRSILFF DKIGLDYVSC SPYRVPVARL AAAQAALKNK K // ID Q9WYJ4_THEMA Unreviewed; 356 AA. AC Q9WYJ4; G4FHS1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35446.1}; GN OrderedLocusNames=TM_0359 {ECO:0000313|EMBL:AAD35446.1}; GN ORFNames=Tmari_0357 {ECO:0000313|EMBL:AGL49282.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35446.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35446.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35446.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49282.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49282.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35446.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49282.1; -; Genomic_DNA. DR PIR; G72386; G72386. DR RefSeq; NP_228170.1; NC_000853.1. DR RefSeq; WP_004083160.1; NZ_CP011107.1. DR STRING; 243274.TM0359; -. DR EnsemblBacteria; AAD35446; AAD35446; TM_0359. DR EnsemblBacteria; AGL49282; AGL49282; Tmari_0357. DR GeneID; 897317; -. DR KEGG; tma:TM0359; -. DR KEGG; tmi:THEMA_02920; -. DR KEGG; tmm:Tmari_0357; -. DR KEGG; tmw:THMA_0367; -. DR PATRIC; 23935599; VBITheMar51294_0364. DR eggNOG; COG0438; LUCA. DR OMA; PNTRHFE; -. DR OrthoDB; EOG6HB9MM; -. DR BioCyc; TMAR243274:GC6P-373-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 356 AA; 41972 MW; 58B3A66B38ECDC98 CRC64; MKIGFLSRWG ATCGVGMHAE ILAREFIRMG HEVVVFAPTE ESASKEVKYY KRTEAQDPEF VKREIYTEVD NVTEEGWVKE EEILKENLDL LIIETFWRVP VKPLTRLIEK LKIPVISVFH EANIFKAREV VKLPCDKIVV FDRRFYDEIL EFYEIPREKV EVISYPVMKP YDAEPERPVS EDKFLFFSFG RQPVEEYCDF LNALKKLRKR FDNVHYWIIR SDGRVDYEAE WITQWQKRPT VEKLYSYLKG SNVHLLPKGN TPNVVVSSTL YQIIASETPI VIRDSRFVET IETDVYGFGP IVKYRNIHDL VHKLELLMLD RELVEDIKKE VRVFVEKYGG DKIAQEFLDL AKTITK // ID Q9X010_THEMA Unreviewed; 678 AA. AC Q9X010; G4FCR8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 87. DE SubName: Full=Flagellar biosynthesis protein FlhA {ECO:0000313|EMBL:AAD35989.1}; GN OrderedLocusNames=TM_0908 {ECO:0000313|EMBL:AAD35989.1}; GN ORFNames=Tmari_0910 {ECO:0000313|EMBL:AGL49835.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35989.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35989.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35989.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49835.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49835.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35989.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49835.1; -; Genomic_DNA. DR PIR; C72319; C72319. DR RefSeq; NP_228716.1; NC_000853.1. DR RefSeq; WP_004080658.1; NZ_CP011107.1. DR STRING; 243274.TM0908; -. DR EnsemblBacteria; AAD35989; AAD35989; TM_0908. DR EnsemblBacteria; AGL49835; AGL49835; Tmari_0910. DR GeneID; 898582; -. DR KEGG; tma:TM0908; -. DR KEGG; tmi:THEMA_00095; -. DR KEGG; tmm:Tmari_0910; -. DR KEGG; tmw:THMA_0930; -. DR PATRIC; 23936747; VBITheMar51294_0922. DR eggNOG; ENOG4105D7B; Bacteria. DR eggNOG; COG1298; LUCA. DR KO; K02400; -. DR OMA; ETKELGW; -. DR OrthoDB; EOG6RZB0J; -. DR BioCyc; TMAR243274:GC6P-938-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR006301; FlhA. DR InterPro; IPR001712; T3SS_FHIPEP. DR Pfam; PF00771; FHIPEP; 1. DR PIRSF; PIRSF005419; FlhA; 1. DR PRINTS; PR00949; TYPE3IMAPROT. DR TIGRFAMs; TIGR01398; FlhA; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AAD35989.1}; KW Cilium {ECO:0000313|EMBL:AAD35989.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35989.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 122 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 190 210 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 231 253 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 273 306 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 678 AA; 75359 MW; 006E13C0B390ED86 CRC64; MKNVDIIVSL MIVAIVLLMV LPVPDRMLDF FQILNITLSM IILFSTMYIR NALELSSFPT LLLVVTLFRL GLNVASTRLI LLEGPKFQGR VIRTFGDFVV KGDYVVGLIV FFILVIIQFI VITRGAERIA EVAARFTLDA MPGKQMSVDA DLNSGLITEE EARKRREDIR READFYGAMD GASKFVRGDA IASIIIVFIN IIGGLLIGML RHGMSLAEAA QEYVILTVGD GLAAQIPALL VSTATGIIVS RAASKENLGK DLVTELSRET KVLLLTGGVL IFLGIFTPIP FFSAILGGAL IFLAVYTSRA VPQEELAGPA PAERPGGPVL STPEEVSEII QSDTVEVEIG YGLIPLADPS QGGDLLDRIT SIRKQLAFEL GLVVSPIRVR DSVLLKPNEY SIKIRGSEVA RYELVPNRLL AINPGTAKEK IPGIPTREPA FNLEAYWIEE WRKEEAQQKG YTVVDPPTVF ATHLSEVLRR HADELLGFKE LELLIEGLKE KFPKLVEDLI PDVLKPAEIK KVLQRLLKEG VSIRNLPTIF ETLLESAEKS KDIDYLVESV RKALKRQIAS MVRSEDGKIH AIVLERDLEQ KLLESLKEIG EERELLLNPE VSRELMNKIS NELGNLMKKG YQPVIVCSSR IRPYFSRYVM RTIPGVYVIS YDEIPDDYTL QIEGVVKL // ID Q9X2G3_THEMA Unreviewed; 813 AA. AC Q9X2G3; G4FGP0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=Cellobiose phosphorylase {ECO:0000313|EMBL:AGL50787.1}; DE EC=2.4.1.- {ECO:0000313|EMBL:AGL50787.1}; DE SubName: Full=Cellobiose-phosphorylase {ECO:0000313|EMBL:AAD36910.1}; GN OrderedLocusNames=TM_1848 {ECO:0000313|EMBL:AAD36910.1}; GN ORFNames=Tmari_1863 {ECO:0000313|EMBL:AGL50787.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36910.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36910.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36910.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50787.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50787.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36910.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50787.1; -; Genomic_DNA. DR PIR; A72203; A72203. DR RefSeq; NP_229644.1; NC_000853.1. DR RefSeq; WP_004082399.1; NZ_CP011107.1. DR STRING; 243274.TM1848; -. DR CAZy; GH94; Glycoside Hydrolase Family 94. DR EnsemblBacteria; AAD36910; AAD36910; TM_1848. DR EnsemblBacteria; AGL50787; AGL50787; Tmari_1863. DR GeneID; 897337; -. DR KEGG; tma:TM1848; -. DR KEGG; tmi:THEMA_04930; -. DR KEGG; tmm:Tmari_1863; -. DR KEGG; tmw:THMA_1898; -. DR PATRIC; 23938685; VBITheMar51294_1869. DR eggNOG; ENOG4105E2V; Bacteria. DR eggNOG; COG3459; LUCA. DR KO; K00702; -. DR OMA; GSAYHQY; -. DR OrthoDB; EOG6ZWJCM; -. DR BioCyc; TMAR243274:GC6P-1899-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.70.98.40; -; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase-like. DR InterPro; IPR009342; Carb-bd_put_dom. DR InterPro; IPR011013; Gal_mutarotase_SF_dom. DR InterPro; IPR033432; GH36_catalytic. DR InterPro; IPR005196; Glyco_hydro_65_N. DR InterPro; IPR010383; Glyco_hydrolase_94. DR Pfam; PF17167; Glyco_hydro_36; 1. DR Pfam; PF06165; Glyco_transf_36; 1. DR SMART; SM01068; CBM_X; 1. DR SUPFAM; SSF48208; SSF48208; 1. DR SUPFAM; SSF74650; SSF74650; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000313|EMBL:AGL50787.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL50787.1}. FT DOMAIN 1 63 CBM_X. {ECO:0000259|SMART:SM01068}. SQ SEQUENCE 813 AA; 93500 MW; 55FC07E7329D8C41 CRC64; MRFGYFDDVN REYVITTPQT PYPWINYLGT EDFFSIISHM AGGYCFYKDA RLRRITRFRY NNVPTDAGGR YFYIREENGD FWTPTWMPVR KDLSFFEARH GLGYTKITGE RNGLRATITY FVPRHFTGEV HYLVLENKAE KPRKIKLFSF IEFCLWNALD DMTNFQRNYS TGEVEIEGSV IYHKTEYRER RNHYAFYSVN QPIDGFDTDR ESFIGLYSGF EAPQAVVEGK PRNSVASGWA PIASHYLEIE LAPSEKKELI FILGYVENPE EEKWEKPGVI NKKRAKEMIE KFKTGEDVEH ALKELREYWD DLLGRIQVET HDEKLNRMVN IWNQYQCMVT FNISRSASYF ESGISRGIGF RDSNQDILGF VHMIPEKARQ RILDLASIQF EDGSTYHQFQ PLTKKGNNEI GGGFNDDPLW LILSTSAYIK ETGDWSILGE EVPFDNDPNK KASLFEHLKR SFYFTVNNLG PHGLPLIGRA DWNDCLNLNC FSKNPDESFQ TTVNALDGRV AESVFIAGLF VLAGKEFVEI CKRRGLEEEA REAEKHVNKM IETTLKYGWD GEWFLRAYDA FGRKVGSKEC EEGKIFIEPQ GMCVMAGIGV DNGYAEKALD SVKKYLDTPY GLVLQQPAYS RYYIELGEIS SYPPGYKENA GIFCHNNPWV AIAETVIGRG DRAFEIYRKI TPAYLEDISE IHRTEPYVYA QMVAGKDAPR HGEAKNSWLT GTAAWSFVAI TQHILGIRPT YDSLVVDPCI PKEWEGFRIT RKFRGSIYDI TVKNPSHVSK GVKEIIVDGK KIEGQVLPVF EDGKVHRVEV VMG // ID Q9WY89_THEMA Unreviewed; 200 AA. AC Q9WY89; G4FHG1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=Electron transport complex subunit E {ECO:0000256|HAMAP-Rule:MF_00478}; GN OrderedLocusNames=TM_0247 {ECO:0000313|EMBL:AAD35338.1}; GN ORFNames=Tmari_0245 {ECO:0000313|EMBL:AGL49171.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35338.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35338.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35338.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49171.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49171.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000256|HAMAP-Rule:MF_00478}. CC -!- SUBUNIT: Composed of six subunits. {ECO:0000256|HAMAP- CC Rule:MF_00478}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00478}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00478}. CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000256|HAMAP- CC Rule:MF_00478, ECO:0000256|SAAS:SAAS00573673}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35338.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49171.1; -; Genomic_DNA. DR PIR; H72398; H72398. DR RefSeq; NP_228061.1; NC_000853.1. DR RefSeq; WP_004082951.1; NZ_CP011107.1. DR STRING; 243274.TM0247; -. DR EnsemblBacteria; AAD35338; AAD35338; TM_0247. DR EnsemblBacteria; AGL49171; AGL49171; Tmari_0245. DR GeneID; 897154; -. DR KEGG; tma:TM0247; -. DR KEGG; tmi:THEMA_03490; -. DR KEGG; tmm:Tmari_0245; -. DR KEGG; tmw:THMA_0254; -. DR PATRIC; 23935369; VBITheMar51294_0250. DR eggNOG; ENOG4105DZB; Bacteria. DR eggNOG; COG4660; LUCA. DR KO; K03613; -. DR OMA; FDGFAMG; -. DR OrthoDB; EOG6GBMG7; -. DR BioCyc; TMAR243274:GC6P-260-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR HAMAP; MF_00478; RsxE_RnfE; 1. DR InterPro; IPR003667; Rnf-Nqr. DR InterPro; IPR010968; RsxE. DR PANTHER; PTHR30586:SF0; PTHR30586:SF0; 1. DR Pfam; PF02508; Rnf-Nqr; 1. DR PIRSF; PIRSF006102; NQR_DE; 1. DR TIGRFAMs; TIGR01948; rnfE; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00478}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00478}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00478}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00478, KW ECO:0000256|SAAS:SAAS00465084}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00478, KW ECO:0000256|SAAS:SAAS00465084}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00478, KW ECO:0000256|SAAS:SAAS00465084}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00478}. FT TRANSMEM 38 58 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00478}. FT TRANSMEM 70 90 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00478}. FT TRANSMEM 92 112 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00478}. FT TRANSMEM 127 147 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00478}. FT TRANSMEM 166 186 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00478}. SQ SEQUENCE 200 AA; 21748 MW; 2EE7D347F61B41D6 CRC64; MSRLRELTKG IIKENPTYVQ VLGMCPTLAV TTSAINGLGM GLATTAVLTM SNVVISLIRK IVPDKIRIPI FIVVIASFVT MIDLLMHGFA YDLWKTLGLF IPLIVVNCII MGRAESFASK HGVLDSMLDG LGVGLGFTGS LVLLGSVREL FGNGTIFGYK VWELKIFLEI LPPGAYITLG LLSALFTYIG IRRKKRGEAK // ID Q9X0S7_THEMA Unreviewed; 333 AA. AC Q9X0S7; G4FEE6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 102. DE SubName: Full=Maltose operon transcriptional repressor MalR, LacI family {ECO:0000313|EMBL:AGL50131.1}; DE SubName: Full=Transcriptional regulator, LacI family {ECO:0000313|EMBL:AAD36275.1}; GN OrderedLocusNames=TM_1200 {ECO:0000313|EMBL:AAD36275.1}; GN ORFNames=Tmari_1207 {ECO:0000313|EMBL:AGL50131.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36275.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36275.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36275.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50131.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50131.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains HTH lacI-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00590899}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36275.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50131.1; -; Genomic_DNA. DR PIR; F72282; F72282. DR RefSeq; NP_229005.1; NC_000853.1. DR RefSeq; WP_004080120.1; NZ_CP011107.1. DR STRING; 243274.TM1200; -. DR EnsemblBacteria; AAD36275; AAD36275; TM_1200. DR EnsemblBacteria; AGL50131; AGL50131; Tmari_1207. DR GeneID; 898284; -. DR KEGG; tma:TM1200; -. DR KEGG; tmi:THEMA_08330; -. DR KEGG; tmm:Tmari_1207; -. DR KEGG; tmw:THMA_1226; -. DR PATRIC; 23937342; VBITheMar51294_1218. DR eggNOG; ENOG4105ETE; Bacteria. DR eggNOG; COG1609; LUCA. DR KO; K02529; -. DR OMA; PRYDIGR; -. DR OrthoDB; EOG6SJJMM; -. DR BioCyc; TMAR243274:GC6P-1230-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR001761; Peripla_BP/Lac1_sug-bd_dom. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR000843; Tscrpt_reg_HTH_LacI. DR Pfam; PF00356; LacI; 1. DR Pfam; PF00532; Peripla_BP_1; 1. DR PRINTS; PR00036; HTHLACI. DR SMART; SM00354; HTH_LACI; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF53822; SSF53822; 1. DR PROSITE; PS00356; HTH_LACI_1; 1. DR PROSITE; PS50932; HTH_LACI_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00590989}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00590865}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00590865}. FT DOMAIN 6 60 HTH lacI-type DNA-binding. FT {ECO:0000259|PROSITE:PS50932}. SQ SEQUENCE 333 AA; 38172 MW; D33D84041C3A657F CRC64; MKKKYVTIRD IAEKAGVSIN TVSRALNNKP DISEETRRKI LKIAQELGYV KNATASSLRS KQTNIVGVII ADSANPFYAE VLKGIEAASR KYGYQIMLMN TERIYENEEK AIEVLLQRRV DGLLITPVQD RSDDIKTLIE RKVPFVIVGR HFEELEVDEI HSDEVKGGYL ATRHLIERGR KNIIMISGYL FKSAAYMRLE GYRKALKEYG IPFSEKMIIE TDIDIESGYR AMREAIEKGL EFEAVFCYND LLAFGVIKAL KECGYRIPED VAVVGYDDIV YSSFICPSLT TVRIKKFEMG FEAFRMLLQR LKGRRKKRKR VILDVELVVR ESG // ID Q9WYR5_THEMA Unreviewed; 470 AA. AC Q9WYR5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 99. DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:AGL49356.1}; DE EC=3.2.1.20 {ECO:0000313|EMBL:AGL49356.1}; DE SubName: Full=Alpha-glucosidase, putative {ECO:0000313|EMBL:AAD35519.1}; GN OrderedLocusNames=TM_0434 {ECO:0000313|EMBL:AAD35519.1}; GN ORFNames=Tmari_0431 {ECO:0000313|EMBL:AGL49356.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35519.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35519.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35519.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49356.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49356.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000256|RuleBase:RU361152}; CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. CC {ECO:0000256|RuleBase:RU361152}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35519.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49356.1; -; Genomic_DNA. DR PIR; E72376; E72376. DR RefSeq; NP_228244.1; NC_000853.1. DR RefSeq; WP_010865118.1; NZ_CP011107.1. DR SMR; Q9WYR5; 4-466. DR STRING; 243274.TM0434; -. DR CAZy; GH4; Glycoside Hydrolase Family 4. DR EnsemblBacteria; AAD35519; AAD35519; TM_0434. DR EnsemblBacteria; AGL49356; AGL49356; Tmari_0431. DR GeneID; 897448; -. DR KEGG; tma:TM0434; -. DR KEGG; tmi:THEMA_02555; -. DR KEGG; tmm:Tmari_0431; -. DR KEGG; tmw:THMA_0440; -. DR PATRIC; 23935753; VBITheMar51294_0440. DR eggNOG; ENOG4107V4V; Bacteria. DR eggNOG; COG1486; LUCA. DR KO; K01187; -. DR KO; K07406; -. DR OMA; VIMECAK; -. DR OrthoDB; EOG6TJ7TJ; -. DR BioCyc; MetaCyc:MONOMER-17961; -. DR BioCyc; TMAR243274:GC6P-449-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR InterPro; IPR019802; GlycHydrolase_4_CS. DR InterPro; IPR001088; Glyco_hydro_4. DR InterPro; IPR022616; Glyco_hydro_4_C. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF02056; Glyco_hydro_4; 1. DR Pfam; PF11975; Glyco_hydro_4C; 1. DR PRINTS; PR00732; GLHYDRLASE4. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF56327; SSF56327; 1. DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361152, KW ECO:0000313|EMBL:AGL49356.1}; KW Hydrolase {ECO:0000256|RuleBase:RU361152, KW ECO:0000313|EMBL:AGL49356.1}; NAD {ECO:0000256|RuleBase:RU361152}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 202 438 Glyco_hydro_4C. FT {ECO:0000259|Pfam:PF11975}. SQ SEQUENCE 470 AA; 54621 MW; 5AAE5B7EEF836319 CRC64; MPTIVFVGAG SVRYTIKLVG DLAKTPDLYG SRLVLMDIDE ERLKATYILV TKYLRELNAE YTVEQTTSLE EALEGADFVI NTALYRAPGH EDGYVHYEIM REVGERHGYY RGIDSQELNM VSDYYTLSNY NHLKMSLDIA KAVEKIAPNA WILQTANPVF EITQLVKRLT KAKIVGFCHG YAHVFHLAKV LGVEPEELDW QVAGVNHAIW MNRFRCRGED LYPKLDEWIE ENASRWEPKN PWDVDFSPAA IDMYRFYGMY PIGDTVRSGT WKYHYDLETK KRWYGKFGGI DNEVERPKFY ESLREQRKRL MELAKEVEKD PTIELTKVWP EVFTTGSESV EQHIPFINAL VNDKKARLVL NVENRGVIKG IPDDVMVEVP VVVDKEGIHP EKIEPDLTDR IKKFYLLPRI LRMEWTLEAF ISGDRRVLEE ILVRDPRTRS YEQAVAVIDD ILNLPFNEEM KKHYSKVGKN // ID Q9WYK9_THEMA Unreviewed; 241 AA. AC Q9WYK9; G4FHT8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 80. DE RecName: Full=UPF0721 transmembrane protein {ECO:0000256|RuleBase:RU363041}; GN OrderedLocusNames=TM_0376 {ECO:0000313|EMBL:AAD35463.1}; GN ORFNames=Tmari_0374 {ECO:0000313|EMBL:AGL49299.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35463.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35463.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35463.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49299.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49299.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363041}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363041}. CC -!- SIMILARITY: Belongs to the UPF0721 family. CC {ECO:0000256|RuleBase:RU363041}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35463.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49299.1; -; Genomic_DNA. DR PIR; F72385; F72385. DR RefSeq; NP_228187.1; NC_000853.1. DR RefSeq; WP_004083192.1; NZ_CP011107.1. DR DNASU; 897347; -. DR EnsemblBacteria; AAD35463; AAD35463; TM_0376. DR EnsemblBacteria; AGL49299; AGL49299; Tmari_0374. DR GeneID; 897347; -. DR KEGG; tma:TM0376; -. DR KEGG; tmi:THEMA_02835; -. DR KEGG; tmm:Tmari_0374; -. DR KEGG; tmw:THMA_0384; -. DR PATRIC; 23935633; VBITheMar51294_0381. DR eggNOG; ENOG4107WBU; Bacteria. DR eggNOG; COG0730; LUCA. DR KO; K07090; -. DR OMA; AYTYYKQ; -. DR OrthoDB; EOG6NPM68; -. DR BioCyc; TMAR243274:GC6P-390-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR InterPro; IPR002781; TM_pro_TauE-like. DR PANTHER; PTHR30269; PTHR30269; 1. DR Pfam; PF01925; TauE; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU363041}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363041}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363041}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 70 89 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 95 113 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 129 158 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 170 189 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 196 217 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 223 240 Helical. {ECO:0000256|RuleBase:RU363041}. SQ SEQUENCE 241 AA; 26253 MW; 7BBF48B59F24D38D CRC64; MIVLVFLGGI LAGFLNVLAG GGSMITLPIL TALGLGIDVA NGTNRIAIIL QNLVAIERFK AKKVLKIKEA ILVALPAIVG AILGSSIAVQ IEKEMLQKIV GVIFLVMAVS LVWKPRIWLE DRFVKRNWVL IYIVFFLIGI YGGFIQAGVG FLLMPAIALL LGYELVKTNA VKVFIVASYN IISLVIFILN GKVNFLYGFI LALGNMTGAW LAATFSIKKG ANWVRWIVFT AVIVVGIRYV F // ID Q9WZ90_THEMA Unreviewed; 388 AA. AC Q9WZ90; G4FDK0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 88. DE SubName: Full=Lipopolysaccharide biosynthesis protein, putative {ECO:0000313|EMBL:AAD35706.1}; GN OrderedLocusNames=TM_0622 {ECO:0000313|EMBL:AAD35706.1}; GN ORFNames=Tmari_0623 {ECO:0000313|EMBL:AGL49548.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35706.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35706.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35706.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49548.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49548.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35706.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49548.1; -; Genomic_DNA. DR PIR; E72354; E72354. DR RefSeq; NP_228431.1; NC_000853.1. DR RefSeq; WP_004081188.1; NZ_CP011107.1. DR STRING; 243274.TM0622; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAD35706; AAD35706; TM_0622. DR EnsemblBacteria; AGL49548; AGL49548; Tmari_0623. DR GeneID; 897709; -. DR KEGG; tma:TM0622; -. DR KEGG; tmm:Tmari_0623; -. DR KEGG; tmw:THMA_0638; -. DR PATRIC; 23936157; VBITheMar51294_0632. DR eggNOG; ENOG4105DNM; Bacteria. DR eggNOG; COG0438; LUCA. DR OMA; HTIHTVA; -. DR OrthoDB; EOG68Q0SH; -. DR BioCyc; TMAR243274:GC6P-647-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 13 182 Glyco_trans_4-like_N. FT {ECO:0000259|Pfam:PF13439}. FT DOMAIN 188 349 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 388 AA; 43648 MW; 6BAA1BE01157F306 CRC64; MIKVLHIIPS LAVGGAEKLV SDMVEFADRS RFDVAVMRIT GTDSFLVEKL TSKGYQVYTI VLDYEAIAPS KVIRRLLRAI KNMRRTYNLL REIRPDIIHS HLSALRIALI PALLCRIPVK VHTIHTVAEK DAKGITRFFN RIAFKFFGFV PVSISQEVAE SVKKLYGRKI STPVIYNGID VQKFSIDQPK RVDRDKTILI NVARLSREKN HALLVRAFSK AVQSCPNLEL WLVGDGELRR DIEELVKQLG LEEKVKFFGV RSDVPELLSQ ADIFVLSSDY EGFGLVVAEA MAAGLPVIAT AIGGIPEILE GGRAGILVPP KDVDALAKAI VELARDEKKR AELSDYGRKL VAERFDIRRT VREYEKLYLE LLEKKKGSKK FRIKGNVL // ID Q9X294_THEMA Unreviewed; 538 AA. AC Q9X294; G4FGG0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 102. DE SubName: Full=TPR repeat-containing protein {ECO:0000313|EMBL:AGL50706.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36836.1}; GN OrderedLocusNames=TM_1773 {ECO:0000313|EMBL:AAD36836.1}; GN ORFNames=Tmari_1782 {ECO:0000313|EMBL:AGL50706.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36836.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36836.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36836.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50706.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50706.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36836.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50706.1; -; Genomic_DNA. DR PIR; D72213; D72213. DR RefSeq; NP_229570.1; NC_000853.1. DR RefSeq; WP_004082319.1; NZ_CP011107.1. DR STRING; 243274.TM1773; -. DR EnsemblBacteria; AAD36836; AAD36836; TM_1773. DR EnsemblBacteria; AGL50706; AGL50706; Tmari_1782. DR GeneID; 897047; -. DR KEGG; tma:TM1773; -. DR KEGG; tmi:THEMA_05360; -. DR KEGG; tmm:Tmari_1782; -. DR KEGG; tmw:THMA_1817; -. DR PATRIC; 23938528; VBITheMar51294_1793. DR eggNOG; ENOG4107YA5; Bacteria. DR eggNOG; COG0457; LUCA. DR OMA; FESPDIF; -. DR OrthoDB; EOG6M9F2Q; -. DR BioCyc; TMAR243274:GC6P-1822-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF13414; TPR_11; 1. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00028; TPR; 5. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50005; TPR; 5. DR PROSITE; PS50293; TPR_REGION; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 103 305 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 538 AA; 63643 MW; 351B118460FFB524 CRC64; MRGGNIKAIV YLPLDPEKAK QNNLPVKLPV LAEDLPKVLE EDRIPLDVIL RGLEAQYEIT KDEYYRSYYV FFLYEKFKQL LREGKLDEAE KILEKAKEVQ YDYRYHFYRG LLLKHRGELG EAEIEMRLAI SMNDRFAPAY FELAGILKEK NEIEDSLLFY EKAYEVNKEF LLPLLKKGDL LLEEGRLEEA IEEYRRILEK DSNFVEVYER LGVIYNQLQR FKEAEKFFKK ALEIERKDHV EYNLSYTLIK LGKLFEALEI LKRLYEKNPD DPMVANEYGL LLKTLGLYEE ALEVFEDAYR RHKEEEILKY NYGTILLHFE KEKAVSILSE ISGELKDRAE FMISLAEKDV VIPSYEEFEW LKDYFFEGTI DVVALSEEID SEDEDAKRRI ERLREGEFPF YDTTLDSSEM LEVILGIMFE SPDIFKMEEN AVKFVSAFYG SSVMIASTIV LTRTFQYFLA EEEPTMEELL RELVAETQDV NWKFSLRLAR FRHADRFDFN RLSDLVIAFL QSIEQGTPVS DDERLKYLLE KLTFQKEG // ID G4FFG0_THEMA Unreviewed; 626 AA. AC G4FFG0; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 11-MAY-2016, entry version 45. DE SubName: Full=Fe-hydrogenase, subunit beta {ECO:0000313|EMBL:AAD36495.1}; DE SubName: Full=NAD-reducing hydrogenase subunit HoxF {ECO:0000313|EMBL:AGL50355.1}; DE EC=1.12.1.2 {ECO:0000313|EMBL:AGL50355.1}; GN OrderedLocusNames=TM_1425 {ECO:0000313|EMBL:AAD36495.1}; GN ORFNames=Tmari_1431 {ECO:0000313|EMBL:AGL50355.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AGL50355.1, ECO:0000313|Proteomes:UP000013901}; RN [1] {ECO:0000313|EMBL:AAD36495.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36495.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50355.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50355.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36495.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50355.1; -; Genomic_DNA. DR PIR; F72256; F72256. DR RefSeq; NP_229225.1; NC_000853.1. DR RefSeq; WP_004081675.1; NZ_CP011107.1. DR STRING; 243274.TM1425; -. DR EnsemblBacteria; AAD36495; AAD36495; TM_1425. DR EnsemblBacteria; AGL50355; AGL50355; Tmari_1431. DR GeneID; 898050; -. DR KEGG; tma:TM1425; -. DR KEGG; tmi:THEMA_07190; -. DR KEGG; tmm:Tmari_1431; -. DR KEGG; tmw:THMA_1455; -. DR eggNOG; ENOG4107EEP; Bacteria. DR eggNOG; COG1145; LUCA. DR eggNOG; COG1894; LUCA. DR KO; K17998; -. DR OMA; LVKIMPY; -. DR BioCyc; TMAR243274:GC6P-1463-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0047985; F:hydrogen dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IBA:GO_Central. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS. DR InterPro; IPR011538; Nuo51_FMN-bd. DR InterPro; IPR019575; Nuop51_4Fe4S-bd. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF01512; Complex1_51K; 1. DR Pfam; PF10589; NADH_4Fe-4S; 1. DR SMART; SM00928; NADH_4Fe-4S; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. DR PROSITE; PS00645; COMPLEX1_51K_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Homeobox {ECO:0000313|EMBL:AGL50355.1}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50355.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 569 598 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 599 626 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 626 AA; 68681 MW; 38D3218E44EA460F CRC64; MFKNAKEFVQ YANKLKTLRE KKLNGVSIYV CVGTGCTAKG ALKVYSAFEE ELKKRNLLGQ VTLEKIDDDK VTLNRTGCCG RCSSGPLVKI MPYRFFYSNV APEDVPEIVD RTVLKGEPIE RLFLTDPLTG EKVPRIEDTT LFKNQDFYIM EAIGESECDS IEDYIARSGY ESLVKALTSM TPEEIIETVK ASGLRGRGGG GFPTGLKWEF TRKAQGDIKF VVCNGDEGDP GAFMNRTLLE RDPHLVLEGM IIAGYAVGAQ KGYAYIRAEY PFAVKMFKKA IEDARKLGLL GENILGTGFS FDLEVKEGAG AFVCGEETAL LASIEGKRGM PRPKPPFPAQ SGLWGKPTLI NNVETYANIP RILRDGVENY RKRGTENSPG TKMFSVAGPL KATGIIEVEF GTTLRDIIYN ICGGFVEGEE FKAVQIGGPS GACLSEDFID MPLDYDTLKK ADAMVGSGGI VVITKKTCMV EVARFFLDFT KRESCGKCVP CREGTMQAYN ILEKFTHGKA TYEDLKTLEH LSKTIKTASL CGLGKTAPNP ILSTLKLFRE EYIAHIEGEC PSGMCTAFKK YVINPDICKG CGLCARSCPQ NAITGERGKP YTIDQEKCVK CGLCASKCPF KAIELV // ID Q9WYF0_THEMA Unreviewed; 59 AA. AC Q9WYF0; G4FHM8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 100. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35402.1}; GN OrderedLocusNames=TM_0314 {ECO:0000313|EMBL:AAD35402.1}; GN ORFNames=Tmari_0312 {ECO:0000313|EMBL:AGL49238.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35402.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35402.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35402.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49238.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49238.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35402.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49238.1; -; Genomic_DNA. DR PIR; A72392; A72392. DR RefSeq; NP_228126.1; NC_000853.1. DR RefSeq; WP_004083052.1; NZ_CP011107.1. DR STRING; 243274.TM0314; -. DR EnsemblBacteria; AAD35402; AAD35402; TM_0314. DR EnsemblBacteria; AGL49238; AGL49238; Tmari_0312. DR GeneID; 897255; -. DR KEGG; tma:TM0314; -. DR KEGG; tmi:THEMA_03155; -. DR KEGG; tmm:Tmari_0312; -. DR KEGG; tmw:THMA_0321; -. DR PATRIC; 23935507; VBITheMar51294_0319. DR eggNOG; ENOG4108E3H; Bacteria. DR eggNOG; COG3350; LUCA. DR OMA; VEKVEYM; -. DR OrthoDB; EOG6J48TT; -. DR BioCyc; TMAR243274:GC6P-327-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 1.10.620.20; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012348; RNR-rel. DR InterPro; IPR011017; TRASH_dom. DR InterPro; IPR007029; YHS_dom. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF04945; YHS; 1. DR SMART; SM00746; TRASH; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 29 53 C2H2-type. {ECO:0000259|PROSITE:PS50157}. SQ SEQUENCE 59 AA; 6887 MW; C3611A435ECB658D CRC64; MKVKDPVCGM KIEKEEAAEK IEYMGKEYYF CSQECAEKFK DNPEQYAHQK NSHGHGCCH // ID Q9WZK6_THEMA Unreviewed; 402 AA. AC Q9WZK6; G4FD76; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 98. DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:AAD35828.1}; DE SubName: Full=Peptidase, S41 family {ECO:0000313|EMBL:AGL49673.1}; GN OrderedLocusNames=TM_0747 {ECO:0000313|EMBL:AAD35828.1}; GN ORFNames=Tmari_0748 {ECO:0000313|EMBL:AGL49673.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35828.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35828.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35828.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49673.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49673.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the peptidase S41A family. CC {ECO:0000256|RuleBase:RU004404}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35828.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49673.1; -; Genomic_DNA. DR PIR; F72340; F72340. DR RefSeq; NP_228556.1; NC_000853.1. DR RefSeq; WP_004080969.1; NZ_CP011107.1. DR STRING; 243274.TM0747; -. DR EnsemblBacteria; AAD35828; AAD35828; TM_0747. DR EnsemblBacteria; AGL49673; AGL49673; Tmari_0748. DR GeneID; 898414; -. DR KEGG; tma:TM0747; -. DR KEGG; tmi:THEMA_00920; -. DR KEGG; tmm:Tmari_0748; -. DR KEGG; tmw:THMA_0765; -. DR PATRIC; 23936414; VBITheMar51294_0760. DR eggNOG; ENOG4105CN1; Bacteria. DR eggNOG; COG0793; LUCA. DR KO; K03797; -. DR OMA; NIMQVEY; -. DR OrthoDB; EOG6PS5W5; -. DR BioCyc; TMAR243274:GC6P-773-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.90.226.10; -; 1. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR001478; PDZ. DR InterPro; IPR004447; Peptidase_S41A. DR InterPro; IPR005151; Tail-specific_protease. DR Pfam; PF13180; PDZ_2; 1. DR Pfam; PF03572; Peptidase_S41; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00245; TSPc; 1. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF52096; SSF52096; 2. DR TIGRFAMs; TIGR00225; prc; 1. DR PROSITE; PS50106; PDZ; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|RuleBase:RU004404}; KW Protease {ECO:0000256|RuleBase:RU004404}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Serine protease {ECO:0000256|RuleBase:RU004404}. FT DOMAIN 94 160 PDZ (DHR). {ECO:0000259|PROSITE:PS50106}. SQ SEQUENCE 402 AA; 44180 MW; C1C50D317D82A4B6 CRC64; MRLNQISKFA IVSVVVLVLA LLLGGSAKTN LTVEEVNKAL EPFFDSLSYI LNYYYEADKL DINKLIDHAI DGLVKGTGDD FSYYQDPETY RENQIEMKGE YGGLGIEVTY DAEHGAIKVV APMYGTPAWR AGLKAGDLII TIDGTPVSKM TYMEAVNNLR GEPGTSVTIE VLRDGEKLTF TIVREKIEIK MVLYSFIETE KGSIGYVRIT RFGEKADSDM KNALDKIFEK GVKGLIIDVR DNPGGYLDVA LKIVSMFVDK GVILKVRNGF GEEDVYESYG NSYPNVPIVL LVNEGSASAS EILTGALKDL GIATVVGRKT FGKGSVQTGF PLSNGGVLFL TTAHYLTPSG KDIHKIGIEP DVLVEESVEE ELHAETREQI EVDPEKDPFV KKGLEVLLEK IK // ID Q9X0P6_THEMA Unreviewed; 490 AA. AC Q9X0P6; G4FEI3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 84. DE SubName: Full=Diguanylate cyclase (GGDEF domain) with PAS/PAC sensor {ECO:0000313|EMBL:AGL50094.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36239.1}; GN OrderedLocusNames=TM_1163 {ECO:0000313|EMBL:AAD36239.1}; GN ORFNames=Tmari_1170 {ECO:0000313|EMBL:AGL50094.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36239.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36239.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36239.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50094.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50094.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains GGDEF domain. CC {ECO:0000256|SAAS:SAAS00496774}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36239.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50094.1; -; Genomic_DNA. DR PIR; A72288; A72288. DR RefSeq; NP_228969.1; NC_000853.1. DR RefSeq; WP_004080207.1; NZ_CP011107.1. DR STRING; 243274.TM1163; -. DR EnsemblBacteria; AAD36239; AAD36239; TM_1163. DR EnsemblBacteria; AGL50094; AGL50094; Tmari_1170. DR GeneID; 898323; -. DR KEGG; tma:TM1163; -. DR KEGG; tmi:THEMA_08520; -. DR KEGG; tmm:Tmari_1170; -. DR KEGG; tmw:THMA_1188; -. DR PATRIC; 23937263; VBITheMar51294_1180. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR OMA; NEWIFSH; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1192-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR029016; GAF_dom-like. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR Pfam; PF00990; GGDEF; 1. DR SMART; SM00267; GGDEF; 1. DR SUPFAM; SSF55073; SSF55073; 1. DR SUPFAM; SSF55781; SSF55781; 1. DR TIGRFAMs; TIGR00254; GGDEF; 1. DR PROSITE; PS50887; GGDEF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 367 490 GGDEF. {ECO:0000259|PROSITE:PS50887}. SQ SEQUENCE 490 AA; 56892 MW; 1D72B5EA4512B961 CRC64; MQVFFYVVSF GFLVFALYLF CHVRKKIEYY RRLEKSFDTI VDGLSKLDPN SPEEEFFQKI LNIAMEVVPE AVKGSVSRIT PSGDWIFVAS RGHIVDLLGK RFPSRYLFRA GRDPVEVNFL DYDRDLFPDD MWKFFERTLR GTKKSLVVGI FSGDEFVGNI ALDSPYSGFS ELSKKVLKSL GNLASTYLLM RKTLANEQQL QKVMSTIFTL LLLFRKSISV EEFLKEALQK IVEASNVFTG GIVFEGNIPV FHTDLEEIPE FDFEESKEEE KIEKLVKDGV HYIVVHLDYK DMPSYHMVFL SNEDIAPSFF SVLNTFAEVV SLYLREYHLH QKYRELALKD PLTEAYSRHY FNEWIFSHMA WLRRNQKKSV LVIMDVDGLK MINDTYGHLM GDKALVEFVK TLKRTVRESD LVFRYGGDEF LLVLVDSTKD NAASVLERVE ENLKDVDLPF KIEFSFGYEE IDGFMPIERA LARADDLLYK NKFEKRGGSE // ID Q9WYP3_THEMA Unreviewed; 395 AA. AC Q9WYP3; G4FHX1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 128. DE SubName: Full=Alcohol dehydrogenase, zinc-containing {ECO:0000313|EMBL:AAD35497.1}; DE SubName: Full=L-threonine 3-dehydrogenase {ECO:0000313|EMBL:AGL49334.1}; DE EC=1.1.1.103 {ECO:0000313|EMBL:AGL49334.1}; GN OrderedLocusNames=TM_0412 {ECO:0000313|EMBL:AAD35497.1}; GN ORFNames=Tmari_0409 {ECO:0000313|EMBL:AGL49334.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35497.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35497.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35497.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49334.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49334.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU361277}; CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000256|RuleBase:RU361277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35497.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49334.1; -; Genomic_DNA. DR PIR; B72381; B72381. DR RefSeq; NP_228222.1; NC_000853.1. DR RefSeq; WP_004083260.1; NZ_CP011107.1. DR PDB; 3IP1; X-ray; 2.09 A; A/B/C/D=2-395. DR PDBsum; 3IP1; -. DR STRING; 243274.TM0412; -. DR DNASU; 897413; -. DR EnsemblBacteria; AAD35497; AAD35497; TM_0412. DR EnsemblBacteria; AGL49334; AGL49334; Tmari_0409. DR GeneID; 897413; -. DR KEGG; tma:TM0412; -. DR KEGG; tmi:THEMA_02665; -. DR KEGG; tmm:Tmari_0409; -. DR KEGG; tmw:THMA_0418; -. DR PATRIC; 23935707; VBITheMar51294_0417. DR eggNOG; ENOG4105CPQ; Bacteria. DR eggNOG; COG1063; LUCA. DR OMA; EFTNAPE; -. DR OrthoDB; EOG64R669; -. DR BioCyc; MetaCyc:MONOMER-17949; -. DR BioCyc; TMAR243274:GC6P-427-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020843; PKS_ER. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3IP1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000256|RuleBase:RU361277}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49334.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000256|RuleBase:RU361277}. FT METAL 66 66 Cadmium 1. {ECO:0000213|PDB:3IP1}. FT METAL 95 95 Cadmium 1; via tele nitrogen. FT {ECO:0000213|PDB:3IP1}. FT METAL 96 96 Cadmium 1. {ECO:0000213|PDB:3IP1}. FT METAL 131 131 Cadmium 2. {ECO:0000213|PDB:3IP1}. FT METAL 134 134 Cadmium 2. {ECO:0000213|PDB:3IP1}. FT METAL 137 137 Cadmium 2. {ECO:0000213|PDB:3IP1}. FT METAL 145 145 Cadmium 2. {ECO:0000213|PDB:3IP1}. FT METAL 193 193 Cadmium 1. {ECO:0000213|PDB:3IP1}. SQ SEQUENCE 395 AA; 43317 MW; 29D2A19F00946397 CRC64; MRAVRLHAKW DPRPEFKLGP KDIEGKLTWL GSKVWRYPEV RVEEVPEPRI EKPTEIIIKV KACGICGSDV HMAQTDEEGY ILYPGLTGFP VTLGHEFSGV VVEAGPEAIN RRTNKRFEIG EPVCAEEMLW CGHCRPCAEG FPNHCENLNE LGFNVDGAFA EYVKVDAKYA WSLRELEGVY EGDRLFLAGS LVEPTSVAYN AVIVRGGGIR PGDNVVILGG GPIGLAAVAI LKHAGASKVI LSEPSEVRRN LAKELGADHV IDPTKENFVE AVLDYTNGLG AKLFLEATGV PQLVWPQIEE VIWRARGINA TVAIVARADA KIPLTGEVFQ VRRAQIVGSQ GHSGHGTFPR VISLMASGMD MTKIISKTVS MEEIPEYIKR LQTDKSLVKV TMLNE // ID Q9X0N1_THEMA Unreviewed; 387 AA. AC Q9X0N1; G4FEK0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36223.1}; GN OrderedLocusNames=TM_1147 {ECO:0000313|EMBL:AAD36223.1}; GN ORFNames=Tmari_1154 {ECO:0000313|EMBL:AGL50078.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36223.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36223.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36223.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50078.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50078.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36223.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50078.1; -; Genomic_DNA. DR PIR; G72288; G72288. DR RefSeq; NP_228953.1; NC_000853.1. DR RefSeq; WP_004080234.1; NZ_CP011107.1. DR STRING; 243274.TM1147; -. DR EnsemblBacteria; AAD36223; AAD36223; TM_1147. DR EnsemblBacteria; AGL50078; AGL50078; Tmari_1154. DR GeneID; 898339; -. DR KEGG; tma:TM1147; -. DR KEGG; tmi:THEMA_08605; -. DR KEGG; tmm:Tmari_1154; -. DR KEGG; tmw:THMA_1171; -. DR PATRIC; 23937231; VBITheMar51294_1164. DR eggNOG; ENOG4105DW3; Bacteria. DR eggNOG; COG3437; LUCA. DR OMA; DILMESK; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1176-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR SUPFAM; SSF52172; SSF52172; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 180 317 HDc. {ECO:0000259|SMART:SM00471}. FT COILED 141 175 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 387 AA; 44779 MW; 9A8DE2463A4CCCFC CRC64; MRLLLYTEDS SVEWIKPLLT QIGVEIVECE HGDINGKLQD VDGVFLVLNT VTDEIVEKIK SVRRKTDRFV LVAVPHNEDW FEALEDAGVD DLIFRPINPS ELVSVIEHMF RTRKFYETKT SHKRTREESW MNIIKSQQKE IVEYVRREES YIRERDKLRR ENRELLEELY TLLLRVIELK DYETHEHTLR VGRISALVAE AMGCSSEFVE LIEKAAPFHD IGKVFIPESI LLKRGKLTSD EYEIMKLHTI FGYELLKTSK NPVLSLAAEV ALFHHEKYNG KGYPHGLKGD EIPLSAQIAA VADSFDAMVS HRPYKIRKSF DEAIREIKDL SGRFYSPFVV KAFVQTIDEI RKLYNWGTKG DDIISNSSHH RKGGTKDGES QSQKSYC // ID Q9X1T4_THEMA Unreviewed; 189 AA. AC Q9X1T4; G4FFY6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 107. DE RecName: Full=RNA polymerase sigma factor {ECO:0000256|RuleBase:RU000716}; GN OrderedLocusNames=TM_1598 {ECO:0000313|EMBL:AAD36665.1}; GN ORFNames=Tmari_1606 {ECO:0000313|EMBL:AGL50530.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36665.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36665.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36665.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50530.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50530.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily. CC {ECO:0000256|RuleBase:RU000716, ECO:0000256|SAAS:SAAS00565917}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36665.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50530.1; -; Genomic_DNA. DR PIR; B72234; B72234. DR RefSeq; NP_229398.1; NC_000853.1. DR RefSeq; WP_004082042.1; NZ_CP011107.1. DR STRING; 243274.TM1598; -. DR EnsemblBacteria; AAD36665; AAD36665; TM_1598. DR EnsemblBacteria; AGL50530; AGL50530; Tmari_1606. DR GeneID; 897942; -. DR KEGG; tma:TM1598; -. DR KEGG; tmi:THEMA_06260; -. DR KEGG; tmm:Tmari_1606; -. DR KEGG; tmw:THMA_1638; -. DR PATRIC; 23938170; VBITheMar51294_1617. DR eggNOG; ENOG4105EMN; Bacteria. DR eggNOG; COG1595; LUCA. DR KO; K03088; -. DR OMA; DYKFRAV; -. DR OrthoDB; EOG6ZD6DW; -. DR BioCyc; TMAR243274:GC6P-1644-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR000838; RNA_pol_sigma70_ECF_CS. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR013249; RNA_pol_sigma70_r4_t2. DR InterPro; IPR013325; RNA_pol_sigma_r2. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04542; Sigma70_r2; 1. DR Pfam; PF08281; Sigma70_r4_2; 1. DR SUPFAM; SSF88659; SSF88659; 1. DR SUPFAM; SSF88946; SSF88946; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. DR PROSITE; PS01063; SIGMA70_ECF; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000716, KW ECO:0000256|SAAS:SAAS00457605}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Sigma factor {ECO:0000256|RuleBase:RU000716, KW ECO:0000256|SAAS:SAAS00458134}; KW Transcription {ECO:0000256|RuleBase:RU000716, KW ECO:0000256|SAAS:SAAS00458134}; KW Transcription regulation {ECO:0000256|RuleBase:RU000716, KW ECO:0000256|SAAS:SAAS00458134}. FT DOMAIN 21 86 Sigma70_r2. {ECO:0000259|Pfam:PF04542}. FT DOMAIN 125 177 Sigma70_r4_2. {ECO:0000259|Pfam:PF08281}. SQ SEQUENCE 189 AA; 22233 MW; A380DA3758416437 CRC64; MNEKKLVEAL KRKEDWAYEV LYREFAPKIG SIAKSFLNTD DVDDVVQDVF LRIFKGIKKF RGDSKLSTWI YRIAVNVCKD YLQKYKKRNE FLTDFQEKDN EEEIYIQPEA KENVLDEVLR SITAERVQKA LEKLSPEDRL LIKLRDIDGL SYEEIASVLQ KPVGTVKSRL HYARKRLGNL LKEGETVER // ID Q9X0V2_THEMA Unreviewed; 326 AA. AC Q9X0V2; G4FEC1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 85. DE SubName: Full=Putative glycoside hydrolase {ECO:0000313|EMBL:AGL50156.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36300.1}; GN OrderedLocusNames=TM_1225 {ECO:0000313|EMBL:AAD36300.1}; GN ORFNames=Tmari_1232 {ECO:0000313|EMBL:AGL50156.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36300.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36300.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36300.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50156.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50156.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36300.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50156.1; -; Genomic_DNA. DR PIR; B72278; B72278. DR RefSeq; NP_229030.1; NC_000853.1. DR RefSeq; WP_004080062.1; NZ_CP011107.1. DR PDB; 1VKD; X-ray; 2.10 A; A/B/C/D/E/F=1-326. DR PDBsum; 1VKD; -. DR STRING; 243274.TM1225; -. DR EnsemblBacteria; AAD36300; AAD36300; TM_1225. DR EnsemblBacteria; AGL50156; AGL50156; Tmari_1232. DR GeneID; 898259; -. DR KEGG; tma:TM1225; -. DR KEGG; tmi:THEMA_08205; -. DR KEGG; tmm:Tmari_1232; -. DR KEGG; tmw:THMA_1251; -. DR PATRIC; 23937392; VBITheMar51294_1243. DR eggNOG; ENOG4105CKB; Bacteria. DR eggNOG; COG2152; LUCA. DR KO; K18785; -. DR OMA; ENAFLPF; -. DR OrthoDB; EOG6HF5W0; -. DR BioCyc; TMAR243274:GC6P-1255-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 2.115.10.20; -; 1. DR InterPro; IPR023296; Glyco_hydro_beta-prop. DR InterPro; IPR007184; Mannoside_phosphorylase. DR Pfam; PF04041; Glyco_hydro_130; 1. DR PIRSF; PIRSF016202; PH1107; 1. DR SUPFAM; SSF75005; SSF75005; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VKD}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50156.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 326 AA; 37258 MW; 44CCF0A99EA7CE6D CRC64; MKVFTEKIPN IPWEERPEGY TGPVWRYSKN PIIGRNPVPK GARVFNSAVV PYNGEFVGVF RIDHKNTRPF LHFGRSKDGI NWEIEPEEIQ WVDVNGEPFQ PSYAYDPRVV KIEDTYYITF CTDDHGPTIG VGMTKDFKTF VRLPNAYVPF NRNGVLFPRK INGKYVMLNR PSDNGHTPFG DIFLSESPDM IHWGNHRFVL GRSSYNWWEN LKIGAGPYPI ETSEGWLLIY HGVTLTCNGY VYSFGAALLD LDDPSKVLYR SRYYLLTPEE EYETVGFVPN VVFPCAALCD ADTGRVAIYY GAADTHVALA FGYIDEIVDF VKRNSM // ID Q9X268_THEMA Unreviewed; 642 AA. AC Q9X268; G4FGD2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein {ECO:0000313|EMBL:AAD36811.1}; DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein OppA {ECO:0000313|EMBL:AGL50678.1}; GN OrderedLocusNames=TM_1746 {ECO:0000313|EMBL:AAD36811.1}; GN ORFNames=Tmari_1754 {ECO:0000313|EMBL:AGL50678.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36811.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36811.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36811.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50678.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50678.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36811.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50678.1; -; Genomic_DNA. DR PIR; E72215; E72215. DR RefSeq; NP_229544.1; NC_000853.1. DR RefSeq; WP_004082278.1; NZ_CP011107.1. DR STRING; 243274.TM1746; -. DR TCDB; 3.A.1.5.15; the atp-binding cassette (abc) superfamily. DR DNASU; 897084; -. DR EnsemblBacteria; AAD36811; AAD36811; TM_1746. DR EnsemblBacteria; AGL50678; AGL50678; Tmari_1754. DR GeneID; 897084; -. DR KEGG; tma:TM1746; -. DR KEGG; tmi:THEMA_05505; -. DR KEGG; tmm:Tmari_1754; -. DR KEGG; tmw:THMA_1788; -. DR PATRIC; 23938468; VBITheMar51294_1764. DR eggNOG; ENOG4107X3N; Bacteria. DR eggNOG; COG4166; LUCA. DR KO; K02035; -. DR OMA; YWQAQHI; -. DR OrthoDB; EOG65TRQQ; -. DR BioCyc; TMAR243274:GC6P-1794-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GOC. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 67 436 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. SQ SEQUENCE 642 AA; 73659 MW; AF5DE7D3D553AE45 CRC64; MRKFVVGFLM VLVAAFYFSE VEVQLPWFGV TNFDPYYWQA QHILAQGTIF EGLFGYVPDP KSLGGVKVVP AVCESYTVSE DGLTYTFYLR KDKRWSNGDP VTAYDFEFAW KRAASPETPT LPLWASPVQY IKNVYDCKSG AKPLDELGVK ALDDYTLQVT LSRPMPSFIN MLVLGGAMPL HRKTVQEHPE DWWKPEYFVG NGPYVIESFT PNYEIVLVRN KYYVGDFPGN VDRIVLKAGG LGLQQYLAGE IDAVFITAVG DYVFALKNKQ LSKELHEESG VQWVGYEITR SLSPVFDDIR IRKALAMAID KKVLTDIVLG GMAIPTHAYC SPDSEIAEAV KGIPYDPEQA KKLLAEAGYP NGKGFPKVKF YITGASDPVA EALVDQWKKV LGITFEIENI ESGQFSTLQW SDFVPWAEPG VCTIGGPVNW QDSGSLMQTA DHTFWFYDYP AEVRQKLYEL REKRESVLRE EGGKTEEEWK EILNRAQELW EKWQEVVNSE PDEFLKKYFL LPAPGELTFI EQINKLYEEW KKATTDEQKI QLWRLAMRAI YNQEYSLVEY TGMNPTNREA RRLWARILYS PYDKAVEYAK KLQQLCVDLA YEVPLYVQKV VYLAKPYLKG IVPYKFSWGP TFFLFKYLTV EK // ID Q9WYN4_THEMA Unreviewed; 113 AA. AC Q9WYN4; G4FHW2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 102. DE SubName: Full=Nitrogen regulatory protein P-II {ECO:0000313|EMBL:AAD35488.1}; GN OrderedLocusNames=TM_0403 {ECO:0000313|EMBL:AAD35488.1}; GN ORFNames=Tmari_0400 {ECO:0000313|EMBL:AGL49325.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35488.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35488.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35488.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49325.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49325.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the P(II) protein family. CC {ECO:0000256|RuleBase:RU003936}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35488.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49325.1; -; Genomic_DNA. DR PIR; A72380; A72380. DR RefSeq; NP_228213.1; NC_000853.1. DR RefSeq; WP_004083241.1; NZ_CP011107.1. DR SMR; Q9WYN4; 1-112. DR STRING; 243274.TM0403; -. DR EnsemblBacteria; AAD35488; AAD35488; TM_0403. DR EnsemblBacteria; AGL49325; AGL49325; Tmari_0400. DR GeneID; 897401; -. DR KEGG; tma:TM0403; -. DR KEGG; tmi:THEMA_02710; -. DR KEGG; tmm:Tmari_0400; -. DR KEGG; tmw:THMA_0409; -. DR PATRIC; 23935689; VBITheMar51294_0408. DR eggNOG; ENOG4108YZA; Bacteria. DR eggNOG; COG0347; LUCA. DR KO; K04751; -. DR OMA; FVYDLQQ; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; TMAR243274:GC6P-418-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro. DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.120; -; 1. DR InterPro; IPR002187; N-reg_PII. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C. DR InterPro; IPR017918; N-reg_PII_CS. DR Pfam; PF00543; P-II; 1. DR PRINTS; PR00340; PIIGLNB. DR SMART; SM00938; P-II; 1. DR SUPFAM; SSF54913; SSF54913; 1. DR PROSITE; PS00638; PII_GLNB_CTER; 1. DR PROSITE; PS51343; PII_GLNB_DOM; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU003936}; KW Transcription regulation {ECO:0000256|RuleBase:RU003936}. SQ SEQUENCE 113 AA; 12603 MW; FAC29024ABCE005B CRC64; MKLIIAVIQP HKLPDVKKAL FDAQVYKMTV MNVLGCGQQK GYTETYRGEV EEVNLLKKVM LLIAVNEEFV EPTIEAIQKG ARTGNIGDGK IFVLDLLDCI RIRTGERGRE AIG // ID Q9X283_THEMA Unreviewed; 635 AA. AC Q9X283; G4FGE9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 104. DE SubName: Full=Transketolase {ECO:0000313|EMBL:AGL50695.1}; DE EC=2.2.1.1 {ECO:0000313|EMBL:AGL50695.1}; DE SubName: Full=Transketolase, putative {ECO:0000313|EMBL:AAD36826.1}; GN OrderedLocusNames=TM_1762 {ECO:0000313|EMBL:AAD36826.1}; GN ORFNames=Tmari_1771 {ECO:0000313|EMBL:AGL50695.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36826.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36826.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36826.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50695.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50695.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the transketolase family. CC {ECO:0000256|SAAS:SAAS00570687}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36826.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50695.1; -; Genomic_DNA. DR PIR; B72215; B72215. DR RefSeq; NP_229559.1; NC_000853.1. DR RefSeq; WP_004082308.1; NZ_CP011107.1. DR STRING; 243274.TM1762; -. DR EnsemblBacteria; AAD36826; AAD36826; TM_1762. DR EnsemblBacteria; AGL50695; AGL50695; Tmari_1771. DR GeneID; 897758; -. DR KEGG; tma:TM1762; -. DR KEGG; tmi:THEMA_05415; -. DR KEGG; tmm:Tmari_1771; -. DR KEGG; tmw:THMA_1806; -. DR PATRIC; 23938504; VBITheMar51294_1781. DR eggNOG; ENOG4105CV1; Bacteria. DR eggNOG; COG0021; LUCA. DR KO; K00615; -. DR OMA; SSIEMYL; -. DR OrthoDB; EOG69GZPF; -. DR BioCyc; TMAR243274:GC6P-1811-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR InterPro; IPR033248; Transketolase_C. DR InterPro; IPR033247; Transketolase_fam. DR InterPro; IPR005474; Transketolase_N. DR PANTHER; PTHR11624; PTHR11624; 1. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR Pfam; PF00456; Transketolase_N; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR SUPFAM; SSF52922; SSF52922; 1. DR PROSITE; PS00801; TRANSKETOLASE_1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Magnesium {ECO:0000256|SAAS:SAAS00460037}; KW Metal-binding {ECO:0000256|SAAS:SAAS00460052}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Thiamine pyrophosphate {ECO:0000256|SAAS:SAAS00459980}; KW Transferase {ECO:0000256|SAAS:SAAS00460013, KW ECO:0000313|EMBL:AGL50695.1}. FT DOMAIN 25 45 TRANSKETOLASE_1. FT {ECO:0000259|PROSITE:PS00801}. SQ SEQUENCE 635 AA; 69985 MW; 5D7F3B627A642FC5 CRC64; MERFPYEKLP ESELKELKEL GRLCRGDILK MTYIANSGHP GGSMSSIDLY LTVFKYAKLR PVDDPARDRI VISHGHTSPG VYAAMARLGF VDLDEVLAGF RHPASVFEGH VTRGVGIIDW TTGNLGQGLS AGLGFALASR FTGKDYHVFV LMSDAEQAKG QVAEARRVAK KYGVTNLTVI IDYNDAQISG RARDVMPVNI KENYLADGWR VIEIDGHDYE QIYLALKEAV EDELNPVAII AKTVMGKGVS FMENEVKYHG KPLNREELEK ALAELGIEND VDVYIEKRKQ LPVEKHKKVY KTYPIKIDTG EPITYTSPTD NRSAFGKAIL DLVKKNVNNP ETTPIVAVDC DLKGSVKLDL LDKEFPERLL EVGVQEHNAA AMAGALSAEG VITFFADFGV FGISETYNQH RLNAINGTNL KVVVTHCGLN VGEDGKTHHG LDYVSGPMNW YGFKVIVPGD PNQTDRVVRY AAKEYGNFVI AMGRSKLPII LDENGKPFFG EGYTFEYGKI DVVRKGDDAV IITYGSTLCE AVNAADELKK EGVNVAVLNV SCPVDLDIET LKMVDGKPVL VVEDHNVFTG LGSFLGTTLL ENGIIPKKYV RVGVPEFAVS GSYTMLYKLY GLDKDGIISR LREML // ID Q9WZ12_THEMA Unreviewed; 376 AA. AC Q9WZ12; G4FDS9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 129. DE SubName: Full=Malate oxidoreductase {ECO:0000313|EMBL:AAD35627.1}; DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:AGL49464.1}; DE EC=1.1.1.38 {ECO:0000313|EMBL:AGL49464.1}; GN OrderedLocusNames=TM_0542 {ECO:0000313|EMBL:AAD35627.1}; GN ORFNames=Tmari_0539 {ECO:0000313|EMBL:AGL49464.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35627.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35627.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35627.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49464.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49464.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3}; CC Note=Divalent metal cations. Prefers magnesium or manganese. CC {ECO:0000256|PIRSR:PIRSR000106-3}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35627.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49464.1; -; Genomic_DNA. DR PIR; C72364; C72364. DR RefSeq; NP_228352.1; NC_000853.1. DR RefSeq; WP_004081360.1; NZ_CP011107.1. DR PDB; 1VL6; X-ray; 2.61 A; A/B/C/D=1-376. DR PDB; 2HAE; X-ray; 3.13 A; A/B/C/D=2-376. DR PDBsum; 1VL6; -. DR PDBsum; 2HAE; -. DR STRING; 243274.TM0542; -. DR DNASU; 897596; -. DR EnsemblBacteria; AAD35627; AAD35627; TM_0542. DR EnsemblBacteria; AGL49464; AGL49464; Tmari_0539. DR GeneID; 897596; -. DR KEGG; tma:TM0542; -. DR KEGG; tmi:THEMA_01965; -. DR KEGG; tmm:Tmari_0539; -. DR KEGG; tmw:THMA_0555; -. DR PATRIC; 23935991; VBITheMar51294_0550. DR eggNOG; ENOG4107QU4; Bacteria. DR eggNOG; COG0281; LUCA. DR KO; K00027; -. DR OMA; CNVPVFH; -. DR OrthoDB; EOG6QCD9W; -. DR BioCyc; TMAR243274:GC6P-566-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.10380; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR012301; Malic_N_dom. DR InterPro; IPR012302; Malic_NAD-bd. DR InterPro; IPR001891; Malic_OxRdtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00390; malic; 2. DR Pfam; PF03949; Malic_M; 1. DR PIRSF; PIRSF000106; ME; 1. DR SMART; SM01274; malic; 1. DR SMART; SM00919; Malic_M; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VL6, ECO:0000213|PDB:2HAE}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000213|PDB:2HAE, ECO:0000256|PIRSR:PIRSR000106-3}; KW NAD {ECO:0000213|PDB:2HAE}; Nucleotide-binding {ECO:0000213|PDB:2HAE}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49464.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000213|PDB:2HAE}. FT DOMAIN 156 376 Malic_M. {ECO:0000259|SMART:SM00919}. FT NP_BIND 186 191 NAD. {ECO:0000213|PDB:2HAE}. FT NP_BIND 211 212 NAD. {ECO:0000213|PDB:2HAE}. FT NP_BIND 259 260 NAD. {ECO:0000213|PDB:2HAE}. FT NP_BIND 281 283 NAD. {ECO:0000213|PDB:2HAE}. FT ACT_SITE 32 32 Proton donor. FT {ECO:0000256|PIRSR:PIRSR000106-1}. FT ACT_SITE 87 87 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR000106-1}. FT METAL 87 87 Zinc. {ECO:0000213|PDB:2HAE}. FT METAL 129 129 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR000106-3}. FT METAL 129 129 Zinc. {ECO:0000213|PDB:2HAE}. FT METAL 130 130 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR000106-3}. FT METAL 130 130 Zinc. {ECO:0000213|PDB:2HAE}. FT METAL 155 155 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR000106-3}. FT METAL 155 155 Zinc. {ECO:0000213|PDB:2HAE}. FT BINDING 159 159 NAD. {ECO:0000213|PDB:2HAE}. FT BINDING 314 314 NAD. {ECO:0000213|PDB:2HAE}. SQ SEQUENCE 376 AA; 41043 MW; 101A5506E3938600 CRC64; MDALEIHRFL KGKIRTALPV EKVDRETLSL LYTPGVADVA RACAEDPEKT YVYTSRWNTV AVVSDGSAVL GLGNIGPYGA LPVMEGKAFL FKAFADIDAF PICLSESEEE KIISIVKSLE PSFGGINLED IGAPKCFRIL QRLSEEMNIP VFHDDQQGTA VVVSAAFLNA LKLTEKKIEE VKVVVNGIGA AGYNIVKFLL DLGVKNVVAV DRKGILNEND PETCLNEYHL EIARITNPER LSGDLETALE GADFFIGVSR GNILKPEWIK KMSRKPVIFA LANPVPEIDP ELAREAGAFI VATGRSDHPN QVNNLLAFPG IMKGAVEKRS KITKNMLLSA VEAIARSCEP EPERIIPEAF DMKVHLNVYT AVKGSA // ID Q9WYU5_THEMA Unreviewed; 431 AA. AC Q9WYU5; G4FDZ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|SAAS:SAAS00376555}; DE EC=6.3.4.21 {ECO:0000256|SAAS:SAAS00376555}; GN OrderedLocusNames=TM_0474 {ECO:0000313|EMBL:AAD35559.1}; GN ORFNames=Tmari_0471 {ECO:0000313|EMBL:AGL49396.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35559.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35559.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35559.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49396.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49396.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Catalyzes the synthesis of beta-nicotinate D- CC ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate CC at the expense of ATP. {ECO:0000256|SAAS:SAAS00564912}. CC -!- CATALYTIC ACTIVITY: Nicotinate + 5-phospho-alpha-D-ribose 1- CC diphosphate + ATP + H(2)O = beta-nicotinate D-ribonucleotide + CC diphosphate + ADP + phosphate. {ECO:0000256|SAAS:SAAS00075180}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D- CC ribonucleotide from nicotinate: step 1/1. CC {ECO:0000256|SAAS:SAAS00075156}. CC -!- SIMILARITY: Belongs to the NAPRTase family. CC {ECO:0000256|SAAS:SAAS00564904}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35559.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49396.1; -; Genomic_DNA. DR PIR; B72372; B72372. DR RefSeq; NP_228284.1; NC_000853.1. DR RefSeq; WP_004081492.1; NZ_CP011107.1. DR STRING; 243274.TM0474; -. DR EnsemblBacteria; AAD35559; AAD35559; TM_0474. DR EnsemblBacteria; AGL49396; AGL49396; Tmari_0471. DR GeneID; 897506; -. DR KEGG; tma:TM0474; -. DR KEGG; tmi:THEMA_02320; -. DR KEGG; tmm:Tmari_0471; -. DR KEGG; tmw:THMA_0483; -. DR PATRIC; 23935845; VBITheMar51294_0481. DR eggNOG; ENOG4107RQP; Bacteria. DR eggNOG; COG1488; LUCA. DR KO; K00763; -. DR OMA; SIATNAY; -. DR OrthoDB; EOG6V7BHF; -. DR BioCyc; TMAR243274:GC6P-494-MONOMER; -. DR UniPathway; UPA00253; UER00457. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.1170.20; -; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR007229; Nic_PRibTrfase-Fam. DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C. DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N. DR PANTHER; PTHR11098; PTHR11098; 3. DR PIRSF; PIRSF000484; NAPRT; 1. DR SUPFAM; SSF51690; SSF51690; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000313|EMBL:AGL49396.1}; KW Ligase {ECO:0000256|SAAS:SAAS00453888, ECO:0000313|EMBL:AGL49396.1}; KW Pyridine nucleotide biosynthesis {ECO:0000256|SAAS:SAAS00453868}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49396.1}. SQ SEQUENCE 431 AA; 49341 MW; 0A2E185E7CFB1E14 CRC64; MKRLSPEVFK VPIDRIRNGY YSDIYFINYV KVLKRDSRHP RVYYQFFPRK DAVICGIDEA LAILKFCTGY YKDEEKAREL FEEILKLDKE MQAASVEMDV QKILELTQKK WDLRLKLNDL WVDKWDEIEV HALYDGEEAK EGEPIMTIEG DPTYFGYLET VLLGVIARAT STATAVKKVV KAARGKPVLF FSARFDHYWV QATDGYAALK AGAFGVSTDA NADYWGVKSM GTMPHALIAC YDGKTEDAAI AFDRHMEEDV NRIVLVDWDN DVIGTTFRVI EKFYEYVMKK PFKLGVTDPS PIIGPGKNKI WGVRFDTSGN LRDKSVVPKD ESSFGVCPEL VWRARQEFDK VGLRDLKIVV SGGFDEKKID LFERLGVPAD AYGVGSRLLR EKVDITADIV EVNGRHCAKV GRYKIENPRL KKVGKRYWEE E // ID Q9X1H1_THEMA Unreviewed; 221 AA. AC Q9X1H1; G4FFJ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 89. DE SubName: Full=Jag protein, putative {ECO:0000313|EMBL:AAD36528.1}; DE SubName: Full=RNA-binding protein Jag {ECO:0000313|EMBL:AGL50390.1}; GN OrderedLocusNames=TM_1460 {ECO:0000313|EMBL:AAD36528.1}; GN ORFNames=Tmari_1466 {ECO:0000313|EMBL:AGL50390.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36528.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36528.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36528.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50390.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50390.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36528.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50390.1; -; Genomic_DNA. DR PIR; E72251; E72251. DR RefSeq; NP_229259.1; NC_000853.1. DR RefSeq; WP_004081749.1; NZ_CP011107.1. DR STRING; 243274.TM1460; -. DR EnsemblBacteria; AAD36528; AAD36528; TM_1460. DR EnsemblBacteria; AGL50390; AGL50390; Tmari_1466. DR GeneID; 897737; -. DR KEGG; tma:TM1460; -. DR KEGG; tmi:THEMA_07015; -. DR KEGG; tmm:Tmari_1466; -. DR KEGG; tmw:THMA_1490; -. DR PATRIC; 23937872; VBITheMar51294_1474. DR eggNOG; ENOG4108Z7S; Bacteria. DR eggNOG; COG1847; LUCA. DR KO; K06346; -. DR OMA; ITLEPMN; -. DR OrthoDB; EOG6XDH3R; -. DR BioCyc; TMAR243274:GC6P-1498-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.30.1370.50; -; 1. DR Gene3D; 3.30.30.80; -; 1. DR InterPro; IPR032782; Jag_N. DR InterPro; IPR001374; R3H_dom. DR Pfam; PF14804; Jag_N; 1. DR Pfam; PF01424; R3H; 1. DR SMART; SM01245; Jag_N; 1. DR SMART; SM00393; R3H; 1. DR SUPFAM; SSF82708; SSF82708; 1. DR PROSITE; PS51061; R3H; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 140 206 R3H. {ECO:0000259|PROSITE:PS51061}. SQ SEQUENCE 221 AA; 25396 MW; 960FD1EA55474F3F CRC64; MKKIVERAPT VEEAIEKVVK KYGLGEGEYT VNVLEKGFHG IFGLFSKEAV VEVQITKAYF ERRLKEFLTE ILQVVDPEVK ITVKSSGRSF FVDVESENAG RLIGKHGKTM GALQHIAMIF LNRLSDTKLN VILDMGDYRE KRKKSLEKIV EEAVKKAISE KTKVVLDPMF SFERKIVHKL VRKHRGVISY SVGVEPYRRV VIEYSATRRE GRRKHDIKES I // ID Q9X1K0_THEMA Unreviewed; 431 AA. AC Q9X1K0; G4FFP9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 108. DE RecName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000256|SAAS:SAAS00013752}; DE EC=2.1.1.- {ECO:0000256|SAAS:SAAS00276898}; GN OrderedLocusNames=TM_1512 {ECO:0000313|EMBL:AAD36579.1}; GN ORFNames=Tmari_1520 {ECO:0000313|EMBL:AGL50444.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36579.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36579.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36579.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50444.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50444.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00013721}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RsmB/NOP family. CC {ECO:0000256|SAAS:SAAS00569170}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36579.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50444.1; -; Genomic_DNA. DR PIR; A72245; A72245. DR RefSeq; NP_229312.1; NC_000853.1. DR RefSeq; WP_004081860.1; NZ_CP011107.1. DR STRING; 243274.TM1512; -. DR EnsemblBacteria; AAD36579; AAD36579; TM_1512. DR EnsemblBacteria; AGL50444; AGL50444; Tmari_1520. DR GeneID; 897990; -. DR KEGG; tma:TM1512; -. DR KEGG; tmi:THEMA_06740; -. DR KEGG; tmm:Tmari_1520; -. DR KEGG; tmw:THMA_1544; -. DR PATRIC; 23937982; VBITheMar51294_1529. DR eggNOG; ENOG4105CYJ; Bacteria. DR eggNOG; COG0144; LUCA. DR KO; K03500; -. DR OMA; LRVNRQH; -. DR OrthoDB; EOG6091D0; -. DR BioCyc; TMAR243274:GC6P-1552-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.940.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR001678; MeTrfase_RsmB/NOP2. DR InterPro; IPR006027; NusB_RsmB_TIM44. DR InterPro; IPR023267; RCMT. DR InterPro; IPR004573; rRNA_ssu_MeTfrase_B. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01189; Methyltr_RsmB-F; 1. DR Pfam; PF01029; NusB; 1. DR PRINTS; PR02008; RCMTFAMILY. DR SUPFAM; SSF48013; SSF48013; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00563; rsmB; 1. DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00423093}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00458366, KW ECO:0000313|EMBL:AGL50444.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW RNA-binding {ECO:0000256|SAAS:SAAS00458301}; KW rRNA processing {ECO:0000256|SAAS:SAAS00423078}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00458383}; KW Transferase {ECO:0000256|SAAS:SAAS00458366, KW ECO:0000313|EMBL:AGL50444.1}. FT DOMAIN 154 430 SAM_MT_RSMB_NOP. FT {ECO:0000259|PROSITE:PS51686}. SQ SEQUENCE 431 AA; 49860 MW; 537FFF172F78A9A5 CRC64; MRTNVRLLAY RLLRKYEKEK FISREDVDSV LSFLDDRDRR FFKELVWGVV RKEELLDWYI NQLLKKKDIP PAVRVALRMG AYQLLFMNSV PDYAAVSETV KLVKNENFKK LVNAVLRRLR TVPEPKELHL VYSHPEWIVN YWRSFLPEEA VLRIMKWNQE PLPVMLRVNS LAATKEEVIK ILAEEGTEAV PGKHAPFSLI VRKLGVPMND SRVINDGLAS VQGESSQLVP FFMELRPGLR VLDTCAAPGG KTTAIAELMK DQGKILAVDI SREKIQLVEK HAKRLKLSSI ETKIADAERL TEYVQDTFDR VLVDAPCTSL GTARNHPEVL RRVNKEDFEK FSEIQLRMVQ QAWQLLEKGG ILLYSTCTVT KEENTEVVKR FVYEQKDVEV IDIRDKMKEF EVEGIWDGYG FLMLPDETIT PFYISVLRKM G // ID Q9X2F2_THEMA Unreviewed; 129 AA. AC Q9X2F2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Putative transposase {ECO:0000313|EMBL:AGL50765.1}; DE SubName: Full=Transposase {ECO:0000313|EMBL:AAD36895.1}; GN OrderedLocusNames=TM_1832 {ECO:0000313|EMBL:AAD36895.1}; GN ORFNames=Tmari_1841 {ECO:0000313|EMBL:AGL50765.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36895.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36895.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36895.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50765.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50765.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36895.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50765.1; -; Genomic_DNA. DR PIR; D72205; D72205. DR RefSeq; NP_229629.1; NC_000853.1. DR RefSeq; WP_008194358.1; NZ_CP011107.1. DR STRING; 243274.TM1832; -. DR EnsemblBacteria; AAD36895; AAD36895; TM_1832. DR EnsemblBacteria; AGL50765; AGL50765; Tmari_1841. DR GeneID; 897619; -. DR KEGG; tma:TM1832; -. DR KEGG; tmi:THEMA_05040; -. DR KEGG; tmm:Tmari_1841; -. DR KEGG; tmw:THMA_1876; -. DR PATRIC; 23938651; VBITheMar51294_1852. DR eggNOG; ENOG4108VIJ; Bacteria. DR eggNOG; COG1943; LUCA. DR KO; K07491; -. DR OMA; HICKERD; -. DR OrthoDB; EOG6PP9P5; -. DR BioCyc; TMAR243274:GC6P-1883-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR Gene3D; 3.30.70.1290; -; 1. DR InterPro; IPR002686; Transposase_17. DR Pfam; PF01797; Y1_Tnp; 1. DR SMART; SM01321; Y1_Tnp; 1. DR SUPFAM; SSF143422; SSF143422; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 129 AA; 15089 MW; 87BCF6E15856AD93 CRC64; MHIKKTRWSH YNLNYHFAWI PKYRRKILVG SIAEELERIL RNTAKQHGIE ILALSIQPDH VHLFVSAPPR FSPAEIANLF KGVSARKLLE KFPELRTKEG LWARSYYVGT AGNVSEETIR RYIEECQDV // ID Q9WY07_THEMA Unreviewed; 181 AA. AC Q9WY07; G4FH74; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35253.1}; GN OrderedLocusNames=TM_0160 {ECO:0000313|EMBL:AAD35253.1}; GN ORFNames=Tmari_0158 {ECO:0000313|EMBL:AGL49084.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35253.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35253.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35253.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1SJ5, ECO:0000213|PDB:1VJL} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-145, AND DISULFIDE BONDS. RX PubMed=15557262; DOI=10.1110/ps.04939904; RA Spraggon G., Pantazatos D., Klock H.E., Wilson I.A., Woods V.L., RA Lesley S.A.; RT "On the use of DXMS to produce more crystallizable proteins: RT structures of the T. maritima proteins TM0160 and TM1171."; RL Protein Sci. 13:3187-3199(2004). RN [3] {ECO:0000313|EMBL:AGL49084.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49084.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35253.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49084.1; -; Genomic_DNA. DR PIR; F72410; F72410. DR RefSeq; NP_227975.1; NC_000853.1. DR RefSeq; WP_004082781.1; NZ_CP011107.1. DR PDB; 1SJ5; X-ray; 2.80 A; A/B=1-145. DR PDB; 1VJL; X-ray; 1.90 A; A/B=1-145. DR PDBsum; 1SJ5; -. DR PDBsum; 1VJL; -. DR SMR; Q9WY07; 1-141. DR STRING; 243274.TM0160; -. DR EnsemblBacteria; AAD35253; AAD35253; TM_0160. DR EnsemblBacteria; AGL49084; AGL49084; Tmari_0158. DR GeneID; 896998; -. DR KEGG; tma:TM0160; -. DR KEGG; tmi:THEMA_04000; -. DR KEGG; tmm:Tmari_0158; -. DR KEGG; tmw:THMA_0156; -. DR PATRIC; 23935168; VBITheMar51294_0161. DR eggNOG; ENOG4105EF4; Bacteria. DR eggNOG; COG1259; LUCA. DR KO; K08999; -. DR OMA; IWMLEEV; -. DR OrthoDB; EOG6TTVSR; -. DR BioCyc; TMAR243274:GC6P-161-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR InterPro; IPR003729; Bi_nuclease_dom. DR Pfam; PF02577; DNase-RNase; 1. DR SUPFAM; SSF103256; SSF103256; 1. DR PROSITE; PS51658; BFN; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1SJ5, ECO:0000213|PDB:1VJL}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 141 BFN. {ECO:0000259|PROSITE:PS51658}. FT DISULFID 38 38 Interchain. {ECO:0000213|PDB:1VJL}. SQ SEQUENCE 181 AA; 20551 MW; E40318189F25C952 CRC64; MRKAWVKTLA LDRVSNTPVV ILGIEGTNRV LPIWIGACEG HALALAMEKM EFPRPLTHDL LLSVLESLEA RVDKVIIHSL KDNTFYATLV IRDLTYTDEE DEEAALIDID SRPSDAIILA VKTGAPIFVS DNLVEKHSIE LEVNETQDEE EEFKKFVENL NIDTFKQMIE KKREEDEEGE S // ID Q9WXT0_THEMA Unreviewed; 320 AA. AC Q9WXT0; G4FGZ0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 125. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35169.1}; DE SubName: Full=Xylobiose ABC transport system, ATP-binding protein 2 {ECO:0000313|EMBL:AGL48998.1}; GN OrderedLocusNames=TM_0075 {ECO:0000313|EMBL:AAD35169.1}; GN ORFNames=Tmari_0072 {ECO:0000313|EMBL:AGL48998.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35169.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35169.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35169.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48998.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48998.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35169.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48998.1; -; Genomic_DNA. DR PIR; C72421; C72421. DR RefSeq; NP_227891.1; NC_000853.1. DR RefSeq; WP_004082591.1; NZ_CP011107.1. DR STRING; 243274.TM0075; -. DR TCDB; 3.A.1.5.13; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35169; AAD35169; TM_0075. DR EnsemblBacteria; AGL48998; AGL48998; Tmari_0072. DR GeneID; 896900; -. DR KEGG; tma:TM0075; -. DR KEGG; tmi:THEMA_04430; -. DR KEGG; tmm:Tmari_0072; -. DR KEGG; tmw:THMA_0071; -. DR PATRIC; 23934990; VBITheMar51294_0073. DR eggNOG; ENOG4105GTU; Bacteria. DR eggNOG; COG4608; LUCA. DR KO; K02032; -. DR OMA; CKFISRC; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-75-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35169.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35169.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 4 255 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 320 AA; 36609 MW; 8A7EEA8B18EF51E2 CRC64; MPLLEIKNLT KIFTIGSIFS RTRIVAVDNV NFDINEAEIF TLAGESGCGK TTTAKIILGF EEPTSGEIIY KGRKIDRVHQ NEKERRELLK EIQAVFQNPF STFNPLRKVD RYFYETLFNL GIADTKKKAE EIIKEKLSAV GISFEEFSEK YPSEFSGGQL QRISIARALL TNPSLLVADE PVSMVDASLR MSIVNLFKDL KEQYGVSVLY ITHDLTTAYY VSDRIAVMFR GNIVELGPAE KVLMEPKHPY TQLLRESVPE PDPKKKWDIR IKLSETEQAE YLRQGCKFAG RCPKAMDICR KEPPPYFEVD GVQVKCWLYR // ID Q9WYM5_THEMA Unreviewed; 245 AA. AC Q9WYM5; G4FHV3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 84. DE SubName: Full=Glutamate synthase [NADPH] putative GlxC chain {ECO:0000313|EMBL:AGL49316.1}; DE EC=1.4.1.13 {ECO:0000313|EMBL:AGL49316.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35479.1}; GN OrderedLocusNames=TM_0394 {ECO:0000313|EMBL:AAD35479.1}; GN ORFNames=Tmari_0391 {ECO:0000313|EMBL:AGL49316.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35479.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35479.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35479.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49316.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49316.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35479.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49316.1; -; Genomic_DNA. DR PIR; C72382; C72382. DR RefSeq; NP_228204.1; NC_000853.1. DR RefSeq; WP_004083223.1; NZ_CP011107.1. DR STRING; 243274.TM0394; -. DR EnsemblBacteria; AAD35479; AAD35479; TM_0394. DR EnsemblBacteria; AGL49316; AGL49316; Tmari_0391. DR GeneID; 897383; -. DR KEGG; tma:TM0394; -. DR KEGG; tmi:THEMA_02760; -. DR KEGG; tmm:Tmari_0391; -. DR KEGG; tmw:THMA_0399; -. DR PATRIC; 23935669; VBITheMar51294_0399. DR eggNOG; ENOG4107WYP; Bacteria. DR eggNOG; COG0070; LUCA. DR OMA; APGNTMD; -. DR OrthoDB; EOG6HJ25M; -. DR BioCyc; TMAR243274:GC6P-408-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC. DR Gene3D; 2.160.20.60; -; 1. DR InterPro; IPR002489; Glu_synth_asu_C. DR InterPro; IPR012061; Glu_synth_lsu_3. DR Pfam; PF01493; GXGXG; 1. DR PIRSF; PIRSF006519; GOGAT_dom3; 1. DR SUPFAM; SSF69336; SSF69336; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49316.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 30 198 GXGXG. {ECO:0000259|Pfam:PF01493}. SQ SEQUENCE 245 AA; 27353 MW; 36E39C814D296BF3 CRC64; MVRIDAKGLH YKKLNDLIWE AVENGEEEIV LDNVCGQRYI GAGIRKKVKI EINGVPGNDL GVFMDGPEII VNGNAQDGVG NTMNAGKIVV HGHAGDIIGY AMRGGHIYIK RNAGYRVGIH MKAYKENYPV VVIGGFARDF LGEYMAGGLL IVLGLEKDED GNIAGNYVGT GMHGGEIFLR GTVEEHKLGK EVKIFQPTEE DINRIKPYVE EFCRLFDYDS EEILNEEFII LKPYTHRPYG RLYAY // ID Q9WZY1_THEMA Unreviewed; 65 AA. AC Q9WZY1; G4FCU6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 101. DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:AAD35960.1}; GN OrderedLocusNames=TM_0879 {ECO:0000313|EMBL:AAD35960.1}; GN ORFNames=Tmari_0881 {ECO:0000313|EMBL:AGL49806.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35960.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35960.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35960.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49806.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49806.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35960.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49806.1; -; Genomic_DNA. DR PIR; A72324; A72324. DR RefSeq; NP_228687.1; NC_000853.1. DR RefSeq; WP_004080714.1; NZ_CP011107.1. DR STRING; 243274.TM0879; -. DR EnsemblBacteria; AAD35960; AAD35960; TM_0879. DR EnsemblBacteria; AGL49806; AGL49806; Tmari_0881. DR GeneID; 898553; -. DR KEGG; tma:TM0879; -. DR KEGG; tmi:THEMA_00240; -. DR KEGG; tmm:Tmari_0881; -. DR KEGG; tmw:THMA_0901; -. DR PATRIC; 23936689; VBITheMar51294_0893. DR eggNOG; ENOG4106147; Bacteria. DR eggNOG; ENOG410ZXTQ; LUCA. DR KO; K00176; -. DR OMA; KQCEMIC; -. DR OrthoDB; EOG6CVV7G; -. DR BioCyc; TMAR243274:GC6P-909-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF00037; Fer4; 1. DR Pfam; PF12837; Fer4_6; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|RuleBase:RU003429}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|RuleBase:RU003429}; KW Iron-sulfur {ECO:0000256|RuleBase:RU003429}; KW Metal-binding {ECO:0000256|RuleBase:RU003429}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 32 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 33 62 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 65 AA; 7132 MW; 190F9F2CE7A78275 CRC64; MGYKIVVNYD WCKACKLCAW ACPTSAITSD EIGKPVTNEN KCIGCLKCEK ICPDMAIEIV SDENA // ID Q9X194_THEMA Unreviewed; 201 AA. AC Q9X194; G4FFB0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 91. DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:AAD36444.1}; DE EC=5.4.2.- {ECO:0000313|EMBL:AGL50305.1}; GN OrderedLocusNames=TM_1374 {ECO:0000313|EMBL:AAD36444.1}; GN ORFNames=Tmari_1381 {ECO:0000313|EMBL:AGL50305.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36444.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36444.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36444.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50305.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50305.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. CC {ECO:0000256|SAAS:SAAS00557523}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36444.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50305.1; -; Genomic_DNA. DR PIR; G72260; G72260. DR RefSeq; NP_229175.1; NC_000853.1. DR RefSeq; WP_004081572.1; NZ_CP011107.1. DR STRING; 243274.TM1374; -. DR DNASU; 898105; -. DR EnsemblBacteria; AAD36444; AAD36444; TM_1374. DR EnsemblBacteria; AGL50305; AGL50305; Tmari_1381. DR GeneID; 898105; -. DR KEGG; tma:TM1374; -. DR KEGG; tmi:THEMA_07465; -. DR KEGG; tmm:Tmari_1381; -. DR KEGG; tmw:THMA_1400; -. DR PATRIC; 23937688; VBITheMar51294_1386. DR eggNOG; ENOG4107TB6; Bacteria. DR eggNOG; COG0406; LUCA. DR KO; K15634; -. DR OMA; PAFKEIV; -. DR OrthoDB; EOG60W7ZT; -. DR BioCyc; TMAR243274:GC6P-1408-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IBA:GOC. DR Gene3D; 3.40.50.1240; -; 1. DR InterPro; IPR013078; His_Pase_superF_clade-1. DR InterPro; IPR029033; His_PPase_superfam. DR InterPro; IPR001345; PG/BPGM_mutase_AS. DR Pfam; PF00300; His_Phos_1; 1. DR SMART; SM00855; PGAM; 1. DR SUPFAM; SSF53254; SSF53254; 1. DR PROSITE; PS00175; PG_MUTASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000313|EMBL:AGL50305.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 201 AA; 23250 MW; 0EE4BA757AAC1341 CRC64; MKLYLIRHGE TIWNEKGLWQ GVTDVPLNER GREQARKLAN SLKRVDAIYS SPLKRSLETA EEIARRFEKE IIVEEDLREC EISLWNGLTV EEAIREYPVE FKKWSSDPNF GMEGLESMRN VQNRVVKAIM KIVSQEKLNG SENVVIVSHS LSLRAFICWI LGLPLYLHRN FKLDNASLSV VEIESKPRLV LLNDTCHLKE S // ID Q9X007_THEMA Unreviewed; 229 AA. AC Q9X007; G4FCS1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 81. DE SubName: Full=Flagellar protein {ECO:0000313|EMBL:AGL49832.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35986.1}; GN OrderedLocusNames=TM_0905 {ECO:0000313|EMBL:AAD35986.1}; GN ORFNames=Tmari_0907 {ECO:0000313|EMBL:AGL49832.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35986.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35986.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35986.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49832.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49832.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35986.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49832.1; -; Genomic_DNA. DR PIR; H72318; H72318. DR RefSeq; NP_228713.1; NC_000853.1. DR RefSeq; WP_004080664.1; NZ_CP011107.1. DR STRING; 243274.TM0905; -. DR EnsemblBacteria; AAD35986; AAD35986; TM_0905. DR EnsemblBacteria; AGL49832; AGL49832; Tmari_0907. DR GeneID; 898579; -. DR KEGG; tma:TM0905; -. DR KEGG; tmi:THEMA_00110; -. DR KEGG; tmm:Tmari_0907; -. DR KEGG; tmw:THMA_0927; -. DR PATRIC; 23936741; VBITheMar51294_0919. DR eggNOG; ENOG41085II; Bacteria. DR eggNOG; COG5581; LUCA. DR OMA; ITMVKEL; -. DR OrthoDB; EOG6SZ1NX; -. DR BioCyc; TMAR243274:GC6P-935-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro. DR InterPro; IPR009875; PilZ_domain. DR InterPro; IPR009926; T3SS_YcgR_N. DR Pfam; PF07238; PilZ; 1. DR Pfam; PF12945; YcgR_2; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AGL49832.1}; KW Cilium {ECO:0000313|EMBL:AGL49832.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AGL49832.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 15 98 T3SS_YcgR_N. {ECO:0000259|Pfam:PF12945}. FT DOMAIN 110 214 PilZ. {ECO:0000259|Pfam:PF07238}. SQ SEQUENCE 229 AA; 26373 MW; C31830C9C87765F4 CRC64; MEYYTELVNA KDVIRPGQNV IVEVSAPEDL EGQYKSSVHD VDFEKRVLTL SMPSFRGRLV PLPRGTRCTV MILDSSAIYV FRTSVLESGR DEDGFPVTKV PFPGRLRKIQ RRRFKRIKIF LEGTYRVASR DEPPKRFVTR DFSAGGMLMV VEDILTPEQI IYVTLDLDED LKLKDHPARV VREAGALETG ERMYGVEFLN VPPALERKLV SFVFKKEIEM RNKERSESE // ID Q9X062_THEMA Unreviewed; 253 AA. AC Q9X062; G4FF23; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 89. DE SubName: Full=Integrase-recombinase protein {ECO:0000313|EMBL:AAD36046.1}; GN OrderedLocusNames=TM_0967 {ECO:0000313|EMBL:AAD36046.1}; GN ORFNames=Tmari_0969 {ECO:0000313|EMBL:AGL49894.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36046.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36046.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36046.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49894.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49894.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the 'phage' integrase family. CC {ECO:0000256|SAAS:SAAS00541913}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36046.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49894.1; -; Genomic_DNA. DR PIR; D72312; D72312. DR RefSeq; NP_228775.1; NC_000853.1. DR RefSeq; WP_004080595.1; NZ_CP011107.1. DR STRING; 243274.TM0967; -. DR EnsemblBacteria; AAD36046; AAD36046; TM_0967. DR EnsemblBacteria; AGL49894; AGL49894; Tmari_0969. DR GeneID; 898705; -. DR KEGG; tma:TM0967; -. DR KEGG; tmi:THEMA_09510; -. DR KEGG; tmm:Tmari_0969; -. DR KEGG; tmw:THMA_0990; -. DR PATRIC; 23936865; VBITheMar51294_0981. DR eggNOG; ENOG4108IYT; Bacteria. DR eggNOG; COG0582; LUCA. DR KO; K04763; -. DR OMA; NDMADVL; -. DR OrthoDB; EOG686NKR; -. DR BioCyc; TMAR243274:GC6P-997-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR Gene3D; 1.10.150.130; -; 1. DR Gene3D; 1.10.443.10; -; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR InterPro; IPR023109; Integrase_recombinase_N. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 97 243 Phage_integrase. FT {ECO:0000259|Pfam:PF00589}. SQ SEQUENCE 253 AA; 29340 MW; 227470DE04DB4A33 CRC64; MDEYLEYLKV VKKRSERTLY QYRSILREFT RFEPITPETW KEYLNTISKN APATQRNKLV VVKNYLNWRA DRGLLNAEER FWNEAEPPRH TVLPKAIELD EVRRIIEACD NPLYRAIFKV LANTGMRVSE IVNLSVHDIS VNETARIRIK GKGNKERIIN VSKELVEELM NSGFFEKKPS VRSIQRAVKR YARKAGIKKK VTPHIFRHSF AVALIERGVP LNKIQALLGH ANISTTSIYL KIASEGIEIP KII // ID Q9WYX0_THEMA Unreviewed; 384 AA. AC Q9WYX0; G4FDX0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 125. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35585.1}; DE SubName: Full=Oligopeptide transport ATP-binding protein OppF {ECO:0000313|EMBL:AGL49422.1}; GN OrderedLocusNames=TM_0500 {ECO:0000313|EMBL:AAD35585.1}; GN ORFNames=Tmari_0497 {ECO:0000313|EMBL:AGL49422.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35585.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35585.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35585.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49422.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49422.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35585.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49422.1; -; Genomic_DNA. DR PIR; C72371; C72371. DR RefSeq; NP_228310.1; NC_000853.1. DR RefSeq; WP_004081444.1; NZ_CP011107.1. DR STRING; 243274.TM0500; -. DR EnsemblBacteria; AAD35585; AAD35585; TM_0500. DR EnsemblBacteria; AGL49422; AGL49422; Tmari_0497. DR GeneID; 897541; -. DR KEGG; tma:TM0500; -. DR KEGG; tmi:THEMA_02170; -. DR KEGG; tmm:Tmari_0497; -. DR KEGG; tmw:THMA_0513; -. DR PATRIC; 23935905; VBITheMar51294_0507. DR eggNOG; ENOG4108JQ7; Bacteria. DR eggNOG; COG4608; LUCA. DR KO; K02032; -. DR OMA; FRREMQI; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-524-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35585.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35585.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 6 315 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 384 AA; 43817 MW; 9E553800B2F003CE CRC64; MSREILRVEN LVKHFPIRAG VFKRIVGWVK AVDGVSFSIN EGETFGLVGE SGCGKTTIGM TLLRLYEPTS GRIIVDNEDT TYYFMPRSKA KKYIKQTYLS RFVNMKESDV EKLEGVDREY ARIFFEEAKG SPKKFMSILL DDLPEKRKKF RREMQIVFQD PYSSLNPRLR VKSIVGEGIV THRIARGKEV EKRIKEILED VGIPSAYVYR FPHEFSGGQR QRIGIARALA LEPKLVVADE AVAALDVSIR SQIINLMEDL QREHKLTYIF ISHDLAVVKH ISDRIGVMYL GKMVELAPKK DLFEKPLHPY TVALMSAIPV PDPTKKRERI ILKGDVPSPI NPPSGCRFHT RCPIAKEICS KEEPAFREVE EGHFVACHFP GELR // ID Q9WZY4_THEMA Unreviewed; 430 AA. AC Q9WZY4; G4FCU3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:AAD35963.1}; DE SubName: Full=O-acetylhomoserine sulfhydrylase / O-succinylhomoserine sulfhydrylase {ECO:0000313|EMBL:AGL49809.1}; DE EC=2.5.1.48 {ECO:0000313|EMBL:AGL49809.1}; DE EC=2.5.1.49 {ECO:0000313|EMBL:AGL49809.1}; GN OrderedLocusNames=TM_0882 {ECO:0000313|EMBL:AAD35963.1}; GN ORFNames=Tmari_0884 {ECO:0000313|EMBL:AGL49809.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35963.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35963.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35963.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49809.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49809.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU362118}; CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. CC {ECO:0000256|RuleBase:RU362118}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35963.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49809.1; -; Genomic_DNA. DR PIR; D72324; D72324. DR RefSeq; NP_228690.1; NC_000853.1. DR RefSeq; WP_004080710.1; NZ_CP011107.1. DR SMR; Q9WZY4; 8-424. DR STRING; 243274.TM0882; -. DR DNASU; 898556; -. DR EnsemblBacteria; AAD35963; AAD35963; TM_0882. DR EnsemblBacteria; AGL49809; AGL49809; Tmari_0884. DR GeneID; 898556; -. DR KEGG; tma:TM0882; -. DR KEGG; tmi:THEMA_00225; -. DR KEGG; tmm:Tmari_0884; -. DR KEGG; tmw:THMA_0904; -. DR PATRIC; 23936695; VBITheMar51294_0896. DR eggNOG; ENOG4108IQK; Bacteria. DR eggNOG; COG2873; LUCA. DR KO; K01740; -. DR OMA; EPAYHGV; -. DR OrthoDB; EOG67DPN3; -. DR BioCyc; TMAR243274:GC6P-912-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC. DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz. DR InterPro; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11808; PTHR11808; 2. DR PANTHER; PTHR11808:SF12; PTHR11808:SF12; 2. DR Pfam; PF01053; Cys_Met_Meta_PP; 1. DR PIRSF; PIRSF001434; CGS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01326; OAH_OAS_sulfhy; 1. DR PROSITE; PS00868; CYS_MET_METAB_PP; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2, KW ECO:0000256|RuleBase:RU362118}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49809.1}. FT MOD_RES 210 210 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR001434-2}. SQ SEQUENCE 430 AA; 47031 MW; 4A3332FCA6DF4B79 CRC64; MDWKKYGYNT RALHAGYEPP EQATGSRAVP IYQTTSYVFR DSDHAARLFA LEEPGFIYTR IGNPTVSVLE ERIAALEEGV GALAVASGQA AITYAILNIA GPGDEIVSGS ALYGGTYNLF RHTLYKKSGI IVKFVDETDP KNIEEAITEK TKAVYLETIG NPGLTVPDFE AIAEIAHRHG VPLIVDNTVA PYIFRPFEHG ADIVVYSATK FIGGHGTSIG GLIVDSGKFD WTNGKFPELV EPDPSYHGVS YVETFKEAAY IAKCRTQLLR DLGSCMSPFN AFLFILGLET LSLRMKKHCE NALKIVEFLK SHPAVSWVNY PIAEGNKTRE NALKYLKEGY GAIVTFGVKG GKEAGKKFID SLTLISHLAN IGDARTLAIH PASTTHQQLT EEEQLKTGVT PDMIRLSVGI EDVEDIIADL DQALRKSQEG // ID Q9WZL6_THEMA Unreviewed; 860 AA. AC Q9WZL6; G4FD66; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 100. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35839.1}; GN OrderedLocusNames=TM_0757 {ECO:0000313|EMBL:AAD35839.1}; GN ORFNames=Tmari_0758 {ECO:0000313|EMBL:AGL49683.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35839.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35839.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35839.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49683.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49683.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35839.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49683.1; -; Genomic_DNA. DR PIR; C72338; C72338. DR RefSeq; NP_228566.1; NC_000853.1. DR RefSeq; WP_004080948.1; NZ_CP011107.1. DR STRING; 243274.TM0757; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAD35839; AAD35839; TM_0757. DR EnsemblBacteria; AGL49683; AGL49683; Tmari_0758. DR GeneID; 898425; -. DR KEGG; tma:TM0757; -. DR KEGG; tmi:THEMA_00865; -. DR KEGG; tmm:Tmari_0758; -. DR KEGG; tmw:THMA_0776; -. DR PATRIC; 23936436; VBITheMar51294_0770. DR eggNOG; ENOG4107R9D; Bacteria. DR eggNOG; COG0463; LUCA. DR OMA; HYGYIWT; -. DR OrthoDB; EOG66F032; -. DR BioCyc; TMAR243274:GC6P-784-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IBA:GO_Central. DR GO; GO:0006011; P:UDP-glucose metabolic process; IBA:GO_Central. DR Gene3D; 1.25.40.10; -; 5. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR013105; TPR_2. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF00535; Glycos_transf_2; 1. DR Pfam; PF07719; TPR_2; 1. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF48452; SSF48452; 3. DR SUPFAM; SSF53448; SSF53448; 1. DR PROSITE; PS50005; TPR; 2. DR PROSITE; PS50293; TPR_REGION; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 492 525 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 860 AA; 100969 MW; 7781CCFA62FB89CF CRC64; MRKCLLSVAM IVKDEEHNIR RALESIKDVV DEIVVVDTGS TDRTPEIVRE YTDKLYFHEW KNDFSEARNF SLKFPTCEWV LILDADEEAS EEFRQNIRSF LESLPEDVNT VYLPTVSYLD WDFKRTEIAS TPRIFRNGTV YYKNIVHNQA VYKPKVVHAP FVIYHYGYIW TRKLKKNKYE RTATLIREQL KTVKNPIEKI YYLIQLYKTE KTGGRKHEEN RIAWETLQEI MKVGKIPPIG LEFLYIFGME LILNGFLEKG EELIDTAIRV FPENPDPYFA KLAIYERRKD WENLYQWGKK FLDVLNKALS QAEKYEFTIT TIKEIGTAHL LMCHACIKLK KWNEAYEHLL KAIENNIDES KFTLTLQIVS EIDESENFQK VLKLVEKIAE HSENLFFDEI VEKIAEFEIE ASEELLNKLP VSRKISKFIL KRLVEKKDFL FEYLTGGDIN SFVEKTGIPG LLFIFDLLKN RETEGRLIRI LSKIEGDEKP NGIVQALIGD LYLKLGNFSE AISRYRKALE LAPEIGNFIK PVIEDLKTRL DPDIEGVYEE LYRYFSGYRE FPFNILEFTK EDAEKLYLIS DHPLAIYTSA VAVFPKSKEK ARALLERIKD VSKLSFYYYR LAKTWEEENP SKAFELHIKA VEENENLGDI ALGRYKYDGL YPNQTFPFMK KEDEIVWAGN ITEKFSGLGV IHPVRAWKRK ENLYYALPHP TDEALKLYKE REKEILKEPP FKVKEEHMIG VLLESDIRDL RIKGEASGLE SILKDLEIEL KEDSKNLLVV SGVEETLDLS KIAEDAERVL LFFFVPDLRD RNNSVWYYPA FRVLRTTHQM KKTLEDLRFS VVKVKALDKN LRFIEALRRL // ID Q9X185_THEMA Unreviewed; 140 AA. AC Q9X185; G4FFA1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Flagellar basal-body rod protein FlgC {ECO:0000256|RuleBase:RU362062}; GN OrderedLocusNames=TM_1365 {ECO:0000313|EMBL:AAD36435.1}; GN ORFNames=Tmari_1372 {ECO:0000313|EMBL:AGL50296.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36435.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36435.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36435.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50296.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50296.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBUNIT: The basal body constitutes a major portion of the CC flagellar organelle and consists of four rings (L,P,S, and M) CC mounted on a central rod. The rod consists of about 26 subunits of CC FlgG in the distal portion, and FlgB, FlgC and FlgF are thought to CC build up the proximal portion of the rod with about 6 subunits CC each. {ECO:0000256|RuleBase:RU362062}. CC -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body CC {ECO:0000256|RuleBase:RU362062}. CC -!- SIMILARITY: Belongs to the flagella basal body rod proteins CC family. {ECO:0000256|SAAS:SAAS00560878}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36435.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50296.1; -; Genomic_DNA. DR PIR; F72263; F72263. DR RefSeq; NP_229166.1; NC_000853.1. DR RefSeq; WP_004081561.1; NZ_CP011107.1. DR STRING; 243274.TM1365; -. DR EnsemblBacteria; AAD36435; AAD36435; TM_1365. DR EnsemblBacteria; AGL50296; AGL50296; Tmari_1372. DR GeneID; 898115; -. DR KEGG; tma:TM1365; -. DR KEGG; tmm:Tmari_1372; -. DR KEGG; tmw:THMA_1390; -. DR PATRIC; 23937668; VBITheMar51294_1377. DR eggNOG; ENOG4108ZC9; Bacteria. DR eggNOG; COG1558; LUCA. DR KO; K02388; -. DR OMA; YVNYPNV; -. DR OrthoDB; EOG6KMB8P; -. DR BioCyc; TMAR243274:GC6P-1398-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030694; C:bacterial-type flagellum basal body, rod; IEA:InterPro. DR GO; GO:0009424; C:bacterial-type flagellum hook; IBA:GO_Central. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IBA:GO_Central. DR InterPro; IPR001444; Flag_bb_rod_N. DR InterPro; IPR019776; Flagellar_basal_body_rod_CS. DR InterPro; IPR010930; Flg_bb/hook_C_dom. DR InterPro; IPR006299; FlgC. DR Pfam; PF00460; Flg_bb_rod; 1. DR Pfam; PF06429; Flg_bbr_C; 1. DR TIGRFAMs; TIGR01395; FlgC; 1. DR PROSITE; PS00588; FLAGELLA_BB_ROD; 1. PE 3: Inferred from homology; KW Bacterial flagellum {ECO:0000256|RuleBase:RU362062}; KW Cell projection {ECO:0000313|EMBL:AAD36435.1}; KW Cilium {ECO:0000313|EMBL:AAD36435.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD36435.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 8 35 Flg_bb_rod. {ECO:0000259|Pfam:PF00460}. FT DOMAIN 89 136 Flg_bbr_C. {ECO:0000259|Pfam:PF06429}. SQ SEQUENCE 140 AA; 15635 MW; 655A926E25CC74EC CRC64; MMSEFEIMNI SATGMSAQRL RVEIVSTNIA NAETTRTETG EPYRRKVPVF AEYLRRTPNG KIESAGVKVV KIEEDPSPFR LVYDPTHPDA DENGYVRMPN VNIVREMVDL INAQRAYDAN VAAFNVTKAM VNSALQIGRG // ID Q9WYA0_THEMA Unreviewed; 366 AA. AC Q9WYA0; G4FHH6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=DNA polymerase III subunit beta {ECO:0000256|PIRNR:PIRNR000804, ECO:0000256|SAAS:SAAS00018186}; DE EC=2.7.7.7 {ECO:0000256|PIRNR:PIRNR000804, ECO:0000256|SAAS:SAAS00018259}; GN OrderedLocusNames=TM_0262 {ECO:0000313|EMBL:AAD35350.1}; GN ORFNames=Tmari_0260 {ECO:0000313|EMBL:AGL49186.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35350.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35350.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35350.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49186.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49186.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme CC responsible for most of the replicative synthesis in bacteria. CC This DNA polymerase also exhibits 3' to 5' exonuclease activity. CC The beta chain is required for initiation of replication once it CC is clamped onto DNA, it slides freely (bidirectional and ATP- CC independent) along duplex DNA. {ECO:0000256|PIRNR:PIRNR000804}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). {ECO:0000256|PIRNR:PIRNR000804, CC ECO:0000256|SAAS:SAAS00018252}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000804, CC ECO:0000256|SAAS:SAAS00346815}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35350.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49186.1; -; Genomic_DNA. DR PIR; E72400; E72400. DR RefSeq; NP_228075.1; NC_000853.1. DR RefSeq; WP_004082966.1; NZ_CP011107.1. DR PDB; 1VPK; X-ray; 2.00 A; A=1-366. DR PDBsum; 1VPK; -. DR STRING; 243274.TM0262; -. DR EnsemblBacteria; AAD35350; AAD35350; TM_0262. DR EnsemblBacteria; AGL49186; AGL49186; Tmari_0260. DR GeneID; 897172; -. DR KEGG; tma:TM0262; -. DR KEGG; tmi:THEMA_03415; -. DR KEGG; tmm:Tmari_0260; -. DR KEGG; tmw:THMA_0269; -. DR PATRIC; 23935401; VBITheMar51294_0266. DR eggNOG; ENOG4105CZ8; Bacteria. DR eggNOG; COG0592; LUCA. DR KO; K02338; -. DR OMA; THQIRLK; -. DR OrthoDB; EOG65J53F; -. DR BioCyc; TMAR243274:GC6P-275-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR InterPro; IPR001001; DNA_polIII_beta. DR InterPro; IPR022635; DNA_polIII_beta_C. DR InterPro; IPR022637; DNA_polIII_beta_cen. DR InterPro; IPR022634; DNA_polIII_beta_N. DR Pfam; PF00712; DNA_pol3_beta; 1. DR Pfam; PF02767; DNA_pol3_beta_2; 1. DR Pfam; PF02768; DNA_pol3_beta_3; 1. DR PIRSF; PIRSF000804; DNA_pol_III_b; 1. DR SMART; SM00480; POL3Bc; 1. DR TIGRFAMs; TIGR00663; dnan; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VPK}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000804, KW ECO:0000256|SAAS:SAAS00425025}; KW DNA replication {ECO:0000256|PIRNR:PIRNR000804, KW ECO:0000256|SAAS:SAAS00425008}; KW DNA-directed DNA polymerase {ECO:0000256|PIRNR:PIRNR000804, KW ECO:0000256|SAAS:SAAS00425005}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000804, KW ECO:0000256|SAAS:SAAS00425005}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|PIRNR:PIRNR000804, KW ECO:0000256|SAAS:SAAS00425005}. FT DOMAIN 1 118 DNA_pol3_beta. FT {ECO:0000259|Pfam:PF00712}. FT DOMAIN 129 242 DNA_pol3_beta_2. FT {ECO:0000259|Pfam:PF02767}. FT DOMAIN 244 364 DNA_pol3_beta_3. FT {ECO:0000259|Pfam:PF02768}. SQ SEQUENCE 366 AA; 40948 MW; F849330209B42A56 CRC64; MKVTVTTLEL KDKITIASKA LAKKSVKPIL AGFLFEVKDG NFYICATDLE TGVKATVNAA EISGEARFVV PGDVIQKMVK VLPDEITELS LEGDALVISS GSTVFRITTM PADEFPEITP AESGITFEVD TSLLEEMVEK VIFAAAKDEF MRNLNGVFWE LHKNLLRLVA SDGFRLALAE EQIENEEEAS FLLSLKSMKE VQNVLDNTTE PTITVRYDGR RVSLSTNDVE TVMRVVDAEF PDYKRVIPET FKTKVVVSRK ELRESLKRVM VIASKGSESV KFEIEENVMR LVSKSPDYGE VVDEVEVQKE GEDLVIAFNP KFIEDVLKHI ETEEIEMNFV DSTSPCQINP LDISGYLYIV MPIRLA // ID Q9WZ62_THEMA Unreviewed; 246 AA. AC Q9WZ62; G4FDM6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=Amino acid ABC transporter, periplasmic amino acid-binding protein {ECO:0000313|EMBL:AAD35678.1}; GN OrderedLocusNames=TM_0593 {ECO:0000313|EMBL:AAD35678.1}; GN ORFNames=Tmari_0592 {ECO:0000313|EMBL:AGL49517.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35678.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35678.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35678.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49517.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49517.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35678.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49517.1; -; Genomic_DNA. DR PIR; B72357; B72357. DR RefSeq; NP_228403.1; NC_000853.1. DR RefSeq; WP_004081258.1; NZ_CP011107.1. DR PDB; 4PRS; X-ray; 1.47 A; A/B=20-246. DR PDB; 4PSH; X-ray; 2.60 A; A/B=20-246. DR PDBsum; 4PRS; -. DR PDBsum; 4PSH; -. DR STRING; 243274.TM0593; -. DR EnsemblBacteria; AAD35678; AAD35678; TM_0593. DR EnsemblBacteria; AGL49517; AGL49517; Tmari_0592. DR GeneID; 897667; -. DR KEGG; tma:TM0593; -. DR KEGG; tmi:THEMA_01695; -. DR KEGG; tmm:Tmari_0592; -. DR KEGG; tmw:THMA_0609; -. DR PATRIC; 23936101; VBITheMar51294_0604. DR eggNOG; ENOG4106PMH; Bacteria. DR eggNOG; COG0834; LUCA. DR KO; K02030; -. DR OMA; TYETIYK; -. DR OrthoDB; EOG6JQH58; -. DR BioCyc; TMAR243274:GC6P-618-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR001320; Iontro_rcpt. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR Pfam; PF00497; SBP_bac_3; 1. DR SMART; SM00062; PBPb; 1. DR SMART; SM00079; PBPe; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4PRS, ECO:0000213|PDB:4PSH}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 29 246 PBPb. {ECO:0000259|SMART:SM00062}. SQ SEQUENCE 246 AA; 27281 MW; 25CC5C36DA4D2B0E CRC64; MKKLLAVSIL LVSIVIFSGA IDEIKSRGYL LVGLSADFPP FEFVDENGNI VGFDVDLAKE IARRLGVELK IVDMTFDGLI PSLLTKKIDV IISGMTITEE RKKVVAFSDP YFDAGQVIVV RKDSDFRPKT YEDLVGKTVA VQIGTTGDIE VSKYDGIKVV RFDKFTDAFL ELKRGRADAV VLDSATARAF VAKNPDLVIS SGVLSSEQYG IAVRKEDTDL LEFINSVLRE LKKSPYDVLI EKWFSE // ID Q9WYW3_THEMA Unreviewed; 229 AA. AC Q9WYW3; G4FDX7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Segregation and condensation protein A {ECO:0000313|EMBL:AGL49415.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35578.1}; GN OrderedLocusNames=TM_0493 {ECO:0000313|EMBL:AAD35578.1}; GN ORFNames=Tmari_0490 {ECO:0000313|EMBL:AGL49415.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35578.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35578.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35578.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49415.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49415.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35578.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49415.1; -; Genomic_DNA. DR PIR; D72370; D72370. DR RefSeq; NP_228303.1; NC_000853.1. DR RefSeq; WP_004081460.1; NZ_CP011107.1. DR STRING; 243274.TM0493; -. DR EnsemblBacteria; AAD35578; AAD35578; TM_0493. DR EnsemblBacteria; AGL49415; AGL49415; Tmari_0490. DR GeneID; 897534; -. DR KEGG; tma:TM0493; -. DR KEGG; tmi:THEMA_02205; -. DR KEGG; tmm:Tmari_0490; -. DR KEGG; tmw:THMA_0506; -. DR PATRIC; 23935891; VBITheMar51294_0500. DR eggNOG; ENOG4108KVX; Bacteria. DR eggNOG; COG1354; LUCA. DR KO; K05896; -. DR OMA; VEYLEHM; -. DR OrthoDB; EOG6CZQPX; -. DR BioCyc; TMAR243274:GC6P-517-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR003768; ScpA. DR Pfam; PF02616; SMC_ScpA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 229 AA; 27483 MW; 0540C68F6B1D170A CRC64; MDLVFKLPVF EGPLDLLLYL VRKKKVDIRE IPISQLADEF VEYLEHMKKL DMKITSDFLE MASTLMELKS KMLIPRVREE EKESIDRKKE ELYRRIEEYS KVKEIVSILK KEENLLKRKR VRVRNVFFEK IEGIEKFREI LKRIWKEEAM REAVHRVKSE TLSVEEMMER ILDEIDGEIE ILRLLSRAEN VYELIVRLLA ILELVKIGKL ILVGDDRIRR YTNAAQGRY // ID Q9WYA7_THEMA Unreviewed; 281 AA. AC Q9WYA7; G4FHI4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN OrderedLocusNames=TM_0270 {ECO:0000313|EMBL:AAD35359.1}; GN ORFNames=Tmari_0268 {ECO:0000313|EMBL:AGL49194.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35359.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35359.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35359.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49194.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49194.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU003862}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35359.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49194.1; -; Genomic_DNA. DR PIR; D72397; D72397. DR RefSeq; NP_228083.1; NC_000853.1. DR RefSeq; WP_004082974.1; NZ_CP011107.1. DR STRING; 243274.TM0270; -. DR EnsemblBacteria; AAD35359; AAD35359; TM_0270. DR EnsemblBacteria; AGL49194; AGL49194; Tmari_0268. DR GeneID; 897184; -. DR KEGG; tma:TM0270; -. DR KEGG; tmi:THEMA_03375; -. DR KEGG; tmm:Tmari_0268; -. DR KEGG; tmw:THMA_0277; -. DR PATRIC; 23935417; VBITheMar51294_0274. DR eggNOG; ENOG4107R32; Bacteria. DR eggNOG; COG0685; LUCA. DR OMA; SIVFFEN; -. DR OrthoDB; EOG67X1QM; -. DR BioCyc; TMAR243274:GC6P-283-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC. DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.220; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR Pfam; PF02219; MTHFR; 1. DR SUPFAM; SSF51730; SSF51730; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862, KW ECO:0000313|EMBL:AGL49194.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 281 AA; 31443 MW; 08DF156CEC7F2414 CRC64; MRKSLEIGKC VVLEVLTPRG TNLGRFMEFT EEAWKTGIDA FTVTDMPMGR VRMAPWAASH LLVESGKDVL MHFTRNTRNM IRIQSDLLGC HALGVKNLLL LSGDNPSHGD YPETTSVNDI DILDLIRLTK LMNEGTDLAG NKIYGKTDFF VGGALNPFSD KDIKRAKQKI EAGVDFLVTQ PLFNSEVAKK IKEELNTKIL ASIVFFENAK QMSYFSSVPG IEIPDEIVNS TEKGDDYLKE KSFESVLRFV EETKGVLDGF YIVAIVKDLE KIRKVVEIAK S // ID Q9X297_THEMA Unreviewed; 152 AA. AC Q9X297; G4FGG3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=Ferric uptake regulation protein {ECO:0000313|EMBL:AAD36839.1}; GN OrderedLocusNames=TM_1776 {ECO:0000313|EMBL:AAD36839.1}; GN ORFNames=Tmari_1786 {ECO:0000313|EMBL:AGL50710.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36839.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36839.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36839.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50710.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50710.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the Fur family. CC {ECO:0000256|SAAS:SAAS00578401}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36839.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50710.1; -; Genomic_DNA. DR PIR; G72213; G72213. DR RefSeq; NP_229573.1; NC_000853.1. DR RefSeq; WP_004082322.1; NZ_CP011107.1. DR STRING; 243274.TM1776; -. DR EnsemblBacteria; AAD36839; AAD36839; TM_1776. DR EnsemblBacteria; AGL50710; AGL50710; Tmari_1786. DR GeneID; 897847; -. DR KEGG; tma:TM1776; -. DR KEGG; tmi:THEMA_05325; -. DR KEGG; tmm:Tmari_1786; -. DR KEGG; tmw:THMA_1820; -. DR PATRIC; 23938534; VBITheMar51294_1796. DR eggNOG; ENOG41090R7; Bacteria. DR eggNOG; COG0735; LUCA. DR KO; K03711; -. DR OMA; GYVIKWH; -. DR OrthoDB; EOG6J48SS; -. DR BioCyc; TMAR243274:GC6P-1825-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR002481; FUR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01475; FUR; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00469751}; KW Metal-binding {ECO:0000256|SAAS:SAAS00514465}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 152 AA; 18210 MW; 50CD116E5A259413 CRC64; MYEELRNELK KRKYRITAQR EMILKIFLES RGRHLGVEEV YRELLNRNVR ISKATVYRSV ELLVELGFLR KLNFGEGLYR YELADRSNRE SHQHVICQKC GRIVEINSEQ VNKIISDISK KTGYVIKWHD LKFYGICPEC QAKEKEEEKR SK // ID Q9WXY5_THEMA Unreviewed; 258 AA. AC Q9WXY5; G4FH46; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 87. DE SubName: Full=Flagellin protein FlaA {ECO:0000313|EMBL:AGL49056.1}; DE SubName: Full=Flagellin, putative {ECO:0000313|EMBL:AAD35225.1}; GN OrderedLocusNames=TM_0132 {ECO:0000313|EMBL:AAD35225.1}; GN ORFNames=Tmari_0130 {ECO:0000313|EMBL:AGL49056.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35225.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35225.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35225.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49056.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49056.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the bacterial flagellin family. CC {ECO:0000256|SAAS:SAAS00588699}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35225.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49056.1; -; Genomic_DNA. DR PIR; B72413; B72413. DR RefSeq; NP_227947.1; NC_000853.1. DR RefSeq; WP_004082721.1; NZ_CP011107.1. DR STRING; 243274.TM0132; -. DR EnsemblBacteria; AAD35225; AAD35225; TM_0132. DR EnsemblBacteria; AGL49056; AGL49056; Tmari_0130. DR GeneID; 896959; -. DR KEGG; tma:TM0132; -. DR KEGG; tmi:THEMA_04145; -. DR KEGG; tmm:Tmari_0130; -. DR KEGG; tmw:THMA_0127; -. DR PATRIC; 23935106; VBITheMar51294_0131. DR eggNOG; ENOG4105IF5; Bacteria. DR eggNOG; COG1344; LUCA. DR KO; K02406; -. DR OMA; TENAQNA; -. DR OrthoDB; EOG6M9DVB; -. DR BioCyc; TMAR243274:GC6P-132-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009420; C:bacterial-type flagellum filament; IEA:InterPro. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR Gene3D; 1.20.1330.10; -; 1. DR InterPro; IPR001492; Flagellin. DR InterPro; IPR001029; Flagellin_D0/D1. DR Pfam; PF00669; Flagellin_N; 1. DR PRINTS; PR00207; FLAGELLIN. PE 3: Inferred from homology; KW Bacterial flagellum {ECO:0000256|SAAS:SAAS00482835}; KW Cell projection {ECO:0000313|EMBL:AAD35225.1}; KW Cilium {ECO:0000313|EMBL:AAD35225.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35225.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 33 128 Flagellin_D0/D1. FT {ECO:0000259|Pfam:PF00669}. SQ SEQUENCE 258 AA; 28938 MW; 7F84FD23B92111AE CRC64; MRVNDVNLMR YIQQLSLERK APTPGSFLFN TVSELAVQQK LRGQIEGYKT TLSQIYNGIG LLNTANAGLE SISTALQRAR ELAVQASNAT LTDVERSMIQ KEYEEIMRGV KRIIQQTTYN EQRVLAGDVR NLVIQTGPNE GQNVTVNIPN LEETLSELFE VDLSTFEGAQ RSLETIDQAL ENISQIRGNV GSWMNRLESS ARSVMNSYTE LFKTESLFEP SVAELLLEST KEDILRQTAL TGILFRMENA GNVLKLLM // ID Q9WZV7_THEMA Unreviewed; 489 AA. AC Q9WZV7; G4FCX1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 125. DE SubName: Full=Osmosensitive K+ channel histidine kinase KdpD {ECO:0000313|EMBL:AGL49780.1}; DE EC=2.7.3.- {ECO:0000313|EMBL:AGL49780.1}; DE SubName: Full=Sensor histidine kinase {ECO:0000313|EMBL:AAD35935.1}; GN OrderedLocusNames=TM_0853 {ECO:0000313|EMBL:AAD35935.1}; GN ORFNames=Tmari_0855 {ECO:0000313|EMBL:AGL49780.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35935.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35935.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35935.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49780.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49780.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- INTERACTION: CC Q9WYT9:TM_0468; NbExp=4; IntAct=EBI-2464828, EBI-2464826; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35935.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49780.1; -; Genomic_DNA. DR PIR; F72324; F72324. DR RefSeq; NP_228662.1; NC_000853.1. DR RefSeq; WP_004080773.1; NZ_CP011107.1. DR PDB; 2C2A; X-ray; 1.90 A; A=233-489. DR PDB; 3DGE; X-ray; 2.80 A; A/B=232-489. DR PDB; 4JAS; X-ray; 3.00 A; A=232-489. DR PDB; 4JAU; X-ray; 2.70 A; A=232-489. DR PDB; 4JAV; X-ray; 3.10 A; A/B=232-489. DR PDB; 4KP4; X-ray; 3.00 A; A/B=271-290. DR PDBsum; 2C2A; -. DR PDBsum; 3DGE; -. DR PDBsum; 4JAS; -. DR PDBsum; 4JAU; -. DR PDBsum; 4JAV; -. DR PDBsum; 4KP4; -. DR DIP; DIP-54544N; -. DR STRING; 243274.TM0853; -. DR EnsemblBacteria; AAD35935; AAD35935; TM_0853. DR EnsemblBacteria; AGL49780; AGL49780; Tmari_0855. DR GeneID; 898525; -. DR KEGG; tma:TM0853; -. DR KEGG; tmi:THEMA_00370; -. DR KEGG; tmm:Tmari_0855; -. DR KEGG; tmw:THMA_0875; -. DR PATRIC; 23936634; VBITheMar51294_0866. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR KO; K02484; -. DR OMA; NEGIFVL; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-883-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2C2A, ECO:0000213|PDB:3DGE, KW ECO:0000213|PDB:4JAS, ECO:0000213|PDB:4JAU}; KW ATP-binding {ECO:0000256|SAAS:SAAS00528924}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Ion channel {ECO:0000313|EMBL:AGL49780.1}; KW Ion transport {ECO:0000313|EMBL:AGL49780.1}; KW Kinase {ECO:0000256|SAAS:SAAS00529081, ECO:0000313|EMBL:AAD35935.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00528924}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00529081, KW ECO:0000313|EMBL:AAD35935.1}; Transport {ECO:0000313|EMBL:AGL49780.1}. FT DOMAIN 257 480 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. FT NP_BIND 380 384 ADP. {ECO:0000213|PDB:2C2A, FT ECO:0000213|PDB:3DGE, FT ECO:0000213|PDB:4JAS}. FT NP_BIND 430 434 ADP. {ECO:0000213|PDB:2C2A, FT ECO:0000213|PDB:3DGE, FT ECO:0000213|PDB:4JAS}. FT NP_BIND 442 446 ADP. {ECO:0000213|PDB:2C2A, FT ECO:0000213|PDB:3DGE, FT ECO:0000213|PDB:4JAS}. FT BINDING 411 411 ADP. {ECO:0000213|PDB:2C2A, FT ECO:0000213|PDB:3DGE, FT ECO:0000213|PDB:4JAU}. FT DISULFID 330 359 {ECO:0000213|PDB:2C2A, FT ECO:0000213|PDB:3DGE, FT ECO:0000213|PDB:4JAS}. SQ SEQUENCE 489 AA; 56017 MW; 40F19F843A4EDDB4 CRC64; MEEIKEQNNR LFLLLSIMIM EFSNAKTESD ILQGLLNLVR KVVDIKEVVL VDENKRKIWG RDIDIKRFEE FIDWSIRQSN PVFVEDELGY VGIVPVVKQD RMFGSLIVLL NHQPSMEETE IFKVLSFLSA VVLENIKLYR ELEETYNYVN VILNGLPEGI FVYSNGEIKF QNEKFKEENF PDEVLRKAIS LSEEAISLRT QRVGEVISGE EFFSITSIPL ILGSEVQALT IVENVTESKE LERLKRIDRM KTEFIANISH ELRTPLTAIK AYAETIYNSL GELDLSTLKE FLEVIIDQSN HLENLLNELL DFSRLERKSL QINREKVDLC DLVESAVNAI KEFASSHNVN VLFESNVPCP VEAYIDPTRI RQVLLNLLNN GVKYSKKDAP DKYVKVILDE KDGGVLIIVE DNGIGIPDHA KDRIFEQFYR VDSSLTYEVP GTGLGLAITK EIVELHGGRI WVESEVGKGS RFFVWIPKDR AGEDNRQDN // ID Q9WYM6_THEMA Unreviewed; 425 AA. AC Q9WYM6; G4FHV4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 106. DE SubName: Full=NADH oxidase, putative {ECO:0000313|EMBL:AAD35480.1}; DE SubName: Full=Nitrite reductase probable [NAD(P)H] subunit {ECO:0000313|EMBL:AGL49317.1}; DE EC=1.7.1.4 {ECO:0000313|EMBL:AGL49317.1}; GN OrderedLocusNames=TM_0395 {ECO:0000313|EMBL:AAD35480.1}; GN ORFNames=Tmari_0392 {ECO:0000313|EMBL:AGL49317.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35480.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35480.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35480.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49317.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49317.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35480.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49317.1; -; Genomic_DNA. DR PIR; D72382; D72382. DR RefSeq; NP_228205.1; NC_000853.1. DR RefSeq; WP_004083225.1; NZ_CP011107.1. DR STRING; 243274.TM0395; -. DR EnsemblBacteria; AAD35480; AAD35480; TM_0395. DR EnsemblBacteria; AGL49317; AGL49317; Tmari_0392. DR GeneID; 897384; -. DR KEGG; tma:TM0395; -. DR KEGG; tmi:THEMA_02755; -. DR KEGG; tmm:Tmari_0392; -. DR KEGG; tmw:THMA_0400; -. DR PATRIC; 23935671; VBITheMar51294_0400. DR eggNOG; ENOG4107RR0; Bacteria. DR eggNOG; COG0446; LUCA. DR OMA; FGLMRDQ; -. DR OrthoDB; EOG6QVRCJ; -. DR BioCyc; TMAR243274:GC6P-409-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-EC. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF07992; Pyr_redox_2; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49317.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 301 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. SQ SEQUENCE 425 AA; 47074 MW; 285145BCBB103ED1 CRC64; MRYVIVGSGP AGLNAIEAIR EVDKEGEILL ITAEKYVGYS RPLITYLLGR KVTEEKMYYR TEDYLREMRV DIKPATRVEK VIPEEKTVVT DSGEEIRYDK LLIATGGKPF VPNIEGLTGK KGVFTFTTWE DEEKVEKYIE ENDVKEAVVL GGGLIGLKTT EALMELGVKV TIVELADRIL SVTFDRKASE IITEALKKEG CSVITNDTVV KVNGDDTVSS VVLKSGKEIP TKLLVIAIGV KPNVEFLKDS GIEINRGIVV NEKMETNVEG VYAAGDCTEF YDLIDGQRKT IAIWPVAVAQ GRVAGYNMAG KNVRYPGGIP MNSVELAGIP TISVGHSNVE DGGYEILTFE EGNTYKKMVL KDNRLVGAIL VNDIDRAGIY TGLILQKLDV SSFKDRLLDE NFGLVYLPKE FRKKMLEGEI KIWLE // ID Q9X0X5_THEMA Unreviewed; 205 AA. AC Q9X0X5; G4FEA0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_01930}; DE EC=2.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01930}; DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000256|HAMAP-Rule:MF_01930}; DE AltName: Full=GAR transformylase {ECO:0000256|HAMAP-Rule:MF_01930}; GN Name=purN {ECO:0000256|HAMAP-Rule:MF_01930}; GN OrderedLocusNames=TM_1248 {ECO:0000313|EMBL:AAD36323.1}; GN ORFNames=Tmari_1253 {ECO:0000313|EMBL:AGL50177.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36323.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36323.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36323.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50177.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50177.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Catalyzes the transfer of a formyl group from 10- CC formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), CC producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and CC tetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01930}. CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + N(1)-(5-phospho-D- CC ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide. {ECO:0000256|HAMAP-Rule:MF_01930}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5- CC phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01930}. CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000256|HAMAP- CC Rule:MF_01930}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36323.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50177.1; -; Genomic_DNA. DR PIR; B72277; B72277. DR RefSeq; NP_229053.1; NC_000853.1. DR RefSeq; WP_004080015.1; NZ_CP011107.1. DR STRING; 243274.TM1248; -. DR DNASU; 898235; -. DR EnsemblBacteria; AAD36323; AAD36323; TM_1248. DR EnsemblBacteria; AGL50177; AGL50177; Tmari_1253. DR GeneID; 898235; -. DR KEGG; tma:TM1248; -. DR KEGG; tmi:THEMA_08095; -. DR KEGG; tmm:Tmari_1253; -. DR KEGG; tmw:THMA_1273; -. DR PATRIC; 23937436; VBITheMar51294_1264. DR eggNOG; ENOG4108V3E; Bacteria. DR eggNOG; COG0299; LUCA. DR KO; K11175; -. DR OMA; LEHKWYP; -. DR OrthoDB; EOG615VP4; -. DR BioCyc; TMAR243274:GC6P-1279-MONOMER; -. DR UniPathway; UPA00074; UER00126. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.170; -; 1. DR HAMAP; MF_01930; PurN; 1. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR001555; GART_AS. DR InterPro; IPR004607; PurN_trans. DR Pfam; PF00551; Formyl_trans_N; 1. DR SUPFAM; SSF53328; SSF53328; 1. DR TIGRFAMs; TIGR00639; PurN; 1. DR PROSITE; PS00373; GART; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01930}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01930, KW ECO:0000256|SAAS:SAAS00476799, ECO:0000313|EMBL:AAD36323.1}. FT DOMAIN 12 183 Formyl_trans_N. FT {ECO:0000259|Pfam:PF00551}. FT REGION 21 23 5'-phosphoribosylglycinamide binding. FT {ECO:0000256|HAMAP-Rule:MF_01930}. FT REGION 91 94 10-formyltetrahydrofolate binding. FT {ECO:0000256|HAMAP-Rule:MF_01930}. FT ACT_SITE 110 110 Proton donor. {ECO:0000256|HAMAP- FT Rule:MF_01930}. FT BINDING 108 108 10-formyltetrahydrofolate. FT {ECO:0000256|HAMAP-Rule:MF_01930}. FT SITE 146 146 Raises pKa of active site His. FT {ECO:0000256|HAMAP-Rule:MF_01930}. SQ SEQUENCE 205 AA; 23598 MW; 383590F84D22E409 CRC64; MCSVLQRRVP PRIVVLASGN GSNFEAIVNA ARSGELSAEI QMLLVDRNCY AIERAKKLQI PWERLEKPWA ESLKKRLEEL NPDLVVLAGF MRILPAEIVE RWKWKIVNIH PSLLPAFPGT HAIEKAYEYG VKVTGITIHF VDEGVDTGPI IFQKAVEIKK DWSLERLEEE IHKIEHRYYP LVIQKVLEGK WKIEGRRVIL EEDIG // ID Q9WYD9_THEMA Unreviewed; 328 AA. AC Q9WYD9; G4FHL7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 123. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35391.1}; DE SubName: Full=Xyloglucan ABC transport system, ATP-binding protein 1 {ECO:0000313|EMBL:AGL49227.1}; GN OrderedLocusNames=TM_0303 {ECO:0000313|EMBL:AAD35391.1}; GN ORFNames=Tmari_0301 {ECO:0000313|EMBL:AGL49227.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35391.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35391.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35391.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49227.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49227.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35391.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49227.1; -; Genomic_DNA. DR PIR; D72393; D72393. DR RefSeq; NP_228115.1; NC_000853.1. DR RefSeq; WP_004083027.1; NZ_CP011107.1. DR STRING; 243274.TM0303; -. DR EnsemblBacteria; AAD35391; AAD35391; TM_0303. DR EnsemblBacteria; AGL49227; AGL49227; Tmari_0301. DR GeneID; 897232; -. DR KEGG; tma:TM0303; -. DR KEGG; tmi:THEMA_03210; -. DR KEGG; tmm:Tmari_0301; -. DR KEGG; tmw:THMA_0310; -. DR PATRIC; 23935485; VBITheMar51294_0308. DR eggNOG; COG0444; LUCA. DR KO; K02031; -. DR OMA; HPYSDGL; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-316-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35391.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35391.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 10 261 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 328 AA; 37011 MW; 9D8BAB0E8245A6D1 CRC64; MEKIAVAENL RAYYFIKSGD KTTSIRAVDN VSLHFFENEV YGIAGESGCG KSTLLKVLFG EIKPPLKLVD GEVVFKLDGE EYRINSMSLD QLKKIRWKYV SYVPQGSMSV LNPVRKIRRI FLDVIEEHTS MSREEAFSRI ESYFEALGLP VRVLDSYPHQ LSGGMRQRVT IALATVLNPK VIFADEPTTA LDVVVQRGVI QLLKKIHKEQ KNTLVIVTHD MGVHAHLATR IGVMYAGRLI EEAETHEIFK NPLHPYTRFL INSLPRFGDR SRKEGTPGSP PSLANLPSGC PFHPRCPIAD QICMEMEPDL IEVARNHKVA CWKVGVER // ID Q9X0J4_THEMA Unreviewed; 200 AA. AC Q9X0J4; G4FEN8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36186.1}; GN OrderedLocusNames=TM_1110 {ECO:0000313|EMBL:AAD36186.1}; GN ORFNames=Tmari_1116 {ECO:0000313|EMBL:AGL50040.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36186.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36186.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36186.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50040.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50040.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36186.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50040.1; -; Genomic_DNA. DR PIR; H72295; H72295. DR RefSeq; NP_228916.1; NC_000853.1. DR RefSeq; WP_004080316.1; NZ_CP011107.1. DR STRING; 243274.TM1110; -. DR EnsemblBacteria; AAD36186; AAD36186; TM_1110. DR EnsemblBacteria; AGL50040; AGL50040; Tmari_1116. DR GeneID; 898655; -. DR KEGG; tma:TM1110; -. DR KEGG; tmi:THEMA_08795; -. DR KEGG; tmm:Tmari_1116; -. DR KEGG; tmw:THMA_1133; -. DR PATRIC; 23937153; VBITheMar51294_1125. DR eggNOG; ENOG4108NYV; Bacteria. DR eggNOG; COG2111; LUCA. DR KO; K05566; -. DR OMA; EVIVFTI; -. DR OrthoDB; EOG61CM0Q; -. DR BioCyc; TMAR243274:GC6P-1139-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007182; MnhB. DR Pfam; PF04039; MnhB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 47 71 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 83 105 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 152 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 177 194 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 85 186 MnhB. {ECO:0000259|Pfam:PF04039}. SQ SEQUENCE 200 AA; 22728 MW; D1D33B94BE9DC6F7 CRC64; MKWVWITIFV VFCFAVLLNG SFEKVQVKFE NPVVKNPITQ IYLLNRVYDT VFEVLVFSLA VLGVSLHMAY LPTPEEIRGI SDVTIRIFAR FIAFFLLVGS LYLALEGHVS PGGGFSAGVA GGTALALIAM VEDFENFERK FERTRAYFLE KFIMIVFLFL VVLILPGRNL IVPANMVVYL KVMLGSWIIV YYFIKHRGLL // ID Q9X2I5_THEMA Unreviewed; 132 AA. AC Q9X2I5; G4FGR4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 87. DE SubName: Full=UPF0047 protein {ECO:0000313|EMBL:AGL50811.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36934.1}; GN OrderedLocusNames=TM_1872 {ECO:0000313|EMBL:AAD36934.1}; GN ORFNames=Tmari_1887 {ECO:0000313|EMBL:AGL50811.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36934.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36934.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36934.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50811.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50811.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36934.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50811.1; -; Genomic_DNA. DR PIR; C72200; C72200. DR RefSeq; NP_229668.1; NC_000853.1. DR RefSeq; WP_004082423.1; NZ_CP011107.1. DR SMR; Q9X2I5; 6-130. DR STRING; 243274.TM1872; -. DR EnsemblBacteria; AAD36934; AAD36934; TM_1872. DR EnsemblBacteria; AGL50811; AGL50811; Tmari_1887. DR GeneID; 897192; -. DR KEGG; tma:TM1872; -. DR KEGG; tmi:THEMA_04810; -. DR KEGG; tmm:Tmari_1887; -. DR KEGG; tmw:THMA_1922; -. DR PATRIC; 23938733; VBITheMar51294_1893. DR eggNOG; ENOG4108YXI; Bacteria. DR eggNOG; COG0432; LUCA. DR OMA; SHYEGNS; -. DR OrthoDB; EOG6065B2; -. DR BioCyc; TMAR243274:GC6P-1923-MONOMER; -. DR BRENDA; 2.5.1.3; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.60.120.460; -; 1. DR InterPro; IPR001602; UPF0047. DR Pfam; PF01894; UPF0047; 1. DR PIRSF; PIRSF004681; UCP004681; 1. DR SUPFAM; SSF111038; SSF111038; 1. DR TIGRFAMs; TIGR00149; TIGR00149_YjbQ; 1. DR PROSITE; PS01314; UPF0047; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 132 AA; 14564 MW; C7648167A6F1C6CC CRC64; MLKRLTVRTS SRTQFVDITS EIVKFIEESK VRNGICVVFV PHTTAGITIN ENADPSVRQD IMNTLNKLVP PSAGYTHLEG NADSHIKASL VGSSVTLIIE NGRPLLGTWQ GIYFCEFDGP RTRSVYVKIV EG // ID Q9X0G3_THEMA Unreviewed; 986 AA. AC Q9X0G3; G4FES4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 84. DE SubName: Full=Putative alpha-L-rhamnosidase {ECO:0000313|EMBL:AGL50002.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36151.1}; GN OrderedLocusNames=TM_1074 {ECO:0000313|EMBL:AAD36151.1}; GN ORFNames=Tmari_1078 {ECO:0000313|EMBL:AGL50002.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36151.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36151.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36151.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50002.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50002.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36151.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50002.1; -; Genomic_DNA. DR PIR; D72299; D72299. DR RefSeq; NP_228880.1; NC_000853.1. DR RefSeq; WP_004080411.1; NZ_CP011107.1. DR STRING; 243274.TM1074; -. DR EnsemblBacteria; AAD36151; AAD36151; TM_1074. DR EnsemblBacteria; AGL50002; AGL50002; Tmari_1078. DR GeneID; 897334; -. DR KEGG; tma:TM1074; -. DR KEGG; tmi:THEMA_08990; -. DR KEGG; tmm:Tmari_1078; -. DR KEGG; tmw:THMA_1096; -. DR PATRIC; 23937077; VBITheMar51294_1087. DR eggNOG; ENOG4105DQ8; Bacteria. DR eggNOG; ENOG410XT3T; LUCA. DR OMA; FMHSRVG; -. DR OrthoDB; EOG6N3CP0; -. DR BioCyc; TMAR243274:GC6P-1103-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.60.120.260; -; 1. DR InterPro; IPR008979; Galactose-bd-like. DR InterPro; IPR033400; RhaM. DR Pfam; PF17132; Glyco_hydro_106; 1. DR SUPFAM; SSF49785; SSF49785; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 986 AA; 115809 MW; E1543D90A39E7246 CRC64; MNLKDLENPG VWYRPAPFWS WNDKLCEEEL LRQIDEMYEK GYGGFFMHSR VGLVTEYLSE EWMRLVRSCA EHARKLGMLA WLYDEDKWPS GFAGGIVPLE KPEHRHKYLT LLKKDQIKPE DEILKKIERD GEEFYVVKRV MKLGDPWFNG TCYVDLLSRE TTEAFLRSTH ERYKKSCGDL FRVSIPGIFT DEPTYLRVHH PKETTLPWTE RFPEEFLRRK GYDIRDHLEE LFFNVKDYMK VRYDFFDVAT SLFIENFTIP YAKWCEENGI FMTGHYMAED TLRGQVEWIG AAMPHYEYMQ IPGIDKLARH LEQVVTIKQV SSAAEQLGKK WVLCETFGTT GQHVSFLHRK WIADWQAVLG VTYINPHLSL YSMRGERKRD YPPNLFYQQP WWKNERFLSD YFARLNHIVT QGKREVKVLM IHPISSAWCV YSKFDDEIDK LNELFDTITK ELVANKIDFH FGDEMILSKH GRVKEAKLRV GEYEYEVVVL PPLLNLKSST VELLNSLAEN GGKVFVLKDF RYGRFFPERV EGKKGRIEFL KKARVFETLE DLIEELKPFF SVDVLDTKTK ENAKAVIAQK RVLEDGSYLL FLANTDIDRE VHCHLELKEK RKHTYAIDLF NFKLVELKEN EFVMFPASSV CIWVTDEEVP AEDEKVVSTG VLLEKEFDFE TALNDFEVKM NSFNVLPVDR VEYFEAGGRV FRNEFVSKIW YEFYRLPDGT PFRVEYSFEV RKKPQKLFLV VECAENLDRI TVNGREVRYE RKSCIFNEEQ NFLDVNFGKM EITDLVREGK NTVVLEGRKE NNITGPGCHT RVKDPENHRP TEVETIYLVG DFSLVNVDET RYVIDAPKIP DHRDITRDGY PFYVGSFTLK KIFECKKDPG KRYFLKLNGV EAASVEVILN GKFLGVLFWR PFMIDITDAL RNGKNELQLV LTNTLFNLIE ANHKADVLEE TFRRPKSFID FEHHTDRYIL LPFGLENVAV LSSSSR // ID Q9WYS8_THEMA Unreviewed; 380 AA. AC Q9WYS8; G4FE23; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 113. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; DE Short=N5-CAIR synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; DE EC=6.3.4.18 {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}; GN Name=purK {ECO:0000256|HAMAP-Rule:MF_01928, GN ECO:0000256|RuleBase:RU361200}; GN OrderedLocusNames=TM_0447 {ECO:0000313|EMBL:AAD35542.1}; GN ORFNames=Tmari_0444 {ECO:0000313|EMBL:AGL49369.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35542.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35542.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35542.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49369.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49369.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5- CC aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5- CC carboxyaminoimidazole ribonucleotide (N5-CAIR). CC {ECO:0000256|HAMAP-Rule:MF_01928}. CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5- CC aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5- CC carboxyaminoimidazole ribonucleotide (N5-CAIR). CC {ECO:0000256|RuleBase:RU361200}. CC -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole CC + HCO(3)(-) = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D- CC ribosyl)imidazole. {ECO:0000256|HAMAP-Rule:MF_01928, CC ECO:0000256|RuleBase:RU361200}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2. CC {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01928, CC ECO:0000256|RuleBase:RU361200}. CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP- CC Rule:MF_01928, ECO:0000256|RuleBase:RU361200, CC ECO:0000256|SAAS:SAAS00575099}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000256|HAMAP- CC Rule:MF_01928}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35542.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49369.1; -; Genomic_DNA. DR PIR; H72374; H72374. DR RefSeq; NP_228257.1; NC_000853.1. DR RefSeq; WP_004081519.1; NZ_CP011107.1. DR PDB; 3AX6; X-ray; 2.20 A; A/B/C/D=1-380. DR PDBsum; 3AX6; -. DR STRING; 243274.TM0447; -. DR EnsemblBacteria; AAD35542; AAD35542; TM_0447. DR EnsemblBacteria; AGL49369; AGL49369; Tmari_0444. DR GeneID; 897466; -. DR KEGG; tma:TM0447; -. DR KEGG; tmi:THEMA_02490; -. DR KEGG; tmm:Tmari_0444; -. DR KEGG; tmw:THMA_0453; -. DR PATRIC; 23935779; VBITheMar51294_0453. DR eggNOG; ENOG4105CY8; Bacteria. DR eggNOG; COG0026; LUCA. DR KO; K01589; -. DR OMA; DSPCGQV; -. DR OrthoDB; EOG6QZMX7; -. DR BioCyc; TMAR243274:GC6P-462-MONOMER; -. DR UniPathway; UPA00074; UER00942. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IBA:GO_Central. DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_01928; PurK; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR003135; ATP-grasp_carboxylate-amine. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR005875; PurK. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF02222; ATP-grasp; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR01161; purK; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3AX6}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS00513347}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200}; Lyase {ECO:0000313|EMBL:AGL49369.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS00513347}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS00513319}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 105 286 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT NP_BIND 169 172 ADP. {ECO:0000213|PDB:3AX6}. FT NP_BIND 169 172 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT NP_BIND 256 257 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 101 101 ADP. {ECO:0000213|PDB:3AX6}. FT BINDING 101 101 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 138 138 ADP. {ECO:0000213|PDB:3AX6}. FT BINDING 138 138 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 177 177 ADP. {ECO:0000213|PDB:3AX6}. FT BINDING 177 177 ATP. {ECO:0000256|HAMAP-Rule:MF_01928}. FT BINDING 244 244 ADP. {ECO:0000213|PDB:3AX6}. FT BINDING 256 256 ADP. {ECO:0000213|PDB:3AX6}. SQ SEQUENCE 380 AA; 42560 MW; EF7C976C5B212CB6 CRC64; MKKIGIIGGG QLGKMMTLEA KKMGFYVIVL DPTPRSPAGQ VADEQIVAGF FDSERIEDLV KGSDVTTYDL EHIDVQTLKK LYNEGYKIHP SPYTLEIIQD KFVQKEFLKK NGIPVPEYKL VKDLESDVRE FGFPVVQKAR KGGYDGRGVF IIKNEKDLEN AIKGETYLEE FVEIEKELAV MVARNEKGEI ACYPVVEMYF DEDANICDTV IAPARIEEKY SKIAREIATS VVEALEGVGI FGIEMFLTKQ GEILVNEIAP RPHNSGHYTI EACVTSQFEQ HIRAIMNLPL GSTELLIPAV MVNLLGEEGY YGKPALIGLE EALAIEGLSL HFYGKKETRP YRKMGHFTVV DRDVERALEK ALRAKKILKV VSEEGAMCQG // ID Q9X0L9_THEMA Unreviewed; 370 AA. AC Q9X0L9; G4FEL3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Branched chain amino acid ABC transporter, periplasmic amino acid-binding protein {ECO:0000313|EMBL:AAD36211.1}; DE SubName: Full=Branched-chain amino acid ABC transporter, amino acid-binding protein {ECO:0000313|EMBL:AGL50065.1}; GN OrderedLocusNames=TM_1135 {ECO:0000313|EMBL:AAD36211.1}; GN ORFNames=Tmari_1141 {ECO:0000313|EMBL:AGL50065.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36211.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36211.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36211.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50065.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50065.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36211.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50065.1; -; Genomic_DNA. DR PIR; C72290; C72290. DR RefSeq; NP_228941.1; NC_000853.1. DR RefSeq; WP_004080272.1; NZ_CP011107.1. DR PDB; 3TD9; X-ray; 1.90 A; A=21-370. DR PDBsum; 3TD9; -. DR STRING; 243274.TM1135; -. DR EnsemblBacteria; AAD36211; AAD36211; TM_1135. DR EnsemblBacteria; AGL50065; AGL50065; Tmari_1141. DR GeneID; 898629; -. DR KEGG; tma:TM1135; -. DR KEGG; tmi:THEMA_08670; -. DR KEGG; tmm:Tmari_1141; -. DR KEGG; tmw:THMA_1158; -. DR PATRIC; 23937205; VBITheMar51294_1151. DR eggNOG; ENOG4107RWU; Bacteria. DR eggNOG; COG0683; LUCA. DR KO; K01999; -. DR OMA; TDVEQDY; -. DR OrthoDB; EOG6S52KK; -. DR BioCyc; TMAR243274:GC6P-1164-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0006865; P:amino acid transport; IEA:InterPro. DR InterPro; IPR028081; Leu-bd. DR InterPro; IPR000709; Leu_Ile_Val-bd. DR InterPro; IPR028082; Peripla_BP_I. DR PANTHER; PTHR30483:SF6; PTHR30483:SF6; 1. DR Pfam; PF13458; Peripla_BP_6; 1. DR SUPFAM; SSF53822; SSF53822; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3TD9}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 21 353 Peripla_BP_6. {ECO:0000259|Pfam:PF13458}. FT BINDING 226 226 Sulfate. {ECO:0000213|PDB:3TD9}. FT BINDING 254 254 Sulfate; via amide nitrogen. FT {ECO:0000213|PDB:3TD9}. SQ SEQUENCE 370 AA; 40130 MW; 53998360F1CF60AA CRC64; MRKVLVTVLL VLTVLSLFSA VKIAVILPMT GGISAFGRMV WEGIQIAHEE KPTVLGEEVE LVLLDTRSEK TEAANAAARA IDKEKVLAII GEVASAHSLA IAPIAEENKV PMVTPASTNP LVTQGRKFVS RVCFIDPFQG AAMAVFAYKN LGAKRVVVFT DVEQDYSVGL SNFFINKFTE LGGQVKRVFF RSGDQDFSAQ LSVAMSFNPD AIYITGYYPE IALISRQARQ LGFTGYILAG DGADAPELIE IGGEAVEGLL FTTHYHPKAA SNPVAKKFVE VYKEKYGKEP AALNALGYDA YMVLLDAIER AGSFDREKIA EEIRKTRNFN GASGIINIDE NGDAIKSVVV NIVKNGSVDF EAVINPDDLK // ID Q9WZ92_THEMA Unreviewed; 350 AA. AC Q9WZ92; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 81. DE SubName: Full=N-acetylglucosaminyl-phosphatidylinositol biosynthesis-related protein {ECO:0000313|EMBL:AAD35708.1}; DE SubName: Full=Putative teichuronic acid biosynthesis glycosyl transferase TuaC {ECO:0000313|EMBL:AGL49550.1}; GN OrderedLocusNames=TM_0624 {ECO:0000313|EMBL:AAD35708.1}; GN ORFNames=Tmari_0625 {ECO:0000313|EMBL:AGL49550.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35708.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35708.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35708.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49550.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49550.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35708.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49550.1; -; Genomic_DNA. DR PIR; E72352; E72352. DR RefSeq; NP_228433.1; NC_000853.1. DR RefSeq; WP_010865169.1; NZ_CP011107.1. DR STRING; 243274.TM0624; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAD35708; AAD35708; TM_0624. DR EnsemblBacteria; AGL49550; AGL49550; Tmari_0625. DR GeneID; 897711; -. DR KEGG; tma:TM0624; -. DR KEGG; tmm:Tmari_0625; -. DR KEGG; tmw:THMA_0640; -. DR PATRIC; 23936161; VBITheMar51294_0634. DR eggNOG; COG0438; LUCA. DR OrthoDB; EOG62NX0X; -. DR BioCyc; TMAR243274:GC6P-649-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49550.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 74 91 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 350 AA; 40051 MW; 567AC3CDD7A2889E CRC64; MLMNTTKIKE RIGHLLIMVM SVLLLELKYS EQPPLIRTLY GVVVTFLVIM QYALFRKHKL VVLGSLFLIR EPNIFFVLST SDVAIIAYVL LELRRLKLKL SIFKEPLDVR DIYLETLENA ARCIFVSRAL LEKAKSFGYS GQNATVIPNG YDPDVFKPMD KNTVRKELGI YKENTHYVGF VGNLIPIKRA DKLPEIFRKI AKELPNTRFL IVGDGALRDK ILKEMKGLDV VFAGRVPQVE VAKYMNAMDV MVLPSRNEGW PCVILEAQAC GTCVIGSSNG GIPEAIGFEK YVVQEGDKFE ERFGKRVVEV LREGYDMNRL MERAKGFTWV KVVERETELY EQIIQAFRRD // ID Q9WZ30_THEMA Unreviewed; 182 AA. AC Q9WZ30; G4FDR1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 91. DE SubName: Full=Ferritin {ECO:0000313|EMBL:AGL49482.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35645.1}; GN OrderedLocusNames=TM_0560 {ECO:0000313|EMBL:AAD35645.1}; GN ORFNames=Tmari_0557 {ECO:0000313|EMBL:AGL49482.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35645.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35645.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35645.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49482.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49482.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the Dps family. CC {ECO:0000256|SAAS:SAAS00563186}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35645.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49482.1; -; Genomic_DNA. DR PIR; G72360; G72360. DR RefSeq; NP_228370.1; NC_000853.1. DR RefSeq; WP_004081317.1; NZ_CP011107.1. DR SMR; Q9WZ30; 4-166. DR STRING; 243274.TM0560; -. DR EnsemblBacteria; AAD35645; AAD35645; TM_0560. DR EnsemblBacteria; AGL49482; AGL49482; Tmari_0557. DR GeneID; 897618; -. DR KEGG; tma:TM0560; -. DR KEGG; tmi:THEMA_01875; -. DR KEGG; tmm:Tmari_0557; -. DR KEGG; tmw:THMA_0573; -. DR PATRIC; 23936027; VBITheMar51294_0568. DR eggNOG; ENOG4108Y4M; Bacteria. DR eggNOG; COG2406; LUCA. DR OMA; TTFYYYT; -. DR OrthoDB; EOG6X3W56; -. DR BioCyc; TMAR243274:GC6P-584-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR008331; Ferritin_DPS_dom. DR InterPro; IPR014490; UCP018063_ferrtn. DR Pfam; PF00210; Ferritin; 1. DR PIRSF; PIRSF018063; Ferrtn_UCP018063; 1. DR SUPFAM; SSF47240; SSF47240; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 21 161 Ferritin. {ECO:0000259|Pfam:PF00210}. SQ SEQUENCE 182 AA; 20620 MW; EE3F44F649CAA0D7 CRC64; MARVAREMVE KAGVDVDKLL ELLIKNAAAE LTTYYYYTIL RANLIGLEGE TIKEIAEVAR IEDRNHFEAL VPRIYELGGK LPDCMKEFHD LSACPPARLP DKPTVQEILR VLVAAERCAV KGYTEICNMT AGKDHRTYEL SLAILNEEIE HESWFSEFLG EGPSGHFMRR GETSPFVSKF LK // ID Q9X050_THEMA Unreviewed; 331 AA. AC Q9X050; G4FF35; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Ribose ABC transport system, permease protein RbsC {ECO:0000313|EMBL:AGL49882.1}; DE SubName: Full=Ribose ABC transporter, permease protein {ECO:0000313|EMBL:AAD36034.1}; GN OrderedLocusNames=TM_0955 {ECO:0000313|EMBL:AAD36034.1}; GN ORFNames=Tmari_0957 {ECO:0000313|EMBL:AGL49882.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36034.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36034.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36034.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49882.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49882.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|SAAS:SAAS00582814}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36034.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49882.1; -; Genomic_DNA. DR PIR; D72314; D72314. DR RefSeq; NP_228763.1; NC_000853.1. DR RefSeq; WP_004080607.1; NZ_CP011107.1. DR STRING; 243274.TM0955; -. DR TCDB; 3.A.1.2.19; the atp-binding cassette (abc) superfamily. DR DNASU; 898690; -. DR EnsemblBacteria; AAD36034; AAD36034; TM_0955. DR EnsemblBacteria; AGL49882; AGL49882; Tmari_0957. DR GeneID; 898690; -. DR KEGG; tma:TM0955; -. DR KEGG; tmi:THEMA_09570; -. DR KEGG; tmm:Tmari_0957; -. DR KEGG; tmw:THMA_0978; -. DR PATRIC; 23936841; VBITheMar51294_0969. DR eggNOG; ENOG4105CNN; Bacteria. DR eggNOG; COG1172; LUCA. DR KO; K10440; -. DR OMA; NVSSYYQ; -. DR OrthoDB; EOG61P6T8; -. DR BioCyc; TMAR243274:GC6P-985-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015749; P:monosaccharide transport; IBA:GOC. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00476327}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAAS:SAAS00476327, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00476193}. FT TRANSMEM 21 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 71 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 102 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 108 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 136 154 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 174 196 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 227 245 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 281 300 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 331 AA; 35067 MW; 2CE2E9E4EFE08217 CRC64; MQVERSRAKI SWYQRISRYQ SIFILLGLIV LFSFLSNRFL TLENFWIILR QTAVNLCIAV GMTFVILTGG IDLSVGSILG FSGAVTAKLL KYGLILSAFG VVLKFNPLGA SIIGVLAGFA IGLFNGFIIT RFNIPPFVAT LGTMTAVRGF IMLLTKGHPI TRLGDSFDFI GSGWFLGIPM PVWIAAIATG VGIFILRKTQ FGRYVYAVGG NEKAAVLSGV NSKLTKLWVY AISGILSAVA GLIVTARLDS AQPNAGLMYE LDAIAATVIG GASLSGGKGT LIGTVVGALI IGVLNDGLVL VGVSPFWQQV AKGFIIIAAV IAEKLGRGEK E // ID Q9WXW1_THEMA Unreviewed; 394 AA. AC Q9WXW1; G4FH21; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 93. DE SubName: Full=DNA helicase {ECO:0000313|EMBL:AGL49029.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35200.1}; GN OrderedLocusNames=TM_0106 {ECO:0000313|EMBL:AAD35200.1}; GN ORFNames=Tmari_0103 {ECO:0000313|EMBL:AGL49029.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35200.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35200.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35200.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49029.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49029.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35200.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49029.1; -; Genomic_DNA. DR PIR; B72419; B72419. DR RefSeq; NP_227922.1; NC_000853.1. DR RefSeq; WP_004082671.1; NZ_CP011107.1. DR STRING; 243274.TM0106; -. DR EnsemblBacteria; AAD35200; AAD35200; TM_0106. DR EnsemblBacteria; AGL49029; AGL49029; Tmari_0103. DR GeneID; 896933; -. DR KEGG; tma:TM0106; -. DR KEGG; tmi:THEMA_04275; -. DR KEGG; tmm:Tmari_0103; -. DR KEGG; tmw:THMA_0102; -. DR PATRIC; 23935052; VBITheMar51294_0104. DR eggNOG; ENOG4107Z0U; Bacteria. DR eggNOG; COG2251; LUCA. DR KO; K06860; -. DR OMA; PECKFCK; -. DR OrthoDB; EOG67HJQH; -. DR BioCyc; TMAR243274:GC6P-106-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR InterPro; IPR019993; RecB_nuclease_TM0106_put. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13482; RNase_H_2; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR03491; TIGR03491; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AGL49029.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Helicase {ECO:0000313|EMBL:AGL49029.1}; KW Hydrolase {ECO:0000313|EMBL:AGL49029.1}; KW Nucleotide-binding {ECO:0000313|EMBL:AGL49029.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 241 386 RNase_H_2. {ECO:0000259|Pfam:PF13482}. SQ SEQUENCE 394 AA; 46450 MW; CB350A163B1BAD83 CRC64; MTISYEDVEN FLVCPRRYYL SKKISKEVSP NFSEELMEAG FPLENPVIVC EFEGHELVSN PDLIVKDRDG WRIILRKSAK RFKDKYILES AYHALVFSRA GLEVSGVEIV SDSFSRKMEN WKNLIPIVED VLREMLTIDD DPHPRVGRHC RYCDFLEDCE GKFFEEKSLL LVNGIGEETY RVLYGMGIET LEDLAEADQR ILEKVFGKEK GKRFVMAARA FLENRVIMIT PPEDLPEGTI VDIEYHPSEE RDFLYGFLIG DEYRYFLEED QGDLIAFLNS LDDESVFYHY HGPEKRKLIS LIGRNKRMNF LDVFTILRNH FVFPVMSYSL KRIAKYLGYD WRTSLNGYEI LRLYEKWKKT RNEELLKQML LYNEDDVRAT KLVLDFMRSY SSFS // ID Q9X279_THEMA Unreviewed; 218 AA. AC Q9X279; G4FGE3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36822.1}; GN OrderedLocusNames=TM_1757 {ECO:0000313|EMBL:AAD36822.1}; GN ORFNames=Tmari_1765 {ECO:0000313|EMBL:AGL50689.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36822.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36822.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36822.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50689.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50689.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36822.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50689.1; -; Genomic_DNA. DR PIR; F72214; F72214. DR RefSeq; NP_229555.1; NC_000853.1. DR RefSeq; WP_004082293.1; NZ_CP011107.1. DR STRING; 243274.TM1757; -. DR EnsemblBacteria; AAD36822; AAD36822; TM_1757. DR EnsemblBacteria; AGL50689; AGL50689; Tmari_1765. DR GeneID; 897860; -. DR KEGG; tma:TM1757; -. DR KEGG; tmi:THEMA_05450; -. DR KEGG; tmm:Tmari_1765; -. DR KEGG; tmw:THMA_1799; -. DR PATRIC; 23938490; VBITheMar51294_1775. DR eggNOG; ENOG4105FNI; Bacteria. DR eggNOG; ENOG4111QV4; LUCA. DR OMA; VANIYRP; -. DR OrthoDB; EOG610452; -. DR BioCyc; TMAR243274:GC6P-1805-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 10 44 CbiA. {ECO:0000259|Pfam:PF01656}. SQ SEQUENCE 218 AA; 24386 MW; 5C63F9B44D5B2BC4 CRC64; MIRILMGSYG SGKTEISINL ALKLKSSGKD VSLVDLDVVT PYFRLRDLKK KLEELGIHVV TVGDNLRYSD LPIIPKNTDW LSSEEAVIDT GGEDGAKAVG ALRHLMNGKN THTYFVVNAF RPFCERPEDI IENLKKISTL SKMKIDFLIN NSNLGDMTTA EVVLEGERIV SEVSRKTGIK VLFTVVPEEL IDPPETDYPL FSIRRFMKRK LGIGGMRT // ID Q9WXT1_THEMA Unreviewed; 778 AA. AC Q9WXT1; G4FGZ1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 98. DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:AGL48999.1}; DE EC=3.2.1.37 {ECO:0000313|EMBL:AGL48999.1}; DE SubName: Full=Xylosidase {ECO:0000313|EMBL:AAD35170.1}; GN OrderedLocusNames=TM_0076 {ECO:0000313|EMBL:AAD35170.1}; GN ORFNames=Tmari_0073 {ECO:0000313|EMBL:AGL48999.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35170.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35170.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35170.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48999.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48999.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. CC {ECO:0000256|RuleBase:RU361161}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35170.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48999.1; -; Genomic_DNA. DR PIR; D72421; D72421. DR RefSeq; NP_227892.1; NC_000853.1. DR RefSeq; WP_004082594.1; NZ_CP011107.1. DR STRING; 243274.TM0076; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR EnsemblBacteria; AAD35170; AAD35170; TM_0076. DR EnsemblBacteria; AGL48999; AGL48999; Tmari_0073. DR GeneID; 896902; -. DR KEGG; tma:TM0076; -. DR KEGG; tmi:THEMA_04425; -. DR KEGG; tmm:Tmari_0073; -. DR KEGG; tmw:THMA_0072; -. DR PATRIC; 23934992; VBITheMar51294_0074. DR eggNOG; ENOG4105D17; Bacteria. DR eggNOG; COG1472; LUCA. DR KO; K05349; -. DR OMA; AIVDAWY; -. DR OrthoDB; EOG6DNT6C; -. DR BioCyc; TMAR243274:GC6P-76-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central. DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC. DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central. DR Gene3D; 3.20.20.300; -; 1. DR Gene3D; 3.40.50.1700; -; 1. DR InterPro; IPR026891; Fn3-like. DR InterPro; IPR026892; Glyco_hydro_3. DR InterPro; IPR019800; Glyco_hydro_3_AS. DR InterPro; IPR002772; Glyco_hydro_3_C. DR InterPro; IPR001764; Glyco_hydro_3_N. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR30620; PTHR30620; 3. DR Pfam; PF14310; Fn3-like; 1. DR Pfam; PF00933; Glyco_hydro_3; 1. DR Pfam; PF01915; Glyco_hydro_3_C; 1. DR PRINTS; PR00133; GLHYDRLASE3. DR SMART; SM01217; Fn3_like; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR SUPFAM; SSF52279; SSF52279; 2. DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361161, KW ECO:0000313|EMBL:AGL48999.1}; KW Hydrolase {ECO:0000256|RuleBase:RU361161, KW ECO:0000313|EMBL:AGL48999.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 778 AA; 86849 MW; 3362B9B0FDA62055 CRC64; MELYRDPSQP IEVRVRDLLS RMTLEEKVAQ LGSVWGYELI DERGKFSREK AKELLKNGIG QITRPGGSTN LEPQEAAELV NEIQRFLVEE TRLGIPAMIH EECLTGYMGL GGTNFPQAIA MASTWDPDLI EKMTTAVRED MRKIGAHQGL APVLDVARDP RWGRTEETFG ESPYLVARMG VSYVKGLQGE DIKKGVVATV KHFAGYSASE GGKNWAPTNI PEREFKEVFL FPFEAAVKEA NVLSVMNSYS EIDGVPCAAN RKLLTDILRK DWGFEGIVVS DYFAVKVLED YHRIARDKSE AARLALEAGI DVELPKTECY QYLKDLVEKG IISEALIDEA VTRVLRLKFM LGLFENPYVE VEKAKIESHR DIALEIARKS IILLKNDGIL PLQKNKKVAL IGPNAGEVRN LLGDYMYLAH IRALLDNIDD VFGNPQIPRE NYERLKKSIE EHMKSIPSVL DAFKEEGIEF EYAKGCEVTG EDRSGFEEAI EIAKKSDVAI VVVGDKSGLT LDCTTGESRD MANLKLPGVQ EELVLEVAKT GKPVVLVLIT GRPYSLKNVV DKVNAILQVW LPGEAGGRAI VDIIYGKVNP SGKLPISFPR SAGQIPVFHY VKPSGGRSHW HGDYVDESTK PLFPFGHGLS YTKFEYSNLR IEPKEVPPAG EVVIKVDVEN IGDRDGDEVV QLYIGREFAS VTRPVKELKG FKRVSLKAKE KKTVVFRLHM DVLAYYNRDM KLVVEPGEFK VMVGSSSEDI RLTGSFSVVG EKREVVGMRK FFTEACEE // ID Q9X143_THEMA Unreviewed; 463 AA. AC Q9X143; G4FI09; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 89. DE SubName: Full=AstB/ChuR-related protein {ECO:0000313|EMBL:AGL50248.1}; DE SubName: Full=AstB/chuR-related protein {ECO:0000313|EMBL:AAD36391.1}; GN OrderedLocusNames=TM_1317 {ECO:0000313|EMBL:AAD36391.1}; GN ORFNames=Tmari_1324 {ECO:0000313|EMBL:AGL50248.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36391.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36391.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36391.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50248.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50248.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36391.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50248.1; -; Genomic_DNA. DR PIR; E72268; E72268. DR RefSeq; NP_229121.1; NC_000853.1. DR RefSeq; WP_004083362.1; NZ_CP011107.1. DR STRING; 243274.TM1317; -. DR EnsemblBacteria; AAD36391; AAD36391; TM_1317. DR EnsemblBacteria; AGL50248; AGL50248; Tmari_1324. DR GeneID; 898165; -. DR KEGG; tma:TM1317; -. DR KEGG; tmi:THEMA_07760; -. DR KEGG; tmm:Tmari_1324; -. DR KEGG; tmw:THMA_1341; -. DR PATRIC; 23937568; VBITheMar51294_1330. DR eggNOG; ENOG4107YPG; Bacteria. DR eggNOG; COG0641; LUCA. DR KO; K06871; -. DR OMA; FISATIH; -. DR OrthoDB; EOG6NWBKW; -. DR BioCyc; TMAR243274:GC6P-1348-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF13186; SPASM; 1. DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00421379}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|SAAS:SAAS00421379}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00421379}; KW Metal-binding {ECO:0000256|SAAS:SAAS00421379}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00421341}. FT DOMAIN 87 242 Radical_SAM. {ECO:0000259|Pfam:PF04055}. FT DOMAIN 346 412 SPASM. {ECO:0000259|Pfam:PF13186}. SQ SEQUENCE 463 AA; 54233 MW; D8B9E091C2615472 CRC64; MITINLPKVF FSLIEAPRNN RYLLDKVNFD FYKLDDSIQI TRKASSYLVR TKAKNVIEEL EKLKKNTLIS LKRKLVKDND ILRLALNVSQ VCRLKCRYCY ANAGTYGNPG FMKRNVLVRT LDFFLSNYNV HNIHIFGGEP LLNIEMIEEM FRILTSKYAK KFNNLRITVA TSLFVSEETI NRFIKIYESY KDKFQIYMVV SLDGPKEIQD NTRPSLDSKS SSFDRIKNNI NLLKQKGFSI SFEVTYTKLH KQLGWNILKI YKYFYTEFNA ANVIISPVYD WNGSLDKNLR IDISIAQEYY EIIASLLEKS RRGDLNDFDR ALLCKLLMNY LNPSDSSGKI IVSTFCPAGS NSFIVDIFGN IYPCQLVVGN LKYRISNVVK DNEEKILKNL KDWRYKALRL FTKARYSKCK DCYFLFYCSR CIFKRDYQKD MFKACDVEKK IIETILEFDP WTLLPLMDNF NGG // ID Q9S5X4_THEMA Unreviewed; 466 AA. AC Q9S5X4; G4FET0; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 11-MAY-2016, entry version 98. DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:AGL49996.1}; DE EC=3.2.1.20 {ECO:0000313|EMBL:AGL49996.1}; DE SubName: Full=Alpha-glucosidase, putative {ECO:0000313|EMBL:AAD36145.1}; GN OrderedLocusNames=TM_1068 {ECO:0000313|EMBL:AAD36145.1}; GN ORFNames=Tmari_1072 {ECO:0000313|EMBL:AGL49996.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36145.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36145.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36145.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49996.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49996.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000256|RuleBase:RU361152}; CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. CC {ECO:0000256|RuleBase:RU361152}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36145.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49996.1; -; Genomic_DNA. DR RefSeq; NP_228874.1; NC_000853.1. DR RefSeq; WP_004080419.1; NZ_CP011107.1. DR SMR; Q9S5X4; 4-464. DR STRING; 243274.TM1068; -. DR CAZy; GH4; Glycoside Hydrolase Family 4. DR DNASU; 897107; -. DR EnsemblBacteria; AAD36145; AAD36145; TM_1068. DR EnsemblBacteria; AGL49996; AGL49996; Tmari_1072. DR GeneID; 897107; -. DR KEGG; tma:TM1068; -. DR KEGG; tmi:THEMA_09020; -. DR KEGG; tmm:Tmari_1072; -. DR KEGG; tmw:THMA_1090; -. DR PATRIC; 23937065; VBITheMar51294_1081. DR eggNOG; ENOG4107V4V; Bacteria. DR eggNOG; COG1486; LUCA. DR KO; K07406; -. DR OMA; WIEKNAS; -. DR OrthoDB; EOG6TJ7TJ; -. DR BioCyc; TMAR243274:GC6P-1097-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR InterPro; IPR019802; GlycHydrolase_4_CS. DR InterPro; IPR001088; Glyco_hydro_4. DR InterPro; IPR022616; Glyco_hydro_4_C. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF02056; Glyco_hydro_4; 1. DR Pfam; PF11975; Glyco_hydro_4C; 1. DR PRINTS; PR00732; GLHYDRLASE4. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF56327; SSF56327; 1. DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361152, KW ECO:0000313|EMBL:AGL49996.1}; KW Hydrolase {ECO:0000256|RuleBase:RU361152, KW ECO:0000313|EMBL:AGL49996.1}; NAD {ECO:0000256|RuleBase:RU361152}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 202 438 Glyco_hydro_4C. FT {ECO:0000259|Pfam:PF11975}. SQ SEQUENCE 466 AA; 54121 MW; 391EB9A92E8051D2 CRC64; MPTIVFVGAG SVRYTIKLVG DLAKTPDLYG SRLVLMDIDE ERLKATYILV TKYLRELNAE YTVEQTTSLE EALEGADFVI NTALYRAPGH EDGYVHYEIM REVGERHGYY RGIDSQELNM VSDYYTLSNY NHLKMSLDIA KAVEKIAPNA WILQTANPVF EITQLVKRLT KAKIVGFCHG YAHVFHLAKV LGVEPEELDW QVAGVNHAIW MNRFRCRGED LYPKLDEWIE ENASRWEPKN PWDVDFSPAA IDMYRFYGMY PIGDTVRSGT WKYHYDLETK KRWYGKFGGI DNEVERPKFY ESLREQRKRL MELAKEVEKD PTIELTKVWP EVFTTGSESV EQHIPFINAL VNDKKARLVL NVENRGVIKG IPDDVMVEVP VVVDKEGIHP EKIEPDLTDR IKKFYLLPRI LRMEWALEAF ISGDRRVLEE ILVRDPRTRS YEQAVAVIDD ILNLPFNEEM KKHYGS // ID Q9WXW8_THEMA Unreviewed; 239 AA. AC Q9WXW8; G4FH28; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=XylU-related protein {ECO:0000313|EMBL:AAD35207.1}; GN OrderedLocusNames=TM_0113 {ECO:0000313|EMBL:AAD35207.1}; GN ORFNames=Tmari_0110 {ECO:0000313|EMBL:AGL49036.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35207.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35207.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35207.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49036.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49036.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35207.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49036.1; -; Genomic_DNA. DR PIR; H72416; H72416. DR RefSeq; NP_227929.1; NC_000853.1. DR RefSeq; WP_004082686.1; NZ_CP011107.1. DR SMR; Q9WXW8; 33-228. DR STRING; 243274.TM0113; -. DR DNASU; 896940; -. DR EnsemblBacteria; AAD35207; AAD35207; TM_0113. DR EnsemblBacteria; AGL49036; AGL49036; Tmari_0110. DR GeneID; 896940; -. DR KEGG; tma:TM0113; -. DR KEGG; tmi:THEMA_04240; -. DR KEGG; tmm:Tmari_0110; -. DR KEGG; tmw:THMA_0109; -. DR PATRIC; 23935066; VBITheMar51294_0111. DR eggNOG; ENOG4107YWN; Bacteria. DR eggNOG; COG0726; LUCA. DR OMA; NEMGLYS; -. DR OrthoDB; EOG6V1M8Q; -. DR BioCyc; TMAR243274:GC6P-113-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.370; -; 1. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR002509; NODB_dom. DR Pfam; PF01522; Polysacc_deac_1; 1. DR SUPFAM; SSF88713; SSF88713; 1. DR PROSITE; PS51677; NODB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 239 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972318. FT DOMAIN 33 212 NodB homology. FT {ECO:0000259|PROSITE:PS51677}. SQ SEQUENCE 239 AA; 27236 MW; 991B3F41DA67B9D1 CRC64; MKRLLVFLSI FLTTVLLFST DSKVNFGEEN GVKLVALTFD DGPDVKLTSA VLGTLEKHGV VATFFVVGQR LNESTRAILE RMISMGCEIG NHSWNYEPLD KKDPETIKDY IERTKDLIKK YTGKEPRFFR PPNLAVSDTM FDVINMPFVS GILGYDWAGC DRDPQKIVSN VLKDIRDGAI ILLHDVQPEP HPIVEVLEIL IPELKKRGYG FVTLSELFKR KGVNPEDPVY RKKMWVYVE // ID Q9X025_THEMA Unreviewed; 377 AA. AC Q9X025; G4FF67; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36004.1}; GN OrderedLocusNames=TM_0923 {ECO:0000313|EMBL:AAD36004.1}; GN ORFNames=Tmari_0925 {ECO:0000313|EMBL:AGL49850.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36004.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36004.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36004.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49850.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49850.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36004.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49850.1; -; Genomic_DNA. DR PIR; D72317; D72317. DR RefSeq; NP_228731.1; NC_000853.1. DR RefSeq; WP_004080639.1; NZ_CP011107.1. DR STRING; 243274.TM0923; -. DR EnsemblBacteria; AAD36004; AAD36004; TM_0923. DR EnsemblBacteria; AGL49850; AGL49850; Tmari_0925. DR GeneID; 898597; -. DR KEGG; tma:TM0923; -. DR KEGG; tmi:THEMA_00020; -. DR KEGG; tmm:Tmari_0925; -. DR KEGG; tmw:THMA_0945; -. DR PATRIC; 23936777; VBITheMar51294_0937. DR eggNOG; ENOG4106F30; Bacteria. DR eggNOG; ENOG410Y7EE; LUCA. DR OMA; RALIYYE; -. DR OrthoDB; EOG690MBB; -. DR BioCyc; TMAR243274:GC6P-953-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF13174; TPR_6; 1. DR SMART; SM00028; TPR; 2. DR SUPFAM; SSF48452; SSF48452; 2. DR PROSITE; PS50005; TPR; 2. DR PROSITE; PS50293; TPR_REGION; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 160 183 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 292 364 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. FT COILED 246 273 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 377 AA; 44171 MW; 84DB528E60310756 CRC64; MNILEKIVRD LISEKRITEA RNLLSLFPEE FPHLELEVEY AARNWKAVKR LYENLPDELK EKYREYYEYA ANQLNIDYSK ETEEALKEIE RKNFQGAASI LESIVKDYPE LVEVVALRYK LALQRNEKRA IEKYRKLLLS LDRTHPALIE TRASSRRIGV FEVFTLSLLV ALLVTTILAF YTLPSRIEVN VPSSENTINI KPVEQRVEDV LANIVILTEN LGKINDSLEK NFSALQENMS PISENIESLK EALTNLESRL SKIESAIART SNKEPSVSVV YVPAREDRIE RAKSLWFLGY MFYLRRDYDE AINRFEIAIK EIGEDNVYFK DDVYYYRALC YYYKGDTSTA RSLFEEFIKL FPDSEYADDA EYFLKRL // ID Q9X1M8_THEMA Unreviewed; 261 AA. AC Q9X1M8; G4FFT0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 93. DE SubName: Full=Flagellar basal-body rod protein FlgG {ECO:0000313|EMBL:AAD36609.1}; GN OrderedLocusNames=TM_1542 {ECO:0000313|EMBL:AAD36609.1}; GN ORFNames=Tmari_1550 {ECO:0000313|EMBL:AGL50474.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36609.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36609.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36609.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50474.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50474.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body CC {ECO:0000256|RuleBase:RU362116}. CC -!- SIMILARITY: Belongs to the flagella basal body rod proteins CC family. {ECO:0000256|RuleBase:RU362116, CC ECO:0000256|SAAS:SAAS00560878}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36609.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50474.1; -; Genomic_DNA. DR PIR; B72243; B72243. DR RefSeq; NP_229342.1; NC_000853.1. DR RefSeq; WP_004081929.1; NZ_CP011107.1. DR STRING; 243274.TM1542; -. DR DNASU; 897975; -. DR EnsemblBacteria; AAD36609; AAD36609; TM_1542. DR EnsemblBacteria; AGL50474; AGL50474; Tmari_1550. DR GeneID; 897975; -. DR KEGG; tma:TM1542; -. DR KEGG; tmi:THEMA_06575; -. DR KEGG; tmm:Tmari_1550; -. DR KEGG; tmw:THMA_1576; -. DR PATRIC; 23938044; VBITheMar51294_1560. DR eggNOG; ENOG4105CGA; Bacteria. DR eggNOG; COG4786; LUCA. DR KO; K02392; -. DR OMA; MYQTIRQ; -. DR OrthoDB; EOG61307X; -. DR BioCyc; TMAR243274:GC6P-1582-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009426; C:bacterial-type flagellum basal body, distal rod; IEA:InterPro. DR GO; GO:0009424; C:bacterial-type flagellum hook; IBA:GO_Central. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IBA:GO_Central. DR InterPro; IPR001444; Flag_bb_rod_N. DR InterPro; IPR019776; Flagellar_basal_body_rod_CS. DR InterPro; IPR020013; Flagellar_FlgE/F/G. DR InterPro; IPR010930; Flg_bb/hook_C_dom. DR InterPro; IPR012836; FlgF. DR InterPro; IPR012834; FlgG_G_neg. DR Pfam; PF00460; Flg_bb_rod; 1. DR Pfam; PF06429; Flg_bbr_C; 1. DR TIGRFAMs; TIGR03506; FlgEFG_subfam; 2. DR TIGRFAMs; TIGR02490; flgF; 1. DR TIGRFAMs; TIGR02488; flgG_G_neg; 1. DR PROSITE; PS00588; FLAGELLA_BB_ROD; 1. PE 3: Inferred from homology; KW Bacterial flagellum {ECO:0000256|RuleBase:RU362116}; KW Cell projection {ECO:0000313|EMBL:AAD36609.1}; KW Cilium {ECO:0000313|EMBL:AAD36609.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD36609.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 35 Flg_bb_rod. {ECO:0000259|Pfam:PF00460}. FT DOMAIN 182 258 Flg_bbr_C. {ECO:0000259|Pfam:PF06429}. SQ SEQUENCE 261 AA; 28044 MW; E57E8FF27FA873A4 CRC64; MMISLYSAAT GMSAQQFKLD TIANNLANVD TTGYKKVRAE FQDLLYQYVK NAGTPTAATS SLPTGLYVGH GVRTAATTRI FTLGNFEQTG NALDLAIAGD GFFQIQLQDG RIAYTRDGSF KMDSEGRIVT SNGLLLVPEI TIPENAVSIN VSPDGIVSAE LQDGTIQELG TITLVRFVNP SGLKSIGDNL YIATPASGDP IEGVPGQDGF GAIKQGFLEK SNVDVVREMV DMITAQRAYE FNSRVIQTAD EMLRTATNVK R // ID Q9X052_THEMA Unreviewed; 217 AA. AC Q9X052; G4FF33; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36036.1}; GN OrderedLocusNames=TM_0957 {ECO:0000313|EMBL:AAD36036.1}; GN ORFNames=Tmari_0959 {ECO:0000313|EMBL:AGL49884.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36036.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36036.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36036.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49884.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49884.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36036.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49884.1; -; Genomic_DNA. DR PIR; F72314; F72314. DR RefSeq; NP_228765.1; NC_000853.1. DR RefSeq; WP_004080605.1; NZ_CP011107.1. DR PDB; 2F4I; X-ray; 2.25 A; A/B/C/D=33-217. DR PDBsum; 2F4I; -. DR STRING; 243274.TM0957; -. DR EnsemblBacteria; AAD36036; AAD36036; TM_0957. DR EnsemblBacteria; AGL49884; AGL49884; Tmari_0959. DR GeneID; 898692; -. DR KEGG; tma:TM0957; -. DR KEGG; tmi:THEMA_09560; -. DR KEGG; tmm:Tmari_0959; -. DR KEGG; tmw:THMA_0980; -. DR PATRIC; 23936845; VBITheMar51294_0971. DR eggNOG; ENOG41067A8; Bacteria. DR eggNOG; ENOG41128U6; LUCA. DR OMA; EYVYGNA; -. DR OrthoDB; EOG6NKQZR; -. DR BioCyc; TMAR243274:GC6P-987-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR014582; UCP033535_lipo. DR Pfam; PF10054; DUF2291; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2F4I}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT MOD_RES 37 37 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 42 42 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 51 51 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 81 81 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 84 84 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 106 106 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 113 113 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 119 119 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 142 142 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 161 161 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 164 164 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 173 173 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 177 177 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 196 196 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. FT MOD_RES 201 201 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2F4I}. SQ SEQUENCE 217 AA; 24716 MW; 83803D45C0100169 CRC64; MKSKLTKRKV ISMIVVFFIL LLIYLSCDVI PIEEMEKGFD PKRYARELWF KLQDMMNEGL GYDAVEVLNT LDENPELAHQ KFAKVVGVSN YRYYIIQGVG EIVEIKDDGI LVKVRENRKV PDLFLSNHIF GNGIVNATGI AKMEDFDRII DFNLTATELN KIVKEEVVNS FLKQLSKGAG SVGSLVRFIA VFTLLKDEEI KYPIEAIPLY LEIQGGF // ID Q9X0M2_THEMA Unreviewed; 284 AA. AC Q9X0M2; G4FEL0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 115. DE SubName: Full=Branched chain amino acid ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36214.1}; DE SubName: Full=Branched-chain amino acid transport ATP-binding protein LivG {ECO:0000313|EMBL:AGL50068.1}; GN OrderedLocusNames=TM_1138 {ECO:0000313|EMBL:AAD36214.1}; GN ORFNames=Tmari_1144 {ECO:0000313|EMBL:AGL50068.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36214.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36214.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36214.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50068.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50068.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36214.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50068.1; -; Genomic_DNA. DR PIR; F72290; F72290. DR RefSeq; NP_228944.1; NC_000853.1. DR RefSeq; WP_004080269.1; NZ_CP011107.1. DR STRING; 243274.TM1138; -. DR EnsemblBacteria; AAD36214; AAD36214; TM_1138. DR EnsemblBacteria; AGL50068; AGL50068; Tmari_1144. DR GeneID; 898626; -. DR KEGG; tma:TM1138; -. DR KEGG; tmi:THEMA_08655; -. DR KEGG; tmm:Tmari_1144; -. DR KEGG; tmw:THMA_1161; -. DR PATRIC; 23937211; VBITheMar51294_1154. DR eggNOG; ENOG4105C0Z; Bacteria. DR eggNOG; COG0411; LUCA. DR KO; K01995; -. DR OMA; TQPRIIM; -. DR OrthoDB; EOG6QK4RR; -. DR BioCyc; TMAR243274:GC6P-1167-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR032823; BCA_ABC_TP_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF12399; BCA_ABC_TP_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD36214.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD36214.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 12 279 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 284 AA; 32266 MW; F53E5F4BC6C3D389 CRC64; MTVTDLSKKP LLLLDHVTMQ FGGLVAVDDF TNEIREGELV GLIGPNGAGK TTVFNVITGI YTPTKGRIVF NDIDITGLRP YQITHLGIAR TFQNIRLFSD MTVLENVLVA QHHVLSNPDA DRILVKHGKP RKGHGRFWFW RAVTKIGYLK KEKEMVERAK DLIKRVGLEK VMYEKASSLP YGEQRKLEIA RALATEPKLI LLDEPAAGMN PKETEDLMEF IKQIRKDFNL TVLLIEHDMK VVMGICERII VMDYGRIIAE GTPKEIQNDP RVIEAYLGRE WESV // ID Q9WYB8_THEMA Unreviewed; 356 AA. AC Q9WYB8; G4FHJ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096}; DE EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096}; DE AltName: Full=Galactose mutarotase {ECO:0000256|PIRNR:PIRNR005096}; GN OrderedLocusNames=TM_0282 {ECO:0000313|EMBL:AAD35370.1}; GN ORFNames=Tmari_0280 {ECO:0000313|EMBL:AGL49206.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35370.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35370.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35370.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49206.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49206.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Converts alpha-aldose to the beta-anomer. CC {ECO:0000256|PIRNR:PIRNR005096}. CC -!- CATALYTIC ACTIVITY: Alpha-D-glucose = beta-D-glucose. CC {ECO:0000256|PIRNR:PIRNR005096}. CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism. CC {ECO:0000256|PIRNR:PIRNR005096}. CC -!- SIMILARITY: Belongs to the aldose epimerase family. CC {ECO:0000256|PIRNR:PIRNR005096}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35370.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49206.1; -; Genomic_DNA. DR PIR; H72395; H72395. DR RefSeq; NP_228094.1; NC_000853.1. DR RefSeq; WP_004082991.1; NZ_CP011107.1. DR STRING; 243274.TM0282; -. DR DNASU; 897200; -. DR EnsemblBacteria; AAD35370; AAD35370; TM_0282. DR EnsemblBacteria; AGL49206; AGL49206; Tmari_0280. DR GeneID; 897200; -. DR KEGG; tma:TM0282; -. DR KEGG; tmi:THEMA_03315; -. DR KEGG; tmm:Tmari_0280; -. DR KEGG; tmw:THMA_0289; -. DR PATRIC; 23935443; VBITheMar51294_0287. DR eggNOG; ENOG4105ENN; Bacteria. DR eggNOG; COG2017; LUCA. DR KO; K01785; -. DR OMA; SPNHPDW; -. DR OrthoDB; EOG69WFM5; -. DR BioCyc; TMAR243274:GC6P-295-MONOMER; -. DR UniPathway; UPA00242; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.70.98.10; -; 1. DR InterPro; IPR015443; Aldose_1-epimerase. DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase. DR InterPro; IPR011013; Gal_mutarotase_SF_dom. DR InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub. DR Pfam; PF01263; Aldose_epim; 1. DR PIRSF; PIRSF005096; GALM; 1. DR SUPFAM; SSF74650; SSF74650; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000256|PIRNR:PIRNR005096}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT ACT_SITE 189 189 Proton donor. FT {ECO:0000256|PIRSR:PIRSR005096-1}. FT ACT_SITE 320 320 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR005096-1}. FT BINDING 257 257 Substrate. FT {ECO:0000256|PIRSR:PIRSR005096-2}. SQ SEQUENCE 356 AA; 39850 MW; F0EEE17F0A28A6EC CRC64; MEYLMSHIEK EFFGATSEGI PVYQYTLINK NGMMAKIITY GAIVRELWVP DSSGTLSDVV LGFDTLQEYE AKNSNFFFGA IVGRYANRIA GGRFEIDGVT YQLALNDGDR PNALHGGVKG FYTRVFKAVP MKTPTGPFLV LKYLSHDGEE GYPGNLDLTV IYTLTNENEL KVEYRATTDK PTVVNLTQHS YFNLSGEGTI LDHELKINAD SYTPVDDNLI PTGEIAPVEG TPFDLRSFKV LRDAIEPLKS TTTKGFDINY VLNGEDGKLK LAAVLRDKRS RRRMEVYTTE PGLQLYTGNF LDVKGKCGTY YGPYSGLCLE AQHFPDSPNH ANFPSTILRP GEEYRQVTVY RFSVEV // ID Q9WYW5_THEMA Unreviewed; 418 AA. AC Q9WYW5; G4FDX5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=PhoH-related protein {ECO:0000313|EMBL:AAD35580.1}; DE SubName: Full=Putative ATPase related to phosphate starvation-inducible protein PhoH {ECO:0000313|EMBL:AGL49417.1}; GN OrderedLocusNames=TM_0495 {ECO:0000313|EMBL:AAD35580.1}; GN ORFNames=Tmari_0492 {ECO:0000313|EMBL:AGL49417.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35580.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35580.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35580.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49417.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49417.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35580.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49417.1; -; Genomic_DNA. DR PIR; F72370; F72370. DR RefSeq; NP_228305.1; NC_000853.1. DR RefSeq; WP_004081454.1; NZ_CP011107.1. DR STRING; 243274.TM0495; -. DR EnsemblBacteria; AAD35580; AAD35580; TM_0495. DR EnsemblBacteria; AGL49417; AGL49417; Tmari_0492. DR GeneID; 897536; -. DR KEGG; tma:TM0495; -. DR KEGG; tmi:THEMA_02195; -. DR KEGG; tmm:Tmari_0492; -. DR KEGG; tmw:THMA_0508; -. DR PATRIC; 23935895; VBITheMar51294_0502. DR eggNOG; ENOG4108IAB; Bacteria. DR eggNOG; COG1875; LUCA. DR KO; K07175; -. DR OMA; LRVELNH; -. DR OrthoDB; EOG6ZKXN6; -. DR BioCyc; TMAR243274:GC6P-519-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 3.40.50.1010; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003714; PhoH. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR Pfam; PF02562; PhoH; 1. DR Pfam; PF13638; PIN_4; 1. DR SMART; SM00670; PINc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF88723; SSF88723; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 130 PINc. {ECO:0000259|SMART:SM00670}. SQ SEQUENCE 418 AA; 47519 MW; A42EB74F86D7C8FB CRC64; MVKNYVLDTN VLIHDPDSIF SFEDNNVIIP LPVLEELDKL KREHGSVGKN AREVIRHLDE LRKKGNLRKG IPLENGGILR VMVLEREVEN VPRFLHERYV DNIILAYVIE LMNREKIPTI LVSKDINLRV KADSLGIPAQ DYLTDRSELE TMPKGYVEID DEELKKQLKV KVTVEKKLDL LDNFYIDLGG VYGKYRKGKV LRVEPFETMG ISPRNREQIF SMDALLDDEI PLVFLVGIAG TGKTLLALAC GLYKVLVEKR YKKLIVTRPT VPMGRDIGYL PGELEKKMKP WLQPIMDNLE LISSLSGLKI KELEKQEILE VEAISFIRGR SIPKQFIIID EAQNLTPHEV KTILTRVGED TKIVLVGDPY QIDTPYLDKD TNGLVYAALK LLESDLSAVI KLEKGERSRL ATIAAELL // ID Q9X1Y0_THEMA Unreviewed; 218 AA. AC Q9X1Y0; G4FG36; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36714.1}; GN OrderedLocusNames=TM_1647 {ECO:0000313|EMBL:AAD36714.1}; GN ORFNames=Tmari_1656 {ECO:0000313|EMBL:AGL50580.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36714.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36714.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36714.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50580.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50580.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36714.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50580.1; -; Genomic_DNA. DR PIR; D72227; D72227. DR RefSeq; NP_229447.1; NC_000853.1. DR RefSeq; WP_004082147.1; NZ_CP011107.1. DR STRING; 243274.TM1647; -. DR EnsemblBacteria; AAD36714; AAD36714; TM_1647. DR EnsemblBacteria; AGL50580; AGL50580; Tmari_1656. DR GeneID; 896893; -. DR KEGG; tma:TM1647; -. DR KEGG; tmi:THEMA_06010; -. DR KEGG; tmm:Tmari_1656; -. DR KEGG; tmw:THMA_1688; -. DR PATRIC; 23938268; VBITheMar51294_1666. DR eggNOG; ENOG4106ES5; Bacteria. DR eggNOG; ENOG410Y2GA; LUCA. DR OMA; SYFVRID; -. DR OrthoDB; EOG6QZMSP; -. DR BioCyc; TMAR243274:GC6P-1693-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 218 AA; 25741 MW; A0AD6AB71B36DCEE CRC64; MKRSSKIVLV IVLIAVALSA VLFLYYRSFL TSPDYKAAEV HYLFRVGDNS YFVRIDDSKR MVFVVSFPKE SFDPERRETI ISERPLSDLE KMENLLDVKA ERAFYSVMSE EEFLKLCQDL LGKQCESFSN FVKEFSKRKL KFFDFLFVGS WLKKFGFNNL NRFSLYKFFE KISNYAVDVF EAPTVTEKPI VIEVQGKKYE RLYLDSEKLK AISEEMKR // ID Q9X022_THEMA Unreviewed; 359 AA. AC Q9X022; G4FF70; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=Alcohol dehydrogenase, iron-containing {ECO:0000313|EMBL:AAD36001.1}; GN OrderedLocusNames=TM_0920 {ECO:0000313|EMBL:AAD36001.1}; GN ORFNames=Tmari_0922 {ECO:0000313|EMBL:AGL49847.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36001.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36001.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36001.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49847.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49847.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36001.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49847.1; -; Genomic_DNA. DR PIR; A72317; A72317. DR RefSeq; NP_228728.1; NC_000853.1. DR RefSeq; WP_004080642.1; NZ_CP011107.1. DR PDB; 1O2D; X-ray; 1.30 A; A/B=2-359. DR PDB; 1VHD; X-ray; 1.60 A; A/B=2-359. DR PDBsum; 1O2D; -. DR PDBsum; 1VHD; -. DR STRING; 243274.TM0920; -. DR EnsemblBacteria; AAD36001; AAD36001; TM_0920. DR EnsemblBacteria; AGL49847; AGL49847; Tmari_0922. DR GeneID; 898594; -. DR KEGG; tma:TM0920; -. DR KEGG; tmi:THEMA_00035; -. DR KEGG; tmm:Tmari_0922; -. DR KEGG; tmw:THMA_0942; -. DR PATRIC; 23936771; VBITheMar51294_0934. DR eggNOG; ENOG4105C0A; Bacteria. DR eggNOG; COG1454; LUCA. DR KO; K00001; -. DR OMA; EKFAWIS; -. DR OrthoDB; EOG686NDV; -. DR BioCyc; TMAR243274:GC6P-950-MONOMER; -. DR BRENDA; 1.1.1.202; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR InterPro; IPR001670; ADH_Fe. DR Pfam; PF00465; Fe-ADH; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O2D, ECO:0000213|PDB:1VHD}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000213|PDB:1O2D}; KW Metal-binding {ECO:0000213|PDB:1O2D, ECO:0000213|PDB:1VHD}; KW NADP {ECO:0000213|PDB:1O2D, ECO:0000213|PDB:1VHD}; KW Nucleotide-binding {ECO:0000213|PDB:1O2D, ECO:0000213|PDB:1VHD}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000213|PDB:1VHD}. FT DOMAIN 7 349 Fe-ADH. {ECO:0000259|Pfam:PF00465}. FT NP_BIND 38 39 NADP. {ECO:0000213|PDB:1O2D, FT ECO:0000213|PDB:1VHD}. FT NP_BIND 68 69 NADP. {ECO:0000213|PDB:1VHD}. FT NP_BIND 96 100 NADP. {ECO:0000213|PDB:1O2D, FT ECO:0000213|PDB:1VHD}. FT NP_BIND 136 137 NADP. {ECO:0000213|PDB:1O2D, FT ECO:0000213|PDB:1VHD}. FT NP_BIND 142 147 NADP. {ECO:0000213|PDB:1O2D, FT ECO:0000213|PDB:1VHD}. FT NP_BIND 174 177 NADP. {ECO:0000213|PDB:1O2D, FT ECO:0000213|PDB:1VHD}. FT METAL 189 189 Iron. {ECO:0000213|PDB:1O2D}. FT METAL 189 189 Zinc. {ECO:0000213|PDB:1VHD}. FT METAL 193 193 Iron; via tele nitrogen. FT {ECO:0000213|PDB:1O2D}. FT METAL 193 193 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:1VHD}. FT METAL 256 256 Iron; via tele nitrogen. FT {ECO:0000213|PDB:1O2D}. FT METAL 256 256 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:1VHD}. FT METAL 270 270 Iron; via tele nitrogen. FT {ECO:0000213|PDB:1O2D}. FT METAL 270 270 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:1VHD}. FT BINDING 43 43 NADP. {ECO:0000213|PDB:1VHD}. FT BINDING 157 157 NADP. {ECO:0000213|PDB:1O2D, FT ECO:0000213|PDB:1VHD}. SQ SEQUENCE 359 AA; 39943 MW; 97871CB8584C70B1 CRC64; MWEFYMPTDV FFGEKILEKR GNIIDLLGKR ALVVTGKSSS KKNGSLDDLK KLLDETEISY EIFDEVEENP SFDNVMKAVE RYRNDSFDFV VGLGGGSPMD FAKAVAVLLK EKDLSVEDLY DREKVKHWLP VVEIPTTAGT GSEVTPYSIL TDPEGNKRGC TLMFPVYAFL DPRYTYSMSD ELTLSTGVDA LSHAVEGYLS RKSTPPSDAL AIEAMKIIHR NLPKAIEGNR EARKKMFVAS CLAGMVIAQT GTTLAHALGY PLTTEKGIKH GKATGMVLPF VMEVMKEEIP EKVDTVNHIF GGSLLKFLKE LGLYEKVAVS SEELEKWVEK GSRAKHLKNT PGTFTPEKIR NIYREALGV // ID Q9WYV4_THEMA Unreviewed; 316 AA. AC Q9WYV4; G4FDY6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Hydroxymethylpyrimidine ABC transporter, substrate-binding component {ECO:0000313|EMBL:AGL49406.1}; DE SubName: Full=Pyrimidine biosynthesis enzyme, putative {ECO:0000313|EMBL:AAD35569.1}; GN OrderedLocusNames=TM_0484 {ECO:0000313|EMBL:AAD35569.1}; GN ORFNames=Tmari_0481 {ECO:0000313|EMBL:AGL49406.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35569.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35569.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35569.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49406.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49406.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35569.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49406.1; -; Genomic_DNA. DR PIR; C72369; C72369. DR RefSeq; NP_228294.1; NC_000853.1. DR RefSeq; WP_004081482.1; NZ_CP011107.1. DR STRING; 243274.TM0484; -. DR EnsemblBacteria; AAD35569; AAD35569; TM_0484. DR EnsemblBacteria; AGL49406; AGL49406; Tmari_0481. DR GeneID; 897523; -. DR KEGG; tma:TM0484; -. DR KEGG; tmi:THEMA_02250; -. DR KEGG; tmm:Tmari_0481; -. DR KEGG; tmw:THMA_0497; -. DR PATRIC; 23935873; VBITheMar51294_0491. DR eggNOG; ENOG4105ET9; Bacteria. DR eggNOG; COG0715; LUCA. DR OMA; GKTYGGW; -. DR OrthoDB; EOG6CZQPK; -. DR BioCyc; TMAR243274:GC6P-508-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR InterPro; IPR027939; NMT1/THI5. DR InterPro; IPR015168; SsuA/THI5. DR PANTHER; PTHR31528; PTHR31528; 1. DR Pfam; PF09084; NMT1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 31 245 NMT1. {ECO:0000259|Pfam:PF09084}. SQ SEQUENCE 316 AA; 36134 MW; E44633CFBD568F13 CRC64; MKRLIFIAMF LISVLALFAE EVTVVLDWYP NTNHTGLYVA KDLGFYREEG LDVKIVQPSR LTAEQLVASG KAEFGVSYQE AVTLSRGEGM PIVSIAAIIQ HNTSGFAWLK DEGIKSVKDW EGKRYGSWGS PIEKATIEYI MRKYGADPSK VIFVNVGQMD FFAGTLNDVF DFAWIFYGWD GVASKVKGIE IEFLPLKDID EVFDYYTPVL ITSESLMKQK PDLVRRFLRA TAKGYEYAIQ HPVEAAKILL KYAPELDEKI VVESQKYLAG QYKADAEKWG YQKEEVWRRY AEWLHSMGFL KEMIDVTKAF TNEFLP // ID Q9X031_THEMA Unreviewed; 389 AA. AC Q9X031; G4FF57; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36014.1}; GN OrderedLocusNames=TM_0933 {ECO:0000313|EMBL:AAD36014.1}; GN ORFNames=Tmari_0935 {ECO:0000313|EMBL:AGL49860.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36014.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36014.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36014.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49860.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49860.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36014.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49860.1; -; Genomic_DNA. DR PIR; E72315; E72315. DR RefSeq; NP_228741.1; NC_000853.1. DR RefSeq; WP_004080629.1; NZ_CP011107.1. DR STRING; 243274.TM0933; -. DR EnsemblBacteria; AAD36014; AAD36014; TM_0933. DR EnsemblBacteria; AGL49860; AGL49860; Tmari_0935. DR GeneID; 898607; -. DR KEGG; tma:TM0933; -. DR KEGG; tmi:THEMA_09685; -. DR KEGG; tmm:Tmari_0935; -. DR KEGG; tmw:THMA_0955; -. DR PATRIC; 23936797; VBITheMar51294_0947. DR eggNOG; ENOG41089B4; Bacteria. DR eggNOG; ENOG41121ZU; LUCA. DR OMA; WLDENTM; -. DR OrthoDB; EOG6SV55G; -. DR BioCyc; TMAR243274:GC6P-963-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.130.10.10; -; 1. DR InterPro; IPR011659; PD40. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR Pfam; PF07676; PD40; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 389 AA; 45019 MW; 58B68831BC86036C CRC64; MKKMFLFIFA IIPLVSFSVV TLDLSMFSTE EASSVLADVQ EKILEFLPKE ATITNSSTAT FSMTFFLSYN ATDNLYVGEW KHGNEVARYE YNPRGYKYYR DFVMECASFP LEKVSFYLFS KNEFPDAFRL TYHPALDEYS DFSSEYFVFS SERLSGNRNL FLIDRKNGDL LSLPVYGSSE YFPRISLDQK YLLFQGSLHG NWGIYYMPIS KDYSSKIKLI SRGRFAAYNP NWLDENTMVY VQEDATSNHL VVKDLVTMRE KTYDLPFDWV FTPAKGNQGI VFVGLKESNF GIYELLPDGT VTVLENSPYN EFDPDVFGNY LIFSSNRDGV FRIYAKDLES GKVWCLTEKI PYDAFYPAFS EDGKLVAFSV YEKGSEPDIW IVRFRVPQD // ID Q9X126_THEMA Unreviewed; 79 AA. AC Q9X126; G4FE49; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36374.1}; GN OrderedLocusNames=TM_1300 {ECO:0000313|EMBL:AAD36374.1}; GN ORFNames=Tmari_1307 {ECO:0000313|EMBL:AGL50231.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36374.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36374.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36374.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50231.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50231.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36374.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50231.1; -; Genomic_DNA. DR PIR; F72269; F72269. DR RefSeq; NP_229104.1; NC_000853.1. DR RefSeq; WP_004079921.1; NZ_CP011107.1. DR STRING; 243274.TM1300; -. DR EnsemblBacteria; AAD36374; AAD36374; TM_1300. DR EnsemblBacteria; AGL50231; AGL50231; Tmari_1307. DR GeneID; 898182; -. DR KEGG; tma:TM1300; -. DR KEGG; tmi:THEMA_07840; -. DR KEGG; tmm:Tmari_1307; -. DR KEGG; tmw:THMA_1325; -. DR PATRIC; 23937540; VBITheMar51294_1316. DR OrthoDB; EOG6H4KDS; -. DR BioCyc; TMAR243274:GC6P-1331-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 79 AA; 8993 MW; 7C50D7AF97EAF36B CRC64; MKIVRRIILT IVILLSLLYT LVFPSPSDDY QTTVRKKTVV HTLLLEKSHS EDLTAGNQIL RFNKSLARLL ISNERGDKG // ID Q9WXP4_THEMA Unreviewed; 416 AA. AC Q9WXP4; G4FGV4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=HDIG domain protein {ECO:0000313|EMBL:AGL48960.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35131.1}; GN OrderedLocusNames=TM_0037 {ECO:0000313|EMBL:AAD35131.1}; GN ORFNames=Tmari_0034 {ECO:0000313|EMBL:AGL48960.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35131.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35131.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35131.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48960.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48960.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35131.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48960.1; -; Genomic_DNA. DR PIR; B72425; B72425. DR RefSeq; NP_227853.1; NC_000853.1. DR RefSeq; WP_004082500.1; NZ_CP011107.1. DR STRING; 243274.TM0037; -. DR EnsemblBacteria; AAD35131; AAD35131; TM_0037. DR EnsemblBacteria; AGL48960; AGL48960; Tmari_0034. DR GeneID; 896860; -. DR KEGG; tma:TM0037; -. DR KEGG; tmi:THEMA_04615; -. DR KEGG; tmm:Tmari_0034; -. DR KEGG; tmw:THMA_0033; -. DR PATRIC; 23934914; VBITheMar51294_0035. DR eggNOG; ENOG4105DHT; Bacteria. DR eggNOG; COG2206; LUCA. DR OMA; IDFMSSI; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-37-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.3210.10; -; 2. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR006675; HDIG_dom. DR Pfam; PF01966; HD; 2. DR SMART; SM00471; HDc; 2. DR TIGRFAMs; TIGR00277; HDIG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 11 143 HDc. {ECO:0000259|SMART:SM00471}. FT DOMAIN 220 351 HDc. {ECO:0000259|SMART:SM00471}. SQ SEQUENCE 416 AA; 48010 MW; 80E8B573C500C249 CRC64; MIQMFINLLE TIPSLGRHSF QVAFLSAQIA EKMNLDPNVS FLSGLIHDLG LILPYEGKTL LDEIDDTFVI VRDTPGKPLH LHSILGSFIT DYVEKLKPIS PIVLKHHFPA SYLDKTEENL ISNIVFISDQ VSRYTMINLD VSPRDILIAL EDMKSFFFPE VFEACREVLN TEFVQWQLEN ILAGYDVTDL LDHHVRNCPD CDKKDLIQIG KIVSFIVDTK SEFTTSHTWR VAVFSEKMAE KAGRNSEDLF IAGLYHDIGK ISVSYKILEK PAKLSDEEYA IMKKHVYFSY LILLPYKDEN WFLPAVRHHE RLDGYGYPFR LKGEEMTLED KIIQVADVFS ALLEERPYRP ANTVEKALSM VREEVKKKKL SQEAFELLES SLEDFDLSSI EVGREIRKEI RTFVNRVVEK FGDYVL // ID Q9X238_THEMA Unreviewed; 191 AA. AC Q9X238; G4FGA0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Proline dipeptidase, putative {ECO:0000313|EMBL:AAD36779.1}; DE SubName: Full=Protein co-occurring with transport systems {ECO:0000313|EMBL:AGL50645.1}; GN OrderedLocusNames=TM_1713 {ECO:0000313|EMBL:AAD36779.1}; GN ORFNames=Tmari_1721 {ECO:0000313|EMBL:AGL50645.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36779.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36779.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36779.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50645.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50645.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36779.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50645.1; -; Genomic_DNA. DR PIR; B72222; B72222. DR RefSeq; NP_229512.1; NC_000853.1. DR RefSeq; WP_004082229.1; NZ_CP011107.1. DR STRING; 243274.TM1713; -. DR EnsemblBacteria; AAD36779; AAD36779; TM_1713. DR EnsemblBacteria; AGL50645; AGL50645; Tmari_1721. DR GeneID; 897882; -. DR KEGG; tma:TM1713; -. DR KEGG; tmi:THEMA_05675; -. DR KEGG; tmm:Tmari_1721; -. DR KEGG; tmw:THMA_1755; -. DR PATRIC; 23938402; VBITheMar51294_1731. DR eggNOG; ENOG4108ZK7; Bacteria. DR eggNOG; COG1739; LUCA. DR KO; K01271; -. DR OMA; HLITSKH; -. DR OrthoDB; EOG6N685N; -. DR BioCyc; TMAR243274:GC6P-1761-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.30.230.30; -; 1. DR InterPro; IPR023582; Impact. DR InterPro; IPR001498; Impact_N. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR020569; UPF0029_Impact_CS. DR PANTHER; PTHR16301; PTHR16301; 1. DR Pfam; PF01205; UPF0029; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR PROSITE; PS00910; UPF0029; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 17 120 UPF0029. {ECO:0000259|Pfam:PF01205}. SQ SEQUENCE 191 AA; 21856 MW; B704E31FCDC4741D CRC64; MEWKTVVKPH TERINVKRSE FYATIFPVKD EKDFREKLKE VSKRDATHNC WAYRIFSPNG ILEHSSDDGE PSGTAGRPIL GALKKYDLMN TAIVVTRYFG GVKLGVRGLI EAYSSAAEMA VKGAELRKLR LMKEFEVEVD YQELNNVFRV VEMMGLELVE MDYTERGAKI LLRGLEVPEN LVIKTIRDVL I // ID Q9WZL4_THEMA Unreviewed; 398 AA. AC Q9WZL4; G4FD68; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 107. DE SubName: Full=Flavoprotein {ECO:0000313|EMBL:AGL49681.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35837.1}; GN OrderedLocusNames=TM_0755 {ECO:0000313|EMBL:AAD35837.1}; GN ORFNames=Tmari_0756 {ECO:0000313|EMBL:AGL49681.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35837.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35837.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35837.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49681.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49681.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35837.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49681.1; -; Genomic_DNA. DR PIR; A72338; A72338. DR RefSeq; NP_228564.1; NC_000853.1. DR RefSeq; WP_004080952.1; NZ_CP011107.1. DR PDB; 1VME; X-ray; 1.80 A; A/B=1-398. DR PDB; 4DIK; X-ray; 1.75 A; A/B=1-398. DR PDB; 4DIL; X-ray; 2.00 A; A/B=1-398. DR PDBsum; 1VME; -. DR PDBsum; 4DIK; -. DR PDBsum; 4DIL; -. DR STRING; 243274.TM0755; -. DR EnsemblBacteria; AAD35837; AAD35837; TM_0755. DR EnsemblBacteria; AGL49681; AGL49681; Tmari_0756. DR GeneID; 898423; -. DR KEGG; tma:TM0755; -. DR KEGG; tmi:THEMA_00875; -. DR KEGG; tmm:Tmari_0756; -. DR KEGG; tmw:THMA_0774; -. DR PATRIC; 23936432; VBITheMar51294_0768. DR eggNOG; ENOG4105CNW; Bacteria. DR eggNOG; COG0426; LUCA. DR OMA; GANEHRL; -. DR OrthoDB; EOG6JMMV0; -. DR BioCyc; TMAR243274:GC6P-782-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR016440; Rubredoxin-O_OxRdtase. DR Pfam; PF00258; Flavodoxin_1; 1. DR PIRSF; PIRSF005243; ROO; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF52218; SSF52218; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VME, ECO:0000213|PDB:4DIK, KW ECO:0000213|PDB:4DIL}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000213|PDB:1VME, ECO:0000213|PDB:4DIK, KW ECO:0000213|PDB:4DIL}; KW Metal-binding {ECO:0000213|PDB:1VME, ECO:0000213|PDB:4DIK, KW ECO:0000213|PDB:4DIL}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 256 398 Flavodoxin-like. FT {ECO:0000259|PROSITE:PS50902}. FT METAL 85 85 Iron oxide (2Fe-O); via tele nitrogen. FT {ECO:0000213|PDB:1VME, FT ECO:0000213|PDB:4DIK, FT ECO:0000213|PDB:4DIL}. FT METAL 87 87 Iron oxide (2Fe-O). FT {ECO:0000213|PDB:1VME, FT ECO:0000213|PDB:4DIK, FT ECO:0000213|PDB:4DIL}. FT METAL 89 89 Iron oxide (2Fe-O). FT {ECO:0000213|PDB:1VME, FT ECO:0000213|PDB:4DIK, FT ECO:0000213|PDB:4DIL}. FT METAL 90 90 Iron oxide (2Fe-O); via tele nitrogen. FT {ECO:0000213|PDB:1VME}. FT METAL 151 151 Iron oxide (2Fe-O); via tele nitrogen. FT {ECO:0000213|PDB:1VME, FT ECO:0000213|PDB:4DIK, FT ECO:0000213|PDB:4DIL}. FT METAL 168 168 Iron oxide (2Fe-O). FT {ECO:0000213|PDB:1VME, FT ECO:0000213|PDB:4DIK, FT ECO:0000213|PDB:4DIL}. FT METAL 228 228 Iron oxide (2Fe-O); via tele nitrogen. FT {ECO:0000213|PDB:1VME, FT ECO:0000213|PDB:4DIK, FT ECO:0000213|PDB:4DIL}. SQ SEQUENCE 398 AA; 45271 MW; 78688C3E78771719 CRC64; MPKIWTERIF DDPEIYVLRI DDDRIRYFEA VWEIPEGISY NAYLVKLNGA NVLIDGWKGN YAKEFIDALS KIVDPKEITH IIVNHTEPDH SGSLPATLKT IGHDVEIIAS NFGKRLLEGF YGIKDVTVVK DGEEREIGGK KFKFVMTPWL HWPDTMVTYL DGILFSCDVG GGYLLPEILD DSNESVVERY LPHVTKYIVT VIGHYKNYIL EGAEKLSSLK IKALLPGHGL IWKKDPQRLL NHYVSVAKGD PKKGKVTVIY DSMYGFVENV MKKAIDSLKE KGFTPVVYKF SDEERPAISE ILKDIPDSEA LIFGVSTYEA EIHPLMRFTL LEIIDKANYE KPVLVFGVHG WAPSAERTAG ELLKETKFRI LSFTEIKGSN MDERKIEEAI SLLKKELE // ID Q9X151_THEMA Unreviewed; 571 AA. AC Q9X151; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 114. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36400.1}; GN OrderedLocusNames=TM_1328 {ECO:0000313|EMBL:AAD36400.1}; GN ORFNames=Tmari_1335 {ECO:0000313|EMBL:AGL50259.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36400.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36400.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36400.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50259.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50259.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36400.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50259.1; -; Genomic_DNA. DR PIR; D72267; D72267. DR RefSeq; NP_229130.1; NC_000853.1. DR RefSeq; WP_010865314.1; NZ_CP011107.1. DR STRING; 243274.TM1328; -. DR EnsemblBacteria; AAD36400; AAD36400; TM_1328. DR EnsemblBacteria; AGL50259; AGL50259; Tmari_1335. DR GeneID; 898154; -. DR KEGG; tma:TM1328; -. DR KEGG; tmi:THEMA_07705; -. DR KEGG; tmm:Tmari_1335; -. DR KEGG; tmw:THMA_1352; -. DR PATRIC; 23937593; VBITheMar51294_1342. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K06148; -. DR OMA; QNSERRG; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1359-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0034040; F:lipid-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0006869; P:lipid transport; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD36400.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD36400.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 23 41 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 159 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 165 183 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 273 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 37 308 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 338 567 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 571 AA; 65400 MW; 5D85530D556DBFDF CRC64; MKFFSASNVR DDIKKFERKY KRYYPIFLLL ESLFLTTNVL TPLLIKKTID SAFYRGSVEE VALFSILYFV VLVSQSFIMY RLNFSVAKHL LNASRAKESK GVYAKILTLP LSFLNSKNTG DYLSIFMRDI PKVASGVYLA RLQFFFNLGF FLVVLSLLFI LNVKLALVVL ASIVLFFVST SILKKMVIRT SQRDQEAYQR FLKRSREVVE GTPVLKQFSG LLFLRDFLDS SAREWSRASI IHSTVNELSN RNIEMNRWVG STIVLAFGVY LLWKGEISVG TLLAFESYMN WIYDIVRMAL TGLTTFFSTV PNWENFTRVF SLPFERASGI DLERFEKLQL KNVHFKYDET PVLTGLNFEI NSGDKIAIVA RSGAGKSTLV SLFNRLLSPT EGEILINGVP IEQYSLQSLR RNIVLVRSND ILFDTTIKNN ITLFEDFPED EIENVLKMCE CDFVKELENG IDTVVGERGT RLSDGQRQRI VLARALIRKP QVLILDEVTS GVDSETEEKI LEKILNEIET VIIVSHRLST IKKASRIIVL NDGRVEAEGT HEELMKKSPL YREIVKSQLM R // ID Q9X181_THEMA Unreviewed; 116 AA. AC Q9X181; G4FF96; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 111. DE SubName: Full=Response regulator {ECO:0000313|EMBL:AAD36430.1}; GN OrderedLocusNames=TM_1360 {ECO:0000313|EMBL:AAD36430.1}; GN ORFNames=Tmari_1367 {ECO:0000313|EMBL:AGL50291.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36430.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36430.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36430.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50291.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50291.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36430.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50291.1; -; Genomic_DNA. DR PIR; A72263; A72263. DR RefSeq; NP_229161.1; NC_000853.1. DR RefSeq; WP_004081556.1; NZ_CP011107.1. DR PDB; 3A0R; X-ray; 3.80 A; B=1-116. DR PDB; 3A0U; X-ray; 1.66 A; A=1-116. DR PDB; 3A10; X-ray; 1.63 A; A=1-116. DR PDBsum; 3A0R; -. DR PDBsum; 3A0U; -. DR PDBsum; 3A10; -. DR DIP; DIP-48291N; -. DR STRING; 243274.TM1360; -. DR EnsemblBacteria; AAD36430; AAD36430; TM_1360. DR EnsemblBacteria; AGL50291; AGL50291; Tmari_1367. DR GeneID; 898120; -. DR KEGG; tma:TM1360; -. DR KEGG; tmi:THEMA_07540; -. DR KEGG; tmm:Tmari_1367; -. DR KEGG; tmw:THMA_1385; -. DR PATRIC; 23937658; VBITheMar51294_1372. DR eggNOG; ENOG4105X4N; Bacteria. DR eggNOG; COG0784; LUCA. DR KO; K02485; -. DR OMA; NKKVDDC; -. DR OrthoDB; EOG6WHNMG; -. DR BioCyc; TMAR243274:GC6P-1393-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR Pfam; PF00072; Response_reg; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3A0R, ECO:0000213|PDB:3A0U, KW ECO:0000213|PDB:3A10}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Magnesium {ECO:0000213|PDB:3A0U, ECO:0000213|PDB:3A10}; KW Metal-binding {ECO:0000213|PDB:3A0U, ECO:0000213|PDB:3A10}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 115 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT METAL 9 9 Magnesium. {ECO:0000213|PDB:3A0U, FT ECO:0000213|PDB:3A10}. FT METAL 52 52 Magnesium. {ECO:0000213|PDB:3A0U, FT ECO:0000213|PDB:3A10}. FT METAL 54 54 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:3A0U, FT ECO:0000213|PDB:3A10}. SQ SEQUENCE 116 AA; 13343 MW; 145302A42E89EB78 CRC64; MKRILVVDDE PNIRELLKEE LQEEGYEIDT AENGEEALKK FFSGNYDLVI LDIEMPGISG LEVAGEIRKK KKDAKIILLT AYSHYRSDLS SWAADEYVVK SFNFDELKEK VKKLLS // ID Q9WXN1_THEMA Unreviewed; 642 AA. AC Q9WXN1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 104. DE SubName: Full=Laminarinase {ECO:0000313|EMBL:AAD35118.1}; DE EC=3.2.1.39 {ECO:0000313|EMBL:AGL48947.1}; GN OrderedLocusNames=TM_0024 {ECO:0000313|EMBL:AAD35118.1}; GN ORFNames=Tmari_0021 {ECO:0000313|EMBL:AGL48947.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35118.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35118.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35118.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48947.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48947.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35118.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48947.1; -; Genomic_DNA. DR PIR; B72428; B72428. DR RefSeq; NP_227840.1; NC_000853.1. DR RefSeq; WP_010865031.1; NZ_CP011107.1. DR PDB; 1GUI; X-ray; 1.90 A; A=489-642. DR PDB; 3AZX; X-ray; 1.80 A; A/B=204-466. DR PDB; 3AZY; X-ray; 1.65 A; A/B/C/D=204-466. DR PDB; 3AZZ; X-ray; 1.81 A; A/B/C/D=204-466. DR PDB; 3B00; X-ray; 1.74 A; A/B/C/D=204-466. DR PDB; 3B01; X-ray; 1.87 A; A/B/C/D=204-466. DR PDBsum; 1GUI; -. DR PDBsum; 3AZX; -. DR PDBsum; 3AZY; -. DR PDBsum; 3AZZ; -. DR PDBsum; 3B00; -. DR PDBsum; 3B01; -. DR STRING; 243274.TM0024; -. DR CAZy; CBM4; Carbohydrate-Binding Module Family 4. DR CAZy; GH16; Glycoside Hydrolase Family 16. DR EnsemblBacteria; AAD35118; AAD35118; TM_0024. DR EnsemblBacteria; AGL48947; AGL48947; Tmari_0021. DR GeneID; 896840; -. DR KEGG; tma:TM0024; -. DR KEGG; tmm:Tmari_0021; -. DR KEGG; tmw:THMA_0020; -. DR PATRIC; 23934888; VBITheMar51294_0022. DR eggNOG; ENOG4105FBU; Bacteria. DR eggNOG; COG2273; LUCA. DR OMA; ARFEFQL; -. DR BioCyc; TMAR243274:GC6P-24-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.60.120.260; -; 2. DR InterPro; IPR003305; CenC_carb-bd. DR InterPro; IPR013320; ConA-like_dom. DR InterPro; IPR008979; Galactose-bd-like. DR InterPro; IPR000757; GH16. DR Pfam; PF02018; CBM_4_9; 2. DR Pfam; PF00722; Glyco_hydro_16; 1. DR SUPFAM; SSF49785; SSF49785; 2. DR SUPFAM; SSF49899; SSF49899; 1. DR PROSITE; PS51762; GH16_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1GUI, ECO:0000213|PDB:3AZX, KW ECO:0000213|PDB:3AZY, ECO:0000213|PDB:3AZZ}; KW Calcium {ECO:0000213|PDB:1GUI, ECO:0000213|PDB:3AZX, KW ECO:0000213|PDB:3AZY, ECO:0000213|PDB:3AZZ}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000313|EMBL:AGL48947.1}; KW Hydrolase {ECO:0000313|EMBL:AGL48947.1}; KW Metal-binding {ECO:0000213|PDB:1GUI, ECO:0000213|PDB:3AZX, KW ECO:0000213|PDB:3AZY, ECO:0000213|PDB:3AZZ}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 210 461 GH16 (glycosyl hydrolase family 16). FT {ECO:0000259|PROSITE:PS51762}. FT METAL 219 219 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:3AZX, FT ECO:0000213|PDB:3AZY, FT ECO:0000213|PDB:3AZZ}. FT METAL 221 221 Calcium 1. {ECO:0000213|PDB:3AZX, FT ECO:0000213|PDB:3AZY, FT ECO:0000213|PDB:3AZZ}. FT METAL 263 263 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:3AZX, FT ECO:0000213|PDB:3AZY, FT ECO:0000213|PDB:3AZZ}. FT METAL 451 451 Calcium 1. {ECO:0000213|PDB:3AZX, FT ECO:0000213|PDB:3AZY, FT ECO:0000213|PDB:3AZZ}. FT METAL 493 493 Calcium 2; via carbonyl oxygen. FT {ECO:0000213|PDB:1GUI}. FT METAL 532 532 Calcium 2; via carbonyl oxygen. FT {ECO:0000213|PDB:1GUI}. FT METAL 635 635 Calcium 2. {ECO:0000213|PDB:1GUI}. SQ SEQUENCE 642 AA; 72540 MW; 6431C9825597BF7E CRC64; MMSRLVFALL LFPVFILAQN ILGNASFDEP ILIAGVDIDP PAEDGSIDTG GNWVFFTNSN GEGTARVENG VLVVEITNGG DHTWSVQIIQ APIRVEKLHK YRVSFRAKAS SQKNIGVKIG GTAGRGWTAY NPGTDESGGM VFELGTDWQK YEFEFVMRQE TDENARFEFQ LGRYTGTVWI DDVVMEDIGV LEVSGEENEI YTEEDEDKVE DWQLVWSQEF DDGVIDPNIW NFEIGNGHAK GIPGWGNGEL EYYTDENAFV ENGCLVIEAR KEQVSDEYGT YDYTSARMTT EGKFEIKYGK IEIRAKLPKG KGIWPALWML GNNIGEVGWP TCGEIDIMEM LGHDTRTVYG TAHGPGYSGG ASIGVAYHLP EGVPDFSEDF HIFSIEWDED EVEWYVDGQL YHVLSKDELA ELGLEWVFDH PFFLILNVAV GGYWPGYPDE TTQFPQRMYI DYIRVYKDMN PETITGEVDD CEYEQAQQQA GPEVTYEQIN NGTFDEPIVN DQANNPDEWF IWQAGDYGIS GARVSDYGVR DGYAYITIAD PGTDTWHIQF NQWIGLYRGK TYTISFKAKA DTPRPINVKI LQNHDPWTNY FAQTVNLTAD WQTFTFTYTH PDDADEVVQI SFELGEGTAT TIYFDDVTVS PQ // ID Q9WYQ9_THEMA Unreviewed; 435 AA. AC Q9WYQ9; G4FHY7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=2,4-dienoyl-CoA reductase [NADPH] {ECO:0000313|EMBL:AGL49350.1}; DE EC=1.3.1.34 {ECO:0000313|EMBL:AGL49350.1}; DE SubName: Full=Oxidoreductase, putative {ECO:0000313|EMBL:AAD35513.1}; GN OrderedLocusNames=TM_0428 {ECO:0000313|EMBL:AAD35513.1}; GN ORFNames=Tmari_0425 {ECO:0000313|EMBL:AGL49350.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35513.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35513.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35513.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49350.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49350.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35513.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49350.1; -; Genomic_DNA. DR PIR; D72379; D72379. DR RefSeq; NP_228238.1; NC_000853.1. DR RefSeq; WP_004083314.1; NZ_CP011107.1. DR STRING; 243274.TM0428; -. DR EnsemblBacteria; AAD35513; AAD35513; TM_0428. DR EnsemblBacteria; AGL49350; AGL49350; Tmari_0425. DR GeneID; 897436; -. DR KEGG; tma:TM0428; -. DR KEGG; tmi:THEMA_02585; -. DR KEGG; tmm:Tmari_0425; -. DR KEGG; tmw:THMA_0434; -. DR PATRIC; 23935741; VBITheMar51294_0434. DR eggNOG; ENOG4105CCY; Bacteria. DR eggNOG; COG1902; LUCA. DR OMA; HGYLGHE; -. DR OrthoDB; EOG6T7N7Q; -. DR BioCyc; TMAR243274:GC6P-443-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0003959; F:NADPH dehydrogenase activity; IBA:GO_Central. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001155; OxRdtase_FMN_N. DR Pfam; PF00724; Oxidored_FMN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49350.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 38 384 Oxidored_FMN. {ECO:0000259|Pfam:PF00724}. SQ SEQUENCE 435 AA; 49378 MW; 8C8015270E5E8946 CRC64; MKKRFKYRTL EEMRWEAITL GIDLPLSGDF DVFRDLVDLG SKTIPNRFVD QPMEGNDAQL DGTPGPLTLR RYRKLAEGGA GVIWVEAIAV SREARGNDRQ LMLTEETVNS FRSFVAEIKS VSLKTKNFEP YIVAQLTHPG RFGKNRKILF HDKFLDEKYG ITEDFPLMSD EELDSLKEQY LRAAKFAKTA GFDAVDIKAC HRYLLSELLA AHTREGKYGG SYENRTKLLK DIVRLVRKEV EIDITVRLNL SDFIPYPYGW GSTEEGTLDF TEPGRLLKEL EELGVKIINV TASTPYLKPH INRPYDEMGK YNPPEHPIVG AMRLLNLAKL AKETLSKTLV VASGFTWFRQ FAPYVAAGML KNGWCDFVGF GRMTFAYPDY PKDILTKGEL DPKKVCITCN KCAELKAAGE SCGCVVRDGE VYLPIYRKME ESKKS // ID Q9X069_THEMA Unreviewed; 96 AA. AC Q9X069; G4FF19; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36053.1}; GN OrderedLocusNames=TM_0974 {ECO:0000313|EMBL:AAD36053.1}; GN ORFNames=Tmari_0977 {ECO:0000313|EMBL:AGL49902.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36053.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36053.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36053.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49902.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49902.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36053.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49902.1; -; Genomic_DNA. DR PIR; C72309; C72309. DR RefSeq; NP_228782.1; NC_000853.1. DR RefSeq; WP_004080591.1; NZ_CP011107.1. DR STRING; 243274.TM0974; -. DR EnsemblBacteria; AAD36053; AAD36053; TM_0974. DR EnsemblBacteria; AGL49902; AGL49902; Tmari_0977. DR GeneID; 898720; -. DR KEGG; tma:TM0974; -. DR KEGG; tmi:THEMA_09475; -. DR KEGG; tmm:Tmari_0977; -. DR KEGG; tmw:THMA_0997; -. DR PATRIC; 23936877; VBITheMar51294_0987. DR eggNOG; ENOG4107GWU; Bacteria. DR eggNOG; COG2188; LUCA. DR OrthoDB; EOG6S26FX; -. DR BioCyc; TMAR243274:GC6P-1004-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR028978; Chorismate_lyase_/UTRA_dom. DR SUPFAM; SSF64288; SSF64288; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 96 AA; 11476 MW; 442A32C31357DA7F CRC64; MVEKSYFHPE VSKSFENEDL TKSLAKLFFN SLKDAKISRI EQVIEPCTRQ EAEHVQNLID AEEFLKMSRW IYVEGRDEPV YYLLLFMRAD LDRIRS // ID Q9WZS0_THEMA Unreviewed; 330 AA. AC Q9WZS0; G4FD11; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Glucosamine-6-phosphate deaminase [isomerizing], alternative {ECO:0000313|EMBL:AGL49739.1}; DE EC=3.5.99.6 {ECO:0000313|EMBL:AGL49739.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35895.1}; GN OrderedLocusNames=TM_0813 {ECO:0000313|EMBL:AAD35895.1}; GN ORFNames=Tmari_0814 {ECO:0000313|EMBL:AGL49739.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35895.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35895.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35895.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49739.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49739.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35895.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49739.1; -; Genomic_DNA. DR PIR; F72331; F72331. DR RefSeq; NP_228622.1; NC_000853.1. DR RefSeq; WP_004080849.1; NZ_CP011107.1. DR PDB; 1J5X; X-ray; 1.80 A; A=1-330. DR PDBsum; 1J5X; -. DR STRING; 243274.TM0813; -. DR EnsemblBacteria; AAD35895; AAD35895; TM_0813. DR EnsemblBacteria; AGL49739; AGL49739; Tmari_0814. DR GeneID; 898481; -. DR KEGG; tma:TM0813; -. DR KEGG; tmi:THEMA_00585; -. DR KEGG; tmm:Tmari_0814; -. DR KEGG; tmw:THMA_0832; -. DR PATRIC; 23936546; VBITheMar51294_0825. DR eggNOG; ENOG4107V1X; Bacteria. DR eggNOG; COG2222; LUCA. DR KO; K00820; -. DR OMA; PLEYRHG; -. DR OrthoDB; EOG6GFGH4; -. DR BioCyc; TMAR243274:GC6P-840-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IEA:UniProtKB-EC. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR InterPro; IPR001347; SIS. DR Pfam; PF01380; SIS; 1. DR PROSITE; PS51464; SIS; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1J5X}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49739.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 31 172 SIS. {ECO:0000259|PROSITE:PS51464}. FT DOMAIN 191 321 SIS. {ECO:0000259|PROSITE:PS51464}. SQ SEQUENCE 330 AA; 37371 MW; B6B179CB2050978C CRC64; MSKTLKEITD QKNELKKFFE NFVLNLEKTE IFSEIQKNLT DEVLFVGCGS SYNLALTISY YFERVLKIRT KAIPAGEVAF QKIPDLEERG LAFLFSRTGN TTEVLLANDV LKKRNHRTIG ITIEEESRLA KESDLPLVFP VREEAIVMTK SFSMILLSLM FLADKIAGNS TERFSELVGY SPEFFDISWK VIEKIDLKEH DHFVFLGMSE FFGVSLESAL KCIEMSLTFS EAYSTLEYRH GPKALVKKGT LVFMQKVSGM DEQEKRLRKE LESLGATVLE VGEGGDIPVS NDWKSAFLRT VPAQILGYQK AISRGISPDK PPHLEKTVVL // ID Q9WZ79_THEMA Unreviewed; 374 AA. AC Q9WZ79; G4FDK9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 87. DE SubName: Full=Lipopolysaccharide biosynthesis protein {ECO:0000313|EMBL:AAD35695.1}; DE SubName: Full=UDP-N-acetylglucosamine 2-epimerase {ECO:0000313|EMBL:AGL49535.1}; DE EC=5.1.3.14 {ECO:0000313|EMBL:AGL49535.1}; GN OrderedLocusNames=TM_0610 {ECO:0000313|EMBL:AAD35695.1}; GN ORFNames=Tmari_0610 {ECO:0000313|EMBL:AGL49535.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35695.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35695.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35695.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49535.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49535.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase CC family. {ECO:0000256|RuleBase:RU003513}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35695.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49535.1; -; Genomic_DNA. DR PIR; F72355; F72355. DR RefSeq; NP_228420.1; NC_000853.1. DR RefSeq; WP_004081214.1; NZ_CP011107.1. DR STRING; 243274.TM0610; -. DR EnsemblBacteria; AAD35695; AAD35695; TM_0610. DR EnsemblBacteria; AGL49535; AGL49535; Tmari_0610. DR GeneID; 897693; -. DR KEGG; tma:TM0610; -. DR KEGG; tmm:Tmari_0610; -. DR KEGG; tmw:THMA_0626; -. DR PATRIC; 23936135; VBITheMar51294_0621. DR eggNOG; ENOG4105EAG; Bacteria. DR eggNOG; COG0381; LUCA. DR KO; K01791; -. DR OMA; RTETEWV; -. DR OrthoDB; EOG6ZSP89; -. DR BioCyc; TMAR243274:GC6P-635-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-EC. DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom. DR InterPro; IPR029767; WecB-like. DR Pfam; PF02350; Epimerase_2; 1. DR TIGRFAMs; TIGR00236; wecB; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000256|RuleBase:RU003513, KW ECO:0000313|EMBL:AGL49535.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 40 364 Epimerase_2. {ECO:0000259|Pfam:PF02350}. SQ SEQUENCE 374 AA; 42813 MW; 21ABAE511BE9F4C6 CRC64; MGREEGRRIS GKSYGLRVLS LVGARPQIIK EAMLHREFKE KGIEEILVHS GQHYDYNMSS VFFEILEIRQ PHYNLNVGSG THGEMTGKIM IEFEKVLLSE KPDLVLVYGD TNTTLSGALV AAKLKIPVAH VEAGLRQHPK DMPEEINRIV TDRVSQLLFC PSKLAVRNLE REGITEGVYF VGDVMYDLFL KMEDRFRYDV FEKLGLKENE FVLVTLHRDF NVDDPVKLRK ILEQLKRVSR EKKVVFPIHP RTKNRVKEFG LENLLEGMVV IDPVDYLNLM GLVKRCWKVV TDSGGLQKEA YFAGKRAIVV MPDTGWRELV EAGWNKLASE ENLFDVTMEE DRSEYPSGLY GDGNAAGKIV EVIEEWFRSL RGIH // ID Q9X207_THEMA Unreviewed; 255 AA. AC Q9X207; G4FG66; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Metal-dependent hydrolases of the beta-lactamase superfamily II {ECO:0000313|EMBL:AGL50611.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36746.1}; GN OrderedLocusNames=TM_1679 {ECO:0000313|EMBL:AAD36746.1}; GN ORFNames=Tmari_1687 {ECO:0000313|EMBL:AGL50611.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36746.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36746.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36746.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50611.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50611.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36746.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50611.1; -; Genomic_DNA. DR PIR; E72226; E72226. DR RefSeq; NP_229479.1; NC_000853.1. DR RefSeq; WP_004082195.1; NZ_CP011107.1. DR PDB; 3H3E; X-ray; 2.75 A; A=2-255. DR PDBsum; 3H3E; -. DR STRING; 243274.TM1679; -. DR EnsemblBacteria; AAD36746; AAD36746; TM_1679. DR EnsemblBacteria; AGL50611; AGL50611; Tmari_1687. DR GeneID; 897900; -. DR KEGG; tma:TM1679; -. DR KEGG; tmi:THEMA_05845; -. DR KEGG; tmm:Tmari_1687; -. DR KEGG; tmw:THMA_1721; -. DR PATRIC; 23938332; VBITheMar51294_1696. DR eggNOG; ENOG4108R8Y; Bacteria. DR eggNOG; COG1237; LUCA. DR KO; K06897; -. DR OMA; KSSWAND; -. DR OrthoDB; EOG6Q8J0D; -. DR BioCyc; TMAR243274:GC6P-1727-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3H3E}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50611.1}; KW Metal-binding {ECO:0000213|PDB:3H3E}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000213|PDB:3H3E}. FT DOMAIN 19 224 Lactamase_B. {ECO:0000259|SMART:SM00849}. FT METAL 57 57 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:3H3E}. FT METAL 59 59 Zinc; via pros nitrogen. FT {ECO:0000213|PDB:3H3E}. FT METAL 170 170 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:3H3E}. FT DISULFID 168 225 {ECO:0000213|PDB:3H3E}. FT DISULFID 223 245 {ECO:0000213|PDB:3H3E}. SQ SEQUENCE 255 AA; 28679 MW; 74A33F1DCEBDD095 CRC64; MRIHVLCDDS SQNGFESEHG FSVLVDSVLF DTGKSDVFLK NARKLGIDLP KDVLISHGHY DHAGGLLYLS GKRVWLRKEA LDQKYSGERY AGADWNEVLK KNTGKFVIER ITEIGKNMFL LGPANLRGKV PTGDFFVERN GERRKDLFED EQTLVVRTKE GLVVITGCSH RGIDNILLDI AETFNERIKM VVGGFHLLKS SDDEIEKIVK AFNELGVETV VPCHCTGERA VDIFKREFLG KIMDCYAGLK LEVSD // ID Q9WZ96_THEMA Unreviewed; 353 AA. AC Q9WZ96; G4FDJ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35712.1}; GN OrderedLocusNames=TM_0628 {ECO:0000313|EMBL:AAD35712.1}; GN ORFNames=Tmari_0629 {ECO:0000313|EMBL:AGL49554.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35712.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35712.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35712.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49554.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49554.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35712.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49554.1; -; Genomic_DNA. DR PIR; A72353; A72353. DR RefSeq; NP_228437.1; NC_000853.1. DR RefSeq; WP_004081176.1; NZ_CP011107.1. DR STRING; 243274.TM0628; -. DR EnsemblBacteria; AAD35712; AAD35712; TM_0628. DR EnsemblBacteria; AGL49554; AGL49554; Tmari_0629. DR GeneID; 897716; -. DR KEGG; tma:TM0628; -. DR KEGG; tmi:THEMA_01520; -. DR KEGG; tmm:Tmari_0629; -. DR KEGG; tmw:THMA_0644; -. DR PATRIC; 23936169; VBITheMar51294_0638. DR OrthoDB; EOG6ZKXNW; -. DR BioCyc; TMAR243274:GC6P-653-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR001296; Glyco_trans_1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 169 323 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 353 AA; 41573 MW; 76A50A9B064D1D71 CRC64; MKAIISSLNF SPGHLSHTIA YAKLFREIGY DVFLWLHKEY KRMIKDIEFP IIWYPEESIG NTDIILFVNV STINHKYAQI LKRKGSKVIY LYHEPWESFR QYLKEGIKQA LKATIAHFFS VRLLKNSDLV IVPSKYALNL YKNKDIKYNE NVLMIPLLFD DELDEEVDIT KKQYFSYIGH AVKGHAFDVY IELIKHIYKQ GVDMKFQIAT RTDLSRLLKK DKILQEMIEK EILKIAHGRP LPNSEINRAY KESFCIWNVY RRSTQSGVLP KAYMFGTPVI ASNIGSFPEF VEAGKTGEIV YLPLNFDMTL DQIIKIKKDL ENYSQRSRQF FLETFYYEVY LKIFKEIINI DHA // ID Q9WZK3_THEMA Unreviewed; 406 AA. AC Q9WZK3; G4FD79; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=Glycosyltransferase {ECO:0000313|EMBL:AGL49670.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35825.1}; GN OrderedLocusNames=TM_0744 {ECO:0000313|EMBL:AAD35825.1}; GN ORFNames=Tmari_0745 {ECO:0000313|EMBL:AGL49670.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35825.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35825.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35825.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49670.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49670.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35825.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49670.1; -; Genomic_DNA. DR PIR; C72340; C72340. DR RefSeq; NP_228553.1; NC_000853.1. DR RefSeq; WP_004080975.1; NZ_CP011107.1. DR STRING; 243274.TM0744; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR DNASU; 898411; -. DR EnsemblBacteria; AAD35825; AAD35825; TM_0744. DR EnsemblBacteria; AGL49670; AGL49670; Tmari_0745. DR GeneID; 898411; -. DR KEGG; tma:TM0744; -. DR KEGG; tmi:THEMA_00935; -. DR KEGG; tmm:Tmari_0745; -. DR KEGG; tmw:THMA_0762; -. DR PATRIC; 23936408; VBITheMar51294_0757. DR eggNOG; ENOG4105BZF; Bacteria. DR eggNOG; COG0438; LUCA. DR OMA; ENYVRED; -. DR OrthoDB; EOG68DD0W; -. DR BioCyc; TMAR243274:GC6P-770-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49670.1}. FT DOMAIN 14 178 Glyco_trans_4-like_N. FT {ECO:0000259|Pfam:PF13439}. FT DOMAIN 188 348 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 406 AA; 47037 MW; 7060C048E31B4BA5 CRC64; MNIAMFSDTY APQINGVATS IRVYKKKLTE RGHKVVVVAP SAPEEEKDVF VVRSIPFPFE PQHRISIAST KNILEFMREN NVQIIHSHSP FFIGFKALRV QEEMGLPHVH TYHTLLPEYR HYIPKPFTPP KRLVEHFSAW FCNMTNVVIA PTEDIKRELE SYGVKRPIEV LPTGIEVEKF EVEAPEELKR KWNPEGKKVV LYAGRIAKEK NLDFLLRVFE SLNAPGIAFI MVGDGPEREE VEEFAKEKGL DLKITGFVPH DEIPLYYKLG DVFVFASKTE TQGLVLLEAL ASGLPVVALK WKGVKDVLKN CEAAVLIEEE NERLFAEKIK HILKNDRLRE ELSTKGREFV RKEWSVDRFV QRLEEIYTRA IEEGPVEINT SLMIKEFVKF EKLKEFFSKI EDRIWR // ID Q9X2C1_THEMA Unreviewed; 299 AA. AC Q9X2C1; G4FGI9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 78. DE SubName: Full=CRISPR-associated protein, family {ECO:0000313|EMBL:AGL50735.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36864.1}; GN OrderedLocusNames=TM_1801 {ECO:0000313|EMBL:AAD36864.1}; GN ORFNames=Tmari_1811 {ECO:0000313|EMBL:AGL50735.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36864.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36864.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36864.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50735.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50735.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36864.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50735.1; -; Genomic_DNA. DR PIR; F72210; F72210. DR RefSeq; NP_229598.1; NC_000853.1. DR RefSeq; WP_004082348.1; NZ_CP011107.1. DR STRING; 243274.TM1801; -. DR EnsemblBacteria; AAD36864; AAD36864; TM_1801. DR EnsemblBacteria; AGL50735; AGL50735; Tmari_1811. DR GeneID; 897834; -. DR KEGG; tma:TM1801; -. DR KEGG; tmi:THEMA_05185; -. DR KEGG; tmm:Tmari_1811; -. DR KEGG; tmw:THMA_1847; -. DR PATRIC; 23938591; VBITheMar51294_1822. DR eggNOG; ENOG4105DWJ; Bacteria. DR eggNOG; COG3649; LUCA. DR KO; K19115; -. DR OMA; TSHFASD; -. DR OrthoDB; EOG6VMTJ9; -. DR BioCyc; TMAR243274:GC6P-1852-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR006482; Cas7_Csh2/Csh2. DR InterPro; IPR013419; CRISPR-assoc_prot_Csh2. DR Pfam; PF05107; Cas_Cas7; 1. DR TIGRFAMs; TIGR02590; cas_Csh2; 1. DR TIGRFAMs; TIGR01595; cas_CT1132; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 242 269 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 299 AA; 34440 MW; 87E46DAEF9343167 CRC64; MNPVKNRSEV LFIYDVKWAN PNGDPLDENR PRFDEETSRL FVTDVRLKRT VRDYLAECYD ETLWVTGEAV VPEDRVKELG IKDVNDACQK CIDIRLFGAV IPQSKKGAME SSITGPVQFR YGTSLHRVKL MTIQGTAAFA TENSKQRSFR EDQVVPYALI AFYGVINQNS AKFTGLTEED VSKLLEGIWM GTKNLITRSK MEHNPRLLMR VVYKEGVNYH SGELDYLVKV VSEKEDEEIR DISELKLDVT ELKQVLESLK DKIERIEYSV DNRLKLAENG EEKPFEEIFG GFQLVKLEW // ID Q9X1K3_THEMA Unreviewed; 136 AA. AC Q9X1K3; G4FFQ2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=Ferric uptake regulation protein {ECO:0000313|EMBL:AAD36582.1}; DE SubName: Full=Peroxide stress regulator {ECO:0000313|EMBL:AGL50447.1}; GN OrderedLocusNames=TM_1515 {ECO:0000313|EMBL:AAD36582.1}; GN ORFNames=Tmari_1523 {ECO:0000313|EMBL:AGL50447.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36582.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36582.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36582.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50447.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50447.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the Fur family. CC {ECO:0000256|SAAS:SAAS00578401}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36582.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50447.1; -; Genomic_DNA. DR PIR; D72245; D72245. DR RefSeq; NP_229315.1; NC_000853.1. DR RefSeq; WP_004081866.1; NZ_CP011107.1. DR STRING; 243274.TM1515; -. DR EnsemblBacteria; AAD36582; AAD36582; TM_1515. DR EnsemblBacteria; AGL50447; AGL50447; Tmari_1523. DR GeneID; 897387; -. DR KEGG; tma:TM1515; -. DR KEGG; tmi:THEMA_06725; -. DR KEGG; tmm:Tmari_1523; -. DR KEGG; tmw:THMA_1547; -. DR PATRIC; 23937988; VBITheMar51294_1532. DR eggNOG; ENOG4105G5W; Bacteria. DR eggNOG; COG0735; LUCA. DR KO; K09825; -. DR OMA; HNGRTYY; -. DR OrthoDB; EOG6J48SS; -. DR BioCyc; TMAR243274:GC6P-1555-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR002481; FUR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01475; FUR; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00469751}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 73 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 136 AA; 15650 MW; 7C2979A31F0E1FF0 CRC64; MTTEEIIERL KSKKVKLTTQ RMEIIKFVSE MKEGHFEAKE LFAILSKKVP SLSIATLYSV LYLLVDLGVI YAFSDGQKTI FDFNPEPHGH FICRECGKIE DVEIRELKLG EVKGKREKIE LVIKGICEEC LKKVKD // ID Q9WZA8_THEMA Unreviewed; 201 AA. AC Q9WZA8; G4FDI3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=HAD superfamily hydrolase {ECO:0000313|EMBL:AGL49566.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35724.1}; GN OrderedLocusNames=TM_0640 {ECO:0000313|EMBL:AAD35724.1}; GN ORFNames=Tmari_0641 {ECO:0000313|EMBL:AGL49566.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35724.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35724.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35724.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49566.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49566.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35724.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49566.1; -; Genomic_DNA. DR PIR; G72350; G72350. DR RefSeq; NP_228449.1; NC_000853.1. DR RefSeq; WP_004081157.1; NZ_CP011107.1. DR STRING; 243274.TM0640; -. DR EnsemblBacteria; AAD35724; AAD35724; TM_0640. DR EnsemblBacteria; AGL49566; AGL49566; Tmari_0641. DR GeneID; 897741; -. DR KEGG; tma:TM0640; -. DR KEGG; tmi:THEMA_01460; -. DR KEGG; tmm:Tmari_0641; -. DR KEGG; tmw:THMA_0656; -. DR PATRIC; 23936193; VBITheMar51294_0650. DR eggNOG; ENOG4108UYS; Bacteria. DR eggNOG; COG1011; LUCA. DR KO; K07025; -. DR OMA; PYNVEGA; -. DR OrthoDB; EOG6M3PHH; -. DR BioCyc; TMAR243274:GC6P-665-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR Pfam; PF13419; HAD_2; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49566.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 181 HAD-like_dom. {ECO:0000259|Pfam:PF13419}. SQ SEQUENCE 201 AA; 24276 MW; A6AA74A63C2AAD10 CRC64; MIRNIVFDLG GVLIDWRPCE YLVESFPEDV AKVLEREIFK HEDWKKMDRG TLPENDLWEK KKKELSEYRE YVEKLEREVP KLLKPIEENV KLLSILKEKN FKLYVLSNYG KIYFEMVRRR YRFFDFFDGM VISSHVGFIK PEKEIYLELI RKYKITPKES LFIDDMEENV KAAEELGFNT IHLPEPSRLK ELLFETLKIG R // ID Q9WZG5_THEMA Unreviewed; 852 AA. AC Q9WZG5; G4FDB8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=ABC-type transporter, permease component {ECO:0000313|EMBL:AGL49631.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35788.1}; GN OrderedLocusNames=TM_0706 {ECO:0000313|EMBL:AAD35788.1}; GN ORFNames=Tmari_0706 {ECO:0000313|EMBL:AGL49631.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35788.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35788.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35788.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49631.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49631.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC {ECO:0000256|SAAS:SAAS00573676}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35788.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49631.1; -; Genomic_DNA. DR PIR; A72343; A72343. DR RefSeq; NP_228515.1; NC_000853.1. DR RefSeq; WP_004081033.1; NZ_CP011107.1. DR STRING; 243274.TM0706; -. DR EnsemblBacteria; AAD35788; AAD35788; TM_0706. DR EnsemblBacteria; AGL49631; AGL49631; Tmari_0706. DR GeneID; 898373; -. DR KEGG; tma:TM0706; -. DR KEGG; tmi:THEMA_01135; -. DR KEGG; tmm:Tmari_0706; -. DR KEGG; tmw:THMA_0721; -. DR PATRIC; 23936330; VBITheMar51294_0718. DR eggNOG; ENOG4108KRX; Bacteria. DR eggNOG; COG0577; LUCA. DR KO; K02004; -. DR OMA; MRENEES; -. DR OrthoDB; EOG62K1RM; -. DR BioCyc; TMAR243274:GC6P-732-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR InterPro; IPR003838; ABC_permease_dom. DR InterPro; IPR025857; MacB_PCD. DR Pfam; PF02687; FtsX; 2. DR Pfam; PF12704; MacB_PCD; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00573687}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00573687, KW ECO:0000256|SAAS:SAAS00573714, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00573714, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00573714, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 239 261 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 287 317 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 337 363 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 384 417 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 423 442 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 454 473 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 505 525 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 726 748 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 769 797 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 817 839 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 17 193 MacB_PCD. {ECO:0000259|Pfam:PF12704}. FT DOMAIN 246 373 FtsX. {ECO:0000259|Pfam:PF02687}. FT DOMAIN 726 844 FtsX. {ECO:0000259|Pfam:PF02687}. SQ SEQUENCE 852 AA; 94477 MW; 126FF505E488C9E6 CRC64; MILKIALRNF TKNLKISLVV ILGLAISLSL VTGALSLSDS INVWKWERIE ENFGNADAVA EPKSPSFLFF SFATSKIDDS EIENLKKQVK GVLPVSEDSA RLNSTLDVLV IATEPEYLSD FVGESLTLNP GEALVGKSIA ELMNLKVGDR ITLLFSSGSK EFTVVKIGEK GFLNFKGESA SLSGTVFINV KDFDGVFPTK CYLHYDLPVE KHEETTIETN LRVRNIKYSF LKSPINKSLA YVTLAFSGIS IFVGFLVFYM FCEDVIRDRS STLVTLRKIG LRKMEEWGIL LLEGFMYSLI SASVGVLIGI FVGKFLLSRF QEVVDVISSS FFHFDKIGFH LSISTLLLSL GLGVLFPMFL FFLKAREITG KPPIYREMRE QLDVSWKLVI FAVLLSFVLF FSELRVFSVV LLSLIIAIKL RNPFIMMALG TLNLGMGLFS SLNLQSEKAF IFSSLNKGSA IFFGVTLLVF SVVLLSKNVF NNLMSRGNLS LLIGLSYVQR FPKKGITVSL TFAFLIFSVT VFNILSASAD RFVQEKVKGG LFGYNFLVLE NPFRSLLAKT SLPVHEELKD PSRVYLYTLK TERGEKMIAF VDESFFRNST LKLLRGSARS LEASDTALIG DPVDLEEITG TLKSILPLGG RKEVKFKVAG IYNKNDYLVP IDMIAPISNV PSDVKPLSLL LGRVEESSAS SVKQFYFSKF AYPFFLDEEF KKLYSGIEGL VSVIKFIFLF GFLSASSGLL LFVLKSYFSR IKIMGTLRAV GMKINQLVAS FLIEHLFFLF GGILIGTVSG VLMGYFVSEA MSESLGTFMV SVPTASILLS LLTVIALASA VMVIPSLMMS KLSPLEAMKE GE // ID Q9WZE3_THEMA Unreviewed; 262 AA. AC Q9WZE3; G4FDE8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 85. DE SubName: Full=Flagellar motor rotation protein MotA {ECO:0000313|EMBL:AGL49601.1}; DE SubName: Full=Motility protein A {ECO:0000313|EMBL:AAD35759.1}; GN OrderedLocusNames=TM_0676 {ECO:0000313|EMBL:AAD35759.1}; GN ORFNames=Tmari_0676 {ECO:0000313|EMBL:AGL49601.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35759.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35759.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35759.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49601.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49601.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35759.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49601.1; -; Genomic_DNA. DR PIR; B72347; B72347. DR RefSeq; NP_228484.1; NC_000853.1. DR RefSeq; WP_004081090.1; NZ_CP011107.1. DR STRING; 243274.TM0676; -. DR EnsemblBacteria; AAD35759; AAD35759; TM_0676. DR EnsemblBacteria; AGL49601; AGL49601; Tmari_0676. DR GeneID; 898344; -. DR KEGG; tma:TM0676; -. DR KEGG; tmi:THEMA_01285; -. DR KEGG; tmm:Tmari_0676; -. DR KEGG; tmw:THMA_0691; -. DR PATRIC; 23936268; VBITheMar51294_0687. DR eggNOG; ENOG4105E14; Bacteria. DR eggNOG; COG1291; LUCA. DR KO; K02556; -. DR OMA; YAPAWGM; -. DR OrthoDB; EOG61P6PS; -. DR BioCyc; TMAR243274:GC6P-701-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro. DR InterPro; IPR000540; Flag_MotA_CS. DR InterPro; IPR022522; Flagellar_motor_stator_MotA. DR InterPro; IPR002898; MotA_ExbB_proton_chnl. DR PANTHER; PTHR30433:SF2; PTHR30433:SF2; 1. DR Pfam; PF01618; MotA_ExbB; 1. DR PROSITE; PS01307; MOTA; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AGL49601.1}; KW Cilium {ECO:0000313|EMBL:AGL49601.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AGL49601.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 29 50 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 149 169 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 201 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 101 217 MotA_ExbB. {ECO:0000259|Pfam:PF01618}. SQ SEQUENCE 262 AA; 28610 MW; 9F0C26F1FE0FC70B CRC64; MDLATLMGLV LVIAALFIGI LTGGGDFAAF INIPSLFITV VGSIAATMVA HPKDKAFKIV NIMLSTLKEP KLDHVSLIQT MVSFSEKARR EGLLSLEENL ESIEDPFMKK ALQLVVDGTD PDLLRNMMET EMELFEEELD GERAVLESAG AYAPAFGMIG TLIGLIQMLK SLNDPETLGP SMAVALITTL YGAILANGVF LPMAEKIKKR RDILVLEKRM ILEAVLSIQA GENPRILEEK LKSFLPEKER QAYEAASQEA TA // ID Q9WYN1_THEMA Unreviewed; 405 AA. AC Q9WYN1; G4FHV9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 117. DE SubName: Full=Sensor histidine kinase {ECO:0000313|EMBL:AAD35485.1}; DE SubName: Full=Two-component system histidine kinase {ECO:0000313|EMBL:AGL49322.1}; GN OrderedLocusNames=TM_0400 {ECO:0000313|EMBL:AAD35485.1}; GN ORFNames=Tmari_0397 {ECO:0000313|EMBL:AGL49322.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35485.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35485.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35485.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49322.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49322.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35485.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49322.1; -; Genomic_DNA. DR PIR; A72383; A72383. DR RefSeq; NP_228210.1; NC_000853.1. DR RefSeq; WP_004083236.1; NZ_CP011107.1. DR STRING; 243274.TM0400; -. DR DNASU; 897393; -. DR EnsemblBacteria; AAD35485; AAD35485; TM_0400. DR EnsemblBacteria; AGL49322; AGL49322; Tmari_0397. DR GeneID; 897393; -. DR KEGG; tma:TM0400; -. DR KEGG; tmi:THEMA_02725; -. DR KEGG; tmm:Tmari_0397; -. DR KEGG; tmw:THMA_0406; -. DR PATRIC; 23935683; VBITheMar51294_0405. DR eggNOG; ENOG4105US7; Bacteria. DR eggNOG; COG0642; LUCA. DR OMA; VESRWGE; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-415-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00528924}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|SAAS:SAAS00529081, ECO:0000313|EMBL:AAD35485.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00528924}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00529081, KW ECO:0000313|EMBL:AAD35485.1}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 16 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 159 184 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 199 405 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. SQ SEQUENCE 405 AA; 45693 MW; CCD0EE7F7E742C05 CRC64; MLPVTSERKA FRKTQLIWTA VFTLSIVLIV AITVGAVFIV EKRRITTQFD GELRRTADLI ERRLRAPGMM GMLRTFRGVD PLFVPRGEAF QFLLPSGEVF LEVGEQIGTP ETPVEEGFST EGNYRIFTKK IDLGDTTIFL RVGKDISDLI ERSKRLLSMY LLVILFSAGG AAVFGYFVSS LALLPVRNAY NSLKRFSMDA SHELKTPLSV LKTSLDVLKY REDLPDDVKN KLGIMEKNVE KMSKQINQLL LLVKSEGSLN SVVKERINLK DFLQQIVDEF KPKAESKGLE LEIDCPEDLF LETEKDTLRV ILENLVDNAV KFTEKGKVIV GARKEGRLTI YVQDTGPGIP KKEQKRIFER FYRISRNTEG SGLGLSIVKE LASRLKAKVI LESEEGKGST FKLVF // ID Q9X1K6_THEMA Unreviewed; 401 AA. AC Q9X1K6; G4FFQ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 103. DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448}; DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448}; GN OrderedLocusNames=TM_1518 {ECO:0000313|EMBL:AAD36585.1}; GN ORFNames=Tmari_1526 {ECO:0000313|EMBL:AGL50450.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36585.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36585.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36585.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50450.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50450.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. {ECO:0000256|RuleBase:RU003448}. CC -!- SIMILARITY: Belongs to the aspartokinase family. CC {ECO:0000256|RuleBase:RU003448}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36585.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50450.1; -; Genomic_DNA. DR PIR; G72245; G72245. DR RefSeq; NP_229318.1; NC_000853.1. DR RefSeq; WP_004081873.1; NZ_CP011107.1. DR STRING; 243274.TM1518; -. DR EnsemblBacteria; AAD36585; AAD36585; TM_1518. DR EnsemblBacteria; AGL50450; AGL50450; Tmari_1526. DR GeneID; 897987; -. DR KEGG; tma:TM1518; -. DR KEGG; tmi:THEMA_06710; -. DR KEGG; tmm:Tmari_1526; -. DR KEGG; tmw:THMA_1550; -. DR PATRIC; 23937994; VBITheMar51294_1535. DR eggNOG; ENOG4105CFH; Bacteria. DR eggNOG; COG0527; LUCA. DR KO; K00928; -. DR OMA; HSRSVEI; -. DR OrthoDB; EOG6NSGHC; -. DR BioCyc; TMAR243274:GC6P-1558-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro. DR Gene3D; 3.40.1160.10; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005260; Asp_kin_monofn. DR InterPro; IPR001341; Asp_kinase_dom. DR InterPro; IPR018042; Aspartate_kinase_CS. DR InterPro; IPR027795; GATS-like_ACT_dom. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF13840; ACT_7; 1. DR PIRSF; PIRSF000726; Asp_kin; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:AAD36585.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU003448, KW ECO:0000313|EMBL:AAD36585.1}. FT DOMAIN 264 346 ACT. {ECO:0000259|PROSITE:PS51671}. FT COILED 306 333 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 401 AA; 43815 MW; 36EEF22B6575BB9A CRC64; MNVVVQKYGG SSVATPERIK NVAQRIKKKV DEGYKVVVVV SAMGKTTDNL IKLAKEISPR PDSRELDMLL ATGEQVSAAL LSMALKDLGV KAKSLNAFQV KIKTTPHHTS ARIVDIDDSV IRENLKDYDV LVVTGFQGVN EHGDLTTLGR GGSDTSAVAL AAKLRVPCEI YSDVDGIYTC DPRVHPRAKK LAYITYDEAL ELTALGAKVL HSRSVEIAKK YGIPIYCASS FTEEEGTMVV ERLPEWLEEP VVTGATISHG QIKVSISFLP KDVKYITAIF EEVGKRALNV DMISLVPSNG KVFLSFTILE DHKEDLDEAL KEALRDVEGW KSTYEGGFAK LSIVGVGMRT SPGVAARFFE ALERAGVTPE LVTTSEIKIS CLVPEEKAEE ALKSVIEEFE L // ID Q9X184_THEMA Unreviewed; 127 AA. AC Q9X184; G4FFA0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=Flagellar basal body rod protein FlgB {ECO:0000256|PIRNR:PIRNR002889}; GN OrderedLocusNames=TM_1364 {ECO:0000313|EMBL:AAD36434.1}; GN ORFNames=Tmari_1371 {ECO:0000313|EMBL:AGL50295.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36434.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36434.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36434.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50295.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50295.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Structural component of flagellum, the bacterial CC motility apparatus. Part of the rod structure of flagellar basal CC body. {ECO:0000256|PIRNR:PIRNR002889}. CC -!- SUBUNIT: The basal body constitutes a major portion of the CC flagellar organelle and consists of a number of rings mounted on a CC central rod. {ECO:0000256|PIRNR:PIRNR002889}. CC -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body CC {ECO:0000256|PIRNR:PIRNR002889}. CC -!- SIMILARITY: Belongs to the flagella basal body rod proteins CC family. {ECO:0000256|PIRNR:PIRNR002889}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36434.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50295.1; -; Genomic_DNA. DR PIR; E72263; E72263. DR RefSeq; NP_229165.1; NC_000853.1. DR RefSeq; WP_004081560.1; NZ_CP011107.1. DR STRING; 243274.TM1364; -. DR EnsemblBacteria; AAD36434; AAD36434; TM_1364. DR EnsemblBacteria; AGL50295; AGL50295; Tmari_1371. DR GeneID; 898116; -. DR KEGG; tma:TM1364; -. DR KEGG; tmi:THEMA_07520; -. DR KEGG; tmm:Tmari_1371; -. DR KEGG; tmw:THMA_1389; -. DR PATRIC; 23937666; VBITheMar51294_1376. DR eggNOG; ENOG4105Q75; Bacteria. DR eggNOG; COG1815; LUCA. DR KO; K02387; -. DR OMA; NYKAKKV; -. DR OrthoDB; EOG6Q8J3B; -. DR BioCyc; TMAR243274:GC6P-1397-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030694; C:bacterial-type flagellum basal body, rod; IEA:InterPro. DR GO; GO:0009424; C:bacterial-type flagellum hook; IBA:GO_Central. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IBA:GO_Central. DR InterPro; IPR001444; Flag_bb_rod_N. DR InterPro; IPR006300; FlgB. DR Pfam; PF00460; Flg_bb_rod; 1. DR PIRSF; PIRSF002889; Rod_FlgB; 1. DR TIGRFAMs; TIGR01396; FlgB; 1. PE 3: Inferred from homology; KW Bacterial flagellum {ECO:0000256|PIRNR:PIRNR002889}; KW Cell projection {ECO:0000313|EMBL:AAD36434.1}; KW Cilium {ECO:0000313|EMBL:AAD36434.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD36434.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 6 36 Flg_bb_rod. {ECO:0000259|Pfam:PF00460}. SQ SEQUENCE 127 AA; 14709 MW; C98A098F63C2A632 CRC64; MFNTNFYTLK QAMDVALLRQ NVHSLNIANV STPGYKRKYV AFEELLKESE MKLKLSKTNE KHLIGSKNVV EPRVLVDNTT TMRNDGNNVD IDYEMVQLVK NGLRYQVLTR LMSLNIDRYN AVLRGVR // ID Q9WXN2_THEMA Unreviewed; 721 AA. AC Q9WXN2; G4FGU2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:AAD35119.1}; DE EC=3.2.1.21 {ECO:0000313|EMBL:AGL48948.1}; GN OrderedLocusNames=TM_0025 {ECO:0000313|EMBL:AAD35119.1}; GN ORFNames=Tmari_0022 {ECO:0000313|EMBL:AGL48948.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35119.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35119.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35119.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48948.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48948.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. CC {ECO:0000256|RuleBase:RU361161}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35119.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48948.1; -; Genomic_DNA. DR PIR; C72428; C72428. DR RefSeq; NP_227841.1; NC_000853.1. DR RefSeq; WP_004082478.1; NZ_CP011107.1. DR STRING; 243274.TM0025; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR EnsemblBacteria; AAD35119; AAD35119; TM_0025. DR EnsemblBacteria; AGL48948; AGL48948; Tmari_0022. DR GeneID; 896841; -. DR KEGG; tma:TM0025; -. DR KEGG; tmi:THEMA_04675; -. DR KEGG; tmm:Tmari_0022; -. DR KEGG; tmw:THMA_0021; -. DR PATRIC; 23934890; VBITheMar51294_0023. DR eggNOG; ENOG4107QK4; Bacteria. DR eggNOG; COG1472; LUCA. DR KO; K05349; -. DR OMA; GWWHTEP; -. DR OrthoDB; EOG6N9468; -. DR BioCyc; TMAR243274:GC6P-25-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central. DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central. DR Gene3D; 3.20.20.300; -; 1. DR Gene3D; 3.40.50.1700; -; 1. DR InterPro; IPR026891; Fn3-like. DR InterPro; IPR026892; Glyco_hydro_3. DR InterPro; IPR019800; Glyco_hydro_3_AS. DR InterPro; IPR002772; Glyco_hydro_3_C. DR InterPro; IPR001764; Glyco_hydro_3_N. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR30620; PTHR30620; 2. DR Pfam; PF14310; Fn3-like; 1. DR Pfam; PF00933; Glyco_hydro_3; 1. DR Pfam; PF01915; Glyco_hydro_3_C; 1. DR PRINTS; PR00133; GLHYDRLASE3. DR SMART; SM01217; Fn3_like; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR SUPFAM; SSF52279; SSF52279; 2. DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361161, KW ECO:0000313|EMBL:AGL48948.1}; KW Hydrolase {ECO:0000256|RuleBase:RU361161, KW ECO:0000313|EMBL:AGL48948.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 721 AA; 81074 MW; 31DB99D23E4CC963 CRC64; MERIDEILSQ LTTEEKVKLV VGVGLPGLFG NPHSRVAGAA GETHPVPRLG IPAFVLADGP AGLRINPTRE NDENTYYTTA FPVEIMLAST WNRDLLEEVG KAMGEEVREY GVDVLLAPAM NIHRNPLCGR NFEYYSEDPV LSGEMASAFV KGVQSQGVGA CIKHFVANNQ ETNRMVVDTI VSERALREIY LKGFEIAVKK ARPWTVMSAY NKLNGKYCSQ NEWLLKKVLR EEWGFDGFVM SDWYAGDNPV EQLKAGNDMI MPGKAYQVNT ERRDEIEEIM EALKEGKLSE EVLDECVRNI LKVLVNAPSF KGYRYSNKPD LESHAEVAYE AGAEGVVLLE NNGVLPFDEN THVAVFGTGQ IETIKGGTGS GDTHPRYTIS ILEGIKERNM KFDEELASTY EEYIKKMRET EEYKPRTDSW GTVIKPKLPE NFLSEKEIKK AAKKNDVAVV VISRISGEGY DRKPVKGDFY LSDDELELIK TVSKEFHDQG KKVVVLLNIG SPIEVASWRD LVDGILLVWQ AGQEMGRIVA DVLVGKINPS GKLPTTFPKD YSDVPSWTFP GEPKDNPQRV VYEEDIYVGY RYYDTFGVEP AYEFGYGLSY TKFEYKDLKI AIDGETLRVS YTITNTGDRA GKEVSQVYIK APKGKIDKPF QELKAFHKTK LLNPGESEEI SLEIPLRDLA SFDGKEWVVE SGEYEVRVGA SSRDIRLRDI FLVEGEKRFK P // ID Q9WXN5_THEMA Unreviewed; 330 AA. AC Q9WXN5; G4FGU5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 126. DE SubName: Full=Beta-glucoside ABC transport system, ATP-binding protein 1 {ECO:0000313|EMBL:AGL48951.1}; DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35122.1}; GN OrderedLocusNames=TM_0028 {ECO:0000313|EMBL:AAD35122.1}; GN ORFNames=Tmari_0025 {ECO:0000313|EMBL:AGL48951.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35122.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35122.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35122.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48951.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48951.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35122.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48951.1; -; Genomic_DNA. DR PIR; F72428; F72428. DR RefSeq; NP_227844.1; NC_000853.1. DR RefSeq; WP_004082481.1; NZ_CP011107.1. DR STRING; 243274.TM0028; -. DR TCDB; 3.A.1.5.16; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35122; AAD35122; TM_0028. DR EnsemblBacteria; AGL48951; AGL48951; Tmari_0025. DR GeneID; 896848; -. DR KEGG; tma:TM0028; -. DR KEGG; tmi:THEMA_04660; -. DR KEGG; tmm:Tmari_0025; -. DR KEGG; tmw:THMA_0024; -. DR PATRIC; 23934896; VBITheMar51294_0026. DR eggNOG; ENOG41060CX; Bacteria. DR eggNOG; ENOG410Y04P; LUCA. DR KO; K02031; -. DR OMA; VESIVFI; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-28-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35122.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35122.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 6 259 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 330 AA; 37305 MW; B8932BACFACC4A04 CRC64; MKEILLKAEN VRAYYKLEKV SVKAVDGLSF EILEDEVIGV VGESGCGKTT LSNVIFMNMV KPLTLVDGKI FLRVNGEFVE LSSMTRDEVK RKFWGKEITI IPQAAMNALM PTIRMEKYVR HLAESHGIDE EELLDKARRR FEEVGLDPLW IKRYPFELSG GMRQRAVIAI ATILNPSLLI ADEPTSALDV VNQKVLLKVL MQMKRQGIVK SIIFITHDIA TVRQIADRMI IMYAGKIVEF APVESLLEKP LHPYTQGLFN SVLTPEPEVK KRGITTIPGA PPNLINPPSG CRFHPRCPHA MDVCKEKEPP LTEIEPGRRV ACWLYMEERA // ID Q9X1V4_THEMA Unreviewed; 893 AA. AC Q9X1V4; G4FG08; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 119. DE SubName: Full=DNA polymerase I {ECO:0000313|EMBL:AGL50552.1}; DE EC=2.7.7.7 {ECO:0000313|EMBL:AGL50552.1}; DE SubName: Full=DNA-directed DNA polymerase I {ECO:0000313|EMBL:AAD36686.1}; GN OrderedLocusNames=TM_1619 {ECO:0000313|EMBL:AAD36686.1}; GN ORFNames=Tmari_1628 {ECO:0000313|EMBL:AGL50552.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36686.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36686.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36686.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50552.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50552.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. CC {ECO:0000256|RuleBase:RU004459}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36686.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50552.1; -; Genomic_DNA. DR PIR; E72232; E72232. DR RefSeq; NP_229419.1; NC_000853.1. DR RefSeq; WP_004082086.1; NZ_CP011107.1. DR STRING; 243274.TM1619; -. DR EnsemblBacteria; AAD36686; AAD36686; TM_1619. DR EnsemblBacteria; AGL50552; AGL50552; Tmari_1628. DR GeneID; 897625; -. DR KEGG; tma:TM1619; -. DR KEGG; tmi:THEMA_06150; -. DR KEGG; tmm:Tmari_1628; -. DR KEGG; tmw:THMA_1660; -. DR PATRIC; 23938212; VBITheMar51294_1638. DR eggNOG; ENOG4105C2M; Bacteria. DR eggNOG; COG0258; LUCA. DR eggNOG; COG0749; LUCA. DR KO; K02335; -. DR OMA; CFDTETT; -. DR OrthoDB; EOG6SJJH7; -. DR BioCyc; TMAR243274:GC6P-1665-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central. DR GO; GO:0071897; P:DNA biosynthetic process; IBA:GOC. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0006261; P:DNA-dependent DNA replication; IBA:GO_Central. DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GOC. DR Gene3D; 3.30.420.10; -; 1. DR Gene3D; 3.40.50.1010; -; 1. DR InterPro; IPR002562; 3'-5'_exonuclease_dom. DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N. DR InterPro; IPR020045; 5-3_exonuclease_C. DR InterPro; IPR002421; 5-3_exonuclease_N. DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom. DR InterPro; IPR018320; DNA_polymerase_1. DR InterPro; IPR002298; DNA_polymerase_A. DR InterPro; IPR008918; HhH2. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF01367; 5_3_exonuc; 1. DR Pfam; PF02739; 5_3_exonuc_N; 1. DR Pfam; PF00476; DNA_pol_A; 1. DR Pfam; PF01612; DNA_pol_A_exo1; 1. DR PRINTS; PR00868; DNAPOLI. DR SMART; SM00474; 35EXOc; 1. DR SMART; SM00475; 53EXOc; 1. DR SMART; SM00279; HhH2; 1. DR SMART; SM00482; POLAc; 1. DR SUPFAM; SSF47807; SSF47807; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR SUPFAM; SSF88723; SSF88723; 1. DR TIGRFAMs; TIGR00593; pola; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-directed DNA polymerase {ECO:0000313|EMBL:AAD36686.1}; KW Hydrolase {ECO:0000256|SAAS:SAAS00427491}; KW Nuclease {ECO:0000256|SAAS:SAAS00427491}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAD36686.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD36686.1}. FT DOMAIN 2 264 53EXOc. {ECO:0000259|SMART:SM00475}. FT DOMAIN 298 484 3'-5' exonuclease. FT {ECO:0000259|SMART:SM00474}. FT DOMAIN 653 860 POLAc. {ECO:0000259|SMART:SM00482}. SQ SEQUENCE 893 AA; 102161 MW; 669EE226DBBB39F3 CRC64; MARLFLFDGT ALAYRAYYAL DRSLSTSTGI PTNATYGVAR MLVRFIKDHI IVGKDYVAVA FDKKAATFRH KLLETYKAQR PKTPDLLIQQ LPYIKKLVEA LGMKVLEVEG YEADDIIATL AVKGLPLFDE IFIVTGDKDM LQLVNEKIKV WRIVKGISDL ELYDAQKVKE KYGVEPQQIP DLLALTGDEI DNIPGVTGIG EKTAVQLLEK YKDLEDILNH VRELPQKVRK ALLRDRENAI LSKKLAILET NVPIEINWEE LRYQGYDREK LLPLLKELEF ASIMKELQLY EESEPVGYRI VKDLVEFEKL IEKLRESPSF AIDLETSSLD PFDCDIVGIS VSFKPKEAYY IPLHHRNAQN LDEKEVLKKL KEILEDPGAK IVGQNLKFDY KVLMVKGVEP VPPYFDTMIA AYLLEPNEKK FNLDDLALKF LGYKMTSYQE LMSFSFPLFG FSFADVPVEK AANYSCEDAD ITYRLYKTLS LKLHEADLEN VFYKIEMPLV NVLARMELNG VYVDTEFLKK LSEEYGKKLE ELAEEIYRIA GEPFNINSPK QVSRILFEKL GIKPRGKTTK TGDYSTRIEV LEELAGEHEI IPLILEYRKI QKLKSTYIDA LPKMVNPKTG RIHASFNQTG TATGRLSSSD PNLQNLPTKS EEGKEIRKAI VPQDPNWWIV SADYSQIELR ILAHLSGDEN LLRAFEEGID VHTLTASRIF NVKPEEVTEE MRRAGKMVNF SIIYGVTPYG LSVRLGVPVK EAEKMIVNYF VLYPKVRDYI QRVVSEAKEK GYVRTLFGRK RDIPQLMARD RNTQAEGERI AINTPIQGTA ADIIKLAMIE IDRELKERKM RSKMIIQVHD ELVFEVPNEE KDALVELVKD RMTNVVKLSV PLEVDVTIGK TWS // ID Q9WZT4_THEMA Unreviewed; 234 AA. AC Q9WZT4; G4FCZ7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 98. DE SubName: Full=ABC transporter, ATP-binding protein, putative {ECO:0000313|EMBL:AAD35909.1}; DE SubName: Full=ABC-type cobalamin/Fe3+-siderophores transport systems ATPase components-like protein {ECO:0000313|EMBL:AGL49754.1}; GN OrderedLocusNames=TM_0827 {ECO:0000313|EMBL:AAD35909.1}; GN ORFNames=Tmari_0829 {ECO:0000313|EMBL:AGL49754.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35909.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35909.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35909.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49754.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49754.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35909.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49754.1; -; Genomic_DNA. DR PIR; G72327; G72327. DR RefSeq; NP_228636.1; NC_000853.1. DR RefSeq; WP_004080826.1; NZ_CP011107.1. DR STRING; 243274.TM0827; -. DR EnsemblBacteria; AAD35909; AAD35909; TM_0827. DR EnsemblBacteria; AGL49754; AGL49754; Tmari_0829. DR GeneID; 898497; -. DR KEGG; tma:TM0827; -. DR KEGG; tmi:THEMA_00505; -. DR KEGG; tmm:Tmari_0829; -. DR KEGG; tmw:THMA_0848; -. DR PATRIC; 23936580; VBITheMar51294_0840. DR eggNOG; ENOG4105TNE; Bacteria. DR eggNOG; ENOG4111UYI; LUCA. DR OMA; CILDHLD; -. DR OrthoDB; EOG64V2D0; -. DR BioCyc; TMAR243274:GC6P-856-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD35909.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD35909.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 8 234 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 234 AA; 27175 MW; 5E6115497B8139D6 CRC64; MKSRKFPIRF ENFSLSVDGK SVLENITLSF VEGMNVLYGP RGSGKSSLLR SIVKLNTEIF NEISRSGSVY LFDQNVEDLD DIYVRKNALY LDTSFIDAMN QYTFDEFLKL ALKRKISLEN FSEKLDDLGI LRMLIRGQKT PLSVFSPAEK ISLLLFILEQ KKPRVILMDC LLDHLDDENL EKIMDMFLKM KEERTFVIST RILQRFLYIA DLLVILNNGR INYTGSPKDF VLRM // ID Q9X2I7_THEMA Unreviewed; 66 AA. AC Q9X2I7; G4FGR6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 117. DE SubName: Full=Cold shock protein {ECO:0000313|EMBL:AAD36936.1}; DE SubName: Full=Cold shock protein CspA {ECO:0000313|EMBL:AGL50813.1}; GN OrderedLocusNames=TM_1874 {ECO:0000313|EMBL:AAD36936.1}; GN ORFNames=Tmari_1889 {ECO:0000313|EMBL:AGL50813.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36936.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36936.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36936.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50813.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50813.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000408, CC ECO:0000256|SAAS:SAAS00557911}. CC -!- SIMILARITY: Contains 1 CSD (cold-shock) domain. CC {ECO:0000256|RuleBase:RU000407}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36936.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50813.1; -; Genomic_DNA. DR PIR; E72200; E72200. DR RefSeq; NP_229670.1; NC_000853.1. DR RefSeq; WP_004082425.1; NZ_CP011107.1. DR SMR; Q9X2I7; 1-65. DR STRING; 243274.TM1874; -. DR EnsemblBacteria; AAD36936; AAD36936; TM_1874. DR EnsemblBacteria; AGL50813; AGL50813; Tmari_1889. DR GeneID; 897562; -. DR KEGG; tma:TM1874; -. DR KEGG; tmi:THEMA_04800; -. DR KEGG; tmm:Tmari_1889; -. DR KEGG; tmw:THMA_1924; -. DR PATRIC; 23938737; VBITheMar51294_1895. DR eggNOG; ENOG4105VEQ; Bacteria. DR eggNOG; COG1278; LUCA. DR KO; K03704; -. DR OMA; FEIQDGH; -. DR OrthoDB; EOG618R0J; -. DR BioCyc; TMAR243274:GC6P-1925-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR019844; Cold-shock_CS. DR InterPro; IPR012156; Cold_shock_CspA. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR002059; CSP_DNA-bd. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF00313; CSD; 1. DR PIRSF; PIRSF002599; Cold_shock_A; 1. DR PRINTS; PR00050; COLDSHOCK. DR SMART; SM00357; CSP; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS00352; COLD_SHOCK; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00444364}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 65 CSP. {ECO:0000259|SMART:SM00357}. SQ SEQUENCE 66 AA; 7623 MW; 094961961F371DB2 CRC64; MRGTVKWFDS KKGYGFITME NGEDIFVHWS AIQMDGFKTL RENETVEFEV QKGTKGPQAV NVRPVR // ID Q9WXV9_THEMA Unreviewed; 344 AA. AC Q9WXV9; G4FH19; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 88. DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35198.1}; GN OrderedLocusNames=TM_0104 {ECO:0000313|EMBL:AAD35198.1}; GN ORFNames=Tmari_0101 {ECO:0000313|EMBL:AGL49027.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35198.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35198.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35198.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49027.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49027.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|SAAS:SAAS00582814}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35198.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49027.1; -; Genomic_DNA. DR PIR; H72418; H72418. DR RefSeq; NP_227920.1; NC_000853.1. DR RefSeq; WP_004082660.1; NZ_CP011107.1. DR STRING; 243274.TM0104; -. DR DNASU; 896931; -. DR EnsemblBacteria; AAD35198; AAD35198; TM_0104. DR EnsemblBacteria; AGL49027; AGL49027; Tmari_0101. DR GeneID; 896931; -. DR KEGG; tma:TM0104; -. DR KEGG; tmi:THEMA_04285; -. DR KEGG; tmm:Tmari_0101; -. DR KEGG; tmw:THMA_0100; -. DR PATRIC; 23935048; VBITheMar51294_0102. DR eggNOG; ENOG4105UIB; Bacteria. DR eggNOG; COG4603; LUCA. DR KO; K02057; -. DR OMA; GPIGHLQ; -. DR OrthoDB; EOG6MSS3R; -. DR BioCyc; TMAR243274:GC6P-104-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015749; P:monosaccharide transport; IBA:GOC. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00476327}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAAS:SAAS00476327, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00476193}. FT TRANSMEM 6 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 76 99 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 141 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 207 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 237 256 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 276 299 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 311 329 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 344 AA; 35925 MW; FC92F8ED16239AE3 CRC64; MNNRVWSFLV PFFSVIIALL IAAVVIILIG QNPVIAYKAM IEGAFGNIQA LADTVIKTTP LILTGLAVGF GFRAGLFNIG AEGQMIMGGI LATVVGMHMR GIPPALAIPL TMIAGMLGGA AWASIAGYLK AKTGAHEVVS TIMLNWIATY ISSYLITGPL AVGSGTPKSP EIAPSAKLPP IVTVGALEMT SGILISILSA VVIYIVLEKT KTGYEVKAVG FNPYAAEYGG INISKNIVMC MAISGALAGL AGALEVMGLH HRFLGTLSGG KGFDGISIAL IGQNHPIGII FASFLIAALR TGSSNMQFVG VPKHIVTIIQ GIVIFLVAAD RIVKTLLRFR KVKR // ID Q9X058_THEMA Unreviewed; 547 AA. AC Q9X058; G4FF27; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 101. DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:AGL49890.1}; DE EC=3.4.24.- {ECO:0000313|EMBL:AGL49890.1}; DE SubName: Full=Oligoendopeptidase, putative {ECO:0000313|EMBL:AAD36042.1}; GN OrderedLocusNames=TM_0963 {ECO:0000313|EMBL:AAD36042.1}; GN ORFNames=Tmari_0965 {ECO:0000313|EMBL:AGL49890.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36042.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36042.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36042.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49890.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49890.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU003435}; CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435}; CC -!- SIMILARITY: Belongs to the peptidase M3 family. CC {ECO:0000256|RuleBase:RU003435}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36042.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49890.1; -; Genomic_DNA. DR PIR; H72311; H72311. DR RefSeq; NP_228771.1; NC_000853.1. DR RefSeq; WP_004080599.1; NZ_CP011107.1. DR STRING; 243274.TM0963; -. DR EnsemblBacteria; AAD36042; AAD36042; TM_0963. DR EnsemblBacteria; AGL49890; AGL49890; Tmari_0965. DR GeneID; 898700; -. DR KEGG; tma:TM0963; -. DR KEGG; tmi:THEMA_09530; -. DR KEGG; tmm:Tmari_0965; -. DR KEGG; tmw:THMA_0986; -. DR PATRIC; 23936857; VBITheMar51294_0977. DR eggNOG; ENOG4105D1I; Bacteria. DR eggNOG; COG1164; LUCA. DR KO; K08602; -. DR OMA; GAPFIFM; -. DR OrthoDB; EOG6RFZT8; -. DR BioCyc; TMAR243274:GC6P-993-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central. DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central. DR Gene3D; 1.10.1370.10; -; 1. DR InterPro; IPR024077; Neurolysin/TOP_dom2. DR InterPro; IPR001567; Pept_M3A_M3B. DR InterPro; IPR011976; Pept_M3B_clade2. DR Pfam; PF01432; Peptidase_M3; 1. DR TIGRFAMs; TIGR02289; M3_not_pepF; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|RuleBase:RU003435}; KW Metal-binding {ECO:0000256|RuleBase:RU003435}; KW Metalloprotease {ECO:0000256|RuleBase:RU003435}; KW Protease {ECO:0000256|RuleBase:RU003435}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000256|RuleBase:RU003435}. SQ SEQUENCE 547 AA; 65451 MW; 937CACFF6EF5C9E2 CRC64; MRWEEVEPVV RELLDFQISS PEEFRTFINK VTDFFDRVRE EHGWLYIKMT VNADKEEFAK AYEEFQKEIV AKLKPYEQKI KEKIVENEHF APRGYEHMIK VIKNDVELFR EENVPLQVKE SILSRNYGTI VGNIEVDFEG EKKTLQQLSV YLRDPDRSTR ELAWRKRYEG IWEVRDKLNK LFDELKEIRH QQALNAGFSN YRDYMHRLKS RFEYTPEDLY RFHEAVEKEV VPYLVERTKI RQRKLGIESV RPWDTAVDVD GKVLKPFSSV EEFMEKTERA LKRLNPTFAE RFRLMREKNL LDLENRKGKA PGGYNHTLPK TGAPFIFMNA VGQPGDVRTI FHELGHSMHS FETLSLPVFY RPHRMEVAEL ASMSLELISM EYWDEFYTDP EDLKKAKIEE LEGALYFLPW CMIVDAFQHW IYTNPDHTPK ERDEYFAYLM DRFNPGVDWS DLDEEKKTRW LFQLHIFEVP FYYIEYGIAQ IGALAIYRNY IEDPEKTLKD YQRFLSVGCS MPVDEVYKTA GIELKFSRDY IREIVDFVAK QIEEIEK // ID Q9WXR0_THEMA Unreviewed; 364 AA. AC Q9WXR0; G4FGW8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Esterase, putative {ECO:0000313|EMBL:AAD35147.1}; GN OrderedLocusNames=TM_0053 {ECO:0000313|EMBL:AAD35147.1}; GN ORFNames=Tmari_0050 {ECO:0000313|EMBL:AGL48976.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35147.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35147.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35147.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48976.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48976.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35147.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48976.1; -; Genomic_DNA. DR PIR; F72423; F72423. DR RefSeq; NP_227869.1; NC_000853.1. DR RefSeq; WP_004082539.1; NZ_CP011107.1. DR STRING; 243274.TM0053; -. DR ESTHER; thema-TM0053; AlphaBeta_hydrolase. DR EnsemblBacteria; AAD35147; AAD35147; TM_0053. DR EnsemblBacteria; AGL48976; AGL48976; Tmari_0050. DR GeneID; 896877; -. DR KEGG; tma:TM0053; -. DR KEGG; tmi:THEMA_04540; -. DR KEGG; tmm:Tmari_0050; -. DR KEGG; tmw:THMA_0049; -. DR PATRIC; 23934946; VBITheMar51294_0051. DR eggNOG; ENOG4106BAW; Bacteria. DR eggNOG; ENOG410XW6F; LUCA. DR OMA; FLENDGM; -. DR OrthoDB; EOG6S52PZ; -. DR BioCyc; TMAR243274:GC6P-53-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.1820; -; 2. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR012908; PGAP1-like. DR Pfam; PF07819; PGAP1; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 364 AA; 40860 MW; 44D1343FEA6AE7A9 CRC64; MRFFLVAIVL LGVSMFGFNI ILESTPTLYD VVEYYAGDWC IFRMVYDGTV DPYNPPLLET NATVIGKVIK WQKPEEKLAE IHKEGSSLNL VVIHGMDPRE YTGEMTEYKK EIEKVFEEIG ERLRINVYLF IYPTLLADPE KSAERFIDLT KDMENIIIFA HSMGGIIAEH IAAKHPGNVK GIIFAGTPHL GSPLANVLFT DPDRYEEEFL IDKKTAENLR AALLISYAGF SATYAPGYRY LLWQRKPLDF SNVPFVNLVG TISLDSVESI PGILLNIMTT SAWDTLGLIG LKLLASSVST MKDDFEETDG MVPCKSASYG GNALVFDADH EDLYKRKDII LEGLSYILFR ILENEVILKK GGSQ // ID Q9X0F2_THEMA Unreviewed; 563 AA. AC Q9X0F2; G4FET6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 109. DE SubName: Full=Beta-glucuronidase {ECO:0000313|EMBL:AAD36143.1}; DE EC=3.2.1.31 {ECO:0000313|EMBL:AGL49990.1}; GN OrderedLocusNames=TM_1062 {ECO:0000313|EMBL:AAD36143.1}; GN ORFNames=Tmari_1066 {ECO:0000313|EMBL:AGL49990.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36143.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36143.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36143.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49990.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49990.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. CC {ECO:0000256|RuleBase:RU361154, ECO:0000256|SAAS:SAAS00568376}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36143.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49990.1; -; Genomic_DNA. DR PIR; A72300; A72300. DR RefSeq; NP_228868.1; NC_000853.1. DR RefSeq; WP_004080425.1; NZ_CP011107.1. DR STRING; 243274.TM1062; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR EnsemblBacteria; AAD36143; AAD36143; TM_1062. DR EnsemblBacteria; AGL49990; AGL49990; Tmari_1066. DR GeneID; 897051; -. DR KEGG; tma:TM1062; -. DR KEGG; tmi:THEMA_09050; -. DR KEGG; tmm:Tmari_1066; -. DR KEGG; tmw:THMA_1084; -. DR PATRIC; 23937053; VBITheMar51294_1075. DR eggNOG; ENOG4105CNT; Bacteria. DR eggNOG; COG3250; LUCA. DR KO; K01195; -. DR OMA; TSLNGKW; -. DR OrthoDB; EOG6DRPFW; -. DR BioCyc; TMAR243274:GC6P-1091-MONOMER; -. DR BRENDA; 3.2.1.31; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 2.60.40.320; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR008979; Galactose-bd-like. DR InterPro; IPR006101; Glyco_hydro_2. DR InterPro; IPR013812; Glyco_hydro_2/20_Ig-like. DR InterPro; IPR006103; Glyco_hydro_2_cat. DR InterPro; IPR023230; Glyco_hydro_2_CS. DR InterPro; IPR006102; Glyco_hydro_2_Ig-like. DR InterPro; IPR006104; Glyco_hydro_2_N. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF00703; Glyco_hydro_2; 1. DR Pfam; PF02836; Glyco_hydro_2_C; 1. DR Pfam; PF02837; Glyco_hydro_2_N; 1. DR PRINTS; PR00132; GLHYDRLASE2. DR SUPFAM; SSF49303; SSF49303; 1. DR SUPFAM; SSF49785; SSF49785; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361154, KW ECO:0000256|SAAS:SAAS00456829, ECO:0000313|EMBL:AGL49990.1}; KW Hydrolase {ECO:0000256|RuleBase:RU361154, KW ECO:0000256|SAAS:SAAS00456829, ECO:0000313|EMBL:AGL49990.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 26 122 Glyco_hydro_2_N. FT {ECO:0000259|Pfam:PF02837}. FT DOMAIN 169 260 Glyco_hydro_2. FT {ECO:0000259|Pfam:PF00703}. FT DOMAIN 266 562 Glyco_hydro_2_C. FT {ECO:0000259|Pfam:PF02836}. SQ SEQUENCE 563 AA; 65683 MW; 98C030B75D33B6C1 CRC64; MVRPQRNKKR FILILNGVWN LEVTSKDRPI AVPGSWNEQY QDLCYEEGPF TYKTTFYVPK ELSQKHIRLY FAAVNTDCEV FLNGEKVGEN HIEYLPFEVD VTGKVKSGEN ELRVVVENRL KVGGFPSKVP DSGTHTVGFF GSFPPANFDF FPYGGIIRPV LIEFTDHARI LDIWVDTSES EPEKKLGKVK VKIEVSEEAV GQEMTIKLGE EEKKIRTSNR FVEGEFILEN ARFWSLEDPY LYPLKVELEK DEYTLDIGIR TISWDEKRLY LNGKPVFLKG FGKHEEFPVL GQGTFYPLMI KDFNLLKWIN ANSFRTSHYP YSEEWLDLAD RLGILVIDEA PHVGITRYHY NPETQKIAED NIRRMIDRHK NHPSVIMWSV ANEPESNHPD AEGFFKALYE TANEMDRTRP VVMVSMMDAP DERTRDVALK YFDIVCVNRY YGWYIYQGRI EEGLQALEKD IEELYARHRK PIFVTEFGAD AIAGIHYDPP QMFSEEYQAE LVEKTIRLLL KKDYIIGTHV WAFADFKTPQ NVRRPILNHK GVFTRDRQPK LVAHVLRRLW SEV // ID Q9X0T1_THEMA Unreviewed; 391 AA. AC Q9X0T1; G4FEE2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 100. DE SubName: Full=Maltose ABC transporter, periplasmic maltose-binding protein {ECO:0000313|EMBL:AAD36279.1}; DE SubName: Full=Maltose/maltodextrin ABC transporter, substrate binding periplasmic protein MalE {ECO:0000313|EMBL:AGL50135.1}; GN OrderedLocusNames=TM_1204 {ECO:0000313|EMBL:AAD36279.1}; GN ORFNames=Tmari_1211 {ECO:0000313|EMBL:AGL50135.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36279.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36279.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36279.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50135.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50135.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36279.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50135.1; -; Genomic_DNA. DR PIR; B72283; B72283. DR RefSeq; NP_229009.1; NC_000853.1. DR RefSeq; WP_004080109.1; NZ_CP011107.1. DR PDB; 2GHA; X-ray; 1.60 A; A/B=19-391. DR PDB; 2GHB; X-ray; 2.10 A; A/B/C=19-391. DR PDBsum; 2GHA; -. DR PDBsum; 2GHB; -. DR STRING; 243274.TM1204; -. DR TCDB; 3.A.1.1.22; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36279; AAD36279; TM_1204. DR EnsemblBacteria; AGL50135; AGL50135; Tmari_1211. DR GeneID; 898280; -. DR KEGG; tma:TM1204; -. DR KEGG; tmi:THEMA_08310; -. DR KEGG; tmm:Tmari_1211; -. DR KEGG; tmw:THMA_1230; -. DR PATRIC; 23937350; VBITheMar51294_1222. DR eggNOG; ENOG4107FKK; Bacteria. DR eggNOG; COG2182; LUCA. DR KO; K10108; -. DR OMA; DIRKSDG; -. DR OrthoDB; EOG60SCM8; -. DR BioCyc; TMAR243274:GC6P-1234-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro. DR GO; GO:0004175; F:endopeptidase activity; IEA:InterPro. DR GO; GO:0005363; F:maltose transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR InterPro; IPR006060; Maltose-bd. DR InterPro; IPR000426; Proteasome_asu_N. DR PRINTS; PR00181; MALTOSEBP. DR SMART; SM00948; Proteasome_A_N; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2GHA, ECO:0000213|PDB:2GHB}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 391 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007217058. FT DOMAIN 105 127 PROTEASOME_ALPHA_1. FT {ECO:0000259|SMART:SM00948}. SQ SEQUENCE 391 AA; 43018 MW; 028CB48D5B4BA350 CRC64; MKKFLVIALL VVSLVVLAQP KLTIWCSEKQ VDILQKLGEE FKAKYGVEVE VQYVNFQDIK SKFLTAAPEG QGADIIVGAH DWVGELAVNG LIEPIPNFSD LKNFYETALN AFSYGGKLYG IPYAMEAIAL IYNKDYVPEP PKTMDELIEI AKQIDEEFGG EVRGFITSAA EFYYIAPFIF GYGGYVFKQT EKGLDVNDIG LANEGAIKGV KLLKRLVDEG ILDPSDNYQI MDSMFREGQA AMIINGPWAI KAYKDAGIDY GVAPIPDLEP GVPARPFVGV QGFMVNAKSP NKLLAIEFLT SFIAKKETMY RIYLGDPRLP SRKDVLELVK DNPDVVGFTL SAANGIPMPN VPQMAAVWAA MNDALNLVVN GKATVEEALK NAVERIKAQI Q // ID Q9WZQ5_THEMA Unreviewed; 293 AA. AC Q9WZQ5; G4FD26; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|PIRNR:PIRNR000446}; DE EC=2.3.1.39 {ECO:0000256|PIRNR:PIRNR000446}; GN OrderedLocusNames=TM_0798 {ECO:0000313|EMBL:AAD35880.1}; GN ORFNames=Tmari_0799 {ECO:0000313|EMBL:AGL49724.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35880.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35880.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35880.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49724.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49724.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: Malonyl-CoA + an [acyl-carrier-protein] = CoA CC + a malonyl-[acyl-carrier-protein]. CC {ECO:0000256|PIRNR:PIRNR000446}. CC -!- SIMILARITY: Belongs to the fabD family. CC {ECO:0000256|PIRNR:PIRNR000446}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35880.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49724.1; -; Genomic_DNA. DR PIR; G72334; G72334. DR RefSeq; NP_228607.1; NC_000853.1. DR RefSeq; WP_004080868.1; NZ_CP011107.1. DR STRING; 243274.TM0798; -. DR EnsemblBacteria; AAD35880; AAD35880; TM_0798. DR EnsemblBacteria; AGL49724; AGL49724; Tmari_0799. DR GeneID; 898466; -. DR KEGG; tma:TM0798; -. DR KEGG; tmi:THEMA_00660; -. DR KEGG; tmm:Tmari_0799; -. DR KEGG; tmw:THMA_0817; -. DR PATRIC; 23936516; VBITheMar51294_0810. DR eggNOG; ENOG4105CJF; Bacteria. DR eggNOG; COG0331; LUCA. DR KO; K00645; -. DR OMA; FHCALMQ; -. DR OrthoDB; EOG6W19KW; -. DR BioCyc; TMAR243274:GC6P-825-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.366.10; -; 2. DR InterPro; IPR001227; Ac_transferase_dom. DR InterPro; IPR014043; Acyl_transferase. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR024925; Malonyl_CoA-ACP_transAc. DR InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD. DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd. DR InterPro; IPR020801; PKS_acyl_transferase. DR Pfam; PF00698; Acyl_transf_1; 1. DR PIRSF; PIRSF000446; Mct; 1. DR SMART; SM00827; PKS_AT; 1. DR SUPFAM; SSF52151; SSF52151; 2. DR SUPFAM; SSF55048; SSF55048; 1. DR TIGRFAMs; TIGR00128; fabD; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|PIRNR:PIRNR000446, KW ECO:0000313|EMBL:AGL49724.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|PIRNR:PIRNR000446, KW ECO:0000313|EMBL:AGL49724.1}. FT ACT_SITE 87 87 {ECO:0000256|PIRSR:PIRSR000446-1}. FT ACT_SITE 193 193 {ECO:0000256|PIRSR:PIRSR000446-1}. SQ SEQUENCE 293 AA; 32966 MW; F98A4FB033A88194 CRC64; MRAFVFPGQG SQYSGMAKDF SVYESSKEIF ERSKKVLGFD ITEIMNGDEE TLKLTENAQP SIYITSYIAF LELEKRGILP DVVAGHSLGE YTALAVAGVY DFETGLYLVR KRGEYMSKAL EPGKGTMAAV IGLNIETIEE VVNSIEGVYI ANYNSHDQVV ISGLKESVEK AMEILKEKGA RRVVELMVSS PFHTPFLEYA REKMKEEVEK VDFKKPRWPI VMNSTAKPTE NPEEIKRNII EQITGPVLWK QSVDTMKKMG VTEFVEVGPK TVLKNLCRRM GANAKHFTEI LSE // ID Q9WZL1_THEMA Unreviewed; 471 AA. AC Q9WZL1; G4FD71; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 102. DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:AGL49678.1}; DE EC=3.2.1.20 {ECO:0000313|EMBL:AGL49678.1}; DE SubName: Full=Alpha-glucosidase, putative {ECO:0000313|EMBL:AAD35834.1}; GN OrderedLocusNames=TM_0752 {ECO:0000313|EMBL:AAD35834.1}; GN ORFNames=Tmari_0753 {ECO:0000313|EMBL:AGL49678.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35834.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35834.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35834.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49678.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49678.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000256|RuleBase:RU361152}; CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. CC {ECO:0000256|RuleBase:RU361152}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35834.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49678.1; -; Genomic_DNA. DR PIR; F72337; F72337. DR RefSeq; NP_228561.1; NC_000853.1. DR RefSeq; WP_004080958.1; NZ_CP011107.1. DR PDB; 1VJT; X-ray; 2.50 A; A=1-471. DR PDBsum; 1VJT; -. DR STRING; 243274.TM0752; -. DR CAZy; GH4; Glycoside Hydrolase Family 4. DR DNASU; 898420; -. DR EnsemblBacteria; AAD35834; AAD35834; TM_0752. DR EnsemblBacteria; AGL49678; AGL49678; Tmari_0753. DR GeneID; 898420; -. DR KEGG; tma:TM0752; -. DR KEGG; tmi:THEMA_00890; -. DR KEGG; tmm:Tmari_0753; -. DR KEGG; tmw:THMA_0771; -. DR PATRIC; 23936426; VBITheMar51294_0765. DR eggNOG; ENOG4107V4V; Bacteria. DR eggNOG; COG1486; LUCA. DR KO; K01187; -. DR KO; K07406; -. DR OMA; RFYGMLP; -. DR OrthoDB; EOG6TJ7TJ; -. DR BioCyc; TMAR243274:GC6P-779-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR InterPro; IPR001088; Glyco_hydro_4. DR InterPro; IPR022616; Glyco_hydro_4_C. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF02056; Glyco_hydro_4; 1. DR Pfam; PF11975; Glyco_hydro_4C; 1. DR PRINTS; PR00732; GLHYDRLASE4. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF56327; SSF56327; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VJT}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361152, KW ECO:0000313|EMBL:AGL49678.1}; KW Hydrolase {ECO:0000256|RuleBase:RU361152, KW ECO:0000313|EMBL:AGL49678.1}; KW NAD {ECO:0000213|PDB:1VJT, ECO:0000256|RuleBase:RU361152}; KW Nucleotide-binding {ECO:0000213|PDB:1VJT}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 205 441 Glyco_hydro_4C. FT {ECO:0000259|Pfam:PF11975}. FT NP_BIND 38 40 NAD. {ECO:0000213|PDB:1VJT}. FT NP_BIND 85 86 NAD. {ECO:0000213|PDB:1VJT}. FT BINDING 10 10 NAD. {ECO:0000213|PDB:1VJT}. FT BINDING 160 160 NAD. {ECO:0000213|PDB:1VJT}. FT BINDING 310 310 NAD. {ECO:0000213|PDB:1VJT}. SQ SEQUENCE 471 AA; 55357 MW; 8C6921EB9978E9D8 CRC64; MKISIIGAGS VRFALQLVGD IAQTEELSRE DTHIYMMDVH ERRLNASYIL ARKYVEELNS PVKIVKTSSL DEAIDGADFI INTAYPYDPR YHDSGSQRWD EVTKVGEKHG YYRGIDSQEL NMVSTYTYVL SSYPDMKLAL EIAEKMKKMA PKAYLMQTAN PVFEITQAVR RWTGANIVGF CHGVAGVYEV FEKLDLDPEE VDWQVAGVNH GIWLNRFRYR GEDAYPLLDE WIEKKLPEWE PKNPWDTQMS PAAMDMYKFY GMLPIGDTVR NGSWKYHYNL ETKKKWFGKF GGIDNEVERP KFHEQLRRAR ERLIKLAEEV QQNPGMKLTE EHPEIFPKGK LSGEQHIPFI NAIANNKRVR LFLNVENQGT LKDFPDDVVM ELPVWVDCCG IHREKVEPDL THRIKIFYLW PRILRMEWNL EAYISRDRKV LEEILIRDPR TKSYEQIVQV LDEIFNLPFN EELRRYYKEK L // ID Q9X099_THEMA Unreviewed; 287 AA. AC Q9X099; G4FEZ2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36086.1}; GN OrderedLocusNames=TM_1004 {ECO:0000313|EMBL:AAD36086.1}; GN ORFNames=Tmari_1008 {ECO:0000313|EMBL:AGL49932.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36086.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36086.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36086.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49932.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49932.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36086.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49932.1; -; Genomic_DNA. DR PIR; F72307; F72307. DR RefSeq; NP_228812.1; NC_000853.1. DR RefSeq; WP_004080542.1; NZ_CP011107.1. DR SMR; Q9X099; 84-249. DR STRING; 243274.TM1004; -. DR EnsemblBacteria; AAD36086; AAD36086; TM_1004. DR EnsemblBacteria; AGL49932; AGL49932; Tmari_1008. DR GeneID; 897267; -. DR KEGG; tma:TM1004; -. DR KEGG; tmi:THEMA_09330; -. DR KEGG; tmm:Tmari_1008; -. DR KEGG; tmw:THMA_1027; -. DR PATRIC; 23936939; VBITheMar51294_1018. DR eggNOG; ENOG4105E37; Bacteria. DR eggNOG; COG2461; LUCA. DR KO; K09155; -. DR OMA; LCDIHME; -. DR OrthoDB; EOG63NMG2; -. DR BioCyc; TMAR243274:GC6P-1034-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR007380; DUF438. DR InterPro; IPR012312; Haemerythrin-like. DR Pfam; PF04282; DUF438; 1. DR Pfam; PF01814; Hemerythrin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 10 75 DUF438. {ECO:0000259|Pfam:PF04282}. FT DOMAIN 88 222 Hemerythrin. {ECO:0000259|Pfam:PF01814}. SQ SEQUENCE 287 AA; 33860 MW; 83C499B3275D0B29 CRC64; MEREKVELFK EVLKKLHKGE DVESLKKQFG ELLSQIPPFE IPVIEQELLK SGEIDVRDII KMCDLHVEFF RGAVSEAGRE IEKLPNGHPL RTLYEENKQI LKDAEALSLL ASSMFSLPKD DPRRKQFYEK LVQHVSELHR IGLTHYTREE MLIFPYIERR GITAVPTVLW SKHDETRLKI RLLLNLLKKE ESDERLKEEA LELSRMLSDM VFRENNILYP TLKVLLTEGE WKAIKMLEKD IGYYKIEVTE EWETPEKPLL PHRNCLRRPI PFRGLGGSRH VYHLQIQ // ID Q9X0V1_THEMA Unreviewed; 368 AA. AC Q9X0V1; G4FEC2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Putative regulator of mannose and mannoside utilization, ROK family {ECO:0000313|EMBL:AGL50155.1}; DE SubName: Full=Transcriptional regulator, XylR-related {ECO:0000313|EMBL:AAD36299.1}; GN OrderedLocusNames=TM_1224 {ECO:0000313|EMBL:AAD36299.1}; GN ORFNames=Tmari_1231 {ECO:0000313|EMBL:AGL50155.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36299.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36299.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36299.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50155.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50155.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36299.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50155.1; -; Genomic_DNA. DR PIR; A72278; A72278. DR RefSeq; NP_229029.1; NC_000853.1. DR RefSeq; WP_004080064.1; NZ_CP011107.1. DR PDB; 2HOE; X-ray; 2.46 A; A=1-368. DR PDBsum; 2HOE; -. DR STRING; 243274.TM1224; -. DR DNASU; 898260; -. DR EnsemblBacteria; AAD36299; AAD36299; TM_1224. DR EnsemblBacteria; AGL50155; AGL50155; Tmari_1231. DR GeneID; 898260; -. DR KEGG; tma:TM1224; -. DR KEGG; tmi:THEMA_08210; -. DR KEGG; tmm:Tmari_1231; -. DR KEGG; tmw:THMA_1250; -. DR PATRIC; 23937390; VBITheMar51294_1242. DR eggNOG; ENOG4105FEY; Bacteria. DR eggNOG; COG1940; LUCA. DR OMA; YENDATA; -. DR OrthoDB; EOG6CGCDC; -. DR BioCyc; TMAR243274:GC6P-1254-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR000600; ROK. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00480; ROK; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2HOE}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT METAL 184 184 Potassium. {ECO:0000213|PDB:2HOE}. FT METAL 187 187 Potassium. {ECO:0000213|PDB:2HOE}. FT METAL 214 214 Potassium; via carbonyl oxygen. FT {ECO:0000213|PDB:2HOE}. FT METAL 230 230 Potassium; via carbonyl oxygen. FT {ECO:0000213|PDB:2HOE}. SQ SEQUENCE 368 AA; 40887 MW; 086F07D6B2C53EC2 CRC64; MPKSVRAENI SRILKRIMKS PVSRVELAEE LGLTKTTVGE IAKIFLEKGI VVEEKDSPKG VGRPTKSLKI SPNCAYVLGI EVTRDEIAAC LIDASMNILA HEAHPLPSQS DREETLNVMY RIIDRAKDMM EKLGSKLSAL TVAAPGPIDT ERGIIIDPRN FPLSQIPLAN LLKEKYGIEV WVENDADMGA VGEKWYTKRD DSFAWILTGK GIGAGIIIDG ELYRGENGYA GEIGYTRVFN GNEYVFLEDV CNENVVLKHV LSMGFSSLAE ARDSGDVRVK EYFDDIARYF SIGLLNLIHL FGISKIVIGG FFKELGENFL KKIKIEVETH LLYKHSVDMS FSKVQEPVIA FGAAVHALEN YLERVTTS // ID Q9WZZ6_THEMA Unreviewed; 209 AA. AC Q9WZZ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35975.1}; GN OrderedLocusNames=TM_0894 {ECO:0000313|EMBL:AAD35975.1}; GN ORFNames=Tmari_0896 {ECO:0000313|EMBL:AGL49821.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35975.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35975.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35975.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49821.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49821.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35975.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49821.1; -; Genomic_DNA. DR PIR; G72321; G72321. DR RefSeq; NP_228702.1; NC_000853.1. DR RefSeq; WP_008193116.1; NZ_CP011107.1. DR PDB; 1ZTC; X-ray; 2.10 A; A/B/C/D=1-209. DR PDBsum; 1ZTC; -. DR STRING; 243274.TM0894; -. DR DNASU; 898568; -. DR EnsemblBacteria; AAD35975; AAD35975; TM_0894. DR EnsemblBacteria; AGL49821; AGL49821; Tmari_0896. DR GeneID; 898568; -. DR KEGG; tma:TM0894; -. DR KEGG; tmi:THEMA_00165; -. DR KEGG; tmm:Tmari_0896; -. DR KEGG; tmw:THMA_0916; -. DR PATRIC; 23936719; VBITheMar51294_0908. DR eggNOG; ENOG4108YGC; Bacteria. DR eggNOG; COG0491; LUCA. DR OMA; RVEFYDI; -. DR OrthoDB; EOG6T4S01; -. DR BioCyc; TMAR243274:GC6P-924-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1ZTC}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 22 199 Lactamase_B. {ECO:0000259|SMART:SM00849}. FT METAL 69 69 Nickel 1; via tele nitrogen. FT {ECO:0000213|PDB:1ZTC}. FT METAL 71 71 Nickel 1; via pros nitrogen. FT {ECO:0000213|PDB:1ZTC}. FT METAL 73 73 Nickel 2. {ECO:0000213|PDB:1ZTC}. FT METAL 74 74 Nickel 2; via tele nitrogen. FT {ECO:0000213|PDB:1ZTC}. FT METAL 140 140 Nickel 1; via tele nitrogen. FT {ECO:0000213|PDB:1ZTC}. FT METAL 162 162 Nickel 1. {ECO:0000213|PDB:1ZTC}. FT METAL 162 162 Nickel 2. {ECO:0000213|PDB:1ZTC}. FT METAL 199 199 Nickel 2; via tele nitrogen. FT {ECO:0000213|PDB:1ZTC}. FT BINDING 95 95 Phosphate. {ECO:0000213|PDB:1ZTC}. FT BINDING 142 142 Phosphate. {ECO:0000213|PDB:1ZTC}. FT BINDING 175 175 Phosphate. {ECO:0000213|PDB:1ZTC}. SQ SEQUENCE 209 AA; 23945 MW; 51F5A95005542A8F CRC64; MELKILVTGG NVFVPGRLNA HFSTVVYLEH KDRRIIIDPG NLSSMDELEE KFSELGISPD DITDVLFTHV HLDHIFNSVL FENATFYVHE VYKTKNYLSF GTIVGRIYSK VISSWKNVVL LKGEESLFDE KVKVFHTPWH AREHLSFLLD TENAGRVLIT GDITPNRLSY YDIIKGYGSV QVKNFLDRVG RIDLLVFPHD APLKPEVKK // ID Q9WZH3_THEMA Unreviewed; 205 AA. AC Q9WZH3; G4FDB0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35796.1}; GN OrderedLocusNames=TM_0714 {ECO:0000313|EMBL:AAD35796.1}; GN ORFNames=Tmari_0714 {ECO:0000313|EMBL:AGL49639.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35796.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35796.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35796.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49639.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49639.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35796.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49639.1; -; Genomic_DNA. DR PIR; A72344; A72344. DR RefSeq; NP_228523.1; NC_000853.1. DR RefSeq; WP_004081022.1; NZ_CP011107.1. DR STRING; 243274.TM0714; -. DR EnsemblBacteria; AAD35796; AAD35796; TM_0714. DR EnsemblBacteria; AGL49639; AGL49639; Tmari_0714. DR GeneID; 898381; -. DR KEGG; tma:TM0714; -. DR KEGG; tmi:THEMA_01095; -. DR KEGG; tmm:Tmari_0714; -. DR KEGG; tmw:THMA_0729; -. DR PATRIC; 23936346; VBITheMar51294_0726. DR eggNOG; ENOG410683J; Bacteria. DR eggNOG; ENOG410XV9X; LUCA. DR OMA; IYTEKND; -. DR OrthoDB; EOG62RSBP; -. DR BioCyc; TMAR243274:GC6P-740-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR010664; LipoPS_assembly_LptC-rel. DR Pfam; PF06835; LptC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 205 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972324. SQ SEQUENCE 205 AA; 23089 MW; FABCF94EE87109D2 CRC64; MKKSLIAFFI LVSLFAFSKT IHIKADFVKP SDERIEYSGS VVLKIEEENF TLNADNLIVK KLSGKWRITE ASSSVTVTLE DGELKGDTLI YDVETRVGTI TGNVKGEFID KTSTETIYIE CEQITFDLEE DVFQGAGKVK IQKGSVEANS EEVVYKRKDG IIELLRSVRL KDKEKDLEME AERVVMDLEE DTMEASSVTV TLEVE // ID Q9WY46_THEMA Unreviewed; 243 AA. AC Q9WY46; G4FHB7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 92. DE SubName: Full=ABC transporter, permease protein, cysTW family {ECO:0000313|EMBL:AAD35295.1}; DE SubName: Full=Hydroxymethylpyrimidine ABC transporter, transmembrane component {ECO:0000313|EMBL:AGL49127.1}; GN OrderedLocusNames=TM_0203 {ECO:0000313|EMBL:AAD35295.1}; GN ORFNames=Tmari_0201 {ECO:0000313|EMBL:AGL49127.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35295.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35295.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35295.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49127.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49127.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35295.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49127.1; -; Genomic_DNA. DR PIR; E72405; E72405. DR RefSeq; NP_228018.1; NC_000853.1. DR RefSeq; WP_004082869.1; NZ_CP011107.1. DR STRING; 243274.TM0203; -. DR EnsemblBacteria; AAD35295; AAD35295; TM_0203. DR EnsemblBacteria; AGL49127; AGL49127; Tmari_0201. DR GeneID; 897073; -. DR KEGG; tma:TM0203; -. DR KEGG; tmi:THEMA_03715; -. DR KEGG; tmm:Tmari_0201; -. DR KEGG; tmw:THMA_0210; -. DR PATRIC; 23935278; VBITheMar51294_0205. DR eggNOG; ENOG4107YPB; Bacteria. DR eggNOG; COG0600; LUCA. DR KO; K02050; -. DR OMA; DIYLPHI; -. DR OrthoDB; EOG6BPDMF; -. DR BioCyc; TMAR243274:GC6P-216-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0042959; F:alkanesulfonate transporter activity; IBA:GO_Central. DR GO; GO:0042918; P:alkanesulfonate transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 57 75 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 87 109 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 115 134 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 155 172 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 211 233 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 49 229 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 243 AA; 27379 MW; 8AB0DA16E5E8896C CRC64; MRAVFGILLV LIAWYLLHFL FPSSLILPGP VETFKVFIKM LNRETFEALL STLLKGLVST FIVIAVGLPV GFFMGISDRV YEFLRPLVTV VQAVPVVSWL VVVIFLWGIG WQGPVVISSL SLIPVAIFTT VSGVRSVDRK LLEVMKVYRV PRRMILKEVY LGSIWPFVLS ILEVSSGNVW KAVVMGEYLC GDSGLGVLIS WARQYVDVPR VYALTIFTVV LGISFERSVK VLARRVWKKW RLS // ID Q9X228_THEMA Unreviewed; 127 AA. AC Q9X228; G4FG89; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36769.1}; GN OrderedLocusNames=TM_1702 {ECO:0000313|EMBL:AAD36769.1}; GN ORFNames=Tmari_1710 {ECO:0000313|EMBL:AGL50634.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36769.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36769.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36769.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50634.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50634.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36769.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50634.1; -; Genomic_DNA. DR PIR; H72220; H72220. DR RefSeq; NP_229502.1; NC_000853.1. DR RefSeq; WP_004082218.1; NZ_CP011107.1. DR STRING; 243274.TM1702; -. DR EnsemblBacteria; AAD36769; AAD36769; TM_1702. DR EnsemblBacteria; AGL50634; AGL50634; Tmari_1710. DR GeneID; 896822; -. DR KEGG; tma:TM1702; -. DR KEGG; tmi:THEMA_05730; -. DR KEGG; tmm:Tmari_1710; -. DR KEGG; tmw:THMA_1744; -. DR PATRIC; 23938378; VBITheMar51294_1719. DR OMA; GISHFSI; -. DR OrthoDB; EOG6NSGJG; -. DR BioCyc; TMAR243274:GC6P-1750-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 127 AA; 14646 MW; 34D585A11A6A40C8 CRC64; MLKLEANYST IEKIVLKSTE GFSQFSLSKE DENLKVKLKH GSFPFSLSVK VKVVSTQKTP DDPIILKVGV PSFLMEMLKS RIEREGLEVH GNEIHIYPKK IARFFEDLIV SRLEFEDDRV ILHLEEV // ID Q9WY00_THEMA Unreviewed; 623 AA. AC Q9WY00; G4FH67; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35246.1}; GN OrderedLocusNames=TM_0153 {ECO:0000313|EMBL:AAD35246.1}; GN ORFNames=Tmari_0151 {ECO:0000313|EMBL:AGL49077.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35246.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35246.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35246.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49077.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49077.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35246.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49077.1; -; Genomic_DNA. DR PIR; G72412; G72412. DR RefSeq; NP_227968.1; NC_000853.1. DR RefSeq; WP_004082768.1; NZ_CP011107.1. DR STRING; 243274.TM0153; -. DR EnsemblBacteria; AAD35246; AAD35246; TM_0153. DR EnsemblBacteria; AGL49077; AGL49077; Tmari_0151. DR GeneID; 896989; -. DR KEGG; tma:TM0153; -. DR KEGG; tmi:THEMA_04035; -. DR KEGG; tmm:Tmari_0151; -. DR KEGG; tmw:THMA_0149; -. DR PATRIC; 23935150; VBITheMar51294_0152. DR eggNOG; ENOG4105E11; Bacteria. DR eggNOG; ENOG410XQIF; LUCA. DR OMA; PNQHIGA; -. DR OrthoDB; EOG6KQ6B5; -. DR BioCyc; TMAR243274:GC6P-154-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR032583; DUF4914. DR Pfam; PF16260; DUF4914; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 623 AA; 70731 MW; C28187B1D4D13C2E CRC64; MKTAILDRFV FSDEVRDIIE NAPEIIIPES RKEILDLAIA GRDLFEVGYE VPGKGFVVEA TVTRCKNGLV VNYPEPYMRR RDPNALVVGD NLETDKPRFR ERFGKEFEPI RQETFEWLKK QELILLPFMA GGYDYGYPAV LIAPKNAGFF VGGLADLQFF VPASEVPENF KPKLYMFLAP PFRHTHFDGK QVVVHYRHNS HYEIFSYNLY PGPSAKKGVY GFLLHVGEKE KWVTAHASAV KVITPYENEL VIMHEGASGG GKSEILEEIH REPDGRIKLA ENIVTGEKFY MELKQSCVLM PVADDMFMCH PKLQTGKKLV AKDAEAGWFI RVDHITEYGS APDLERLTIH PPEPLIFLNI YAVPNSTALI WEHIEDEPGK PCPNPRVIIP KRFMKNAVSE PVKVDVRSFG VRTPPCTKEK PTYGIVGLMQ ILPPALAWLW RLVAPRGHAN PSIVSTKGMT SEGVGSFWPF SSGKMVRLAN ILLEQIIDTP ETRYILVPNQ YIGAYKVGFM PEWIAREYLS RRGGVRFRPD QLVPSKCSLL GFSLKEMKIE GNTIPKELLQ PHLQSEVGEE AYEKGAQELK DFFKRELKKF LTEDLNPVGR EIIQCCLDDG SLDDYLKIIP MNF // ID Q9WYZ7_THEMA Unreviewed; 406 AA. AC Q9WYZ7; G4FDU4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 112. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TM_0527 {ECO:0000313|EMBL:AAD35612.1}; GN ORFNames=Tmari_0524 {ECO:0000313|EMBL:AGL49449.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35612.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35612.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35612.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49449.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49449.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Contains 1 Hflx-type G (guanine nucleotide-binding) CC domain. {ECO:0000256|HAMAP-Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35612.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49449.1; -; Genomic_DNA. DR PIR; E72366; E72366. DR RefSeq; NP_228337.1; NC_000853.1. DR RefSeq; WP_004081386.1; NZ_CP011107.1. DR STRING; 243274.TM0527; -. DR EnsemblBacteria; AAD35612; AAD35612; TM_0527. DR EnsemblBacteria; AGL49449; AGL49449; Tmari_0524. DR GeneID; 897579; -. DR KEGG; tma:TM0527; -. DR KEGG; tmm:Tmari_0524; -. DR KEGG; tmw:THMA_0540; -. DR PATRIC; 23935961; VBITheMar51294_0535. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; WVTKLEY; -. DR OrthoDB; EOG60SCM2; -. DR BioCyc; TMAR243274:GC6P-551-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00900}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 187 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NP_BIND 193 200 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 218 222 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 240 243 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 306 309 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT NP_BIND 330 332 GTP. {ECO:0000256|HAMAP-Rule:MF_00900}. FT COILED 153 180 {ECO:0000256|SAM:Coils}. FT METAL 200 200 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00900}. FT METAL 220 220 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 406 AA; 46476 MW; 7E4B3DEC1145160A CRC64; MIVAVGKDEE KIKESLEEMK GLCKTLGVEV VEWLWQKRAK PDPATYLGKG KLQKLKEVVE FCEADLVVVD DEITPVQYKN MQSELNVDVL DRTQVILEIF ARHATSEEGK LQVEMASLLY ELPRLVGKGE ELSRLGGGIG TRGPGEPLLE VLRRHIKNRI AQLRKRLKEI EQERNTQRKQ RLEKKIPHVS IVGYTNAGKS TLLKVLTDSD VYVADKLFAT LEPVTRRLKL KSGRVILVSD TVGFIRKLPH TIVSAFKATL EEIKYSDVLI HLVDASDPYL EEKMKASEKV LEEIGADKIP RILVFNKIDL CPRERIETLK WKYPEALFIS AEKRIGLDQL LDRLEEVISQ RDVQETLKVP LEKIGQIYAL KDRLEILNED YREGYALITL KTDRETLEML KRKVAS // ID Q9X1V6_THEMA Unreviewed; 222 AA. AC Q9X1V6; G4FG10; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=Glycerophosphoryl diester phosphodiesterase {ECO:0000313|EMBL:AGL50554.1}; DE EC=3.1.4.46 {ECO:0000313|EMBL:AGL50554.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36688.1}; GN OrderedLocusNames=TM_1621 {ECO:0000313|EMBL:AAD36688.1}; GN ORFNames=Tmari_1630 {ECO:0000313|EMBL:AGL50554.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36688.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36688.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36688.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50554.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50554.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36688.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50554.1; -; Genomic_DNA. DR PIR; G72232; G72232. DR RefSeq; NP_229421.1; NC_000853.1. DR RefSeq; WP_004082090.1; NZ_CP011107.1. DR PDB; 1O1Z; X-ray; 1.60 A; A=2-222. DR PDBsum; 1O1Z; -. DR STRING; 243274.TM1621; -. DR EnsemblBacteria; AAD36688; AAD36688; TM_1621. DR EnsemblBacteria; AGL50554; AGL50554; Tmari_1630. DR GeneID; 897683; -. DR KEGG; tma:TM1621; -. DR KEGG; tmi:THEMA_06140; -. DR KEGG; tmm:Tmari_1630; -. DR KEGG; tmw:THMA_1662; -. DR PATRIC; 23938216; VBITheMar51294_1640. DR eggNOG; ENOG41082N2; Bacteria. DR eggNOG; COG0584; LUCA. DR KO; K01126; -. DR OMA; NVPMEAI; -. DR OrthoDB; EOG6ZKXQR; -. DR BioCyc; TMAR243274:GC6P-1667-MONOMER; -. DR BRENDA; 3.1.4.46; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:UniProtKB-EC. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.190; -; 1. DR InterPro; IPR004129; GlyceroP-diester-Pdiesterase. DR InterPro; IPR030395; GP_PDE_dom. DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR PANTHER; PTHR23344; PTHR23344; 1. DR Pfam; PF03009; GDPD; 1. DR SUPFAM; SSF51695; SSF51695; 1. DR PROSITE; PS51704; GP_PDE; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O1Z}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50554.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 222 GP-PDE. {ECO:0000259|PROSITE:PS51704}. FT DOMAIN 15 48 PI-PLC X-box. FT {ECO:0000259|PROSITE:PS50007}. SQ SEQUENCE 222 AA; 25701 MW; BFE07C0D1E9A7684 CRC64; MIVLGHRGYS AKYLENTLEA FMKAIEAGAN GVELDVRLSK DGKVVVSHDE DLKRLFGLDV KIRDATVSEL KELTDGKITT LKEVFENVSD DKIINIEIKE REAADAVLEI SKKRKNLIFS SFDLDLLDEK FKGTKYGYLI DEENYGSIEN FVERVEKERP YSLHVPYQAF ELEYAVEVLR SFRKKGIVIF VWTLNDPEIY RKIRREIDGV ITDEVELFVK LR // ID Q9WYQ7_THEMA Unreviewed; 405 AA. AC Q9WYQ7; G4FHY5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AGL49348.1}; DE SubName: Full=PHT4-related protein {ECO:0000313|EMBL:AAD35511.1}; GN OrderedLocusNames=TM_0426 {ECO:0000313|EMBL:AAD35511.1}; GN ORFNames=Tmari_0423 {ECO:0000313|EMBL:AGL49348.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35511.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35511.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35511.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49348.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49348.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35511.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49348.1; -; Genomic_DNA. DR PIR; B72379; B72379. DR RefSeq; NP_228236.1; NC_000853.1. DR RefSeq; WP_004083303.1; NZ_CP011107.1. DR STRING; 243274.TM0426; -. DR DNASU; 897432; -. DR EnsemblBacteria; AAD35511; AAD35511; TM_0426. DR EnsemblBacteria; AGL49348; AGL49348; Tmari_0423. DR GeneID; 897432; -. DR KEGG; tma:TM0426; -. DR KEGG; tmi:THEMA_02595; -. DR KEGG; tmm:Tmari_0423; -. DR KEGG; tmw:THMA_0432; -. DR PATRIC; 23935737; VBITheMar51294_0432. DR eggNOG; ENOG4105CZR; Bacteria. DR eggNOG; COG0673; LUCA. DR OMA; YFRRAPW; -. DR OrthoDB; EOG61P6MW; -. DR BioCyc; TMAR243274:GC6P-441-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000683; Oxidoreductase_N. DR Pfam; PF01408; GFO_IDH_MocA; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 127 GFO_IDH_MocA. {ECO:0000259|Pfam:PF01408}. SQ SEQUENCE 405 AA; 46448 MW; FEA5FD1FAD94D3E8 CRC64; MKEISVVLVG IGGYGNKYVE YILREGREKG VRISGVVDPY PQNSRFYDEL RSLNVPMYNT LEEFYSHHTA DLAIISSPIH YHCEQTCTAV RNGSHVLCEK PAAATVKEVK KMIECREKYG KIVAIGYQWS YNPAVLKLKE DILAGKFGKP VLFKTLVLWP RDTAYYRRNS WAGKLKVNNR WVLDSVAGNA TAHFLHNMLF LLGEKMEESA YPESMVAELY RANDIESFDT CALKMTVRKI PVLFFATHAV KERKGPVFEY RFEKARVICN YPEYPESEEN LLVVYEDGRK EIYGPTDHGS MRKLWVVVDA ARGRKEFICT LESAMAHTIA INGAHVSMKE IQDFPTELKR VEGEPPMIWV EGLKEAMERA YEEEKIFSEL NLPWAKRGEE VKLENFEGLE GEITC // ID Q9X093_THEMA Unreviewed; 108 AA. AC Q9X093; G4FEZ8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 108. DE SubName: Full=Heavy metal resistance transcriptional regulator {ECO:0000313|EMBL:AAD36080.1}; DE SubName: Full=Regulatory protein, ArsR {ECO:0000313|EMBL:AGL49927.1}; GN OrderedLocusNames=TM_0998 {ECO:0000313|EMBL:AAD36080.1}; GN ORFNames=Tmari_1002 {ECO:0000313|EMBL:AGL49927.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36080.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36080.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36080.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49927.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49927.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 HTH arsR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36080.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49927.1; -; Genomic_DNA. DR PIR; H72306; H72306. DR RefSeq; NP_228806.1; NC_000853.1. DR RefSeq; WP_004080556.1; NZ_CP011107.1. DR STRING; 243274.TM0998; -. DR EnsemblBacteria; AAD36080; AAD36080; TM_0998. DR EnsemblBacteria; AGL49927; AGL49927; Tmari_1002. DR GeneID; 897771; -. DR KEGG; tma:TM0998; -. DR KEGG; tmi:THEMA_09360; -. DR KEGG; tmm:Tmari_1002; -. DR KEGG; tmw:THMA_1020; -. DR PATRIC; 23936927; VBITheMar51294_1012. DR eggNOG; ENOG41085QB; Bacteria. DR eggNOG; COG0640; LUCA. DR KO; K03892; -. DR OMA; CEMMEIL; -. DR OrthoDB; EOG6W9X9K; -. DR BioCyc; TMAR243274:GC6P-1028-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01022; HTH_5; 1. DR PRINTS; PR00778; HTHARSR. DR SMART; SM00418; HTH_ARSR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50987; HTH_ARSR_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000711}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU000711}; KW Transcription regulation {ECO:0000256|RuleBase:RU000711}. FT DOMAIN 1 88 HTH arsR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50987}. SQ SEQUENCE 108 AA; 12618 MW; F025A3595D10FE01 CRC64; MKLHELFHIL SNETRLKILT LLLEKEMCVC QILASIGTTQ PNISQHLHVL KNHGIVKSRR EDSFVYYSID ERFLEKYPFL ITILERARKE YGVKAVNSCS LQNLSNKE // ID Q9X1L2_THEMA Unreviewed; 145 AA. AC Q9X1L2; G4FFR4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Rubrerythrin {ECO:0000313|EMBL:AGL50458.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36593.1}; GN OrderedLocusNames=TM_1526 {ECO:0000313|EMBL:AAD36593.1}; GN ORFNames=Tmari_1534 {ECO:0000313|EMBL:AGL50458.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36593.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36593.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36593.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50458.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50458.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36593.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50458.1; -; Genomic_DNA. DR PIR; B72241; B72241. DR RefSeq; NP_229326.1; NC_000853.1. DR RefSeq; WP_004081893.1; NZ_CP011107.1. DR PDB; 1VJX; X-ray; 2.30 A; A=1-145. DR PDBsum; 1VJX; -. DR STRING; 243274.TM1526; -. DR EnsemblBacteria; AAD36593; AAD36593; TM_1526. DR EnsemblBacteria; AGL50458; AGL50458; Tmari_1534. DR GeneID; 897983; -. DR KEGG; tma:TM1526; -. DR KEGG; tmi:THEMA_06660; -. DR KEGG; tmm:Tmari_1534; -. DR KEGG; tmw:THMA_1560; -. DR PATRIC; 23938012; VBITheMar51294_1544. DR eggNOG; COG1633; LUCA. DR OMA; YLSGYAF; -. DR OrthoDB; EOG6KQ6GS; -. DR BioCyc; TMAR243274:GC6P-1566-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR003251; Rubrerythrin. DR Pfam; PF02915; Rubrerythrin; 1. DR SUPFAM; SSF47240; SSF47240; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VJX}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 140 Rubrerythrin. {ECO:0000259|Pfam:PF02915}. SQ SEQUENCE 145 AA; 17194 MW; 80F684DE0F07BAC3 CRC64; MKVSDILTVA IRLEEEGERF YRELSEHFNG EIKKTFLELA DQERIHAEIF RKMSDQENWD EVDSYLAGYA FYEVFPDTSE ILRRKDLTLK EVLDIAISVE KDSIILYYEL KDGLVNSDAQ KTVKKIIDQE KEHLRKLLEM KREST // ID Q9WYY1_THEMA Unreviewed; 192 AA. AC Q9WYY1; G4FDW0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35596.1}; DE SubName: Full=Uracil-DNA glycosylase, family 4 {ECO:0000313|EMBL:AGL49432.1}; GN OrderedLocusNames=TM_0511 {ECO:0000313|EMBL:AAD35596.1}; GN ORFNames=Tmari_0507 {ECO:0000313|EMBL:AGL49432.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35596.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35596.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35596.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49432.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49432.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35596.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49432.1; -; Genomic_DNA. DR PIR; E72368; E72368. DR RefSeq; NP_228321.1; NC_000853.1. DR RefSeq; WP_004081422.1; NZ_CP011107.1. DR PDB; 1L9G; X-ray; 2.50 A; A=1-192. DR PDB; 1VK2; X-ray; 1.90 A; A=1-192. DR PDBsum; 1L9G; -. DR PDBsum; 1VK2; -. DR STRING; 243274.TM0511; -. DR DNASU; 897555; -. DR EnsemblBacteria; AAD35596; AAD35596; TM_0511. DR EnsemblBacteria; AGL49432; AGL49432; Tmari_0507. DR GeneID; 897555; -. DR KEGG; tma:TM0511; -. DR KEGG; tmi:THEMA_02120; -. DR KEGG; tmm:Tmari_0507; -. DR KEGG; tmw:THMA_0523; -. DR PATRIC; 23935927; VBITheMar51294_0518. DR eggNOG; ENOG4108UN4; Bacteria. DR eggNOG; COG1573; LUCA. DR KO; K02334; -. DR OMA; DFYICNI; -. DR OrthoDB; EOG6S26GH; -. DR BioCyc; TMAR243274:GC6P-535-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.470.10; -; 1. DR InterPro; IPR005273; Ura-DNA_glyco_family4_dom. DR InterPro; IPR005122; Uracil-DNA_glycosylase-like. DR Pfam; PF03167; UDG; 1. DR SMART; SM00986; UDG; 1. DR SUPFAM; SSF52141; SSF52141; 1. DR TIGRFAMs; TIGR00758; UDG_fam4; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1L9G, ECO:0000213|PDB:1VK2}; KW 4Fe-4S {ECO:0000213|PDB:1L9G, ECO:0000213|PDB:1VK2}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000213|PDB:1L9G, ECO:0000213|PDB:1VK2}; KW Iron-sulfur {ECO:0000213|PDB:1L9G, ECO:0000213|PDB:1VK2}; KW Metal-binding {ECO:0000213|PDB:1L9G, ECO:0000213|PDB:1VK2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 32 182 UDG. {ECO:0000259|SMART:SM00986}. FT METAL 18 18 Iron-sulfur (4Fe-4S). FT {ECO:0000213|PDB:1L9G, FT ECO:0000213|PDB:1VK2}. FT METAL 21 21 Iron-sulfur (4Fe-4S). FT {ECO:0000213|PDB:1L9G, FT ECO:0000213|PDB:1VK2}. FT METAL 89 89 Iron-sulfur (4Fe-4S). FT {ECO:0000213|PDB:1L9G, FT ECO:0000213|PDB:1VK2}. FT METAL 105 105 Iron-sulfur (4Fe-4S). FT {ECO:0000213|PDB:1L9G, FT ECO:0000213|PDB:1VK2}. SQ SEQUENCE 192 AA; 21501 MW; 6978DE0721EF1BD1 CRC64; MYTREELMEI VSERVKKCTA CPLHLNRTNV VVGEGNLDTR IVFVGEGPGE EEDKTGRPFV GRAGMLLTEL LRESGIRRED VYICNVVKCR PPNNRTPTPE EQAACGHFLL AQIEIINPDV IVALGATALS FFVDGKKVSI TKVRGNPIDW LGGKKVIPTF HPSYLLRNRS NELRRIVLED IEKAKSFIKK EG // ID Q9WYU0_THEMA Unreviewed; 197 AA. AC Q9WYU0; G4FE01; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35553.1}; GN OrderedLocusNames=TM_0469 {ECO:0000313|EMBL:AAD35553.1}; GN ORFNames=Tmari_0466 {ECO:0000313|EMBL:AGL49391.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35553.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35553.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35553.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49391.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49391.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35553.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49391.1; -; Genomic_DNA. DR PIR; E72374; E72374. DR RefSeq; NP_228279.1; NC_000853.1. DR RefSeq; WP_004081497.1; NZ_CP011107.1. DR STRING; 243274.TM0469; -. DR EnsemblBacteria; AAD35553; AAD35553; TM_0469. DR EnsemblBacteria; AGL49391; AGL49391; Tmari_0466. DR GeneID; 897500; -. DR KEGG; tma:TM0469; -. DR KEGG; tmi:THEMA_02345; -. DR KEGG; tmm:Tmari_0466; -. DR KEGG; tmw:THMA_0478; -. DR PATRIC; 23935835; VBITheMar51294_0476. DR eggNOG; ENOG41085WF; Bacteria. DR eggNOG; COG5011; LUCA. DR OMA; TEGFHPK; -. DR OrthoDB; EOG6XQ3NQ; -. DR BioCyc; TMAR243274:GC6P-489-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR018768; DUF2344. DR Pfam; PF10105; DUF2344; 1. DR TIGRFAMs; TIGR03936; sam_1_link_chp; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 125 DUF2344. {ECO:0000259|Pfam:PF10105}. SQ SEQUENCE 197 AA; 22919 MW; 41E2C8E3C09180EC CRC64; MKIVLRFKKK GMRRFLSTLE SIKLVERSIR RADFSIVFTE GFHPKPKMSF LDAMPVGVVN LAFYVELFVK NISEKHIETL KSILPKDFAL ESAWIFDGNI NELVNSYRFL VISEKPVDLE KTILKKNKKV SFKESLLDFE ISSGKKYHIF RYTQKREKLI NPLLLAEEGT FFLPICEEAM TEHGPLSSLL ERRGTRV // ID Q9WY18_THEMA Unreviewed; 151 AA. AC Q9WY18; G4FH85; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Hydrolase, HAD subfamily IIIA {ECO:0000313|EMBL:AGL49095.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35264.1}; GN OrderedLocusNames=TM_0171 {ECO:0000313|EMBL:AAD35264.1}; GN ORFNames=Tmari_0169 {ECO:0000313|EMBL:AGL49095.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35264.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35264.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35264.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49095.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49095.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35264.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49095.1; -; Genomic_DNA. DR PIR; A72409; A72409. DR RefSeq; NP_227986.1; NC_000853.1. DR RefSeq; WP_004082803.1; NZ_CP011107.1. DR STRING; 243274.TM0171; -. DR EnsemblBacteria; AAD35264; AAD35264; TM_0171. DR EnsemblBacteria; AGL49095; AGL49095; Tmari_0169. DR GeneID; 897010; -. DR KEGG; tma:TM0171; -. DR KEGG; tmi:THEMA_03945; -. DR KEGG; tmm:Tmari_0169; -. DR KEGG; tmw:THMA_0167; -. DR PATRIC; 23935190; VBITheMar51294_0172. DR eggNOG; ENOG4108WJV; Bacteria. DR eggNOG; COG2179; LUCA. DR KO; K07015; -. DR OMA; IWRAGKP; -. DR OrthoDB; EOG66B44K; -. DR BioCyc; TMAR243274:GC6P-172-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006549; HAD-SF_hydro_IIIA. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|SAAS:SAAS00455242, KW ECO:0000313|EMBL:AGL49095.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 151 AA; 17835 MW; D854245206F03B0A CRC64; MKVERVERVE DIDFEGLLKE GYTCFFFDFD NTLVPWKESK LEESKRRLLI ELAKKARVVV VSNGKPRKVD LPVMFIWRAG KPFSLKLWRF LKKEKIDPKR CVMIGDQIFT DVLTGKIFGF RVIKVEPISA KEFFGTKILR FFEKILEGKV R // ID Q9WYC3_THEMA Unreviewed; 577 AA. AC Q9WYC3; G4FHK1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 121. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35375.1}; DE SubName: Full=Lipid A export ATP-binding/permease protein MsbA {ECO:0000313|EMBL:AGL49211.1}; GN OrderedLocusNames=TM_0287 {ECO:0000313|EMBL:AAD35375.1}; GN ORFNames=Tmari_0285 {ECO:0000313|EMBL:AGL49211.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35375.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35375.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35375.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49211.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49211.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35375.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49211.1; -; Genomic_DNA. DR PIR; E72396; E72396. DR RefSeq; NP_228099.1; NC_000853.1. DR RefSeq; WP_004083000.1; NZ_CP011107.1. DR PDB; 3QF4; X-ray; 2.90 A; A=2-577. DR PDB; 4Q4A; X-ray; 2.60 A; A=2-577. DR PDB; 4Q4H; X-ray; 2.53 A; A=2-577. DR PDB; 4Q4J; X-ray; 3.20 A; A=2-577. DR PDB; 4Q7K; X-ray; 1.80 A; A=330-577. DR PDBsum; 3QF4; -. DR PDBsum; 4Q4A; -. DR PDBsum; 4Q4H; -. DR PDBsum; 4Q4J; -. DR PDBsum; 4Q7K; -. DR STRING; 243274.TM0287; -. DR TCDB; 3.A.1.135.5; the atp-binding cassette (abc) superfamily. DR DNASU; 897207; -. DR EnsemblBacteria; AAD35375; AAD35375; TM_0287. DR EnsemblBacteria; AGL49211; AGL49211; Tmari_0285. DR GeneID; 897207; -. DR KEGG; tma:TM0287; -. DR KEGG; tmi:THEMA_03290; -. DR KEGG; tmm:Tmari_0285; -. DR KEGG; tmw:THMA_0294; -. DR PATRIC; 23935453; VBITheMar51294_0292. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K06147; -. DR OMA; FRYFENT; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-300-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0034040; F:lipid-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006869; P:lipid transport; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3QF4, ECO:0000213|PDB:4Q4A, KW ECO:0000213|PDB:4Q4H, ECO:0000213|PDB:4Q4J}; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35375.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Magnesium {ECO:0000213|PDB:3QF4, ECO:0000213|PDB:4Q4A}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000213|PDB:3QF4, ECO:0000213|PDB:4Q4A}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35375.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 133 151 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 174 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 229 258 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 278 297 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 16 298 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 332 567 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT NP_BIND 368 374 ATP analog. {ECO:0000213|PDB:3QF4, FT ECO:0000213|PDB:4Q4A}. FT METAL 373 373 Magnesium. {ECO:0000213|PDB:3QF4}. FT METAL 414 414 Magnesium. {ECO:0000213|PDB:3QF4}. FT BINDING 105 105 ATP analog. {ECO:0000213|PDB:4Q4A}. FT BINDING 341 341 ATP analog. {ECO:0000213|PDB:3QF4, FT ECO:0000213|PDB:4Q4A}. FT BINDING 414 414 ATP analog. {ECO:0000213|PDB:3QF4, FT ECO:0000213|PDB:4Q4A}. SQ SEQUENCE 577 AA; 64360 MW; A53DFED7694B8F44 CRC64; MKTLARYLKP YWIFAVLAPL FMVVEVICDL SQPTLLARIV DEGIARGDFS LVLKTGILML IVALIGAVGG IGCTVFASYA SQNFGADLRR DLFRKVLSFS ISNVNRFHTS SLITRLTNDV TQLQNLVMML LRIVVRAPLL FVGGIVMAVS INVKLSSVLI FLIPPIVLLF VWLTKKGNPL FRKIQESTDE VNRVVRENLL GVRVVRAFRR EEYENENFRK ANESLRRSII SAFSLIVFAL PLFIFIVNMG MIAVLWFGGV LVRNNQMEIG SIMAYTNYLM QIMFSLMMIG NILNFIVRAS ASAKRVLEVL NEKPAIEEAD NALALPNVEG SVSFENVEFR YFENTDPVLS GVNFSVKPGS LVAVLGETGS GKSTLMNLIP RLIDPERGRV EVDELDVRTV KLKDLRGHIS AVPQETVLFS GTIKENLKWG REDATDDEIV EAAKIAQIHD FIISLPEGYD SRVERGGRNF SGGQKQRLSI ARALVKKPKV LILDDCTSSV DPITEKRILD GLKRYTKGCT TFIITQKIPT ALLADKILVL HEGKVAGFGT HKELLEHCKP YREIYESQFG NGVMNDA // ID Q9WYV2_THEMA Unreviewed; 1415 AA. AC Q9WYV2; G4FDY8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=(R)-2-hydroxyglutaryl-CoA dehydratase activator-related protein {ECO:0000313|EMBL:AAD35567.1}; GN OrderedLocusNames=TM_0482 {ECO:0000313|EMBL:AAD35567.1}; GN ORFNames=Tmari_0479 {ECO:0000313|EMBL:AGL49404.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35567.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35567.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35567.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49404.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49404.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35567.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49404.1; -; Genomic_DNA. DR PIR; A72369; A72369. DR RefSeq; NP_228292.1; NC_000853.1. DR RefSeq; WP_004081484.1; NZ_CP011107.1. DR STRING; 243274.TM0482; -. DR EnsemblBacteria; AAD35567; AAD35567; TM_0482. DR EnsemblBacteria; AGL49404; AGL49404; Tmari_0479. DR GeneID; 897521; -. DR KEGG; tma:TM0482; -. DR KEGG; tmi:THEMA_02260; -. DR KEGG; tmm:Tmari_0479; -. DR KEGG; tmw:THMA_0495; -. DR PATRIC; 23935869; VBITheMar51294_0489. DR eggNOG; ENOG4105CIZ; Bacteria. DR eggNOG; COG1924; LUCA. DR eggNOG; COG3580; LUCA. DR eggNOG; COG3581; LUCA. DR OMA; GEIYVRR; -. DR OrthoDB; EOG6B6258; -. DR BioCyc; TMAR243274:GC6P-506-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR002731; ATPase_BadF. DR InterPro; IPR018709; CoA_activase_DUF2229. DR InterPro; IPR008275; CoA_E_activase. DR Pfam; PF01869; BcrAD_BadFG; 2. DR Pfam; PF09989; DUF2229; 1. DR TIGRFAMs; TIGR00241; CoA_E_activ; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 76 233 BcrAD_BadFG. {ECO:0000259|Pfam:PF01869}. FT DOMAIN 286 539 BcrAD_BadFG. {ECO:0000259|Pfam:PF01869}. FT DOMAIN 640 849 DUF2229. {ECO:0000259|Pfam:PF09989}. SQ SEQUENCE 1415 AA; 159943 MW; 5D7DAD84F9F8AD01 CRC64; MTGVCIGSSS VSFYSEKEKG NLPHNGDPLA LLSMMIPTFL DEGPVVITGR KTRKIIDLPQ ISEAEATEIA YRHLIKKYGK VEAVVSAGGE NTILYRVNDK GIITGIYTGS KCASGTGEFF LQQLQRMGIS LEEANSVETE EYYELSSRCT VFCKSDCTHA LNKGVPKELV LNGLGKVMAD KIVELAHKAG VKKVLLVGGT TRNRLMLKHL ERVLEVIVPE EALFFEAYGA YLWGKLNGVV SKKTFTIKKE EITSFPTHEP LKKYLHMVEF KEMPFQQARD GDVCVLGIDV GSTTTKAVLM RYDDEAILAG VYLRTLGDPI RAARQCYSSI LEQLNGTKVK IIGLGVTGSG RKIVGLYSQT DAVYNEIMAH AKAAAHFDPE VDTIFEIGGQ DAKYTYLVNG VPADYAMNEA CSAGTGSFLE EAAGESLGVH YTEIGDLALK GENPPNFSDQ CAAFIGSDVK TAVNEGISKE DICAGLVYSV CMNYLNRVKG SRPVGKKIFM QGGVCYNKAV PVAMAALVGK SIVVPPHPGL MGAYGVALLT KENLELGFLE KKEFKLKELI SREVRYRGTF ICPGGKEKCD RKCEIRIIEI DGKRFPFGGA CNRYENVLRH ANIDSTKYNF VKNREKYIFH FKREVKGTKT IGLSRSLAMN NLFPLFYTFL TELGFDVVIP EKSDRRGWEM MNSEFCFPVE LSHGYMYDLI SKNPDLIFVP RLRGIKVENS ENYNVFCPFV QSEVDWLTSA FPELEEKLVT GYFDFSRGDE KEEFLRVAER LGRSREEGER AFEKAWKAFN ERFNLIKKQW DEFLKVLDES EFGVVLFGRS YNAFSSDANM GIPEKFATRG IPIINFDSIP FEDEKGYRNM YWSWGEMILK AARFVEKHPK LFGVYITNFS CGPDSFIISY FRDIMAKKPS LVLELDSHTA DAGIETRIEA FIDIVKSYLR LQRKNEERKS AKRPQTVLEK NTLYVITPDG ERLRLNDERV KVVFPSMGQF GSQCLSAAFR YYGVRSDVCP PPDVEEFKLG RGNSLSKECL PLQLTLGSLI KYIREKATDD EIILYFMPET MGPCRFGQYS VFMNLWLDRN NVRNVTLFGL NSENAYAGLG IAFRIRAWLA IVVSDVFFDV ERAVMTLARD KEEAKKVLEG CREKILNSLA NDSLRDFFKT LDEVSEILSG VERIMDYEKA PKVLLTGEIY VRRDEFSRKH LENLMEKNGI IMHISPVHEW IYYTDYLYLN RLISPNSTRV DRLKKRIEIL VKRYVERRVK KILEKSGFYR VQMVDVEAIV DAAKDYLNPK LTGEAILTIG TILHEIVNHY DGVISIGPFG CMPSRIAEAV VKKGLKEQKE KTTGVLRKVL DEFGDLPVIH IESDGNPFTP TVQSKLEAFM FQVRRLRNYL NGLLNTENTL EETEETLPEN IRVDS // ID Q9WZX2_THEMA Unreviewed; 221 AA. AC Q9WZX2; G4FCV6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=Glutaredoxin-like protein {ECO:0000313|EMBL:AGL49795.1}; DE SubName: Full=Glutaredoxin-related protein {ECO:0000313|EMBL:AAD35950.1}; GN OrderedLocusNames=TM_0868 {ECO:0000313|EMBL:AAD35950.1}; GN ORFNames=Tmari_0870 {ECO:0000313|EMBL:AGL49795.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35950.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35950.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35950.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49795.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49795.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35950.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49795.1; -; Genomic_DNA. DR PIR; G72322; G72322. DR RefSeq; NP_228677.1; NC_000853.1. DR RefSeq; WP_004080736.1; NZ_CP011107.1. DR STRING; 243274.TM0868; -. DR EnsemblBacteria; AAD35950; AAD35950; TM_0868. DR EnsemblBacteria; AGL49795; AGL49795; Tmari_0870. DR GeneID; 898541; -. DR KEGG; tma:TM0868; -. DR KEGG; tmi:THEMA_00295; -. DR KEGG; tmm:Tmari_0870; -. DR KEGG; tmw:THMA_0890; -. DR PATRIC; 23936664; VBITheMar51294_0881. DR eggNOG; ENOG4108UYR; Bacteria. DR eggNOG; COG0526; LUCA. DR OMA; MVEAIEY; -. DR OrthoDB; EOG6HTNW9; -. DR BioCyc; TMAR243274:GC6P-898-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 2. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR011903; Glutaredoxin-like_dom. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF13192; Thioredoxin_3; 2. DR SUPFAM; SSF52833; SSF52833; 2. DR TIGRFAMs; TIGR02187; GlrX_arch; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 127 221 Glutaredoxin. FT {ECO:0000259|PROSITE:PS51354}. SQ SEQUENCE 221 AA; 25158 MW; BF535BF2703D4E2E CRC64; MGILSDKDIA YLKDLFGKEL KRKVKIVFFK TEDKTRCQYC EITEQVLEEL VSVDPKLELE IHDFDSDKEA VEKYQVEMVP ATILLPEDGK DYGIRFYGVP SGHEFGTLIQ DIITVSEGKP QLSEESIQKL QSLEEPIRIS VFVTPTCPYC PRAVLMAHNM AMASDKIIGE MIEANEYWEL SEKFGVSSVP HIVVNRDPSK FFVGAYPEKE FINEVLRLAK G // ID Q9WZS1_THEMA Unreviewed; 364 AA. AC Q9WZS1; G4FD10; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 102. DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000256|PIRNR:PIRNR038994}; DE EC=3.5.1.25 {ECO:0000256|PIRNR:PIRNR038994}; GN OrderedLocusNames=TM_0814 {ECO:0000313|EMBL:AAD35896.1}; GN ORFNames=Tmari_0815 {ECO:0000313|EMBL:AGL49740.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35896.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35896.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35896.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49740.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49740.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: N-acetyl-D-glucosamine 6-phosphate + H(2)O = CC D-glucosamine 6-phosphate + acetate. CC {ECO:0000256|PIRNR:PIRNR038994}. CC -!- SIMILARITY: Belongs to the nagA family. CC {ECO:0000256|PIRNR:PIRNR038994}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35896.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49740.1; -; Genomic_DNA. DR PIR; G72331; G72331. DR RefSeq; NP_228623.1; NC_000853.1. DR RefSeq; WP_004080848.1; NZ_CP011107.1. DR PDB; 1O12; X-ray; 2.50 A; A/B=1-364. DR PDBsum; 1O12; -. DR STRING; 243274.TM0814; -. DR EnsemblBacteria; AAD35896; AAD35896; TM_0814. DR EnsemblBacteria; AGL49740; AGL49740; Tmari_0815. DR GeneID; 898482; -. DR KEGG; tma:TM0814; -. DR KEGG; tmi:THEMA_00580; -. DR KEGG; tmm:Tmari_0815; -. DR KEGG; tmw:THMA_0833; -. DR PATRIC; 23936548; VBITheMar51294_0826. DR eggNOG; ENOG4105CE4; Bacteria. DR eggNOG; COG1820; LUCA. DR KO; K01443; -. DR OMA; KRITHFP; -. DR OrthoDB; EOG6W45T4; -. DR BioCyc; TMAR243274:GC6P-841-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central. DR Gene3D; 2.30.40.10; -; 3. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR003764; GlcNAc_6-P_deAcase. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF01979; Amidohydro_1; 1. DR PIRSF; PIRSF038994; NagA; 1. DR SUPFAM; SSF51338; SSF51338; 2. DR SUPFAM; SSF51556; SSF51556; 1. DR TIGRFAMs; TIGR00221; nagA; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O12}; KW Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR038994}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR038994, KW ECO:0000313|EMBL:AGL49740.1}; Iron {ECO:0000213|PDB:1O12}; KW Metal-binding {ECO:0000213|PDB:1O12}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 40 360 Amidohydro-rel. FT {ECO:0000259|Pfam:PF01979}. FT REGION 200 201 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR038994-2}. FT REGION 288 290 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR038994-2}. FT ACT_SITE 255 255 Proton donor/acceptor. FT {ECO:0000256|PIRSR:PIRSR038994-1}. FT METAL 115 115 Iron. {ECO:0000213|PDB:1O12}. FT METAL 176 176 Iron; via tele nitrogen. FT {ECO:0000213|PDB:1O12}. FT METAL 197 197 Iron; via tele nitrogen. FT {ECO:0000213|PDB:1O12}. FT BINDING 126 126 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR038994-2}. FT BINDING 208 208 Substrate. FT {ECO:0000256|PIRSR:PIRSR038994-2}. FT BINDING 232 232 Substrate; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR038994-2}. SQ SEQUENCE 364 AA; 40202 MW; 54FA26A32F830221 CRC64; MIVEKVLIVD PIDGEFTGDV EIEEGKIVKV EKRECIPRGV LMPGFVDPHI HGVVGADTMN CDFSEMEEFL YSQGVTTFLA TTVSTSLEKM KEILRKARDY ILENPSTSLL GVHLEGPYIS KEKKGAHSEK HIRPPSEREL SEIDSPAKML TFAPEIESSE LLLRLVKRDI VLSAGHSIAT FEEFMKFYKE GVKRITHFPN GLKPLHHREI GITGAGLLLD DVKLELICDG VHLSREMVKL VYKVKKANGI VLVTDSISAA GLKDGTTTLG DLVVKVKDGV PRLEDGTLAG STLFFSQAVK NFRKFTGCSI TELAKVSSYN SCVELGLDDR GRIAEGTRAD LVLLDEDLNV VMTIKEGEVV FRSR // ID Q9WZX0_THEMA Unreviewed; 305 AA. AC Q9WZX0; G4FCV8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Putative stomatin/prohibitin-family membrane protease subunit YbbK {ECO:0000313|EMBL:AGL49793.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35948.1}; GN OrderedLocusNames=TM_0866 {ECO:0000313|EMBL:AAD35948.1}; GN ORFNames=Tmari_0868 {ECO:0000313|EMBL:AGL49793.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35948.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35948.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35948.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49793.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49793.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35948.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49793.1; -; Genomic_DNA. DR PIR; E72322; E72322. DR RefSeq; NP_228675.1; NC_000853.1. DR RefSeq; WP_004080738.1; NZ_CP011107.1. DR STRING; 243274.TM0866; -. DR EnsemblBacteria; AAD35948; AAD35948; TM_0866. DR EnsemblBacteria; AGL49793; AGL49793; Tmari_0868. DR GeneID; 898539; -. DR KEGG; tma:TM0866; -. DR KEGG; tmi:THEMA_00305; -. DR KEGG; tmm:Tmari_0868; -. DR KEGG; tmw:THMA_0888; -. DR PATRIC; 23936660; VBITheMar51294_0879. DR eggNOG; ENOG4105C36; Bacteria. DR eggNOG; COG0330; LUCA. DR OMA; SRERINM; -. DR OrthoDB; EOG6J48MH; -. DR BioCyc; TMAR243274:GC6P-896-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR001107; Band_7. DR InterPro; IPR018080; Band_7/stomatin-like_CS. DR InterPro; IPR001972; Stomatin_fam. DR PANTHER; PTHR10264; PTHR10264; 1. DR Pfam; PF01145; Band_7; 1. DR PRINTS; PR00721; STOMATIN. DR SMART; SM00244; PHB; 1. DR SUPFAM; SSF117892; SSF117892; 1. DR PROSITE; PS01270; BAND_7; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49793.1}; KW Protease {ECO:0000313|EMBL:AGL49793.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 18 175 PHB. {ECO:0000259|SMART:SM00244}. SQ SEQUENCE 305 AA; 34547 MW; 0355346FB1C570E6 CRC64; MLIALVVLVF FLIVLAASSI RIVRPYERGL VERLGKFKRE VGAGVHFIIP FFERMIKVDM REKVIDVPPQ EVITRDNVVV TVDAVIYYEI TDAYRVVYNV SNFEMATIKL AQTNLRNVIG ELELDQTLTS RERINMKLRT VLDEATDKWG VRITRVEIKK IDPPQDITDA MSKQMKAERT KRAAILEAEG YKQAEILKAE GQKNAAILRA EGEAEAIKRV AEANMQKLIL EARGQAEAIK LVFNAIHEGN PTKDLLTVRY LETLKEMANG QATKIFLPFE ASSILASLGA ISEIFKKEEN KRDEK // ID Q9X1R2_THEMA Unreviewed; 267 AA. AC Q9X1R2; G4FFW4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Hemolysin {ECO:0000313|EMBL:AAD36643.1}; DE SubName: Full=RNA binding methyltransferase FtsJ like protein {ECO:0000313|EMBL:AGL50508.1}; GN OrderedLocusNames=TM_1576 {ECO:0000313|EMBL:AAD36643.1}; GN ORFNames=Tmari_1584 {ECO:0000313|EMBL:AGL50508.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36643.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36643.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36643.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50508.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50508.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36643.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50508.1; -; Genomic_DNA. DR PIR; A72238; A72238. DR RefSeq; NP_229376.1; NC_000853.1. DR RefSeq; WP_004081998.1; NZ_CP011107.1. DR STRING; 243274.TM1576; -. DR EnsemblBacteria; AAD36643; AAD36643; TM_1576. DR EnsemblBacteria; AGL50508; AGL50508; Tmari_1584. DR GeneID; 897545; -. DR KEGG; tma:TM1576; -. DR KEGG; tmi:THEMA_06400; -. DR KEGG; tmm:Tmari_1584; -. DR KEGG; tmw:THMA_1611; -. DR PATRIC; 23938116; VBITheMar51294_1595. DR eggNOG; ENOG4105DX0; Bacteria. DR eggNOG; COG1189; LUCA. DR KO; K06442; -. DR OMA; QVLVNKM; -. DR OrthoDB; EOG6VB6ZH; -. DR BioCyc; TMAR243274:GC6P-1617-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR Gene3D; 3.10.290.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR004538; Haemolysin_A/TlyA. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR002942; S4_RNA-bd. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01728; FtsJ; 1. DR Pfam; PF01479; S4; 1. DR PIRSF; PIRSF005578; TlyA; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00478; tly; 1. DR PROSITE; PS50889; S4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Methyltransferase {ECO:0000313|EMBL:AGL50508.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL50508.1}. FT DOMAIN 5 65 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 267 AA; 30045 MW; F47AAEE2F2AE6092 CRC64; MADKKRLDQL VLERGLVESR EKAKVLILAG KVLVNGERVT KASKLVPEDA NVELLEEPKY VSRGGYKLES AFESFKIDVS GKVACDIGAS TGGFTDFLLQ RGAKKVYAVD VGYGQLHWKL RNDPRVVVME KVNARYLNPD DLGEKVDVVT CDVSFISLKK IIPAISRILK NIGDAVLLVK PQFEAPRKFV KKGIVKDPGV HLEVLEEIRK SLIENGFVVK GCCFSKIKGT EGNIEYFFWV KKEGENAEID LRKIVEEAWR FFGERER // ID Q9X0B4_THEMA Unreviewed; 153 AA. AC Q9X0B4; G4FEX4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36101.1}; GN OrderedLocusNames=TM_1024 {ECO:0000313|EMBL:AAD36101.1}; GN ORFNames=Tmari_1026 {ECO:0000313|EMBL:AGL49950.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36101.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36101.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36101.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49950.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49950.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36101.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49950.1; -; Genomic_DNA. DR PIR; G72302; G72302. DR RefSeq; NP_228830.1; NC_000853.1. DR RefSeq; WP_004080504.1; NZ_CP011107.1. DR STRING; 243274.TM1024; -. DR EnsemblBacteria; AAD36101; AAD36101; TM_1024. DR EnsemblBacteria; AGL49950; AGL49950; Tmari_1026. DR GeneID; 897336; -. DR KEGG; tma:TM1024; -. DR KEGG; tmi:THEMA_09240; -. DR KEGG; tmm:Tmari_1026; -. DR KEGG; tmw:THMA_1045; -. DR PATRIC; 23936977; VBITheMar51294_1037. DR BioCyc; TMAR243274:GC6P-1053-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.10.109.10; -; 1. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR Pfam; PF00717; Peptidase_S24; 1. DR SUPFAM; SSF51306; SSF51306; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 61 107 Peptidase_S24. FT {ECO:0000259|Pfam:PF00717}. SQ SEQUENCE 153 AA; 17720 MW; DDEB0327B5FDE234 CRC64; MEEKVEFILE VRSIPVYGDE FSPRLRKFFP IDYEPVERVT VPTSKKADYA VMISSNLKPF SIKEGDYILI SLDDEPQEGD LVAVLVKDFR ITVGRVKERQ EDIFVVEVGN EVGIYRCFIF PYLDQLHRSS FELSFNPYVL GKITAILRKK PAH // ID Q9X217_THEMA Unreviewed; 292 AA. AC Q9X217; G4FG78; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Protein YicC {ECO:0000313|EMBL:AGL50623.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36758.1}; GN OrderedLocusNames=TM_1691 {ECO:0000313|EMBL:AAD36758.1}; GN ORFNames=Tmari_1699 {ECO:0000313|EMBL:AGL50623.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36758.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36758.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36758.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50623.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50623.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36758.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50623.1; -; Genomic_DNA. DR PIR; E72223; E72223. DR RefSeq; NP_229491.1; NC_000853.1. DR RefSeq; WP_004082207.1; NZ_CP011107.1. DR STRING; 243274.TM1691; -. DR EnsemblBacteria; AAD36758; AAD36758; TM_1691. DR EnsemblBacteria; AGL50623; AGL50623; Tmari_1699. DR GeneID; 897894; -. DR KEGG; tma:TM1691; -. DR KEGG; tmi:THEMA_05785; -. DR KEGG; tmm:Tmari_1699; -. DR KEGG; tmw:THMA_1733; -. DR PATRIC; 23938356; VBITheMar51294_1708. DR eggNOG; ENOG4105DSJ; Bacteria. DR eggNOG; COG1561; LUCA. DR OMA; PGYLSMK; -. DR OrthoDB; EOG61KBKV; -. DR BioCyc; TMAR243274:GC6P-1739-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR005229; CHP00255. DR InterPro; IPR013551; DUF1732. DR InterPro; IPR013527; YicC-like_N. DR Pfam; PF08340; DUF1732; 1. DR Pfam; PF03755; YicC_N; 1. DR TIGRFAMs; TIGR00255; TIGR00255; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 154 YicC_N. {ECO:0000259|Pfam:PF03755}. FT DOMAIN 209 292 DUF1732. {ECO:0000259|Pfam:PF08340}. SQ SEQUENCE 292 AA; 33717 MW; B904929EE1D311E7 CRC64; MIKSMTGFSR VEKVSGPYQF RVEMKSLNSK GLNIINQLPG YLSMKEIELN NLVQEYVSRG KVQTRVQVKF LEPPKVLEID KNVVRAYYSM LDEIVGELSL PEPVKLSDLL NFREVFRIEL SDEEIENIWN HLVPILREAL EKLVEERKKE GQKIGADLKR ILEDLSSRVE EIEKISDQLP ALYREKIKEE VEKILPQDVS VKEDILENHV AFMATKADIR EEITRLRSHI KRALELIESD EPVGMNLDFL GQEMLRELNT ILSKSISGEI TSLALEGKVL VSQFREQIQN VE // ID Q9WYL6_THEMA Unreviewed; 651 AA. AC Q9WYL6; G4FHU6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 83. DE SubName: Full=Ribonucleotide reductase of class III (Anaerobic), large subunit {ECO:0000313|EMBL:AGL49308.1}; DE EC=1.17.4.2 {ECO:0000313|EMBL:AGL49308.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35470.1}; GN OrderedLocusNames=TM_0385 {ECO:0000313|EMBL:AAD35470.1}; GN ORFNames=Tmari_0383 {ECO:0000313|EMBL:AGL49308.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35470.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35470.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35470.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49308.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49308.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35470.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49308.1; -; Genomic_DNA. DR PIR; A72384; A72384. DR RefSeq; NP_228195.1; NC_000853.1. DR RefSeq; WP_004083208.1; NZ_CP011107.1. DR PDB; 4COI; X-ray; 1.94 A; A/B=1-651. DR PDB; 4COJ; X-ray; 2.48 A; A/B=1-651. DR PDB; 4COL; X-ray; 1.96 A; A/B=1-651. DR PDB; 4COM; X-ray; 1.92 A; A/B=1-651. DR PDB; 4CON; X-ray; 2.12 A; A/B=1-651. DR PDB; 4U3E; X-ray; 1.64 A; A/B=1-651. DR PDBsum; 4COI; -. DR PDBsum; 4COJ; -. DR PDBsum; 4COL; -. DR PDBsum; 4COM; -. DR PDBsum; 4CON; -. DR PDBsum; 4U3E; -. DR STRING; 243274.TM0385; -. DR EnsemblBacteria; AAD35470; AAD35470; TM_0385. DR EnsemblBacteria; AGL49308; AGL49308; Tmari_0383. DR GeneID; 897362; -. DR KEGG; tma:TM0385; -. DR KEGG; tmi:THEMA_02795; -. DR KEGG; tmm:Tmari_0383; -. DR KEGG; tmw:THMA_0392; -. DR PATRIC; 23935653; VBITheMar51294_0391. DR eggNOG; ENOG4105CJD; Bacteria. DR eggNOG; COG1328; LUCA. DR KO; K00527; -. DR OMA; IAYNYRI; -. DR OrthoDB; EOG65QWG9; -. DR BioCyc; TMAR243274:GC6P-399-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR014192; Anaer_RNR_III. DR InterPro; IPR012833; NrdD. DR Pfam; PF13597; NRDD; 1. DR TIGRFAMs; TIGR02827; RNR_anaer_Bdell; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4COI, ECO:0000213|PDB:4COJ, KW ECO:0000213|PDB:4COL, ECO:0000213|PDB:4COM}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000213|PDB:4COI, ECO:0000213|PDB:4COJ, KW ECO:0000213|PDB:4COL, ECO:0000213|PDB:4COM}; KW Nucleotide-binding {ECO:0000213|PDB:4COJ}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49308.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000213|PDB:4COI, ECO:0000213|PDB:4COJ, KW ECO:0000213|PDB:4COL, ECO:0000213|PDB:4COM}. FT DOMAIN 75 644 NRDD. {ECO:0000259|Pfam:PF13597}. FT NP_BIND 112 115 CTP. {ECO:0000213|PDB:4COJ}. FT NP_BIND 221 227 CTP. {ECO:0000213|PDB:4COJ}. FT NP_BIND 499 502 CTP. {ECO:0000213|PDB:4COJ}. FT METAL 594 594 Zinc. {ECO:0000213|PDB:4COI, FT ECO:0000213|PDB:4COJ, FT ECO:0000213|PDB:4COL}. FT METAL 598 598 Zinc; via pros nitrogen. FT {ECO:0000213|PDB:4COI, FT ECO:0000213|PDB:4COJ, FT ECO:0000213|PDB:4COL}. FT METAL 605 605 Zinc. {ECO:0000213|PDB:4COI, FT ECO:0000213|PDB:4COJ, FT ECO:0000213|PDB:4COL}. FT METAL 608 608 Zinc. {ECO:0000213|PDB:4COI, FT ECO:0000213|PDB:4COJ, FT ECO:0000213|PDB:4COL}. FT BINDING 358 358 CTP; via carbonyl oxygen. FT {ECO:0000213|PDB:4COJ}. SQ SEQUENCE 651 AA; 75581 MW; 40D2CB4DFA6CD527 CRC64; MKVQYSFERE FEELMSDLLS KYGYEMFQMD GLGDQLDVVK FTEDFVRRGI IESTIDANAN VRVTNISTYF IEISKPHTYL YSLYRIWQKM KEMFGKGVAD EFVEAQINGA VYLHDRHHAA LMPYCFAYTL KPIVEKGLPF IKTIKSEPAK HLSTFIQHVI QFVMFASNQS SGAVGLPDFF VWMWYFVKKD LKEGIIPRDK LDWYIEQHFQ ILTYSLNQPI RTTQSPYTNF TYLDRNYIKA IFEGERYPDG SLITDHVEDI IALQKHYWEW VSRERERQMF TFPVLTASLL YKDGKFLDED SARFINKINM KWQDTNWYIS DSIDAVASCC RLTSSTQTLK KFSLSSEEEE KLKGRMNSIG GSDLNIGSFK VITVNLPRIA LESGGDREKY LQILRHRVQL IKKALAAVRE IIKERISEGL LPLYENGLML LNRQYGTIGV TGVWESASIM GLTTEDIDGL KYTEEGEVFV DNVLDTIREE AEKGYHEYGF TFNIEQVPAE KAAVTLAQKD RFLFGEKQPF EIYSNQWVPL MANTDVLNRI RYSGKWDKKV SGGAILHINL GESFKTEEES FNMVKMIADM GVMYFAFNTK ISVCEDGHAF YGERCPVCGK AKVDEYMRIV GYLVPVSAFN KERREIEYPR RQFYDSLTIR R // ID Q9WYR1_THEMA Unreviewed; 271 AA. AC Q9WYR1; G4FHY9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE SubName: Full=Binding-protein-dependent transport systems inner membrane component {ECO:0000313|EMBL:AGL49352.1}; DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35515.1}; GN OrderedLocusNames=TM_0430 {ECO:0000313|EMBL:AAD35515.1}; GN ORFNames=Tmari_0427 {ECO:0000313|EMBL:AGL49352.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35515.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35515.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35515.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49352.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49352.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35515.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49352.1; -; Genomic_DNA. DR PIR; F72379; F72379. DR RefSeq; NP_228240.1; NC_000853.1. DR RefSeq; WP_004083318.1; NZ_CP011107.1. DR STRING; 243274.TM0430; -. DR TCDB; 3.A.1.1.39; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35515; AAD35515; TM_0430. DR EnsemblBacteria; AGL49352; AGL49352; Tmari_0427. DR GeneID; 897441; -. DR KEGG; tma:TM0430; -. DR KEGG; tmm:Tmari_0427; -. DR KEGG; tmw:THMA_0436; -. DR PATRIC; 23935745; VBITheMar51294_0436. DR eggNOG; ENOG4108NJ6; Bacteria. DR eggNOG; ENOG4110PHZ; LUCA. DR KO; K17243; -. DR OMA; QIFWRIV; -. DR OrthoDB; EOG693GR8; -. DR BioCyc; TMAR243274:GC6P-445-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 7 27 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 70 92 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 104 128 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 134 155 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 176 199 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 238 256 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 66 256 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 271 AA; 30914 MW; D28964E0CFE56F53 CRC64; MLTKTIKWIF IVFMLVVFML PVFYAVVSSF KPMSEIYSYP PTIFPKKPSL EGYINVIKEY DLLTYLRNTL FVATVATVIT VLVSVMTGYG LAKGKFWGIR PVNSMFTMTM FVSAQVIMVP LFVVIRSLGL INSLWGLIIP AVYTPTGMFM AVQYMKDIPD ELLESAKIDG ANEWQIFWRI VFPLSKPLVA ALAIFSFTWR WNDFVLPLLV VNRRNLYTLQ LALATIQEEY GGAEWNTILA FSTLTIIPTL IIFLLFQRLF MKGIMAGGLK Y // ID Q9X195_THEMA Unreviewed; 336 AA. AC Q9X195; G4FFB1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=ABC transporter, periplasmic spermidine putrescine-binding protein PotD {ECO:0000313|EMBL:AGL50306.1}; DE SubName: Full=Spermidine/putrescine ABC transporter, periplasmic spermidine/putrescine-binding protein {ECO:0000313|EMBL:AAD36445.1}; GN OrderedLocusNames=TM_1375 {ECO:0000313|EMBL:AAD36445.1}; GN ORFNames=Tmari_1382 {ECO:0000313|EMBL:AGL50306.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36445.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36445.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36445.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50306.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50306.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36445.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50306.1; -; Genomic_DNA. DR PIR; H72260; H72260. DR RefSeq; NP_229176.1; NC_000853.1. DR RefSeq; WP_004081573.1; NC_000853.1. DR STRING; 243274.TM1375; -. DR EnsemblBacteria; AAD36445; AAD36445; TM_1375. DR EnsemblBacteria; AGL50306; AGL50306; Tmari_1382. DR GeneID; 898103; -. DR KEGG; tma:TM1375; -. DR KEGG; tmm:Tmari_1382; -. DR PATRIC; 23937692; VBITheMar51294_1387. DR eggNOG; ENOG4108HM4; Bacteria. DR eggNOG; COG0687; LUCA. DR KO; K11069; -. DR OMA; KNPDAAH; -. DR OrthoDB; EOG66XBH9; -. DR BioCyc; TMAR243274:GC6P-1410-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:InterPro. DR GO; GO:0019808; F:polyamine binding; IEA:InterPro. DR GO; GO:0015846; P:polyamine transport; IEA:InterPro. DR InterPro; IPR001188; Sperm_putr-bd. DR PIRSF; PIRSF019574; Periplasmic_polyamine_BP; 1. DR PRINTS; PR00909; SPERMDNBNDNG. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 336 AA; 38975 MW; 1FEB259C39BC0B2A CRC64; MMKKVFLVLL VVLAIPIFAK ATLYIYNWAD YIPEDVIRAF EEKYDCRVVY DTYASNEEMY AKFKAGGGKG YDLIFPSGDY VSIMKKEGML QKLDLSKIPN FKYLDKDILA KTTYDPNHEY SVPYMMGSTV VIVNKKYVKE YEKSWSIFDR EDLRGRMTLL DDMREVLGAA LKYLGYSVNT KNPKELEEAK QVVLRWKKNI AKFDASSYAD GIVSGEYWVV HGYAEDVYQR IPEGEEKYFD FFIPKEGGTL WIDNMVIPKG AKNVDLAYKF INFILEPENA AKIADYLGLP SPNVEARKYM QTEPIYTIED LKNCEFIEDV GEALELYNKI WLEIIM // ID Q9X1B2_THEMA Unreviewed; 98 AA. AC Q9X1B2; G4FFC8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36463.1}; GN OrderedLocusNames=TM_1392 {ECO:0000313|EMBL:AAD36463.1}; GN ORFNames=Tmari_1399 {ECO:0000313|EMBL:AGL50323.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36463.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36463.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36463.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50323.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50323.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36463.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50323.1; -; Genomic_DNA. DR PIR; A72259; A72259. DR RefSeq; NP_229193.1; NC_000853.1. DR RefSeq; WP_004081600.1; NZ_CP011107.1. DR STRING; 243274.TM1392; -. DR EnsemblBacteria; AAD36463; AAD36463; TM_1392. DR EnsemblBacteria; AGL50323; AGL50323; Tmari_1399. DR GeneID; 898084; -. DR KEGG; tma:TM1392; -. DR KEGG; tmi:THEMA_07355; -. DR KEGG; tmm:Tmari_1399; -. DR KEGG; tmw:THMA_1421; -. DR PATRIC; 23937730; VBITheMar51294_1404. DR eggNOG; ENOG4108E57; Bacteria. DR eggNOG; ENOG41103IR; LUCA. DR OMA; NTIAARC; -. DR OrthoDB; EOG6K403Z; -. DR BioCyc; TMAR243274:GC6P-1429-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR014995; DUF1844. DR Pfam; PF08899; DUF1844; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 98 AA; 11573 MW; A88E5C5A6C68A29B CRC64; MEEKKEKLSM KDLILLFFST ISARCWARLG LTEDEYGDFY QDLEEARLGI DMLDAIFNKI KGLVDEEVRR EMEGVLSTLK LNYFHQYQKS KKKETKNA // ID Q9X1Z2_THEMA Unreviewed; 210 AA. AC Q9X1Z2; G4FG53; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=Ribosomal RNA small subunit methyltransferase C {ECO:0000313|EMBL:AGL50597.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36731.1}; GN OrderedLocusNames=TM_1664 {ECO:0000313|EMBL:AAD36731.1}; GN ORFNames=Tmari_1673 {ECO:0000313|EMBL:AGL50597.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36731.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36731.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36731.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50597.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50597.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36731.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50597.1; -; Genomic_DNA. DR PIR; F72224; F72224. DR RefSeq; NP_229464.1; NC_000853.1. DR RefSeq; WP_004082182.1; NZ_CP011107.1. DR STRING; 243274.TM1664; -. DR EnsemblBacteria; AAD36731; AAD36731; TM_1664. DR EnsemblBacteria; AGL50597; AGL50597; Tmari_1673. DR GeneID; 897115; -. DR KEGG; tma:TM1664; -. DR KEGG; tmi:THEMA_05925; -. DR KEGG; tmm:Tmari_1673; -. DR KEGG; tmw:THMA_1705; -. DR PATRIC; 23938302; VBITheMar51294_1683. DR eggNOG; ENOG4107XZB; Bacteria. DR eggNOG; COG2813; LUCA. DR OMA; ITNPPIR; -. DR OrthoDB; EOG67X1ZC; -. DR BioCyc; TMAR243274:GC6P-1710-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR Pfam; PF05175; MTS; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Methyltransferase {ECO:0000313|EMBL:AGL50597.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL50597.1}. FT DOMAIN 32 197 MTS. {ECO:0000259|Pfam:PF05175}. SQ SEQUENCE 210 AA; 24068 MW; 39E48BD14057B0AA CRC64; MSEKFEHYYT VEPTSKLKVR EARLVLKNGH EYIFKTPSGV YSYGKIDKAT QVLLENLKVH GKKVLDLGCG YGVIGIVLKK EYPDLEVYMS DINKRAVEFA KINAKDHNVE VDIRWGNLYE PWEDMKFDMI VCNPPIVAGK KVWMEIVKSA PEFLEEGGSL QIVAYHNKGG RRIRDFMKEV FGNVEELCKT GGIRVYRSVK GLKEDEDNAE // ID Q9X086_THEMA Unreviewed; 584 AA. AC Q9X086; G4FF04; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36070.1}; GN OrderedLocusNames=TM_0991 {ECO:0000313|EMBL:AAD36070.1}; GN ORFNames=Tmari_0994 {ECO:0000313|EMBL:AGL49919.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36070.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36070.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36070.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49919.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49919.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36070.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49919.1; -; Genomic_DNA. DR PIR; E72308; E72308. DR RefSeq; NP_228799.1; NC_000853.1. DR RefSeq; WP_004080566.1; NZ_CP011107.1. DR EnsemblBacteria; AAD36070; AAD36070; TM_0991. DR EnsemblBacteria; AGL49919; AGL49919; Tmari_0994. DR GeneID; 898714; -. DR KEGG; tma:TM0991; -. DR KEGG; tmi:THEMA_09395; -. DR KEGG; tmm:Tmari_0994; -. DR KEGG; tmw:THMA_1013; -. DR PATRIC; 23936911; VBITheMar51294_1004. DR eggNOG; ENOG4105D66; Bacteria. DR eggNOG; COG1479; LUCA. DR eggNOG; COG3472; LUCA. DR OMA; QADFAMS; -. DR OrthoDB; EOG68Q0Q4; -. DR BioCyc; TMAR243274:GC6P-1021-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR004919; DUF262. DR Pfam; PF03235; DUF262; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 14 226 DUF262. {ECO:0000259|Pfam:PF03235}. SQ SEQUENCE 584 AA; 68561 MW; 75A795F5E9580965 CRC64; MNGLLFKKVD YSVGGLLENI DSGEIGLPDI QRPFVWDTTR VRDLFDSMYR GYPIGTLLFW ENGFPGEHRT IGTGPKKKVP RLLVVDGQQR LTALYSVMKG VPIVDKNFRQ RRLRIAFNPL EEKFEVTNTS IERDPTWISD ISILWQEGFA LYDFISSFMK RLEERRGLTE EERQRIPRSI QKLVNLVNYP MTALEISASA TEEQVSEIFV RINSRGRTLN QADFILTLMS VFWDEGRKQL EEFCRRAKNP PSDNRPSPYN PYFKPQPDQL LRVDVVLAFR RARLEYVYSI LRGKDLQTGE FSPERRDEQF DRLEKAQKEV LNLQNWHDFL KVIKRAGYIH HSLITSEMAL VYTYSLWLIG KQDFGLDQHT LRDLMARWFF MSSLTSRYSS SAETRMEQDL TLIRGCSSSE EFVRTLEQEI SAVLTNDYWN VTLPNELATA SARNPGQYAF FAALCLLDAP VLYSSMKVRD LLDPTSQSHR SALERHHLFP RKYLEKLGIK DNHDINQVAN FALVEWHDNV EIGDRPPSDY APEYERRFPP DKLTEMYWYH ALPEGWYNMD YWTFLEERRR RMAEIIRKGF ESLK // ID Q9X106_THEMA Unreviewed; 125 AA. AC Q9X106; G4FE69; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36354.1}; GN OrderedLocusNames=TM_1279 {ECO:0000313|EMBL:AAD36354.1}; GN ORFNames=Tmari_1284 {ECO:0000313|EMBL:AGL50208.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36354.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36354.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36354.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50208.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50208.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36354.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50208.1; -; Genomic_DNA. DR PIR; C72273; C72273. DR RefSeq; NP_229084.1; NC_000853.1. DR RefSeq; WP_004079956.1; NZ_CP011107.1. DR STRING; 243274.TM1279; -. DR EnsemblBacteria; AAD36354; AAD36354; TM_1279. DR EnsemblBacteria; AGL50208; AGL50208; Tmari_1284. DR GeneID; 898204; -. DR KEGG; tma:TM1279; -. DR KEGG; tmi:THEMA_07940; -. DR KEGG; tmm:Tmari_1284; -. DR KEGG; tmw:THMA_1304; -. DR PATRIC; 23937496; VBITheMar51294_1294. DR OMA; TTSMAFG; -. DR OrthoDB; EOG6FBX09; -. DR BioCyc; TMAR243274:GC6P-1310-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 125 AA; 14127 MW; 1541C588FD173C44 CRC64; MKKIILALLV IVSVQMMGDV FVSFSYDFSE GETVSSVGMD TGEFTAGVEL WDFSSICFFV GAVRNLDLGD FMFTLETRVG FSSKPYLAVV NFFWKKHEGV KWGFGYSITL KDSSIRFPLF VRLGW // ID Q9WYD6_THEMA Unreviewed; 611 AA. AC Q9WYD6; G4FHL4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 84. DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein, putative {ECO:0000313|EMBL:AAD35388.1}; DE SubName: Full=Xyloglucan ABC transport system, sugar-binding protein {ECO:0000313|EMBL:AGL49224.1}; GN OrderedLocusNames=TM_0300 {ECO:0000313|EMBL:AAD35388.1}; GN ORFNames=Tmari_0298 {ECO:0000313|EMBL:AGL49224.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35388.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35388.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35388.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49224.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49224.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35388.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49224.1; -; Genomic_DNA. DR PIR; A72393; A72393. DR RefSeq; NP_228112.1; NC_000853.1. DR RefSeq; WP_004083020.1; NZ_CP011107.1. DR STRING; 243274.TM0300; -. DR TCDB; 3.A.1.5.30; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35388; AAD35388; TM_0300. DR EnsemblBacteria; AGL49224; AGL49224; Tmari_0298. DR GeneID; 897225; -. DR KEGG; tma:TM0300; -. DR KEGG; tmi:THEMA_03225; -. DR KEGG; tmm:Tmari_0298; -. DR KEGG; tmw:THMA_0307; -. DR PATRIC; 23935479; VBITheMar51294_0305. DR eggNOG; COG0747; LUCA. DR KO; K02035; -. DR OMA; PNISAQI; -. DR OrthoDB; EOG63JR4Z; -. DR BioCyc; TMAR243274:GC6P-313-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GOC. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 611 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972219. FT DOMAIN 73 483 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. SQ SEQUENCE 611 AA; 70824 MW; 0FDE18A2D07FA76F CRC64; MKRFLFVAVL FTIFAASFAQ FLNVPREQTV IVPGPKTANP GDFNVIAGWK DPHRGIQQLL LEPLWMDDPV RGEIINALAE TGPIYNEDFT KMIVKLRKGV YWSDGVPFTA DDVVFTVEMC MKYPEMARHM EFNEYIDKVY KEDDYTVVFE LKKPNTRFHT YFIDRWGYWW PMPKHVFEKV EDPVGFTFNP PVGTGPYVLK DYDPAGYWVL WERREDWQRT PTGMIFGMPK PKYVLFYAYE TDEKITLAFL QNQLDAAGIG PQALKALLKR SKYVKLYSDF PFVPLVDPVV GGITINTAKY PFNMKEVRWA LALALDIVKL SETEEGNMLI SALHIPPLPL YRKLYYEPLE EWLQNLTVNG VKVYDPDVPL KIAEVAKRYG WNVPDDPEKI KLGVGSGWWK HLPDVAEQLL LSVGFKRDKN GKWLLPNGTP WKIQLGTNPN DLVAFGVAQQ WREFGIDVDV ITTYISGINE GNFEVLITGN WPAPEPWGGH ADLHRTLYFF HSKYQNKPLG EGVGHVSRWF DERLDKIIDE MEKLDWNDPR NIEFGREGLK ILAEELPTIP IGTIGVLTTA LVYNDYYWTN WPTLENPYMM PYWHWSQFKY LLTFLEPTGR K // ID Q9WYE9_THEMA Unreviewed; 319 AA. AC Q9WYE9; G4FHM7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=K+ channel, beta subunit {ECO:0000313|EMBL:AAD35401.1}; DE SubName: Full=Voltage-gated potassium channel beta subunit {ECO:0000313|EMBL:AGL49237.1}; GN OrderedLocusNames=TM_0313 {ECO:0000313|EMBL:AAD35401.1}; GN ORFNames=Tmari_0311 {ECO:0000313|EMBL:AGL49237.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35401.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35401.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35401.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49237.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49237.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35401.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49237.1; -; Genomic_DNA. DR PIR; H72391; H72391. DR RefSeq; NP_228125.1; NC_000853.1. DR RefSeq; WP_004083050.1; NZ_CP011107.1. DR STRING; 243274.TM0313; -. DR EnsemblBacteria; AAD35401; AAD35401; TM_0313. DR EnsemblBacteria; AGL49237; AGL49237; Tmari_0311. DR GeneID; 897254; -. DR KEGG; tma:TM0313; -. DR KEGG; tmi:THEMA_03160; -. DR KEGG; tmm:Tmari_0311; -. DR KEGG; tmw:THMA_0320; -. DR PATRIC; 23935505; VBITheMar51294_0318. DR eggNOG; ENOG4105CPC; Bacteria. DR eggNOG; COG0667; LUCA. DR OMA; MGLVVWS; -. DR OrthoDB; EOG6NSGJH; -. DR BioCyc; TMAR243274:GC6P-326-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red/Kv-b. DR InterPro; IPR005399; K_chnl_volt-dep_bsu_KCNAB-rel. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PRINTS; PR01577; KCNABCHANNEL. DR SUPFAM; SSF51430; SSF51430; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Ion channel {ECO:0000313|EMBL:AAD35401.1}; KW Ion transport {ECO:0000313|EMBL:AAD35401.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000313|EMBL:AAD35401.1}. FT DOMAIN 15 317 Aldo_ket_red. {ECO:0000259|Pfam:PF00248}. SQ SEQUENCE 319 AA; 36172 MW; E4B1F32F41719B39 CRC64; MEYRKVGKWG VKISELSLGS WLTFGKQLDL DTATEVVKKA FNSGINFFDT AEAYAGGIAE AMLGKILKNF RREDLVVSTK IFWGGSGPND LGLSKKHLLE GTWNSLKRLQ MDYVDILYCH RPDPNVPMEE VVFAMDYILR EGLALYWGTS EWSAKEIEEA HRVCKELGVM PPIVEQPQYN MFVRERVEKE YAPLYEKYGM GLTTYSPLAS GLLSGKYNNG IPEGSRLATF PQVRKWLEEG GLLNEKTFKK LRKLQNIADQ LGASLPQLAI AWILKNKNVS SVILGVSRPE QLEENLKAVE IKEKLTEDVM EEIEKILNE // ID Q9X102_THEMA Unreviewed; 87 AA. AC Q9X102; G4FE73; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE RecName: Full=Antitoxin {ECO:0000256|RuleBase:RU362080}; GN OrderedLocusNames=TM_1275 {ECO:0000313|EMBL:AAD36350.1}; GN ORFNames=Tmari_1280 {ECO:0000313|EMBL:AGL50204.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36350.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36350.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36350.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50204.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50204.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Antitoxin component of a toxin-antitoxin (TA) module. CC {ECO:0000256|RuleBase:RU362080}. CC -!- SIMILARITY: Belongs to the phD/YefM antitoxin family. CC {ECO:0000256|RuleBase:RU362080}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36350.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50204.1; -; Genomic_DNA. DR PIR; G72272; G72272. DR RefSeq; NP_229080.1; NC_000853.1. DR RefSeq; WP_004079961.1; NZ_CP011107.1. DR STRING; 243274.TM1275; -. DR EnsemblBacteria; AAD36350; AAD36350; TM_1275. DR EnsemblBacteria; AGL50204; AGL50204; Tmari_1280. DR GeneID; 898208; -. DR KEGG; tma:TM1275; -. DR KEGG; tmi:THEMA_07960; -. DR KEGG; tmm:Tmari_1280; -. DR KEGG; tmw:THMA_1300; -. DR PATRIC; 23937488; VBITheMar51294_1290. DR eggNOG; ENOG4105WY2; Bacteria. DR eggNOG; COG2161; LUCA. DR OMA; VWELYLL; -. DR OrthoDB; EOG651T2N; -. DR BioCyc; TMAR243274:GC6P-1306-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.1620.10; -; 1. DR InterPro; IPR006442; Antitoxin_Phd/YefM. DR Pfam; PF02604; PhdYeFM_antitox; 1. DR TIGRFAMs; TIGR01552; phd_fam; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 87 AA; 10142 MW; E097A192446C8577 CRC64; MDLSRVSFYS LADAKARFSQ VVEEAKTKDV VVTKNGVPAV AVIDYEKYKK LMEFMDEILD TYLLDIGNVE KYLELKRYFE FNDSQEV // ID Q9X1D6_THEMA Unreviewed; 382 AA. AC Q9X1D6; G4FFF5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Inositol-1-phosphate synthase {ECO:0000313|EMBL:AGL50350.1}; DE EC=5.5.1.4 {ECO:0000313|EMBL:AGL50350.1}; DE SubName: Full=Myo-inositol-1-phosphate synthase-related protein {ECO:0000313|EMBL:AAD36489.1}; GN OrderedLocusNames=TM_1419 {ECO:0000313|EMBL:AAD36489.1}; GN ORFNames=Tmari_1426 {ECO:0000313|EMBL:AGL50350.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36489.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36489.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36489.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50350.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50350.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36489.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50350.1; -; Genomic_DNA. DR PIR; H72255; H72255. DR RefSeq; NP_229219.1; NC_000853.1. DR RefSeq; WP_004081662.1; NZ_CP011107.1. DR PDB; 3CIN; X-ray; 1.70 A; A=1-382. DR PDBsum; 3CIN; -. DR STRING; 243274.TM1419; -. DR EnsemblBacteria; AAD36489; AAD36489; TM_1419. DR EnsemblBacteria; AGL50350; AGL50350; Tmari_1426. DR GeneID; 898056; -. DR KEGG; tma:TM1419; -. DR KEGG; tmi:THEMA_07215; -. DR KEGG; tmm:Tmari_1426; -. DR KEGG; tmw:THMA_1450; -. DR PATRIC; 23937786; VBITheMar51294_1431. DR eggNOG; ENOG4105CZA; Bacteria. DR eggNOG; COG1260; LUCA. DR KO; K01858; -. DR OMA; KEFGTVY; -. DR OrthoDB; EOG6F2946; -. DR BioCyc; TMAR243274:GC6P-1457-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0006021; P:inositol biosynthetic process; IEA:InterPro. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR002587; Myo-inos-1-P_Synthase. DR InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11510; PTHR11510; 1. DR Pfam; PF01658; Inos-1-P_synth; 1. DR Pfam; PF07994; NAD_binding_5; 1. DR PIRSF; PIRSF015578; Myoinos-ppht_syn; 1. DR SUPFAM; SSF51735; SSF51735; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3CIN}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000313|EMBL:AGL50350.1}; KW Magnesium {ECO:0000213|PDB:3CIN}; KW Metal-binding {ECO:0000213|PDB:3CIN}; NAD {ECO:0000213|PDB:3CIN}; KW Nucleotide-binding {ECO:0000213|PDB:3CIN}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 212 317 Inos-1-P_synth. FT {ECO:0000259|Pfam:PF01658}. FT NP_BIND 11 12 NAD. {ECO:0000213|PDB:3CIN}. FT NP_BIND 131 133 NAD. {ECO:0000213|PDB:3CIN}. FT METAL 189 189 Magnesium. {ECO:0000213|PDB:3CIN}. FT METAL 354 354 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:3CIN}. FT METAL 356 356 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:3CIN}. FT METAL 359 359 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:3CIN}. FT BINDING 53 53 NAD. {ECO:0000213|PDB:3CIN}. FT BINDING 58 58 NAD. {ECO:0000213|PDB:3CIN}. FT BINDING 87 87 NAD; via carbonyl oxygen. FT {ECO:0000213|PDB:3CIN}. FT BINDING 91 91 NAD. {ECO:0000213|PDB:3CIN}. FT BINDING 163 163 NAD. {ECO:0000213|PDB:3CIN}. FT BINDING 211 211 NAD. {ECO:0000213|PDB:3CIN}. FT BINDING 316 316 NAD; via carbonyl oxygen. FT {ECO:0000213|PDB:3CIN}. SQ SEQUENCE 382 AA; 42194 MW; A8F82638387B5603 CRC64; MVKVLILGQG YVASTFVAGL EKLRKGEIEP YGVPLARELP IGFEDIKIVG SYDVDRAKIG KKLSEVVKQY WNDVDSLTSD PEIRKGVHLG SVRNLPIEAE GLEDSMTLKE AVDTLVKEWT ELDPDVIVNT CTTEAFVPFG NKEDLLKAIE NNDKERLTAT QVYAYAAALY ANKRGGAAFV NVIPTFIAND PAFVELAKEN NLVVFGDDGA TGATPFTADV LSHLAQRNRY VKDVAQFNIG GNMDFLALTD DGKNKSKEFT KSSIVKDILG YDAPHYIKPT GYLEPLGDKK FIAIHIEYVS FNGATDELMI NGRINDSPAL GGLLVDLVRL GKIALDRKEF GTVYPVNAFY MKNPGPAEEK NIPRIIAYEK MRIWAGLKPK WL // ID Q9WZ46_THEMA Unreviewed; 179 AA. AC Q9WZ46; G4FDP3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:AGL49500.1}; DE EC=2.3.1.- {ECO:0000313|EMBL:AGL49500.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35662.1}; GN OrderedLocusNames=TM_0577 {ECO:0000313|EMBL:AAD35662.1}; GN ORFNames=Tmari_0575 {ECO:0000313|EMBL:AGL49500.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35662.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35662.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35662.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49500.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49500.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35662.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49500.1; -; Genomic_DNA. DR PIR; D72360; D72360. DR RefSeq; NP_228387.1; NC_000853.1. DR RefSeq; WP_004081283.1; NZ_CP011107.1. DR STRING; 243274.TM0577; -. DR EnsemblBacteria; AAD35662; AAD35662; TM_0577. DR EnsemblBacteria; AGL49500; AGL49500; Tmari_0575. DR GeneID; 897645; -. DR KEGG; tma:TM0577; -. DR KEGG; tmi:THEMA_01785; -. DR KEGG; tmm:Tmari_0575; -. DR KEGG; tmw:THMA_0591; -. DR PATRIC; 23936063; VBITheMar51294_0586. DR eggNOG; ENOG4105WCN; Bacteria. DR eggNOG; COG0454; LUCA. DR OMA; EAIMPRG; -. DR OrthoDB; EOG6NKR5W; -. DR BioCyc; TMAR243274:GC6P-601-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031248; C:protein acetyltransferase complex; IBA:GO_Central. DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IBA:GO_Central. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000313|EMBL:AGL49500.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49500.1}. FT DOMAIN 14 179 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 179 AA; 20886 MW; FC0CEF7EC299BF15 CRC64; MFPRKELLKD GSLLLIREAS IWDARRIVEY LKEVTSETDF LITRPDEVYD VSTERNYIRM YRSNPGKLMI VGEINREIVS LLTFTGFGRK RTKHVGEIGI SVKKRYWNIG IGTRMITSAI EWARRNGFIR IQLEVLKSNE RAISLYRKLG FELEGIKRKA VRRDDGSFED VLVMALLLD // ID Q9WZV2_THEMA Unreviewed; 363 AA. AC Q9WZV2; G4FCX6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=GTP-binding protein YqeH, required for biogenesis of 30S ribosome subunit {ECO:0000313|EMBL:AGL49775.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35930.1}; GN OrderedLocusNames=TM_0848 {ECO:0000313|EMBL:AAD35930.1}; GN ORFNames=Tmari_0850 {ECO:0000313|EMBL:AGL49775.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35930.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35930.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35930.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49775.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49775.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35930.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49775.1; -; Genomic_DNA. DR PIR; A72327; A72327. DR RefSeq; NP_228657.1; NC_000853.1. DR RefSeq; WP_004080778.1; NZ_CP011107.1. DR STRING; 243274.TM0848; -. DR EnsemblBacteria; AAD35930; AAD35930; TM_0848. DR EnsemblBacteria; AGL49775; AGL49775; Tmari_0850. DR GeneID; 898519; -. DR KEGG; tma:TM0848; -. DR KEGG; tmi:THEMA_00400; -. DR KEGG; tmm:Tmari_0850; -. DR KEGG; tmw:THMA_0869; -. DR PATRIC; 23936622; VBITheMar51294_0861. DR eggNOG; ENOG4105CQW; Bacteria. DR eggNOG; COG1161; LUCA. DR KO; K06948; -. DR OMA; HYNEVQD; -. DR OrthoDB; EOG6Z6FPR; -. DR BioCyc; TMAR243274:GC6P-877-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR019988; GTP-bd_ribosome_bgen_YqeH. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03597; GTPase_YqeH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 159 213 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. SQ SEQUENCE 363 AA; 41975 MW; 090B86A6073E79CE CRC64; MRCPGCGAAI QFDDPKKPGY IPREVFEKRL EEGKEILCQR CFRMKHYGKL EPVEFDWDFK NQLKSYLGGF DVVVWVIDIF DFEGTYREDI AEILKGKRVI YVINKIDLLP RAVTVKEIKE WVKKRIKTKN TDDIRIVSAE KNFGLTSLVK YLSRLTDKAL VVGVTNVGKS SLLNKICTHE NTISPFPGTT LGILKRKVKE ANLYLYDTPG IMTSDRILDL LDPECQKRVL PREELSRKTF KPDNGRTIFM GGLCRFDIHF ETEKNPIFLL FSSKEVTFHE TRRERADELM RNRLGDLLIP PCSKTKFENF KWKRETFTLK EGEELAVAGL GWMSVRRGPF TVEVTVPDSV KLVVREALVN PKR // ID Q9WY38_THEMA Unreviewed; 288 AA. AC Q9WY38; G4FHA9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Guanosine pentaphosphate phosphohydrolase, putative {ECO:0000313|EMBL:AAD35287.1}; GN OrderedLocusNames=TM_0195 {ECO:0000313|EMBL:AAD35287.1}; GN ORFNames=Tmari_0193 {ECO:0000313|EMBL:AGL49119.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35287.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35287.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35287.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49119.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49119.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35287.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49119.1; -; Genomic_DNA. DR PIR; C72407; C72407. DR RefSeq; NP_228010.1; NC_000853.1. DR RefSeq; WP_004082845.1; NC_000853.1. DR STRING; 243274.TM0195; -. DR EnsemblBacteria; AAD35287; AAD35287; TM_0195. DR EnsemblBacteria; AGL49119; AGL49119; Tmari_0193. DR GeneID; 897064; -. DR KEGG; tma:TM0195; -. DR KEGG; tmi:THEMA_03755; -. DR KEGG; tmm:Tmari_0193; -. DR eggNOG; ENOG4107VTZ; Bacteria. DR eggNOG; COG0248; LUCA. DR KO; K01524; -. DR OMA; FGTAFFR; -. DR OrthoDB; EOG6MPWXC; -. DR BioCyc; TMAR243274:GC6P-208-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR InterPro; IPR003695; Ppx_GppA. DR Pfam; PF02541; Ppx-GppA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD35287.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 39 266 Ppx-GppA. {ECO:0000259|Pfam:PF02541}. SQ SEQUENCE 288 AA; 32116 MW; 1B6F79582FCA81F1 CRC64; MIAVLDMGTN SFILLVVSEK GETILEEVHE VGIASGNLEK AKEVFKECVE KAEKMGAELH IFGTAFFRKH PDIFQQITGG RGEILPEEKE AYYSYISVAK DFGKKDILVA DLGGGSLELA WKDGYVSLEL GTHVLNRTFS LTLPYIEPVD GIVEYVMKRL PEVKKDELFG VGGSFVALAA LMKGKWDLEI LHGSVLKLEE VEKLVDKIKR MSFEDVKNLK VLPEGREKTI LAGGIVTIAL LRKYSPRMTV STRGYRYGIV WEILEKRWRA RGDSNPQPPD PQSGALSN // ID Q9WZN1_THEMA Unreviewed; 73 AA. AC Q9WZN1; G4FD50; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35855.1}; GN OrderedLocusNames=TM_0773 {ECO:0000313|EMBL:AAD35855.1}; GN ORFNames=Tmari_0774 {ECO:0000313|EMBL:AGL49699.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35855.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35855.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35855.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49699.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49699.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35855.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49699.1; -; Genomic_DNA. DR PIR; C72337; C72337. DR RefSeq; NP_228582.1; NC_000853.1. DR RefSeq; WP_004080917.1; NZ_CP011107.1. DR STRING; 243274.TM0773; -. DR EnsemblBacteria; AAD35855; AAD35855; TM_0773. DR EnsemblBacteria; AGL49699; AGL49699; Tmari_0774. DR GeneID; 898441; -. DR KEGG; tma:TM0773; -. DR KEGG; tmi:THEMA_00785; -. DR KEGG; tmm:Tmari_0774; -. DR KEGG; tmw:THMA_0792; -. DR PATRIC; 23936468; VBITheMar51294_0786. DR eggNOG; ENOG41061AI; Bacteria. DR eggNOG; ENOG410XV4S; LUCA. DR OMA; KRDNFTF; -. DR OrthoDB; EOG6HJ2D1; -. DR BioCyc; TMAR243274:GC6P-800-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR021320; DUF2905. DR Pfam; PF11146; DUF2905; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 69 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 73 AA; 8424 MW; 945661FD6E91CA0E CRC64; MFQGIGKFLI LMGLILVAFG ILLILFERIP FLGKLPGDIV IKRKNFVFYF PLMTSLIISL LVSFILYLIS RMR // ID Q9X129_THEMA Unreviewed; 253 AA. AC Q9X129; G4FE46; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36377.1}; GN OrderedLocusNames=TM_1303 {ECO:0000313|EMBL:AAD36377.1}; GN ORFNames=Tmari_1310 {ECO:0000313|EMBL:AGL50234.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36377.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36377.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36377.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50234.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50234.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36377.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50234.1; -; Genomic_DNA. DR PIR; A72270; A72270. DR RefSeq; NP_229107.1; NC_000853.1. DR RefSeq; WP_004079916.1; NZ_CP011107.1. DR STRING; 243274.TM1303; -. DR DNASU; 898179; -. DR EnsemblBacteria; AAD36377; AAD36377; TM_1303. DR EnsemblBacteria; AGL50234; AGL50234; Tmari_1310. DR GeneID; 898179; -. DR KEGG; tma:TM1303; -. DR KEGG; tmi:THEMA_07825; -. DR KEGG; tmm:Tmari_1310; -. DR KEGG; tmw:THMA_1328; -. DR PATRIC; 23937546; VBITheMar51294_1319. DR eggNOG; ENOG4107G29; Bacteria. DR eggNOG; COG0842; LUCA. DR KO; K01992; -. DR OMA; FYIRIAS; -. DR OrthoDB; EOG6D5G17; -. DR BioCyc; TMAR243274:GC6P-1334-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR InterPro; IPR013525; ABC_2_trans. DR Pfam; PF01061; ABC2_membrane; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 80 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 104 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 129 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 219 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 5 206 ABC2_membrane. FT {ECO:0000259|Pfam:PF01061}. SQ SEQUENCE 253 AA; 29152 MW; 3B6F106152AE87C9 CRC64; MRKILHLVLK EMKIRLKYRF VWVNMALTPF FIIGPYVFSS RIADVNSLAE NVLIGALLWY WLNQYFFGVG DGFTEEREEG ALISVVLAPI SLLAFLFSKA ADTFLMNLYI TFFTLLFFYL SGIKLEIHLY FLLLLAVSGV YITFFSIFFA ALSLWKKRIR SINSTAQFFF GVLSGMVNPV ENFPSYVRLI SYMIPLTYLI SIGRSIIKNG NMSGFVPQLL ILTGLSFAYL ILGVWLLKKA ENEIRKKGEW ESW // ID Q9WYJ1_THEMA Unreviewed; 401 AA. AC Q9WYJ1; G4FHR8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 98. DE SubName: Full=Threonine dehydratase {ECO:0000313|EMBL:AGL49279.1}; DE EC=4.3.1.19 {ECO:0000313|EMBL:AGL49279.1}; DE SubName: Full=Threonine dehydratase catabolic {ECO:0000313|EMBL:AAD35443.1}; GN OrderedLocusNames=TM_0356 {ECO:0000313|EMBL:AAD35443.1}; GN ORFNames=Tmari_0354 {ECO:0000313|EMBL:AGL49279.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35443.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35443.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35443.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49279.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49279.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35443.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49279.1; -; Genomic_DNA. DR PIR; D72386; D72386. DR RefSeq; NP_228167.1; NC_000853.1. DR RefSeq; WP_004083156.1; NZ_CP011107.1. DR STRING; 243274.TM0356; -. DR EnsemblBacteria; AAD35443; AAD35443; TM_0356. DR EnsemblBacteria; AGL49279; AGL49279; Tmari_0354. DR GeneID; 897314; -. DR KEGG; tma:TM0356; -. DR KEGG; tmi:THEMA_02935; -. DR KEGG; tmm:Tmari_0354; -. DR KEGG; tmw:THMA_0364; -. DR PATRIC; 23935593; VBITheMar51294_0361. DR eggNOG; ENOG4108E2G; Bacteria. DR eggNOG; COG1171; LUCA. DR KO; K01754; -. DR OMA; WLRDIYT; -. DR OrthoDB; EOG6ZSP7D; -. DR BioCyc; TMAR243274:GC6P-370-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central. DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central. DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS. DR InterPro; IPR005789; Thr_deHydtase_catblc. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF01842; ACT; 1. DR Pfam; PF00291; PALP; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR01127; ilvA_1Cterm; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000313|EMBL:AGL49279.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 326 401 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 401 AA; 43110 MW; 4D757A8F83786180 CRC64; MITLEDIKEA QRTLKNVVHR TALAYSSVLS EVTGGEIYLK MENLQKTGSF KIRGAYNKIA HLSEEERKRG VVAASAGNHA QGVALAAQIF GIPATIVMPR YAPLSKITKT RNLGAQVILE GNIFDEAYEA ALRIQEKTGA VFVHPFNDPH VIAGQGTIGL EIMEDLPDVE VVVVPVGGGG LISGVSVAIK SMNPEVKVIG VQTENMPSMI ASLRRGRAER VEGKPTLADG IAVKKPGDLT FELVKKYVDE MVAVNEEEIA DAILFLLEQA KVVAEGAGAV GVAAVLNKLD VKGKKVAIVI SGGNIDVNMI DRIINKGLVK SGRKVFIETF VMDRPGALKE LLGIVAELGA NVLSVFHNRS AKEVPIGFAK IELELETVDE KHVEEIERVL IAKGYEVRIV G // ID Q9X026_THEMA Unreviewed; 286 AA. AC Q9X026; G4FF66; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Radical activating enzyme {ECO:0000313|EMBL:AGL49851.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36005.1}; GN OrderedLocusNames=TM_0924 {ECO:0000313|EMBL:AAD36005.1}; GN ORFNames=Tmari_0926 {ECO:0000313|EMBL:AGL49851.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36005.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36005.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36005.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49851.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49851.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|PIRSR:PIRSR004869-50}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|PIRSR:PIRSR004869-50}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36005.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49851.1; -; Genomic_DNA. DR PIR; E72317; E72317. DR RefSeq; NP_228732.1; NC_000853.1. DR RefSeq; WP_004080638.1; NZ_CP011107.1. DR STRING; 243274.TM0924; -. DR EnsemblBacteria; AAD36005; AAD36005; TM_0924. DR EnsemblBacteria; AGL49851; AGL49851; Tmari_0926. DR GeneID; 898598; -. DR KEGG; tma:TM0924; -. DR KEGG; tmi:THEMA_00015; -. DR KEGG; tmm:Tmari_0926; -. DR KEGG; tmw:THMA_0946; -. DR PATRIC; 23936779; VBITheMar51294_0938. DR eggNOG; ENOG4105KN9; Bacteria. DR eggNOG; COG1313; LUCA. DR KO; K04070; -. DR OMA; VTPTHQI; -. DR OrthoDB; EOG6677SM; -. DR BioCyc; TMAR243274:GC6P-954-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004869; PflX_prd; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|PIRSR:PIRSR004869-50}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR004869-50}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR004869-50}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR004869-50}. FT DOMAIN 62 216 Radical_SAM. {ECO:0000259|Pfam:PF04055}. FT METAL 67 67 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. FT METAL 71 71 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. FT METAL 74 74 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. SQ SEQUENCE 286 AA; 32669 MW; BCC3F0EF13DF7BBE CRC64; MKSELFYRKL EKCDLCPRNC GVNRLMGEKG ACGVANSPVV SSWGPHFGEE RILVGRGGSG TVFFTYCNLK CVYCQNYEIS QLGIGKEITV EDLLRIFTEL QDMGVENLNL VTPTHQIPFI VDAFERMEKE IPVVYNCGGY ESVDTIISLE GFVDIYMPDF KYSDPELGEK LSGVKDYPRF ALEALKVMID QMGEPVIRNG VMKKGVLVRH LVLPGFLEDS FGVIDLLSTL EPKPLVNIMA QFYPAYRAKE YGLDRFITRD EYLKVVEYAK KKKLNLIEVE RWLRWL // ID Q9WZ04_THEMA Unreviewed; 193 AA. AC Q9WZ04; G4FDT7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 116. DE SubName: Full=RNA polymerase sigma-H factor, putative {ECO:0000313|EMBL:AAD35619.1}; DE SubName: Full=RNA polymerase sporulation specific sigma factor SigH {ECO:0000313|EMBL:AGL49456.1}; GN OrderedLocusNames=TM_0534 {ECO:0000313|EMBL:AAD35619.1}; GN ORFNames=Tmari_0531 {ECO:0000313|EMBL:AGL49456.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35619.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35619.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35619.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49456.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49456.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the sigma-70 factor family. CC {ECO:0000256|SAAS:SAAS00565852}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35619.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49456.1; -; Genomic_DNA. DR PIR; D72367; D72367. DR RefSeq; NP_228344.1; NC_000853.1. DR RefSeq; WP_004081373.1; NZ_CP011107.1. DR STRING; 243274.TM0534; -. DR EnsemblBacteria; AAD35619; AAD35619; TM_0534. DR EnsemblBacteria; AGL49456; AGL49456; Tmari_0531. DR GeneID; 897586; -. DR KEGG; tma:TM0534; -. DR KEGG; tmi:THEMA_02005; -. DR KEGG; tmm:Tmari_0531; -. DR KEGG; tmw:THMA_0547; -. DR PATRIC; 23935975; VBITheMar51294_0542. DR eggNOG; ENOG41081QE; Bacteria. DR eggNOG; COG1595; LUCA. DR KO; K03091; -. DR OMA; PIYDEDS; -. DR OrthoDB; EOG6PP9M7; -. DR BioCyc; TMAR243274:GC6P-558-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR000943; RNA_pol_sigma70. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR013249; RNA_pol_sigma70_r4_t2. DR InterPro; IPR013325; RNA_pol_sigma_r2. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04542; Sigma70_r2; 1. DR Pfam; PF08281; Sigma70_r4_2; 1. DR SUPFAM; SSF88659; SSF88659; 1. DR SUPFAM; SSF88946; SSF88946; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. DR PROSITE; PS00715; SIGMA70_1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00457605}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Sigma factor {ECO:0000256|SAAS:SAAS00458134}; KW Transcription {ECO:0000256|SAAS:SAAS00458134}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00458134}. FT DOMAIN 53 66 RNA_pol_sigma70. FT {ECO:0000259|PROSITE:PS00715}. SQ SEQUENCE 193 AA; 22178 MW; D4672E0F97E5E7D3 CRC64; MLKYRLRSKR VEELVEYAQA GFKEAIDLIV EKYYPMVVKI ASQYFASWAE HEDIVQNGLV GLIKAIFYYD KTKSSFTSFA WRSVDSEIKS FLTYLNRKKN RMLSDAVNVD GMEKEEDDAP FEVPDSETDV ARSAFSGIIL ETVLELLNEK EKEIFLRWLD GCSYSEIAKE LGVNTKKVDN TVQKVKRMIS GLG // ID Q9WXR4_THEMA Unreviewed; 331 AA. AC Q9WXR4; G4FGX3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 117. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35152.1}; DE SubName: Full=Xylose-regulated ABC transporter, ATP-binding protein 1 {ECO:0000313|EMBL:AGL48981.1}; GN OrderedLocusNames=TM_0058 {ECO:0000313|EMBL:AAD35152.1}; GN ORFNames=Tmari_0055 {ECO:0000313|EMBL:AGL48981.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35152.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35152.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35152.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48981.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48981.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35152.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48981.1; -; Genomic_DNA. DR PIR; C72424; C72424. DR RefSeq; NP_227874.1; NC_000853.1. DR RefSeq; WP_004082546.1; NZ_CP011107.1. DR STRING; 243274.TM0058; -. DR TCDB; 3.A.1.5.29; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35152; AAD35152; TM_0058. DR EnsemblBacteria; AGL48981; AGL48981; Tmari_0055. DR GeneID; 896882; -. DR KEGG; tma:TM0058; -. DR KEGG; tmi:THEMA_04515; -. DR KEGG; tmm:Tmari_0055; -. DR KEGG; tmw:THMA_0054; -. DR PATRIC; 23934956; VBITheMar51294_0056. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR KO; K02031; -. DR OMA; KLNTSIM; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-58-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS00554975, KW ECO:0000313|EMBL:AAD35152.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00554975, KW ECO:0000313|EMBL:AAD35152.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 7 261 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 331 AA; 37225 MW; CB4B6299D582A2CB CRC64; MEKVLEIRDL KVYFDLTEGT VKAVDGVSFD IRRGEILGLV GESGCGKSVT AQSILRILPK SARIVNGEIV FHRNGKTLDL TRLDPEGEEI RDIRGKDISM IFQEPMASFS PVYTVGAQMI EAILLHENVS KEEARKRVVE MLKKVKIPNA EKVVDMYPFE LSGGMLQRCM IAMAMSLNPT LLLADEPTTA LDVTIQAQIL YLMKELQKEY HSSILLITHD MGVVAQMADR VAVMYLGNIV ETAEVFELFK NPLHPYTQAL LRSIPKIGIR KTRLETIKGM VPDPYNLPTG CRFHNRCEKF MKGLCDVKEP PEVEVKPGHK VKCFLYGGEK E // ID Q9X244_THEMA Unreviewed; 144 AA. AC Q9X244; G4FGA7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=GNAT family acetyltransferase YjcF {ECO:0000313|EMBL:AGL50652.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36786.1}; GN OrderedLocusNames=TM_1720 {ECO:0000313|EMBL:AAD36786.1}; GN ORFNames=Tmari_1728 {ECO:0000313|EMBL:AGL50652.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36786.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36786.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36786.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50652.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50652.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36786.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50652.1; -; Genomic_DNA. DR PIR; D72219; D72219. DR RefSeq; NP_229519.1; NC_000853.1. DR RefSeq; WP_004082236.1; NZ_CP011107.1. DR STRING; 243274.TM1720; -. DR EnsemblBacteria; AAD36786; AAD36786; TM_1720. DR EnsemblBacteria; AGL50652; AGL50652; Tmari_1728. DR GeneID; 897228; -. DR KEGG; tma:TM1720; -. DR KEGG; tmi:THEMA_05640; -. DR KEGG; tmm:Tmari_1728; -. DR KEGG; tmw:THMA_1762; -. DR PATRIC; 23938416; VBITheMar51294_1738. DR eggNOG; ENOG41082BV; Bacteria. DR eggNOG; ENOG41121PI; LUCA. DR OMA; FIGTARI; -. DR OrthoDB; EOG6DZF58; -. DR BioCyc; TMAR243274:GC6P-1768-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR Pfam; PF13673; Acetyltransf_10; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL50652.1}. FT DOMAIN 3 143 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 144 AA; 16972 MW; CA3654DFE31562DC CRC64; MKVIFFENDE ELLREALNIR RKVFVEEQGV PEEEELDGKD PESVHVLLEK EGKFIGTARI RKIDDGTFKI ERVAILKEER RKGHGRFLME SIERELSSKG VQKIVLNAQI QVREFYERLG YRAEGEIFYE ANIPHVRMVK VVKR // ID Q9X036_THEMA Unreviewed; 254 AA. AC Q9X036; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 100. DE SubName: Full=Methyltransferase {ECO:0000313|EMBL:AGL49865.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:AGL49865.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36019.1}; GN OrderedLocusNames=TM_0938 {ECO:0000313|EMBL:AAD36019.1}; GN ORFNames=Tmari_0940 {ECO:0000313|EMBL:AGL49865.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36019.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36019.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36019.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49865.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49865.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36019.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49865.1; -; Genomic_DNA. DR PIR; B72316; B72316. DR RefSeq; NP_228746.1; NC_000853.1. DR RefSeq; WP_010865221.1; NZ_CP011107.1. DR STRING; 243274.TM0938; -. DR EnsemblBacteria; AAD36019; AAD36019; TM_0938. DR EnsemblBacteria; AGL49865; AGL49865; Tmari_0940. DR GeneID; 898612; -. DR KEGG; tma:TM0938; -. DR KEGG; tmi:THEMA_09660; -. DR KEGG; tmm:Tmari_0940; -. DR KEGG; tmw:THMA_0960; -. DR PATRIC; 23936807; VBITheMar51294_0952. DR eggNOG; ENOG4108D32; Bacteria. DR eggNOG; ENOG410ZRMN; LUCA. DR OMA; FYKLANI; -. DR OrthoDB; EOG69WFPC; -. DR BioCyc; TMAR243274:GC6P-968-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR029063; SAM-dependent_MTases. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Methyltransferase {ECO:0000313|EMBL:AGL49865.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49865.1}. SQ SEQUENCE 254 AA; 29564 MW; 4021BA89358F5611 CRC64; MGNIYKRFAR VFHEGPYTSF SRRIAKNFAK ILENFHIRGK KVLDVACGEG TFAVEIAKQG FKVVGVDLSS EMLKFARKRA KEESISVVFL KKDMRELDFH EEFDIVTCWF DSLNYLLDYK DLKKTFEKVH EALKTGGAFL FDMNTVYGLL MANQEGPVYI QQDGKDIFEV QTIEFDLEES VATFYVTVFE RKEEELWERF DEIHRERGYR VKEIASALSE TGFVFSFYED LLSKSPLTSY SRRLWCAARK VSAG // ID Q9WYF8_THEMA Unreviewed; 336 AA. AC Q9WYF8; G4FHN6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=ABC transporter, periplasmic substrate-binding protein, putative {ECO:0000313|EMBL:AAD35410.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL49246.1}; GN OrderedLocusNames=TM_0322 {ECO:0000313|EMBL:AAD35410.1}; GN ORFNames=Tmari_0320 {ECO:0000313|EMBL:AGL49246.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35410.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35410.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35410.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49246.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49246.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35410.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49246.1; -; Genomic_DNA. DR PIR; E72389; E72389. DR RefSeq; NP_228134.1; NC_000853.1. DR RefSeq; WP_004083072.1; NZ_CP011107.1. DR PDB; 2HPG; X-ray; 1.90 A; A/B/C/D=17-336. DR PDBsum; 2HPG; -. DR STRING; 243274.TM0322; -. DR EnsemblBacteria; AAD35410; AAD35410; TM_0322. DR EnsemblBacteria; AGL49246; AGL49246; Tmari_0320. DR GeneID; 897265; -. DR KEGG; tma:TM0322; -. DR KEGG; tmi:THEMA_03115; -. DR KEGG; tmm:Tmari_0320; -. DR KEGG; tmw:THMA_0329; -. DR PATRIC; 23935523; VBITheMar51294_0327. DR eggNOG; ENOG4105DR6; Bacteria. DR eggNOG; COG1638; LUCA. DR OMA; PYYDEYL; -. DR OrthoDB; EOG6NWBMZ; -. DR BioCyc; TMAR243274:GC6P-335-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR InterPro; IPR004682; TRAP_DctP. DR InterPro; IPR018389; TRAP_DctP/TeaA. DR Pfam; PF03480; DctP; 1. DR PIRSF; PIRSF006470; DctB; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2HPG}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 336 AA; 38142 MW; 1A4B885615321A3A CRC64; MSRRLLLILV LGVFLVSAVF GAKYTLRFGH VLAPGEPYHQ AFLKWAKAVE EKTNGDVRIE VFPSSQLGVE EDIIEQIRMG APVGWNTDSA RLGMYVKDIG VMNLAYFIDF MGAKTPEEAI EVLKKIKQSP TMQKWLKELE QRFGIKVLSF YWVQGYRHFV TNKPIRKPED LNGLRIRTPG APAWQESIRS LGAIPVAVNF GEIYTAVQTR AVDGAELTYA NVYNGGLYEV LKYMSETGHF LLINFEIVSA DWFNSLPKEY QKIIEEEMDK AGIEVSLKIM KELEEEYKQK CIEKGMAVIP ASEIDKEAFM EKAKQAYKNL GLENALNQLI KEVKGE // ID Q9WZ52_THEMA Unreviewed; 434 AA. AC Q9WZ52; G4FDN7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 107. DE SubName: Full=Lipopolysaccharide biosynthesis protein {ECO:0000313|EMBL:AAD35668.1}; DE SubName: Full=UDP-glucose dehydrogenase {ECO:0000313|EMBL:AGL49506.1}; DE EC=1.1.1.22 {ECO:0000313|EMBL:AGL49506.1}; GN OrderedLocusNames=TM_0583 {ECO:0000313|EMBL:AAD35668.1}; GN ORFNames=Tmari_0581 {ECO:0000313|EMBL:AGL49506.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35668.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35668.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35668.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49506.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49506.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase CC family. {ECO:0000256|PIRNR:PIRNR000124}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35668.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49506.1; -; Genomic_DNA. DR PIR; H72358; H72358. DR RefSeq; NP_228393.1; NC_000853.1. DR RefSeq; WP_004081274.1; NZ_CP011107.1. DR STRING; 243274.TM0583; -. DR EnsemblBacteria; AAD35668; AAD35668; TM_0583. DR EnsemblBacteria; AGL49506; AGL49506; Tmari_0581. DR GeneID; 897653; -. DR KEGG; tma:TM0583; -. DR KEGG; tmi:THEMA_01750; -. DR KEGG; tmm:Tmari_0581; -. DR KEGG; tmw:THMA_0598; -. DR PATRIC; 23936077; VBITheMar51294_0592. DR eggNOG; ENOG4107SIZ; Bacteria. DR eggNOG; COG0677; LUCA. DR OMA; SMLAIQG; -. DR OrthoDB; EOG65F8TP; -. DR BioCyc; TMAR243274:GC6P-608-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR017476; UDP-Glc/GDP-Man. DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C. DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer. DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N. DR InterPro; IPR028359; UDP_ManNAc/GlcNAc_DH. DR PANTHER; PTHR11374; PTHR11374; 1. DR Pfam; PF00984; UDPG_MGDP_dh; 1. DR Pfam; PF03720; UDPG_MGDP_dh_C; 1. DR Pfam; PF03721; UDPG_MGDP_dh_N; 1. DR PIRSF; PIRSF500136; UDP_ManNAc_DH; 1. DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1. DR SMART; SM00984; UDPG_MGDP_dh_C; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52413; SSF52413; 1. DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49506.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 327 423 UDPG_MGDP_dh_C. FT {ECO:0000259|SMART:SM00984}. SQ SEQUENCE 434 AA; 48690 MW; ACC8D92E5B8335BC CRC64; MLKEKLLSKT ALLGVIGLGY VGLPLAVEKA KAGYRVLGFD IQKKRVDMVN RGENYIGDVV DEDLKDLVEK GMIRATTDFS EMKNCDVVTI CVPTPLGKYK EPDLTYVINT AKEIAKYLHR EMLVVLESTT YPGTTEEVVL PILESTGLKV GKDFYLAFSP ERVDPGNKIY KTKNTPKVVG GVTEKCTELA KILYENVLEA PVHTVSSPRA AEMAKVLENT FRLVNISLIN EVAIVARRMG INIWEVIDAA ATKPFGFMPF YPGPGAGGHC IPIDPFYLAY KAKEYDVRLD LVEMAGEIND FMPEYVVMRV QDILNERKKP LNGSKVLLLG VAYKGDIDDT RESPALKVWD HLEKKKAVVE FFDPYVPEVK RGDRIHRRVE LTEEYLKGVD IVVITTAHKN GVDYDFVVKN APVVFDTKNI TKDVKENRDK IILL // ID Q9X0S3_THEMA Unreviewed; 319 AA. AC Q9X0S3; G4FEF0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 124. DE SubName: Full=Dipeptide transport ATP-binding protein DppF {ECO:0000313|EMBL:AGL50127.1}; DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36271.1}; GN OrderedLocusNames=TM_1196 {ECO:0000313|EMBL:AAD36271.1}; GN ORFNames=Tmari_1203 {ECO:0000313|EMBL:AGL50127.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36271.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36271.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36271.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50127.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50127.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36271.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50127.1; -; Genomic_DNA. DR PIR; A72284; A72284. DR RefSeq; NP_229001.1; NC_000853.1. DR RefSeq; WP_004080132.1; NZ_CP011107.1. DR STRING; 243274.TM1196; -. DR EnsemblBacteria; AAD36271; AAD36271; TM_1196. DR EnsemblBacteria; AGL50127; AGL50127; Tmari_1203. DR GeneID; 898288; -. DR KEGG; tma:TM1196; -. DR KEGG; tmi:THEMA_08350; -. DR KEGG; tmm:Tmari_1203; -. DR KEGG; tmw:THMA_1222; -. DR PATRIC; 23937334; VBITheMar51294_1214. DR eggNOG; ENOG4105GTU; Bacteria. DR eggNOG; COG4608; LUCA. DR KO; K02032; -. DR OMA; SRAKHIR; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1226-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36271.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36271.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 5 253 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 319 AA; 36171 MW; DB564B7A4C171A80 CRC64; MEDTLILKNL TKVYSIGSLL FRSKITAVDD VSFSLKRAEI FTLAGESGCG KSTTAKMILG FEEPTSGDII FEGNSIQWWK KRKKDFLRKV QAVFQNPFES FNPLLTVDDI FFETVMNYGL ANSRNEAEKL IDEKLQLVGL KFEDINGRYQ SELSGGQLQR ASIARSLLSN PSLLIADEPV SMVDASLRMS IVNLFAKLRD QLGVSVIYIT HDLATAYYVS DRIAIMFRGN IVETGPVDKV LIDPKHPYTQ LLRESIPDPD PEKKWSREIT VSDTEYEEYL KEGCKFAGRC PYVKEICRRE KPDDVLVDGV LVKCHIYKK // ID Q9X0F8_THEMA Unreviewed; 252 AA. AC Q9X0F8; G4FES9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 105. DE SubName: Full=Transcriptional regulator of rhamnose utilization, DeoR family {ECO:0000313|EMBL:AGL49997.1}; DE SubName: Full=Transcriptional regulator, DeoR family {ECO:0000313|EMBL:AAD36146.1}; GN OrderedLocusNames=TM_1069 {ECO:0000313|EMBL:AAD36146.1}; GN ORFNames=Tmari_1073 {ECO:0000313|EMBL:AGL49997.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36146.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36146.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36146.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49997.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49997.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 HTH deoR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000712}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36146.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49997.1; -; Genomic_DNA. DR PIR; G72298; G72298. DR RefSeq; NP_228875.1; NC_000853.1. DR RefSeq; WP_004080418.1; NZ_CP011107.1. DR STRING; 243274.TM1069; -. DR DNASU; 897151; -. DR EnsemblBacteria; AAD36146; AAD36146; TM_1069. DR EnsemblBacteria; AGL49997; AGL49997; Tmari_1073. DR GeneID; 897151; -. DR KEGG; tma:TM1069; -. DR KEGG; tmi:THEMA_09015; -. DR KEGG; tmm:Tmari_1073; -. DR KEGG; tmw:THMA_1091; -. DR PATRIC; 23937067; VBITheMar51294_1082. DR eggNOG; ENOG4105E98; Bacteria. DR eggNOG; COG1349; LUCA. DR OMA; FQTVPTD; -. DR OrthoDB; EOG6XSZXW; -. DR BioCyc; TMAR243274:GC6P-1098-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014036; DeoR_C. DR InterPro; IPR001034; DeoR_HTH. DR InterPro; IPR018356; Tscrpt_reg_HTH_DeoR_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00455; DeoRC; 1. DR Pfam; PF08220; HTH_DeoR; 1. DR PRINTS; PR00037; HTHLACR. DR SMART; SM00420; HTH_DEOR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS00894; HTH_DEOR_1; 1. DR PROSITE; PS51000; HTH_DEOR_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000712, KW ECO:0000256|SAAS:SAAS00589027}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU000712, KW ECO:0000256|SAAS:SAAS00132188}; KW Transcription regulation {ECO:0000256|RuleBase:RU000712, KW ECO:0000256|SAAS:SAAS00132188}. FT DOMAIN 2 57 HTH deoR-type DNA-binding. FT {ECO:0000259|PROSITE:PS51000}. SQ SEQUENCE 252 AA; 28484 MW; 9393B7F65919561E CRC64; MKEERLKEIL DIVDRNGFIS MKDLQEQLGV SMITVRRDVA ELVKRNLVKK VHGGIRKVNY FEKETDFMKR LSINREAKEK IAQLALNFVE DGDIIFLDAS TTAHIFAKHL ASSQKSVHVI TNNLLTAMEL SKNSDISVVL LTGKVNPENL AVEGSLTIEC GKKFSVKKAF VSCRGVTAEE GTYEINTMEM GIKGIFVERA EEIFVLADFS KIGKRSLAHL IPAEKIDHLI TDRKPPENQY EIFREKGVEI VY // ID Q9X0V9_THEMA Unreviewed; 355 AA. AC Q9X0V9; G4FEB4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 127. DE SubName: Full=Sugar ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36307.1}; DE SubName: Full=Sugar-binding transport ATP-binding protein {ECO:0000313|EMBL:AGL50163.1}; GN OrderedLocusNames=TM_1232 {ECO:0000313|EMBL:AAD36307.1}; GN ORFNames=Tmari_1239 {ECO:0000313|EMBL:AGL50163.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36307.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36307.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36307.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50163.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50163.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00562907}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36307.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50163.1; -; Genomic_DNA. DR PIR; A72279; A72279. DR RefSeq; NP_229037.1; NC_000853.1. DR RefSeq; WP_004080048.1; NZ_CP011107.1. DR SMR; Q9X0V9; 1-354. DR STRING; 243274.TM1232; -. DR EnsemblBacteria; AAD36307; AAD36307; TM_1232. DR EnsemblBacteria; AGL50163; AGL50163; Tmari_1239. DR GeneID; 898252; -. DR KEGG; tma:TM1232; -. DR KEGG; tmi:THEMA_08170; -. DR KEGG; tmm:Tmari_1239; -. DR KEGG; tmw:THMA_1258; -. DR PATRIC; 23937406; VBITheMar51294_1250. DR eggNOG; ENOG4108IJ9; Bacteria. DR eggNOG; COG3839; LUCA. DR KO; K10112; -. DR OMA; RLQLTKC; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1262-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00452173, ECO:0000313|EMBL:AAD36307.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00452173, ECO:0000313|EMBL:AAD36307.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00452289}. FT DOMAIN 4 234 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 355 AA; 39814 MW; 44F330C0316CE3EF CRC64; MAQVKIDGVK KYFGNVRALD GIDLVVNEGE FLVLLGPSGC GKTTLLRCIA GLEQVTGGKI FFNDRDVTNL PPKDRNISMV FQSYAVWPHM KVYDNIAYPL KLKKVPKEEI EKRVKWAADL LHISELLDRY PAQLSGGQRQ RVAVARAIVH EPEVLLMDEP LSNLDALLRV KMRSELKKLQ ERIGVTTIYV THDQTEAMTM GDRIAVMNQG KLQQVGTPSE IYHHPVNIFV AGFVGSPQMN FLEMEVRSEG NSVVLQNGEI KIPAKTDPGA KKVILGIRPE NVYLEEKPNT LKLEGEVYFA EKLMSDTILH LNVGSEKIVA KIPGDVDFRS GEKITFFLDV EKIHLFHPET GERIS // ID Q9WZW5_THEMA Unreviewed; 293 AA. AC Q9WZW5; G4FCW3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 103. DE RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464}; GN Name=secF {ECO:0000256|HAMAP-Rule:MF_01464}; GN OrderedLocusNames=TM_0861 {ECO:0000313|EMBL:AAD35943.1}; GN ORFNames=Tmari_0863 {ECO:0000313|EMBL:AGL49788.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35943.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35943.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35943.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49788.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49788.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts CC with the SecYEG preprotein conducting channel. SecDF uses the CC proton motive force (PMF) to complete protein translocation after CC the ATP-dependent function of SecA. {ECO:0000256|HAMAP- CC Rule:MF_01464, ECO:0000256|SAAS:SAAS00541769}. CC -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec CC protein translocation apparatus which comprises SecA, SecYEG and CC auxiliary proteins SecDF. Other proteins may also be involved. CC {ECO:0000256|HAMAP-Rule:MF_01464}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01464}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01464}. CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01464}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35943.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49788.1; -; Genomic_DNA. DR PIR; F72325; F72325. DR RefSeq; NP_228670.1; NC_000853.1. DR RefSeq; WP_004080745.1; NZ_CP011107.1. DR STRING; 243274.TM0861; -. DR EnsemblBacteria; AAD35943; AAD35943; TM_0861. DR EnsemblBacteria; AGL49788; AGL49788; Tmari_0863. DR GeneID; 898534; -. DR KEGG; tma:TM0861; -. DR KEGG; tmi:THEMA_00330; -. DR KEGG; tmm:Tmari_0863; -. DR KEGG; tmw:THMA_0883; -. DR PATRIC; 23936650; VBITheMar51294_0874. DR eggNOG; ENOG4107VRQ; Bacteria. DR eggNOG; COG0341; LUCA. DR KO; K03074; -. DR OMA; RSINTMM; -. DR OrthoDB; EOG676Z5R; -. DR BioCyc; TMAR243274:GC6P-891-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR GO; GO:0015031; P:protein transport; IBA:GO_Central. DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01464_B; SecF_B; 1. DR InterPro; IPR022813; SecD/SecF_arch_bac. DR InterPro; IPR022645; SecD/SecF_bac. DR InterPro; IPR022646; SecD/SecF_CS. DR InterPro; IPR005665; SecF_bac. DR InterPro; IPR000731; SSD. DR Pfam; PF07549; Sec_GG; 1. DR Pfam; PF02355; SecD_SecF; 1. DR PRINTS; PR01755; SECFTRNLCASE. DR TIGRFAMs; TIGR00916; 2A0604s01; 1. DR TIGRFAMs; TIGR00966; 3a0501s07; 1. DR PROSITE; PS50156; SSD; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01464}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425143}; KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425069}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Translocation {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425069}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425143}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425143}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01464, KW ECO:0000256|SAAS:SAAS00425069}. FT TRANSMEM 13 33 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 136 156 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 158 178 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 179 199 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 247 267 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 268 288 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01464}. FT DOMAIN 154 289 SSD (sterol-sensing). FT {ECO:0000259|PROSITE:PS50156}. SQ SEQUENCE 293 AA; 32716 MW; EBA8363448C8CBCE CRC64; MRKEIDFMGK SKIFITISLI LIAISIVSIF TKGFNFGVEF TGGSEIIVRF ENKEVTENDI RAAISQISEE FANARIVEVR SAGDPSNVQK YSIIVPKTYE PDEKQKIQEE MEKLLSGKVV SFNEISGTAA EEIRRGTWTA ILVALVVLLI YITIRFRFIF GVAAVVALIH DVLITMGFFS LFGYEINVAA VAAFLTLLGY SLNDTIVLSD RIRENMRRYR GRNMVNIVNM SINQVLARTI NTSLTTFFVV FVLLLFAGNA VKPFAFGMTV GTIVGTYSSL YVASPIIVKW TKQ // ID Q9S5X9_THEMA Unreviewed; 434 AA. AC Q9S5X9; G4FG42; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 11-MAY-2016, entry version 100. DE SubName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000313|EMBL:AAD36720.1}; DE EC=2.4.2.2 {ECO:0000313|EMBL:AGL50586.1}; GN OrderedLocusNames=TM_1653 {ECO:0000313|EMBL:AAD36720.1}; GN ORFNames=Tmari_1662 {ECO:0000313|EMBL:AGL50586.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36720.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36720.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36720.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50586.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50586.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS00431861}. CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside CC phosphorylase family. {ECO:0000256|SAAS:SAAS00547054}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36720.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50586.1; -; Genomic_DNA. DR PIR; B72228; B72228. DR RefSeq; NP_229453.1; NC_000853.1. DR RefSeq; WP_004082160.1; NZ_CP011107.1. DR SMR; Q9S5X9; 1-433. DR STRING; 243274.TM1653; -. DR EnsemblBacteria; AAD36720; AAD36720; TM_1653. DR EnsemblBacteria; AGL50586; AGL50586; Tmari_1662. DR GeneID; 897914; -. DR KEGG; tma:TM1653; -. DR KEGG; tmi:THEMA_05980; -. DR KEGG; tmm:Tmari_1662; -. DR KEGG; tmw:THMA_1694; -. DR PATRIC; 23938280; VBITheMar51294_1672. DR eggNOG; ENOG4105CMW; Bacteria. DR eggNOG; COG0213; LUCA. DR KO; K00756; -. DR OMA; ESVPGFH; -. DR OrthoDB; EOG61ZTGG; -. DR BioCyc; TMAR243274:GC6P-1699-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004645; F:phosphorylase activity; IEA:InterPro. DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro. DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro. DR Gene3D; 3.40.1030.10; -; 1. DR Gene3D; 3.90.1170.30; -; 1. DR InterPro; IPR000312; Glycosyl_Trfase_fam3. DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom. DR InterPro; IPR013102; PYNP_C. DR InterPro; IPR018090; Pyrmidine_PPas_bac/euk. DR InterPro; IPR017872; Pyrmidine_PPase_CS. DR InterPro; IPR000053; Thymidine/pyrmidine_PPase. DR PANTHER; PTHR10515; PTHR10515; 1. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR Pfam; PF07831; PYNP_C; 1. DR PIRSF; PIRSF000478; TP_PyNP; 1. DR SMART; SM00941; PYNP_C; 1. DR SUPFAM; SSF47648; SSF47648; 1. DR SUPFAM; SSF52418; SSF52418; 1. DR SUPFAM; SSF54680; SSF54680; 1. DR TIGRFAMs; TIGR02644; Y_phosphoryl; 1. DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000256|SAAS:SAAS00431890, KW ECO:0000313|EMBL:AGL50586.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00431890, KW ECO:0000313|EMBL:AGL50586.1}. FT DOMAIN 345 419 PYNP_C. {ECO:0000259|SMART:SM00941}. SQ SEQUENCE 434 AA; 47129 MW; 7E9881549893B2D6 CRC64; MRAYDVILKK RNGEKLSREE IEFMVGGYVK GEIPDYQMAA FLMAVYFRHL DEEETYYFTE TMMRSGEVLD LSEIPGTKVD KHSTGGVGDK TTLVVAPLVA SAGVPVAKMS GRALGHTGGT IDKLESIPGF RTELSLEEFI KNVKKYGIAI VGQTGNLVPA DKKIYALRDA TATVDEISLI ASSIMSKKLA GGSDAFVLDV KFGTGAFMKG FEDAKKLAFL MLRIAQQHGK KAVAVLSNMD QPLGKAVGNS LEVIEAIETL KGNGPEDLKE LSLTLGALML ELAGVADFEE GKKILQEKLE TGEALDKFRL LVKAQGGNER VVDDPWRVLP VAEQVVEFSA AREGFVSKID AEKVGIASMM LGAGRKKKED RIDHSVGIIV EKKLGDSVKK GEAIARLFVS DRSDVESALK LLKEAYVISD SPSEPPRVVE EVIK // ID Q9X057_THEMA Unreviewed; 238 AA. AC Q9X057; G4FF28; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Beta-propeller domains of methanol dehydrogenase type {ECO:0000313|EMBL:AGL49889.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36041.1}; GN OrderedLocusNames=TM_0962 {ECO:0000313|EMBL:AAD36041.1}; GN ORFNames=Tmari_0964 {ECO:0000313|EMBL:AGL49889.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36041.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36041.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36041.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49889.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49889.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36041.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49889.1; -; Genomic_DNA. DR PIR; G72311; G72311. DR RefSeq; NP_228770.1; NC_000853.1. DR RefSeq; WP_004080600.1; NZ_CP011107.1. DR STRING; 243274.TM0962; -. DR EnsemblBacteria; AAD36041; AAD36041; TM_0962. DR EnsemblBacteria; AGL49889; AGL49889; Tmari_0964. DR GeneID; 898699; -. DR KEGG; tma:TM0962; -. DR KEGG; tmi:THEMA_09535; -. DR KEGG; tmm:Tmari_0964; -. DR KEGG; tmw:THMA_0985; -. DR PATRIC; 23936855; VBITheMar51294_0976. DR eggNOG; ENOG4105HA9; Bacteria. DR eggNOG; COG1512; LUCA. DR KO; K06872; -. DR OMA; KEGEYDK; -. DR OrthoDB; EOG644ZVP; -. DR BioCyc; TMAR243274:GC6P-992-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007621; TPM_dom. DR Pfam; PF04536; TPM_phosphatase; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 176 196 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 30 153 TPM_phosphatase. FT {ECO:0000259|Pfam:PF04536}. SQ SEQUENCE 238 AA; 25797 MW; C2AC04257B1B4FF7 CRC64; MRKIFLLIFI VSSVLLLSVE FPKPTPYKYV NDYVGVLDKT TVEKIISVGK ELENKTTAQV VVVVVPSLSG LTVEEYANRL FREWGIGQKE KNNGVLLLVA MNDRKVRIEV GYGLEGAIPD GKAGRILDEY VIPYFKNGEY SKGIYYGYLA IANEVAKEYG VELTGTSDLP ERGTDISGIS IIVIVIAFII FSSIMGRGRR WYRGPRFPGG FGGSRGGSGG FGGFGEGSSG GGGASRGW // ID Q9X1M1_THEMA Unreviewed; 299 AA. AC Q9X1M1; G4FFS3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 110. DE SubName: Full=Chain A of octaprenyl pyrophosphate synthase {ECO:0000313|EMBL:AGL50467.1}; DE SubName: Full=Octoprenyl-diphosphate synthase, putative {ECO:0000313|EMBL:AAD36602.1}; GN OrderedLocusNames=TM_1535 {ECO:0000313|EMBL:AAD36602.1}; GN ORFNames=Tmari_1543 {ECO:0000313|EMBL:AGL50467.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36602.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36602.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36602.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1VG2, ECO:0000213|PDB:1VG3, ECO:0000213|PDB:1VG4} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS). RX PubMed=15196010; DOI=10.1021/bi036336d; RA Guo R.T., Kuo C.J., Ko T.P., Chou C.C., Liang P.H., Wang A.H.; RT "A molecular ruler for chain elongation catalyzed by octaprenyl RT pyrophosphate synthase and its structure-based engineering to produce RT unprecedented long chain trans-prenyl products."; RL Biochemistry 43:7678-7686(2004). RN [3] {ECO:0000213|PDB:1V4E, ECO:0000213|PDB:1V4H, ECO:0000213|PDB:1V4I} RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS). RX PubMed=14617622; DOI=10.1074/jbc.M310161200; RA Guo R.T., Kuo C.J., Chou C.C., Ko T.P., Shr H.L., Liang P.H., RA Wang A.H.; RT "Crystal structure of octaprenyl pyrophosphate synthase from RT hyperthermophilic Thermotoga maritima and mechanism of product chain RT length determination."; RL J. Biol. Chem. 279:4903-4912(2004). RN [4] {ECO:0000213|PDB:1WKZ, ECO:0000213|PDB:1WL0, ECO:0000213|PDB:1WL1} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS). RA Guo R.T., Kuo C.J., Cheng Y.S., Cheng Y.L., Liang P.H., Wang A.H.-J.; RT "Biochemical and Structural Basis for Octaprenyl Pyrophosphate RT Synthase."; RL Submitted (JUN-2004) to the PDB data bank. RN [5] {ECO:0000213|PDB:2AZL} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS). RX PubMed=16291686; DOI=10.1128/JB.187.23.8137-8148.2005; RA Sun H.Y., Ko T.P., Kuo C.J., Guo R.T., Chou C.C., Liang P.H., RA Wang A.H.; RT "Homodimeric hexaprenyl pyrophosphate synthase from the RT thermoacidophilic crenarchaeon Sulfolobus solfataricus displays RT asymmetric subunit structures."; RL J. Bacteriol. 187:8137-8148(2005). RN [6] {ECO:0000313|EMBL:AGL50467.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50467.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. CC {ECO:0000256|RuleBase:RU004466}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36602.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50467.1; -; Genomic_DNA. DR PIR; C72242; C72242. DR RefSeq; NP_229335.1; NC_000853.1. DR RefSeq; WP_004081914.1; NZ_CP011107.1. DR PDB; 1V4E; X-ray; 2.28 A; A/B=1-299. DR PDB; 1V4H; X-ray; 2.80 A; A=1-299. DR PDB; 1V4I; X-ray; 2.40 A; A=1-299. DR PDB; 1V4J; X-ray; 2.85 A; A/B=1-299. DR PDB; 1V4K; X-ray; 2.45 A; A=1-299. DR PDB; 1VG2; X-ray; 3.10 A; A=1-299. DR PDB; 1VG3; X-ray; 2.70 A; A=1-299. DR PDB; 1VG4; X-ray; 3.30 A; A/B=1-299. DR PDB; 1VG6; X-ray; 3.35 A; A=1-299. DR PDB; 1VG7; X-ray; 3.40 A; A=1-299. DR PDB; 1WKZ; X-ray; 3.40 A; A/B=1-299. DR PDB; 1WL0; X-ray; 3.20 A; A/B=1-299. DR PDB; 1WL1; X-ray; 3.45 A; A/B=1-299. DR PDB; 1WL2; X-ray; 2.80 A; A=1-299. DR PDB; 1WL3; X-ray; 3.50 A; A/B=1-299. DR PDB; 2AZL; X-ray; 2.80 A; A=1-299. DR PDBsum; 1V4E; -. DR PDBsum; 1V4H; -. DR PDBsum; 1V4I; -. DR PDBsum; 1V4J; -. DR PDBsum; 1V4K; -. DR PDBsum; 1VG2; -. DR PDBsum; 1VG3; -. DR PDBsum; 1VG4; -. DR PDBsum; 1VG6; -. DR PDBsum; 1VG7; -. DR PDBsum; 1WKZ; -. DR PDBsum; 1WL0; -. DR PDBsum; 1WL1; -. DR PDBsum; 1WL2; -. DR PDBsum; 1WL3; -. DR PDBsum; 2AZL; -. DR SMR; Q9X1M1; 9-288. DR STRING; 243274.TM1535; -. DR EnsemblBacteria; AAD36602; AAD36602; TM_1535. DR EnsemblBacteria; AGL50467; AGL50467; Tmari_1543. DR GeneID; 897656; -. DR KEGG; tma:TM1535; -. DR KEGG; tmi:THEMA_06610; -. DR KEGG; tmm:Tmari_1543; -. DR KEGG; tmw:THMA_1569; -. DR PATRIC; 23938030; VBITheMar51294_1553. DR eggNOG; ENOG4105EAH; Bacteria. DR eggNOG; COG0142; LUCA. DR KO; K02523; -. DR OMA; RDWNGLM; -. DR OrthoDB; EOG6TN43W; -. DR BioCyc; TMAR243274:GC6P-1575-MONOMER; -. DR BRENDA; 2.5.1.90; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.600.10; -; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR017446; Polyprenyl_synth-rel. DR PANTHER; PTHR12001; PTHR12001; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SUPFAM; SSF48576; SSF48576; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1V4E, ECO:0000213|PDB:1V4H, KW ECO:0000213|PDB:1V4I, ECO:0000213|PDB:1V4J}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU004466}. SQ SEQUENCE 299 AA; 33858 MW; 8924C8CD98C418F9 CRC64; MTKNKLNQNS YELEKVKERI EQILSQFFPE QIMKDLPLYG KMLRVRLSIL SFKNRGVEIG EDAISSLAAL ELVHLASLLH DDVIDGARFR RGKETINFMY GDKAAVAAGD LVLVSAFHTV EEIGNNKLRR AFLNVIGKMS EAELIEQLSR YKPITKEEYL RIVEGKSGAL FGLALQLPAL LEGELGEDLY NLGVTIGTIY QMFDDIMDFA GMEKIGKDGF LDLKNGVASF PLVTAMEKFP EARQMFENRD WSGLMSFMRE KGILKECEET LKVLVKNVII ENSWLRDFVD GIFKIKISS // ID Q9WZ03_THEMA Unreviewed; 516 AA. AC Q9WZ03; G4FDT8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35618.1}; DE SubName: Full=Oligopeptide transport system permease protein OppC {ECO:0000313|EMBL:AGL49455.1}; GN OrderedLocusNames=TM_0533 {ECO:0000313|EMBL:AAD35618.1}; GN ORFNames=Tmari_0530 {ECO:0000313|EMBL:AGL49455.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35618.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35618.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35618.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49455.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49455.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032, CC ECO:0000256|SAAS:SAAS00537635}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35618.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49455.1; -; Genomic_DNA. DR PIR; C72367; C72367. DR RefSeq; NP_228343.1; NC_000853.1. DR RefSeq; WP_004081374.1; NZ_CP011107.1. DR STRING; 243274.TM0533; -. DR EnsemblBacteria; AAD35618; AAD35618; TM_0533. DR EnsemblBacteria; AGL49455; AGL49455; Tmari_0530. DR GeneID; 897585; -. DR KEGG; tma:TM0533; -. DR KEGG; tmi:THEMA_02010; -. DR KEGG; tmm:Tmari_0530; -. DR KEGG; tmw:THMA_0546; -. DR PATRIC; 23935973; VBITheMar51294_0541. DR eggNOG; ENOG4105C2T; Bacteria. DR eggNOG; COG1173; LUCA. DR KO; K02034; -. DR OMA; MWRAFKK; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-557-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR025966; OppC_N. DR Pfam; PF00528; BPD_transp_1; 1. DR Pfam; PF12911; OppC_N; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00496716}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496716, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496724}. FT TRANSMEM 38 56 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 311 337 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 349 368 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 374 395 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 430 448 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 482 503 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 307 503 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 516 AA; 59014 MW; D327332747E1EBF1 CRC64; MAEEKTMIEN GEIEFKERVL SRRELVWRAF KRNKLGMFGL YVLIVLYLMA LFADFLSPHH PYEQSLKHSF APPTKIHREY KGERVGAYVL PTISYVDKAT FERKFYEMLF PKRLVLDVFG TQVEYEIGKD GVTGFSFMLD EEYYIVPKDG TMKYAGSTTK VVDYLLFGYD EKVLTKGEAD IETSSEAAKD TYFGKYGFRL GLNSPDEIEK VVIKEKLNMI LVKKGEDIEM ITGKVIDYDY KTYPVKWFVK SWGGDAKNRI GYLFWIFPFH YHLFGVDNYD NNEYVRLYIM GADQYGRDVW SRIVFASRIS LSIGFIGMFI TFALSLVFGG ISGYYGGIVD EFMMRFSEII MSLPGFYLLI LLRSLLPLDI PSTQVYVLLV FILSFIGWAG RARVIRGMVL SIKQREFVEA ARALGFPDTR ILFRHVLPNT ASYLIVAATL AIPGYILGEA SLSFLGLGIR EPSASWGLML AQAQNVTYMT KYPWLLIPGI FIFITVLSFN FVGDALRDAL DPRSLG // ID Q9WYW4_THEMA Unreviewed; 167 AA. AC Q9WYW4; G4FDX6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=Segregation and condensation protein B {ECO:0000256|SAAS:SAAS00459865}; GN OrderedLocusNames=TM_0494 {ECO:0000313|EMBL:AAD35579.1}; GN ORFNames=Tmari_0491 {ECO:0000313|EMBL:AGL49416.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35579.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35579.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35579.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49416.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49416.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Participates in chromosomal partition during cell CC division. May act via the formation of a condensin-like complex CC containing Smc and ScpA that pull DNA away from mid-cell into both CC cell halves. {ECO:0000256|SAAS:SAAS00459874}. CC -!- SUBUNIT: Homodimer. Homodimerization may be required to stabilize CC the binding of ScpA to the Smc head domains. Component of a CC cohesin-like complex composed of ScpA, ScpB and the Smc homodimer, CC in which ScpA and ScpB bind to the head domain of Smc. The CC presence of the three proteins is required for the association of CC the complex with DNA. {ECO:0000256|SAAS:SAAS00459884}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00570510}. CC -!- SIMILARITY: Belongs to the ScpB family. CC {ECO:0000256|SAAS:SAAS00570500}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35579.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49416.1; -; Genomic_DNA. DR PIR; E72370; E72370. DR RefSeq; NP_228304.1; NC_000853.1. DR RefSeq; WP_004081456.1; NZ_CP011107.1. DR STRING; 243274.TM0494; -. DR EnsemblBacteria; AAD35579; AAD35579; TM_0494. DR EnsemblBacteria; AGL49416; AGL49416; Tmari_0491. DR GeneID; 897535; -. DR KEGG; tma:TM0494; -. DR KEGG; tmi:THEMA_02200; -. DR KEGG; tmm:Tmari_0491; -. DR KEGG; tmw:THMA_0507; -. DR PATRIC; 23935893; VBITheMar51294_0501. DR eggNOG; ENOG41085JM; Bacteria. DR eggNOG; COG1386; LUCA. DR KO; K06024; -. DR OMA; FKDESMI; -. DR OrthoDB; EOG6CZQQQ; -. DR BioCyc; TMAR243274:GC6P-518-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0051304; P:chromosome separation; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 2. DR InterPro; IPR005234; ScpB_csome_segregation. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04079; SMC_ScpB; 1. DR PIRSF; PIRSF019345; ScpB; 1. DR SUPFAM; SSF46785; SSF46785; 2. DR TIGRFAMs; TIGR00281; TIGR00281; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|SAAS:SAAS00459868}; KW Cell division {ECO:0000256|SAAS:SAAS00459868}; KW Chromosome partition {ECO:0000256|SAAS:SAAS00459850}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00459854}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 167 AA; 18833 MW; EB3F7E01224865F9 CRC64; MQLKAAIEAL IFASNGITLE RLIKILEKDP EEIKRALEEL KKEYEDEAHG VVLREVNGRY RFFTKPEYAG FVSKLSGRKY KNLTDTQMEV VALLLISGPI PKSEIDAFRG KDSSAVLSSL QRMGIVRKKR KGKSYLYQLS PSFVESTMLD EILKEVSQKL SSDGGES // ID Q9WYK2_THEMA Unreviewed; 369 AA. AC Q9WYK2; G4FHT0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=Multidrug-efflux transporter, major facilitator superfamily (MFS) {ECO:0000313|EMBL:AGL49291.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35455.1}; GN OrderedLocusNames=TM_0368 {ECO:0000313|EMBL:AAD35455.1}; GN ORFNames=Tmari_0366 {ECO:0000313|EMBL:AGL49291.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35455.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35455.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35455.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49291.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49291.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35455.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49291.1; -; Genomic_DNA. DR PIR; F72384; F72384. DR RefSeq; NP_228179.1; NC_000853.1. DR RefSeq; WP_004083179.1; NZ_CP011107.1. DR STRING; 243274.TM0368; -. DR EnsemblBacteria; AAD35455; AAD35455; TM_0368. DR EnsemblBacteria; AGL49291; AGL49291; Tmari_0366. DR GeneID; 897327; -. DR KEGG; tma:TM0368; -. DR KEGG; tmi:THEMA_02875; -. DR KEGG; tmm:Tmari_0366; -. DR KEGG; tmw:THMA_0376; -. DR PATRIC; 23935617; VBITheMar51294_0373. DR eggNOG; ENOG4108729; Bacteria. DR eggNOG; COG0477; LUCA. DR OMA; MAFPYLS; -. DR OrthoDB; EOG6KHFWD; -. DR BioCyc; TMAR243274:GC6P-382-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 52 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 89 110 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 122 144 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 150 169 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 258 277 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 283 304 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 316 339 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 345 364 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 369 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 369 AA; 40448 MW; 8BD3519267F8C33B CRC64; MLFLTNVLRS MGTMSFNLLI QLRMKEIGAT LFLIGLLSSL QGAMNTFSNV FWGRISDKIG KRKVFIILSL VLASAFYPLY AVIDVPSAIL IVSMIIAFFN GMYPPAAMAL SSTAKKMSLG FSLYNSSNSL GMLLSRISIG FLLMFMDLKL AFVFFSIVVA VSVIPALGLK EEKIQKKKEE DFHFGRKVME HGIWALYLGS LLRQMGTSGS MSLIAVYLNE RFHYSASTIG FITAVNPLVQ IPSHFLFGKM VEKVDPKFIS VLGIFMSSLV PFLMMIPENW APVLAYAFLG ASFGAFINGS NNFLGRRFHY LQRGRALGLL SSARFLGATI GPFLAGLLAE KSYSLMFSTL GLAVLSGGIV VLLFTKGGD // ID Q9WYA2_THEMA Unreviewed; 239 AA. AC Q9WYA2; G4FHH8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 114. DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887}; DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887}; GN OrderedLocusNames=TM_0264 {ECO:0000313|EMBL:AAD35352.1}; GN ORFNames=Tmari_0262 {ECO:0000313|EMBL:AGL49188.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35352.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35352.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35352.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49188.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49188.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family. CC {ECO:0000256|RuleBase:RU003887, ECO:0000256|SAAS:SAAS00545889}. CC -!- SIMILARITY: Contains S4 RNA-binding domain. CC {ECO:0000256|SAAS:SAAS00568442}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35352.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49188.1; -; Genomic_DNA. DR PIR; G72400; G72400. DR RefSeq; NP_228077.1; NC_000853.1. DR RefSeq; WP_004082968.1; NZ_CP011107.1. DR STRING; 243274.TM0264; -. DR DNASU; 897175; -. DR EnsemblBacteria; AAD35352; AAD35352; TM_0264. DR EnsemblBacteria; AGL49188; AGL49188; Tmari_0262. DR GeneID; 897175; -. DR KEGG; tma:TM0264; -. DR KEGG; tmi:THEMA_03405; -. DR KEGG; tmm:Tmari_0262; -. DR KEGG; tmw:THMA_0271; -. DR PATRIC; 23935405; VBITheMar51294_0268. DR eggNOG; ENOG4105I08; Bacteria. DR eggNOG; COG1187; LUCA. DR KO; K06183; -. DR OMA; YTHRVIS; -. DR OrthoDB; EOG6130DV; -. DR BioCyc; TMAR243274:GC6P-277-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F. DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00093; TIGR00093; 1. DR PROSITE; PS01149; PSI_RSU; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000256|RuleBase:RU003887, KW ECO:0000256|SAAS:SAAS00429931}; Lyase {ECO:0000313|EMBL:AGL49188.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW RNA-binding {ECO:0000256|SAAS:SAAS00568463}. FT DOMAIN 1 66 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 239 AA; 27160 MW; D974C5047FCAF16E CRC64; MRLDRYLSNS GVGTRKEVKK LIKQGRVTVN GRVVLDPGHP VLENDAVALD GEVVRFHKKV YILFYKPSGY VTSTKDPHSE TIMEFLPPLK GIFPVGRLDK DAEGLLIITN DGDFAHRVIS PKWSVEKEYI VKVEGEVTED KIEKLKNGVT LRDGFFAKAK RVEKLSNDTL KIVITEGKYH QIKRMTAAVG LKTVHLKRTR IGGLVLPDDM KPGEYRFLSE EEVKKVFERE DQKEDTPRS // ID Q9X0F5_THEMA Unreviewed; 367 AA. AC Q9X0F5; G4FET3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD36140.1}; DE SubName: Full=Putative rhamnose ABC transporter, permease component 2 {ECO:0000313|EMBL:AGL49993.1}; GN OrderedLocusNames=TM_1065 {ECO:0000313|EMBL:AAD36140.1}; GN ORFNames=Tmari_1069 {ECO:0000313|EMBL:AGL49993.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36140.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36140.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36140.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49993.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49993.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032, CC ECO:0000256|SAAS:SAAS00537635}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36140.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49993.1; -; Genomic_DNA. DR PIR; D72300; D72300. DR RefSeq; NP_228871.1; NC_000853.1. DR RefSeq; WP_004080422.1; NZ_CP011107.1. DR STRING; 243274.TM1065; -. DR TCDB; 3.A.1.5.12; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36140; AAD36140; TM_1065. DR EnsemblBacteria; AGL49993; AGL49993; Tmari_1069. DR GeneID; 897050; -. DR KEGG; tma:TM1065; -. DR KEGG; tmi:THEMA_09035; -. DR KEGG; tmm:Tmari_1069; -. DR KEGG; tmw:THMA_1087; -. DR PATRIC; 23937059; VBITheMar51294_1078. DR eggNOG; ENOG4105C2T; Bacteria. DR eggNOG; COG1173; LUCA. DR KO; K02034; -. DR OMA; QPIRFFC; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1094-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR025966; OppC_N. DR Pfam; PF00528; BPD_transp_1; 1. DR Pfam; PF12911; OppC_N; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00496716}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496716, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496724}. FT TRANSMEM 29 51 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 164 188 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 224 246 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 285 310 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 330 353 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 158 354 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 367 AA; 42128 MW; 001669B75CF16D92 CRC64; MKKREQMEEK FYYASQWQLI WWRFRKHKLA VIGGVVLLII YVFAIFCEFF APYDPNKYNY RYPYAPPQRI HFFHEGKFIG PFVYGYTYTV DLETLRRIYK EDKSKIFKIK FFVRGDEYKF WGIWKTNIHF IGVEDGHMFL LGTDSLGRDM LSRIIYGARI STSIGLIGVF LSFILGVAIG GISGYFGGAV DNFIQRTIEI IKSIPTIPLW LALSAALPQN WPPLRVYFVI VIILSLTGWT DLARVVRSRF LSLREEDFVM AAKFMGASEA RIIFRHMLPS FMSHLIASIT LSIPGMILGE TSLSFLGLGL RPPVISWGVL LQEAQNLTVV ALYPWLLIPV VFVITTVLCF NFVGDGLRDA ADPYANM // ID Q9WYI8_THEMA Unreviewed; 335 AA. AC Q9WYI8; G4FHR5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 88. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35440.1}; GN OrderedLocusNames=TM_0353 {ECO:0000313|EMBL:AAD35440.1}; GN ORFNames=Tmari_0351 {ECO:0000313|EMBL:AGL49276.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35440.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35440.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35440.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49276.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49276.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) CC (TC 8.A.1) family. {ECO:0000256|SAAS:SAAS00568556}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35440.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49276.1; -; Genomic_DNA. DR PIR; A72386; A72386. DR RefSeq; NP_228164.1; NC_000853.1. DR RefSeq; WP_004083145.1; NZ_CP011107.1. DR STRING; 243274.TM0353; -. DR EnsemblBacteria; AAD35440; AAD35440; TM_0353. DR EnsemblBacteria; AGL49276; AGL49276; Tmari_0351. DR GeneID; 897309; -. DR KEGG; tma:TM0353; -. DR KEGG; tmi:THEMA_02950; -. DR KEGG; tmm:Tmari_0351; -. DR KEGG; tmw:THMA_0361; -. DR PATRIC; 23935587; VBITheMar51294_0358. DR eggNOG; ENOG41082RW; Bacteria. DR eggNOG; COG0845; LUCA. DR OMA; FTAKITH; -. DR OrthoDB; EOG622PMC; -. DR BioCyc; TMAR243274:GC6P-367-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR006143; RND_pump_MFP. DR TIGRFAMs; TIGR01730; RND_mfp; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 335 AA; 36528 MW; 2CB469FA33BF16C4 CRC64; MKKWITLLII AVLVVLVAVV IFLNRASAQT VSEKDATSTQ APVFLTYTVT KENETVEIVG QVTADTKKVT SKVSGDVLEI YVEEGDVVQV GQKIAKIDDT DYQISYLSAL NSYKTSPTEI NRLNLEKAKE NLENTTVVSP VSGVVQAVNV DVGDRVSVGT SIVTIVETDT LRVEGSISEY DLKNVKEGMK AVFTFEQLGL TLTGKVKRIS PVAETSGGVT VIPVEFSFDQ TPPSLVIPGL TCDVEIIIKE ATSSFFIPKE AVRQDQNGYY VMKQTPQGPQ KVYVELGEEL NDKIEIKKGV SEGDVLLLIP SQQEIQRLRT RQGLPMFGPG GGRAR // ID Q9X0Q9_THEMA Unreviewed; 225 AA. AC Q9X0Q9; G4FEG9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 99. DE SubName: Full=2-haloalkanoic acid dehalogenase {ECO:0000313|EMBL:AGL50108.1}; DE EC=3.8.1.2 {ECO:0000313|EMBL:AGL50108.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36252.1}; GN OrderedLocusNames=TM_1177 {ECO:0000313|EMBL:AAD36252.1}; GN ORFNames=Tmari_1184 {ECO:0000313|EMBL:AGL50108.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36252.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36252.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36252.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50108.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50108.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36252.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50108.1; -; Genomic_DNA. DR PIR; D72286; D72286. DR RefSeq; NP_228982.1; NC_000853.1. DR RefSeq; WP_004080184.1; NZ_CP011107.1. DR STRING; 243274.TM1177; -. DR EnsemblBacteria; AAD36252; AAD36252; TM_1177. DR EnsemblBacteria; AGL50108; AGL50108; Tmari_1184. DR GeneID; 898309; -. DR KEGG; tma:TM1177; -. DR KEGG; tmi:THEMA_08450; -. DR KEGG; tmm:Tmari_1184; -. DR KEGG; tmw:THMA_1202; -. DR PATRIC; 23937294; VBITheMar51294_1195. DR eggNOG; ENOG410805Q; Bacteria. DR eggNOG; COG1011; LUCA. DR KO; K07025; -. DR OMA; PDARIFD; -. DR OrthoDB; EOG6W19QD; -. DR BioCyc; TMAR243274:GC6P-1206-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0018784; F:(S)-2-haloacid dehalogenase activity; IEA:UniProtKB-EC. DR Gene3D; 1.10.150.240; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR011951; HAD-SF_hydro_IA_YjjG/YfnB. DR InterPro; IPR023198; PGP_dom2. DR Pfam; PF13419; HAD_2; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. DR TIGRFAMs; TIGR02254; YjjG/YfnB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50108.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 196 HAD-like_dom. {ECO:0000259|Pfam:PF13419}. SQ SEQUENCE 225 AA; 26245 MW; 9EB0563E35CFF49E CRC64; MKKGVLFDLD GTILDFEKSE DQALKRTFLK YGIPLTEDQV FLYREINRKW WKLLAEGKVS KDVVVVARFE EFLKTLNIPL DPRKVAKDYL EFLSEEAHFL PGAEEFLERL KKKDLRMAVV TNGVRFVQEK RSRKLKLDRF FEFVLTSEEA GVEKPDPRIF WLALERMKLK KEEVLYVGDD FSSDLEGARN AGIDFVLFSS DGDSSGDFPV ARNFKELEKI VEEFL // ID Q9WZW1_THEMA Unreviewed; 293 AA. AC Q9WZW1; G4FCW7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 110. DE RecName: Full=Riboflavin biosynthesis protein {ECO:0000256|PIRNR:PIRNR004491}; DE EC=2.7.1.26 {ECO:0000256|PIRNR:PIRNR004491}; DE EC=2.7.7.2 {ECO:0000256|PIRNR:PIRNR004491}; GN OrderedLocusNames=TM_0857 {ECO:0000313|EMBL:AAD35939.1}; GN ORFNames=Tmari_0859 {ECO:0000313|EMBL:AGL49784.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35939.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35939.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35939.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1MRZ} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS). RX PubMed=12910462; DOI=10.1002/prot.10353; RA Wang W., Kim R., Jancarik J., Yokota H., Kim S.H.; RT "Crystal structure of a flavin-binding protein from Thermotoga RT maritima."; RL Proteins 52:633-635(2003). RN [3] {ECO:0000213|PDB:1T6X, ECO:0000213|PDB:1T6Y, ECO:0000213|PDB:1T6Z} RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH ADP; AMP AND RP FMN. RA Shin D.H., Wang W., Kim R., Yokota H., Kim S.-H.; RT "Crystal structure of ADP bound FAD synthetase."; RL Submitted (MAY-2004) to the PDB data bank. RN [4] {ECO:0000213|PDB:1S4M} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS). RX PubMed=15468322; DOI=10.1002/prot.20207; RA Wang W., Kim R., Yokota H., Kim S.H.; RT "Crystal structure of flavin binding to FAD synthetase of Thermotoga RT maritima."; RL Proteins 58:246-248(2005). RN [5] {ECO:0000213|PDB:2I1L} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS). RA Wang W., Shin D.H., Yokota H., Kim R., Kim S.-H.; RT "Crystal structure of the C2 form of FAD synthetase from Thermotoga RT maritima."; RL Submitted (AUG-2006) to the PDB data bank. RN [6] {ECO:0000313|EMBL:AGL49784.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49784.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD. CC {ECO:0000256|PIRNR:PIRNR004491}. CC -!- CATALYTIC ACTIVITY: ATP + riboflavin = ADP + FMN. CC {ECO:0000256|PIRNR:PIRNR004491}. CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: CC step 1/1. {ECO:0000256|PIRNR:PIRNR004491}. CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from CC riboflavin (ATP route): step 1/1. {ECO:0000256|PIRNR:PIRNR004491}. CC -!- SIMILARITY: Belongs to the ribF family. CC {ECO:0000256|PIRNR:PIRNR004491}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35939.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49784.1; -; Genomic_DNA. DR PIR; B72325; B72325. DR RefSeq; NP_228666.1; NC_000853.1. DR RefSeq; WP_004080749.1; NZ_CP011107.1. DR PDB; 1MRZ; X-ray; 1.90 A; A/B=1-293. DR PDB; 1S4M; X-ray; 2.10 A; A/B=1-293. DR PDB; 1T6X; X-ray; 2.29 A; A/B=1-293. DR PDB; 1T6Y; X-ray; 2.80 A; A/B=1-293. DR PDB; 1T6Z; X-ray; 2.40 A; A/B=1-293. DR PDB; 2I1L; X-ray; 2.50 A; A/B=1-293. DR PDBsum; 1MRZ; -. DR PDBsum; 1S4M; -. DR PDBsum; 1T6X; -. DR PDBsum; 1T6Y; -. DR PDBsum; 1T6Z; -. DR PDBsum; 2I1L; -. DR SMR; Q9WZW1; 1-288. DR STRING; 243274.TM0857; -. DR EnsemblBacteria; AAD35939; AAD35939; TM_0857. DR EnsemblBacteria; AGL49784; AGL49784; Tmari_0859. DR GeneID; 898530; -. DR KEGG; tma:TM0857; -. DR KEGG; tmi:THEMA_00350; -. DR KEGG; tmm:Tmari_0859; -. DR KEGG; tmw:THMA_0879; -. DR PATRIC; 23936642; VBITheMar51294_0870. DR eggNOG; ENOG4105DTN; Bacteria. DR eggNOG; COG0196; LUCA. DR KO; K11753; -. DR OMA; FPTANMR; -. DR OrthoDB; EOG6QP0ZV; -. DR BioCyc; TMAR243274:GC6P-887-MONOMER; -. DR UniPathway; UPA00276; UER00406. DR UniPathway; UPA00277; UER00407. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-EC. DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro. DR Gene3D; 2.40.30.30; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR015864; FAD_synthase. DR InterPro; IPR023468; Riboflavin_kinase. DR InterPro; IPR002606; Riboflavin_kinase_bac. DR InterPro; IPR015865; Riboflavin_kinase_bac/euk. DR InterPro; IPR023465; Riboflavin_kinase_domain. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR22749; PTHR22749; 1. DR Pfam; PF06574; FAD_syn; 1. DR Pfam; PF01687; Flavokinase; 1. DR PIRSF; PIRSF004491; FAD_Synth; 1. DR SMART; SM00904; Flavokinase; 1. DR SUPFAM; SSF82114; SSF82114; 1. DR TIGRFAMs; TIGR00083; ribF; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1MRZ, ECO:0000213|PDB:1S4M, KW ECO:0000213|PDB:1T6X, ECO:0000213|PDB:1T6Y}; KW ATP-binding {ECO:0000256|PIRNR:PIRNR004491}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW FAD {ECO:0000256|PIRNR:PIRNR004491}; KW Flavoprotein {ECO:0000213|PDB:1T6Y, ECO:0000256|PIRNR:PIRNR004491}; KW FMN {ECO:0000213|PDB:1T6Y, ECO:0000256|PIRNR:PIRNR004491}; KW Kinase {ECO:0000256|PIRNR:PIRNR004491, ECO:0000313|EMBL:AAD35939.1}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR004491}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491, KW ECO:0000313|EMBL:AAD35939.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|PIRNR:PIRNR004491, KW ECO:0000313|EMBL:AAD35939.1}. FT DOMAIN 155 282 Flavokinase. {ECO:0000259|SMART:SM00904}. FT NP_BIND 7 8 AMP. {ECO:0000213|PDB:1T6Y}. FT NP_BIND 12 15 AMP. {ECO:0000213|PDB:1T6Y}. FT NP_BIND 99 101 AMP. {ECO:0000213|PDB:1T6Y}. FT NP_BIND 127 128 AMP. {ECO:0000213|PDB:1T6Y}. FT NP_BIND 179 182 ADP. {ECO:0000213|PDB:1T6X, FT ECO:0000213|PDB:1T6Y}. FT NP_BIND 231 242 ADP. {ECO:0000213|PDB:1T6X, FT ECO:0000213|PDB:1T6Y}. FT NP_BIND 255 258 FMN. {ECO:0000213|PDB:1T6Y}. FT BINDING 135 135 AMP; via carbonyl oxygen. FT {ECO:0000213|PDB:1T6Y}. FT BINDING 215 215 FMN. {ECO:0000213|PDB:1T6Y}. SQ SEQUENCE 293 AA; 33614 MW; 42B56B582C03BEB4 CRC64; MVVSIGVFDG VHIGHQKVLR TMKEIAFFRK DDSLIYTISY PPEYFLPDFP GLLMTVESRV EMLSRYARTV VLDFFRIKDL TPEGFVERYL SGVSAVVVGR DFRFGKNASG NASFLRKKGV EVYEIEDVVV QGKRVSSSLI RNLVQEGRVE EIPAYLGRYF EIEGIVHKDR EFGRKLGFPT ANIDRGNEKL VDLKRGVYLV RVHLPDGKKK FGVMNVGFRP TVGDARNVKY EVYILDFEGD LYGQRLKLEV LKFMRDEKKF DSIEELKAAI DQDVKSARNM IDDIINSKFE KEG // ID Q9WZF5_THEMA Unreviewed; 216 AA. AC Q9WZF5; G4FDD3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 96. DE SubName: Full=Putative O-methyltransferase {ECO:0000313|EMBL:AGL49616.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35773.1}; GN OrderedLocusNames=TM_0691 {ECO:0000313|EMBL:AAD35773.1}; GN ORFNames=Tmari_0691 {ECO:0000313|EMBL:AGL49616.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35773.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35773.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35773.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49616.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49616.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35773.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49616.1; -; Genomic_DNA. DR PIR; A72345; A72345. DR RefSeq; NP_228500.1; NC_000853.1. DR RefSeq; WP_004081068.1; NZ_CP011107.1. DR STRING; 243274.TM0691; -. DR EnsemblBacteria; AAD35773; AAD35773; TM_0691. DR EnsemblBacteria; AGL49616; AGL49616; Tmari_0691. DR GeneID; 898358; -. DR KEGG; tma:TM0691; -. DR KEGG; tmi:THEMA_01210; -. DR KEGG; tmm:Tmari_0691; -. DR KEGG; tmw:THMA_0706; -. DR PATRIC; 23936300; VBITheMar51294_0703. DR eggNOG; ENOG4108320; Bacteria. DR eggNOG; COG4123; LUCA. DR OMA; HEIMCTI; -. DR OrthoDB; EOG6G20PN; -. DR BioCyc; TMAR243274:GC6P-717-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Methyltransferase {ECO:0000313|EMBL:AGL49616.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49616.1}. SQ SEQUENCE 216 AA; 24407 MW; FE30D559F2ED35D3 CRC64; MKFDPDIIRC VEIVDAGPQH RPTHASSLLV WYTRPSKNVR SVLELGSGVG TVSFALAKLY NVKVVGVEKE KELYEKALEG ISLNKLEERV SFVNSSVEEL SFPPESFDMV VSNPPHHTKV KSPNRLRAST RSIERRDIEG FVQATFRFLK NGGTAVYVLS PENLMEWLEM FVSFRLEPKR MCFVHGKIEK AATLVLLRLR KNGKRGLIVD PPVILS // ID Q9X073_THEMA Unreviewed; 184 AA. AC Q9X073; G4FF17; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 110. DE SubName: Full=UPF0033 protein {ECO:0000313|EMBL:AGL49906.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36057.1}; GN OrderedLocusNames=TM_0978 {ECO:0000313|EMBL:AAD36057.1}; GN ORFNames=Tmari_0981 {ECO:0000313|EMBL:AGL49906.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36057.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36057.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36057.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49906.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49906.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the UPF0033 family. CC {ECO:0000256|SAAS:SAAS00585298}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36057.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49906.1; -; Genomic_DNA. DR PIR; G72309; G72309. DR RefSeq; NP_228786.1; NC_000853.1. DR RefSeq; WP_004080587.1; NZ_CP011107.1. DR STRING; 243274.TM0978; -. DR EnsemblBacteria; AAD36057; AAD36057; TM_0978. DR EnsemblBacteria; AGL49906; AGL49906; Tmari_0981. DR GeneID; 898724; -. DR KEGG; tma:TM0978; -. DR KEGG; tmi:THEMA_09460; -. DR KEGG; tmm:Tmari_0981; -. DR KEGG; tmw:THMA_1000; -. DR PATRIC; 23936885; VBITheMar51294_0991. DR eggNOG; ENOG4105NZ6; Bacteria. DR eggNOG; COG0425; LUCA. DR eggNOG; COG0640; LUCA. DR OMA; IGPVMKI; -. DR OrthoDB; EOG6QCD6D; -. DR BioCyc; TMAR243274:GC6P-1008-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 2. DR Gene3D; 3.30.110.40; -; 1. DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom. DR InterPro; IPR001455; TusA-like. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF12840; HTH_20; 1. DR Pfam; PF01206; TusA; 1. DR SMART; SM00418; HTH_ARSR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF64307; SSF64307; 1. DR PROSITE; PS50987; HTH_ARSR_2; 1. DR PROSITE; PS01148; UPF0033; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 93 HTH arsR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50987}. SQ SEQUENCE 184 AA; 20760 MW; 192AB09A1EF8C32D CRC64; MGQRGSVLTL FKTLSNQTRL DILMLLRDSC LTASEVAEKL KINPSTAYRY LNQMVKAGIL KVVKTPEGDR YDFSSVQVFR MLEAAVELLH ENEKEKKISS IISVEESPGS KKFLDMRGQI CPVPEITTRK ELEKLQPGET LIVMCDYPLS GERITSFSLR EGYEVATEQI GPVTKIYIKK PQSL // ID Q9WYJ0_THEMA Unreviewed; 328 AA. AC Q9WYJ0; G4FHR7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35442.1}; GN OrderedLocusNames=TM_0355 {ECO:0000313|EMBL:AAD35442.1}; GN ORFNames=Tmari_0353 {ECO:0000313|EMBL:AGL49278.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35442.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35442.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35442.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49278.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49278.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35442.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49278.1; -; Genomic_DNA. DR PIR; C72386; C72386. DR RefSeq; NP_228166.1; NC_000853.1. DR RefSeq; WP_004083154.1; NZ_CP011107.1. DR STRING; 243274.TM0355; -. DR EnsemblBacteria; AAD35442; AAD35442; TM_0355. DR EnsemblBacteria; AGL49278; AGL49278; Tmari_0353. DR GeneID; 897311; -. DR KEGG; tma:TM0355; -. DR KEGG; tmi:THEMA_02940; -. DR KEGG; tmm:Tmari_0353; -. DR KEGG; tmw:THMA_0363; -. DR PATRIC; 23935591; VBITheMar51294_0360. DR eggNOG; ENOG4106KY3; Bacteria. DR eggNOG; ENOG410YNTF; LUCA. DR OMA; STDYQIA; -. DR OrthoDB; EOG6XHC22; -. DR BioCyc; TMAR243274:GC6P-369-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR003423; OMP_efflux. DR Pfam; PF02321; OEP; 2. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 328 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006753471. FT COILED 132 159 {ECO:0000256|SAM:Coils}. FT COILED 201 240 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 328 AA; 37575 MW; 1430D6F698C80B63 CRC64; MKNLLVVLLS LVSVLSFSVS LNDVLQTALA SSTDYQIAQI SLESATMDYE KAKLEATNKR SELSAELSYY NNLQSYRNSL KSAYQDVLGR IFNLLTADLS YEIAQLNFEN AQEDYKTSQE LFKKNLISEN DLKDSELTLE EASNNLLSAQ KDLEEAQKDY EEIFSVEVSE IELPLIDYQN LVGEDEYLDN LSSVKIAELN MKIAEYDLNN LSASASKYEQ KKAELNYKKS KMNYDEALKE AKDSYKSTLD SLEIAFLNLK VLKEKIELNE NILKDYQERY EKGLISKKEL NTQKINLLNI KKNYLNSLRS YYISIVNLLI DAGKEVSF // ID Q9X0D9_THEMA Unreviewed; 339 AA. AC Q9X0D9; G4FEU9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Deblocking aminopeptidase {ECO:0000313|EMBL:AGL49977.1}; DE EC=3.4.11.- {ECO:0000313|EMBL:AGL49977.1}; DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:AAD36126.1}; GN OrderedLocusNames=TM_1049 {ECO:0000313|EMBL:AAD36126.1}; GN ORFNames=Tmari_1053 {ECO:0000313|EMBL:AGL49977.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36126.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36126.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36126.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49977.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49977.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36126.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49977.1; -; Genomic_DNA. DR PIR; C72301; C72301. DR RefSeq; NP_228855.1; NC_000853.1. DR RefSeq; WP_004080462.1; NZ_CP011107.1. DR PDB; 2FVG; X-ray; 2.01 A; A=1-339. DR PDBsum; 2FVG; -. DR STRING; 243274.TM1049; -. DR EnsemblBacteria; AAD36126; AAD36126; TM_1049. DR EnsemblBacteria; AGL49977; AGL49977; Tmari_1053. DR GeneID; 897058; -. DR KEGG; tma:TM1049; -. DR KEGG; tmi:THEMA_09115; -. DR KEGG; tmm:Tmari_1053; -. DR KEGG; tmw:THMA_1071; -. DR PATRIC; 23937027; VBITheMar51294_1062. DR eggNOG; ENOG4105CN9; Bacteria. DR eggNOG; COG1363; LUCA. DR KO; K01179; -. DR OMA; CSRYIHT; -. DR OrthoDB; EOG6V4GDH; -. DR BioCyc; TMAR243274:GC6P-1078-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR Gene3D; 2.40.30.40; -; 1. DR InterPro; IPR008007; Peptidase_M42. DR InterPro; IPR023367; Peptidase_M42_dom2. DR Pfam; PF05343; Peptidase_M42; 1. DR PIRSF; PIRSF001123; PepA_GA; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2FVG}; KW Aminopeptidase {ECO:0000313|EMBL:AGL49977.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49977.1}; KW Protease {ECO:0000313|EMBL:AGL49977.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT ACT_SITE 196 196 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR001123-1}. SQ SEQUENCE 339 AA; 37329 MW; A822338E6AF77FBD CRC64; MYLKELSMMP GVSGDEGKVR DFIKSKIEGL VDNLYTDVLG NLIALKRGRD SSKKLLVSAH MDEVGFVVSK IEKDGKVSFL PVGGVDPRIL PGKVVQVKNL KGVIGYRPIH LQRDEENTPP RFENLRIDFG FSSADEAKKY VSIGDYVSFV SDYIEKNGRA VGKAFDDRAG CSVLIDVLES GVSPAYDTYF VFTVQEETGL RGSAVVVEQL KPTCAIVVET TTAGDNPELE ERKWATHLGD GPAITFYHRG YVIPKEIFQT IVDTAKNNDI PFQMKRRTAG GTDAGRYART AYGVPAGVIS TPARYIHSPN SIIDLNDYEN TKKLIKVLVE EGKIVEVVS // ID Q9WY70_THEMA Unreviewed; 545 AA. AC Q9WY70; G4FHE2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 105. DE SubName: Full=NADP-reducing hydrogenase, subunit C {ECO:0000313|EMBL:AAD35319.1}; GN OrderedLocusNames=TM_0228 {ECO:0000313|EMBL:AAD35319.1}; GN ORFNames=Tmari_0226 {ECO:0000313|EMBL:AGL49152.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35319.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35319.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35319.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49152.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49152.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35319.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49152.1; -; Genomic_DNA. DR PIR; F72401; F72401. DR RefSeq; NP_228042.1; NC_000853.1. DR RefSeq; WP_004082918.1; NZ_CP011107.1. DR STRING; 243274.TM0228; -. DR DNASU; 897127; -. DR EnsemblBacteria; AAD35319; AAD35319; TM_0228. DR EnsemblBacteria; AGL49152; AGL49152; Tmari_0226. DR GeneID; 897127; -. DR KEGG; tma:TM0228; -. DR KEGG; tmi:THEMA_03585; -. DR KEGG; tmm:Tmari_0226; -. DR KEGG; tmw:THMA_0235; -. DR PATRIC; 23935331; VBITheMar51294_0231. DR eggNOG; ENOG4107EEP; Bacteria. DR eggNOG; COG1894; LUCA. DR KO; K00335; -. DR OMA; FCGLGQS; -. DR OrthoDB; EOG6W9XGK; -. DR BioCyc; TMAR243274:GC6P-241-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IBA:GO_Central. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS. DR InterPro; IPR011538; Nuo51_FMN-bd. DR InterPro; IPR019575; Nuop51_4Fe4S-bd. DR InterPro; IPR019554; Soluble_ligand-bd. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF01512; Complex1_51K; 1. DR Pfam; PF10589; NADH_4Fe-4S; 1. DR Pfam; PF10531; SLBB; 1. DR SMART; SM00928; NADH_4Fe-4S; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00645; COMPLEX1_51K_2; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00445598}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|SAAS:SAAS00445598}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00445598}; KW Metal-binding {ECO:0000256|SAAS:SAAS00445598}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 433 478 NADH_4Fe-4S. {ECO:0000259|SMART:SM00928}. SQ SEQUENCE 545 AA; 60003 MW; 83676307CBC7A610 CRC64; MKPITVLVSV DSNSVLMGAR HFLNYFRDLV KEHNLEDTVD VLETGSMGIY PEGVIVSVLP DGVFYVVRNE LDVRRIFEEH ILKGRRVLDL EIPESQIKGT VEVEKVAEET RIVLKNVGEI DPTRIEEYIA RDGYFALAKA LQMEPGEIIE EIKRSGLRGR GGAGFPTGLK WEFTYKASAD QKYVLCNADE GEPGTFKDRL IMEGDPHSLI EGMIIAGYAV GATKGYIYIR GEYHSSIEIL KKAVEQAYEY GFLGENILGS GFNFDLKIRL GAGAYVAGEE TALIESIEGK PARPRLKPPY PPTFGLFGKP TVVNNVETFV NVPRIIMNGA EWFKKFGTES SPGTKVFSLV GNVVRKGIVE VPMGVTVRDL IFKFGGGIEG GRKLKVVQTG GSAGTFIGPD KLDVPLDFDS YAKYGVSLGS GVILVADETH CVVDLALTVM RFFEHESCGK CTPCREGTRM IVNILERISR GEGKKEDLDT LREIARNAGE TSFCGLGQSI PVPLLSIVDN FEEEFKAHIG ADKCPVGVCE FKKKKEKKKI GVRKP // ID Q9WZ34_THEMA Unreviewed; 159 AA. AC Q9WZ34; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35649.1}; GN OrderedLocusNames=TM_0564 {ECO:0000313|EMBL:AAD35649.1}; GN ORFNames=Tmari_0562 {ECO:0000313|EMBL:AGL49487.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35649.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35649.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35649.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49487.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49487.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35649.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49487.1; -; Genomic_DNA. DR PIR; C72361; C72361. DR RefSeq; NP_228374.1; NC_000853.1. DR RefSeq; WP_010865148.1; NC_000853.1. DR STRING; 243274.TM0564; -. DR DNASU; 897626; -. DR EnsemblBacteria; AAD35649; AAD35649; TM_0564. DR EnsemblBacteria; AGL49487; AGL49487; Tmari_0562. DR GeneID; 897626; -. DR KEGG; tma:TM0564; -. DR KEGG; tmm:Tmari_0562; -. DR PATRIC; 23936037; VBITheMar51294_0573. DR eggNOG; ENOG4108Z1H; Bacteria. DR eggNOG; COG1853; LUCA. DR OMA; NTMTANW; -. DR OrthoDB; EOG6ZWJMK; -. DR BioCyc; TMAR243274:GC6P-588-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IBA:GO_Central. DR Gene3D; 2.30.110.10; -; 1. DR InterPro; IPR002563; Flavin_Rdtase-like_dom. DR InterPro; IPR012349; Split_barrel_FMN-bd. DR Pfam; PF01613; Flavin_Reduct; 1. DR SMART; SM00903; Flavin_Reduct; 1. DR SUPFAM; SSF50475; SSF50475; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 8 147 Flavin_Reduct. FT {ECO:0000259|SMART:SM00903}. SQ SEQUENCE 159 AA; 18625 MW; D4FEF70BC3E13A2C CRC64; MNVYEGLLED LREGRVILTS KAGNRVNGMT IGWGFFGIIW EEEYFISAVR PQRFTWRLVK ESKRFTLNFL SEEYREALNY FGRVSGYQEN KFEKGLLHLD ELEGFTAPIK EAHTLIECSV TFASNVEPFV LPVEIIDKFY KDHGFHTLFF GKIEKVLQR // ID Q9X138_THEMA Unreviewed; 77 AA. AC Q9X138; G4FE39; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36386.1}; DE SubName: Full=YcfA family protein {ECO:0000313|EMBL:AGL50242.1}; GN OrderedLocusNames=TM_1312 {ECO:0000313|EMBL:AAD36386.1}; GN ORFNames=Tmari_1318 {ECO:0000313|EMBL:AGL50242.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36386.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36386.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36386.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50242.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50242.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36386.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50242.1; -; Genomic_DNA. DR PIR; B72271; B72271. DR RefSeq; NP_229116.1; NC_000853.1. DR RefSeq; WP_004079902.1; NZ_CP011107.1. DR STRING; 243274.TM1312; -. DR EnsemblBacteria; AAD36386; AAD36386; TM_1312. DR EnsemblBacteria; AGL50242; AGL50242; Tmari_1318. DR GeneID; 898170; -. DR KEGG; tma:TM1312; -. DR KEGG; tmi:THEMA_07785; -. DR KEGG; tmm:Tmari_1318; -. DR KEGG; tmw:THMA_1336; -. DR eggNOG; ENOG41067RR; Bacteria. DR eggNOG; ENOG410XUD5; LUCA. DR OMA; GMINKII; -. DR OrthoDB; EOG6Q5P24; -. DR BioCyc; TMAR243274:GC6P-1343-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003729; F:mRNA binding; IEA:InterPro. DR InterPro; IPR012933; HicA_mRNA_interferase. DR Pfam; PF07927; HicA_toxin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 77 AA; 8984 MW; 62400A61B645280F CRC64; MSYLPIVDPK TMEKVLLKLG FQRVRQKGSH VFYRHSNGKY TTIPFHAKET CPSHLIRKII REAGISVEEF KKVLENL // ID Q9X189_THEMA Unreviewed; 464 AA. AC Q9X189; G4FFA5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Iron-sulfur cluster assembly protein SufB {ECO:0000313|EMBL:AGL50300.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36440.1}; GN OrderedLocusNames=TM_1369 {ECO:0000313|EMBL:AAD36440.1}; GN ORFNames=Tmari_1376 {ECO:0000313|EMBL:AGL50300.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36440.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36440.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36440.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50300.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50300.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36440.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50300.1; -; Genomic_DNA. DR PIR; B72260; B72260. DR RefSeq; NP_229170.1; NC_000853.1. DR RefSeq; WP_004081565.1; NZ_CP011107.1. DR STRING; 243274.TM1369; -. DR EnsemblBacteria; AAD36440; AAD36440; TM_1369. DR EnsemblBacteria; AGL50300; AGL50300; Tmari_1376. DR GeneID; 898110; -. DR KEGG; tma:TM1369; -. DR KEGG; tmi:THEMA_07490; -. DR KEGG; tmm:Tmari_1376; -. DR KEGG; tmw:THMA_1395; -. DR PATRIC; 23937678; VBITheMar51294_1381. DR eggNOG; ENOG4105DIW; Bacteria. DR eggNOG; COG0719; LUCA. DR KO; K09014; -. DR OMA; YPYVDVR; -. DR OrthoDB; EOG60KN0V; -. DR BioCyc; TMAR243274:GC6P-1403-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR InterPro; IPR010231; SUF_FeS_clus_asmbl_SufB. DR InterPro; IPR000825; SUF_FeS_clus_asmbl_SufBD. DR Pfam; PF01458; UPF0051; 1. DR TIGRFAMs; TIGR01980; sufB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 464 AA; 51900 MW; 5C043CE2FDB908CD CRC64; MMERLIIDDS RFNFVPKVKT AYKAPPGLDE KLIMEISRAK DEPEWMLKHR LESLKVFNEW HNPRFGVDIS GLDLGKIVSY IKPDAKKSTS WEEVPEEVKE AFDKLGIPEA ERKYLAGVGA QLDSEIVYQN MKKELEKMGV IFLDMESAVR EYPDLVKKYF MKLVPITDHK FAALHGAIWS GGTFLYVPAG VKIPMPLQAY FLMSNPGMGQ FEHTIIVAEE GSEVTFIEGC SAPRYNIINL HAGMVEIYVK KGAKVKYLTI QNWSKNTYNL NTKRSIVDEE GSMTWVSGSL GSQKTMLYPM TILKGKGARA ESMSITYAGP GQHMDTGSKV VHLAPYTSSI VSAKSISLGG GWAFYRGLLK ITKEAVKSKA SVECAALMLD NRSKSDTVPI IEVETDRADV GHEARIGRIG EDQIFYLMSR GLSEQEAKAM IVKGFVEPVV KELPFEYAVE LNKLLELEIE KSIG // ID Q9X094_THEMA Unreviewed; 32 AA. AC Q9X094; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36081.1}; GN OrderedLocusNames=TM_0999 {ECO:0000313|EMBL:AAD36081.1}; GN ORFNames=Tmari_1003 {ECO:0000313|EMBL:AGL49928.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36081.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36081.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36081.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49928.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49928.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36081.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49928.1; -; Genomic_DNA. DR PIR; A72307; A72307. DR RefSeq; NP_228807.1; NC_000853.1. DR RefSeq; WP_010865239.1; NZ_CP011107.1. DR STRING; 243274.TM0999; -. DR DNASU; 896842; -. DR EnsemblBacteria; AAD36081; AAD36081; TM_0999. DR EnsemblBacteria; AGL49928; AGL49928; Tmari_1003. DR GeneID; 896842; -. DR KEGG; tma:TM0999; -. DR KEGG; tmm:Tmari_1003; -. DR KEGG; tmw:THMA_1021; -. DR BioCyc; TMAR243274:GC6P-1029-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 32 AA; 3936 MW; 905589C0456BB34A CRC64; MKEYEARQFK VCYMNSPEKA QENLCFFQLF VL // ID Q9WXQ4_THEMA Unreviewed; 405 AA. AC Q9WXQ4; G4FGW3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Transposase, putative {ECO:0000313|EMBL:AAD35141.1}; GN OrderedLocusNames=TM_0047 {ECO:0000313|EMBL:AAD35141.1}; GN ORFNames=Tmari_0044 {ECO:0000313|EMBL:AGL48970.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35141.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35141.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35141.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48970.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48970.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35141.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48970.1; -; Genomic_DNA. DR PIR; D72426; D72426. DR RefSeq; NP_227863.1; NC_000853.1. DR RefSeq; WP_004082517.1; NZ_CP011107.1. DR STRING; 243274.TM0047; -. DR EnsemblBacteria; AAD35141; AAD35141; TM_0047. DR EnsemblBacteria; AGL48970; AGL48970; Tmari_0044. DR GeneID; 896871; -. DR KEGG; tma:TM0047; -. DR KEGG; tmi:THEMA_04570; -. DR KEGG; tmm:Tmari_0044; -. DR KEGG; tmw:THMA_0043; -. DR PATRIC; 23934934; VBITheMar51294_0045. DR eggNOG; ENOG4108K3X; Bacteria. DR eggNOG; COG0675; LUCA. DR KO; K07496; -. DR OMA; RRINQNL; -. DR OrthoDB; EOG6DRPD6; -. DR BioCyc; TMAR243274:GC6P-47-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR001959; Transposase_2. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR Pfam; PF01385; OrfB_IS605; 1. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 162 283 OrfB_IS605. {ECO:0000259|Pfam:PF01385}. FT DOMAIN 302 368 OrfB_Zn_ribbon. FT {ECO:0000259|Pfam:PF07282}. SQ SEQUENCE 405 AA; 46214 MW; 03AE7F2A16933B3E CRC64; MSRYVIRTYK VPVPVELYPL CSELNRIAAR IYNKTMSLVK KIKNKKGFWL SPNTAQKYIL RWSSAIDIHT HSKQAMVQLY FQALNSYFVA VKTNPHAKPP YKRKNFLPFI WKNQAIKLLP DGKVKLSMGR NREPFVIPTT LPAGTTIRQA KLVYEAGRYY LHLAIEVKSE HKRGQSQKVM SVDVGILRPI TCFDGSEVIS YHGGVLNSIL RYRNKRLADI QRALSRCQKG SRRYKKLSRA KRRVLYKTRN QINDVLHKIT SHFIGLCVQK NIGTIVVGDI TNIRERTNGN DNFNQKLHQW AFRKLMSQIE YKAQIFGIEV VRISEAHTSK TCPVCGTQNR PSGRNYKCAG CGFEYHRDGV GAINIWKRYL GTKSQVVAGL APARGVRFNP HLCGHGAISA PWKAA // ID Q9WZ64_THEMA Unreviewed; 419 AA. AC Q9WZ64; G4FDM4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Glycerol-3-phosphate ABC transporter, periplasmic glycerol-3-phosphate-binding protein {ECO:0000313|EMBL:AGL49519.1}; DE SubName: Full=Sugar ABC transporter, periplasmic sugar-binding protein, putative {ECO:0000313|EMBL:AAD35680.1}; GN OrderedLocusNames=TM_0595 {ECO:0000313|EMBL:AAD35680.1}; GN ORFNames=Tmari_0594 {ECO:0000313|EMBL:AGL49519.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35680.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35680.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35680.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49519.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49519.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35680.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49519.1; -; Genomic_DNA. DR PIR; D72357; D72357. DR RefSeq; NP_228405.1; NC_000853.1. DR RefSeq; WP_004081252.1; NZ_CP011107.1. DR STRING; 243274.TM0595; -. DR EnsemblBacteria; AAD35680; AAD35680; TM_0595. DR EnsemblBacteria; AGL49519; AGL49519; Tmari_0594. DR GeneID; 897670; -. DR KEGG; tma:TM0595; -. DR KEGG; tmi:THEMA_01685; -. DR KEGG; tmm:Tmari_0594; -. DR KEGG; tmw:THMA_0611; -. DR PATRIC; 23936105; VBITheMar51294_0606. DR eggNOG; ENOG4105BZ7; Bacteria. DR eggNOG; COG1653; LUCA. DR KO; K02027; -. DR OMA; YSNWTAK; -. DR OrthoDB; EOG696BSN; -. DR BioCyc; TMAR243274:GC6P-620-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 419 AA; 47317 MW; 26D5C7BFC28453A2 CRC64; MKKFLVALMV ILSVFALAKV KVTFWHAMGG GHGKTLQEIV NTFNELHPDI EVEAVYVGNY GALSQKLLAA AQAGELPTIS QAYSNWTAKL IQSGVVQPLN EFVNDPKIGL TKEEWEDIFK PLRDNCMWGD TIYAVPFNKS LYVLYYNADA FAMYGVDVPK TIDELYEAAR IMTEDFDGDG KIDQYGFGFR TTVDFFQILL TLRGGSILKQ VDGKWVSNID SQETRDVLAF VKKMVDDGIA YSQGGYLDGI FGQQKIMMYI STIAGRPYVE KSTKGKFTWS WAPVPTWVTN KVPFAGTDII MFNTASEEEK KAAWEFMKYL ISPEVTAYWA INTGYIPVRR SALETSIWKE AAKSDPLLEI PLKQIDNAVF DPQIGVWYEI RTVVGNMFSD FINGKVDMET AIKTADQKIR EYLKEEYGE // ID Q9X211_THEMA Unreviewed; 124 AA. AC Q9X211; G4FG72; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=RNA binding protein, contains ribosomal protein S1 domain {ECO:0000313|EMBL:AGL50617.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36752.1}; GN OrderedLocusNames=TM_1685 {ECO:0000313|EMBL:AAD36752.1}; GN ORFNames=Tmari_1693 {ECO:0000313|EMBL:AGL50617.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36752.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36752.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36752.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50617.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50617.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36752.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50617.1; -; Genomic_DNA. DR PIR; G72222; G72222. DR RefSeq; NP_229485.1; NC_000853.1. DR RefSeq; WP_004082201.1; NZ_CP011107.1. DR STRING; 243274.TM1685; -. DR EnsemblBacteria; AAD36752; AAD36752; TM_1685. DR EnsemblBacteria; AGL50617; AGL50617; Tmari_1693. DR GeneID; 897897; -. DR KEGG; tma:TM1685; -. DR KEGG; tmi:THEMA_05815; -. DR KEGG; tmm:Tmari_1693; -. DR KEGG; tmw:THMA_1727; -. DR PATRIC; 23938344; VBITheMar51294_1702. DR eggNOG; ENOG41082W9; Bacteria. DR eggNOG; COG1098; LUCA. DR KO; K07571; -. DR OMA; KWELSLK; -. DR OrthoDB; EOG6WT8CC; -. DR BioCyc; TMAR243274:GC6P-1733-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS50126; S1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Ribonucleoprotein {ECO:0000313|EMBL:AGL50617.1}; KW Ribosomal protein {ECO:0000313|EMBL:AGL50617.1}. FT DOMAIN 4 72 S1 motif. {ECO:0000259|PROSITE:PS50126}. SQ SEQUENCE 124 AA; 14336 MW; B57213155A18FD24 CRC64; MKVGELVKGK VSKIVKYGAF VDIEGGERGF IHISKISKNY VKRIEDYLHE GQEISAKVIG RARNGGWELS LKDLEEETPK TGEKSEEKKN MDFEKKLSRF LKESSQKLSE YKKRLEKKGR RSAW // ID Q9X061_THEMA Unreviewed; 268 AA. AC Q9X061; G4FF24; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=ATP-utilizing enzyme of the PP-loop superfamily {ECO:0000313|EMBL:AGL49893.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36045.1}; GN OrderedLocusNames=TM_0966 {ECO:0000313|EMBL:AAD36045.1}; GN ORFNames=Tmari_0968 {ECO:0000313|EMBL:AGL49893.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36045.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36045.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36045.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49893.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49893.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36045.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49893.1; -; Genomic_DNA. DR PIR; C72312; C72312. DR RefSeq; NP_228774.1; NC_000853.1. DR RefSeq; WP_004080596.1; NZ_CP011107.1. DR STRING; 243274.TM0966; -. DR DNASU; 898704; -. DR EnsemblBacteria; AAD36045; AAD36045; TM_0966. DR EnsemblBacteria; AGL49893; AGL49893; Tmari_0968. DR GeneID; 898704; -. DR KEGG; tma:TM0966; -. DR KEGG; tmi:THEMA_09515; -. DR KEGG; tmm:Tmari_0968; -. DR KEGG; tmw:THMA_0989; -. DR PATRIC; 23936863; VBITheMar51294_0980. DR eggNOG; ENOG4105DVM; Bacteria. DR eggNOG; COG1606; LUCA. DR KO; K06864; -. DR OMA; DKPAQPC; -. DR OrthoDB; EOG6VXF76; -. DR BioCyc; TMAR243274:GC6P-996-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR005232; CHP00268. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF02540; NAD_synthase; 1. DR PIRSF; PIRSF006661; PP-lp_UCP006661; 1. DR TIGRFAMs; TIGR00268; TIGR00268; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 14 79 NAD_synthase. {ECO:0000259|Pfam:PF02540}. SQ SEQUENCE 268 AA; 30674 MW; BEF8B08D8635A6E6 CRC64; MDKLQRISEA IKSKKKLVVM FSGGVDSTLL AKLAREVLGK NAVALTIDSP VIPRKEIEEA KNLANLIGIR HEFIELNELK SRHLIENPPD RCYLCRKLRD NIVKNWAREN GFDVIADGLN FSDLQDYRPG VKASTEDGIW HPFIDFEVTK EEIREYSKKL GLPTWDKPAM ACLCSRFPYG FGLNEERVRM VEKAENFLRE LGFREVRVRF FPYKTAVVEV GRDEMELLMG KRTDIVLALQ KIGFSFVTLD LEGFASGKLN RTIEGMSK // ID Q9X1T9_THEMA Unreviewed; 422 AA. AC Q9X1T9; G4FFZ1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 102. DE SubName: Full=Niacin transporter NiaP {ECO:0000313|EMBL:AGL50535.1}; DE SubName: Full=Permease, putative {ECO:0000313|EMBL:AAD36670.1}; GN OrderedLocusNames=TM_1603 {ECO:0000313|EMBL:AAD36670.1}; GN ORFNames=Tmari_1611 {ECO:0000313|EMBL:AGL50535.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36670.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36670.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36670.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50535.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50535.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36670.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50535.1; -; Genomic_DNA. DR PIR; G72234; G72234. DR RefSeq; NP_229403.1; NC_000853.1. DR RefSeq; WP_004082050.1; NZ_CP011107.1. DR STRING; 243274.TM1603; -. DR EnsemblBacteria; AAD36670; AAD36670; TM_1603. DR EnsemblBacteria; AGL50535; AGL50535; Tmari_1611. DR GeneID; 897483; -. DR KEGG; tma:TM1603; -. DR KEGG; tmi:THEMA_06235; -. DR KEGG; tmm:Tmari_1611; -. DR KEGG; tmw:THMA_1643; -. DR PATRIC; 23938180; VBITheMar51294_1622. DR eggNOG; ENOG4107QI3; Bacteria. DR eggNOG; ENOG410XQKC; LUCA. DR KO; K08369; -. DR OMA; KEDYMDL; -. DR OrthoDB; EOG6WHNRM; -. DR BioCyc; TMAR243274:GC6P-1649-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR005829; Sugar_transporter_CS. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 45 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 87 104 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 110 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 165 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 171 189 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 240 257 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 277 296 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 303 322 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 328 350 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 362 382 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 394 413 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 19 417 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 422 AA; 47153 MW; 13F9DC5649A1338D CRC64; MRIDEIVEKY VDRKTQRRFL ILTSIAWMFD AAGVMLLSFV LPYVIKEWNL TSTQGATIAS ATFLGMLFGA LSVGFVADLL GRKVSNLFFF IVTITFTFLS GFSSSFETLL VLRGLSGFGY GGLMPSFNAY LAEFTSIRLR GRYLVLLESS WAVGSILIGL FAVNVLPNWR WVFWIFSIGY LFVPVFLRMP ETPKYAFLKG GKEALERSLG KRVEEEVELP KKEKVPILAL LKREHLKDTV VIWIAWFVVS FVYYALFTWA PRIFSSLGVS VVKSSWFTFY MMVAQLPGYL SAAYFIEKWG RKASLGVYFI GTGLAALLWA NVRGDASLLA AALVLSFFCL GVWGLVYAYT PELYPTSLRG TGNGAAGVWA RIAGIIAPYY TGFMMEKGKS IAETLAWISA MAMFAGVIVL IFGRETKGKY VD // ID Q9X0Q2_THEMA Unreviewed; 618 AA. AC Q9X0Q2; G4FEH6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=Two-component response regulator {ECO:0000313|EMBL:AGL50101.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36245.1}; GN OrderedLocusNames=TM_1170 {ECO:0000313|EMBL:AAD36245.1}; GN ORFNames=Tmari_1177 {ECO:0000313|EMBL:AGL50101.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36245.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36245.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36245.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50101.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50101.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36245.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50101.1; -; Genomic_DNA. DR PIR; E72285; E72285. DR RefSeq; NP_228975.1; NC_000853.1. DR RefSeq; WP_004080199.1; NZ_CP011107.1. DR STRING; 243274.TM1170; -. DR EnsemblBacteria; AAD36245; AAD36245; TM_1170. DR EnsemblBacteria; AGL50101; AGL50101; Tmari_1177. DR GeneID; 898316; -. DR KEGG; tma:TM1170; -. DR KEGG; tmi:THEMA_08485; -. DR KEGG; tmm:Tmari_1177; -. DR KEGG; tmw:THMA_1195; -. DR PATRIC; 23937280; VBITheMar51294_1188. DR eggNOG; ENOG4105DW3; Bacteria. DR eggNOG; COG0834; LUCA. DR eggNOG; COG2206; LUCA. DR KO; K02030; -. DR OMA; HLETNYL; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1199-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR Pfam; PF01966; HD; 1. DR Pfam; PF00497; SBP_bac_3; 1. DR SMART; SM00471; HDc; 1. DR SMART; SM00062; PBPb; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 245 271 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 22 239 PBPb. {ECO:0000259|SMART:SM00062}. FT DOMAIN 441 576 HDc. {ECO:0000259|SMART:SM00471}. FT COILED 268 323 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 618 AA; 71575 MW; 911B092295BA504E CRC64; MIGIRGIVLL FLILSISIFS QPLRIALDED YAPFSFYDEN GNLVGISVDF WKLFSEKTGV EVELVPVKWY RSQELLTEKK IDAIDQIFKT PEREKVLSFS RPIFEMRSCV FFRKDLPIKD FSDLSSYVVG ALRGEGSVKT LLEKNPDVEF EFFDDYSSIV KALKEKKISV FLGDDIATRY YLSKGNLLPE FRTLHLETNY LHVAVLKGNE SVLSLINSGL SRISEGEKND IIRNYVPLVL VTPPWFLRVV FYGTAAFVIS FGIALTFIYS LRRKVEERTL QLKEANEELK AQNEEIEDLY QEVSASQEEL EKLYGEIREL DERFRESVRR MAKLVFIKDK SRFSFEVGQI VKYLLNVKNL KVILDDRAPE KVEGTVFEIS HSNEKHGYIV LEGDLSEDEK GVLESLLTIV SAIYTYRKLI SRERKLYRDI VKTWVKALEY YDYYTKGHSE EAAYYAVEIG RMFDLGDEKL EKLYWAGLLH DIGKIYVPQV VLNKTSKLDE REFELIKIHP VRGYELVKEI EGFEDVAIWI RHHHERWDGK GYPDGLKGEE IPFEARVLCV ADSYQAMRSD RPYKRGKSVE ESIQELRRNA GRQFDPVIVE KFIEFLEGGG DLGTGHQG // ID Q9X001_THEMA Unreviewed; 221 AA. AC Q9X001; G4FCS6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35980.1}; GN OrderedLocusNames=TM_0899 {ECO:0000313|EMBL:AAD35980.1}; GN ORFNames=Tmari_0901 {ECO:0000313|EMBL:AGL49826.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35980.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35980.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35980.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49826.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49826.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35980.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49826.1; -; Genomic_DNA. DR PIR; B72318; B72318. DR RefSeq; NP_228707.1; NC_000853.1. DR RefSeq; WP_004080671.1; NZ_CP011107.1. DR STRING; 243274.TM0899; -. DR DNASU; 898573; -. DR EnsemblBacteria; AAD35980; AAD35980; TM_0899. DR EnsemblBacteria; AGL49826; AGL49826; Tmari_0901. DR GeneID; 898573; -. DR KEGG; tma:TM0899; -. DR KEGG; tmi:THEMA_00140; -. DR KEGG; tmm:Tmari_0901; -. DR KEGG; tmw:THMA_0921; -. DR PATRIC; 23936729; VBITheMar51294_0913. DR OMA; ENEMIRV; -. DR OrthoDB; EOG62VNRP; -. DR BioCyc; TMAR243274:GC6P-929-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 221 AA; 25112 MW; 0DDAE2593866B3AB CRC64; MFGKIAALIK KWIEGFLLEL KGPPVEKADP SFQLPAVREQ PFQNKVNVFS LKEETTVHEG TTSEQQLSVK ECSLENEIRC RTGTPEILIS GPYLFNPELS DTSFHSENVH FTVDVKTIPS KEMDVFSNTD IPILWRTRIK REVLVDRKKI EGALKVLLDS LKDRKIDRIK FVGYYKNVPA GKISLLSSDL LVEIDEGPSK NLVVFELEIN GEKKHVFISV Q // ID Q9X0H2_THEMA Unreviewed; 282 AA. AC Q9X0H2; G4FER2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36163.1}; GN OrderedLocusNames=TM_1086 {ECO:0000313|EMBL:AAD36163.1}; GN ORFNames=Tmari_1090 {ECO:0000313|EMBL:AGL50014.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36163.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36163.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36163.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50014.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50014.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36163.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50014.1; -; Genomic_DNA. DR PIR; F72297; F72297. DR RefSeq; NP_228892.1; NC_000853.1. DR RefSeq; WP_004080391.1; NZ_CP011107.1. DR PDB; 3DCL; X-ray; 2.25 A; A/B/C/D/E=2-282. DR PDB; 3N99; X-ray; 2.38 A; A/B/C/D/E/G/H/I/J/K/L/M/N/O/P/S/T/U/V/X/a/b/c/d/e/g/h/i/j/k=1-282. DR PDBsum; 3DCL; -. DR PDBsum; 3N99; -. DR STRING; 243274.TM1086; -. DR EnsemblBacteria; AAD36163; AAD36163; TM_1086. DR EnsemblBacteria; AGL50014; AGL50014; Tmari_1090. DR GeneID; 897094; -. DR KEGG; tma:TM1086; -. DR KEGG; tmi:THEMA_08925; -. DR KEGG; tmm:Tmari_1090; -. DR KEGG; tmw:THMA_1108; -. DR PATRIC; 23937101; VBITheMar51294_1099. DR eggNOG; ENOG4107JW4; Bacteria. DR eggNOG; ENOG410XP78; LUCA. DR OMA; GHGPGVT; -. DR OrthoDB; EOG686NFZ; -. DR BioCyc; TMAR243274:GC6P-1115-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR029433; DUF4438. DR Pfam; PF14505; DUF4438; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3DCL, ECO:0000213|PDB:3N99}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT METAL 41 41 Potassium; via carbonyl oxygen. FT {ECO:0000213|PDB:3DCL}. FT METAL 42 42 Potassium; via carbonyl oxygen. FT {ECO:0000213|PDB:3DCL}. FT METAL 44 44 Potassium. {ECO:0000213|PDB:3DCL}. FT METAL 62 62 Potassium; via carbonyl oxygen. FT {ECO:0000213|PDB:3DCL}. FT METAL 64 64 Potassium; via carbonyl oxygen. FT {ECO:0000213|PDB:3DCL}. FT METAL 66 66 Potassium. {ECO:0000213|PDB:3DCL}. SQ SEQUENCE 282 AA; 30043 MW; AC6481F0B02CDF6C CRC64; MRTNKDRLVR ISVVGEIAPA KMRSPYSVTT EGTVRVIPVL GGITYNVKVG DSAYGWAGDH VEPGVSVMAR RKEEEIPLMT LSCIGNEVIV MSGDAKGSRG FVTGKHGGVN HVLVHFEEEV LGKLMVGDKI LIKAWGQGLK LLDHPDVKVM NIDPDLFEKL GIQEKNGKIH VPVVAKIPAH MMGSGIGASS SASTDYDIMA SNPEDLGVAD LKLGDIVAIQ DHDNSYGVGK YRKGAVSIGV VVHSACVSAG HGPGVVVIMT GDESKILPEE VERANISDYL VR // ID Q9X2G8_THEMA Unreviewed; 273 AA. AC Q9X2G8; G4FGP5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD36915.1}; GN OrderedLocusNames=TM_1853 {ECO:0000313|EMBL:AAD36915.1}; GN ORFNames=Tmari_1868 {ECO:0000313|EMBL:AGL50792.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36915.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36915.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36915.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50792.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50792.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36915.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50792.1; -; Genomic_DNA. DR PIR; F72203; F72203. DR RefSeq; NP_229649.1; NC_000853.1. DR RefSeq; WP_004082404.1; NZ_CP011107.1. DR STRING; 243274.TM1853; -. DR EnsemblBacteria; AAD36915; AAD36915; TM_1853. DR EnsemblBacteria; AGL50792; AGL50792; Tmari_1868. DR GeneID; 897788; -. DR KEGG; tma:TM1853; -. DR KEGG; tmi:THEMA_04905; -. DR KEGG; tmm:Tmari_1868; -. DR KEGG; tmw:THMA_1903; -. DR PATRIC; 23938695; VBITheMar51294_1874. DR eggNOG; ENOG41060SR; Bacteria. DR eggNOG; COG0395; LUCA. DR KO; K02026; -. DR OMA; PSFVIMA; -. DR OrthoDB; EOG693GR8; -. DR BioCyc; TMAR243274:GC6P-1904-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 30 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 71 94 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 106 130 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 136 156 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 194 215 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 235 260 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 71 260 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 273 AA; 31734 MW; 0699AD3025B7C8B7 CRC64; MRKKMGEIIL HGVMILLALI WIYPYVWLFL SSIKPPEEIF TRFFPSRITL EHYKYIFTMA EKMERPFLRA FFNSLFVTLT VTFSVVFTSS IIAYGLSKLR FKGSNAVFNF IIFQMLFPGF MFIIPLFVLI RKLGLYNTYS AMIVPFLMSA WSLFMLTQSY KTIPQDYIEA AKIDGASTLW IIFRVMVPLS RSTLSIVGLF TFIGIWDNFL WPLMVVKDYN KMPLSVLLAT FNHEYAAYVG PLMAGSVIQT LPMVLIFLIF RKQFLQGISM SFK // ID Q9X267_THEMA Unreviewed; 207 AA. AC Q9X267; G4FGD1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36810.1}; GN OrderedLocusNames=TM_1745 {ECO:0000313|EMBL:AAD36810.1}; GN ORFNames=Tmari_1753 {ECO:0000313|EMBL:AGL50677.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36810.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36810.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36810.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50677.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50677.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36810.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50677.1; -; Genomic_DNA. DR PIR; D72215; D72215. DR RefSeq; NP_229543.1; NC_000853.1. DR RefSeq; WP_004082277.1; NZ_CP011107.1. DR STRING; 243274.TM1745; -. DR EnsemblBacteria; AAD36810; AAD36810; TM_1745. DR EnsemblBacteria; AGL50677; AGL50677; Tmari_1753. DR GeneID; 897866; -. DR KEGG; tma:TM1745; -. DR KEGG; tmi:THEMA_05510; -. DR KEGG; tmm:Tmari_1753; -. DR KEGG; tmw:THMA_1787; -. DR PATRIC; 23938466; VBITheMar51294_1763. DR OMA; YPMRAER; -. DR OrthoDB; EOG661H7R; -. DR BioCyc; TMAR243274:GC6P-1793-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 207 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006753489. FT COILED 105 132 {ECO:0000256|SAM:Coils}. FT COILED 138 165 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 207 AA; 24013 MW; 4EEAFC0E55C925BC CRC64; MKRFFVVMLV LTVALGVFAA GYRGFAERPA FERQPMGYAQ QFPGCGGGLG YGPNAPMYER PQMRAERGFG YGLKLQIRDE EQLKLALKTR IAEALNNLDL NDDQLKELYN VAKETKEQLD SLKEKFVQLH EEYYNALVKR DTKTAEDLKD QIDDLRDEVQ DIYKDFADKV DDIITVDQYR KFRGDKRMLF VLLTDEGFEV LEEMVQE // ID Q9X0G5_THEMA Unreviewed; 157 AA. AC Q9X0G5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 92. DE RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039}; DE EC=3.1.4.- {ECO:0000256|RuleBase:RU362039}; GN OrderedLocusNames=TM_1076 {ECO:0000313|EMBL:AAD36153.1}; GN ORFNames=Tmari_1080 {ECO:0000313|EMBL:AGL50004.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36153.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36153.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36153.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50004.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50004.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|RuleBase:RU362039}; CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CC YfcE family. {ECO:0000256|RuleBase:RU362039}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36153.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50004.1; -; Genomic_DNA. DR PIR; D72296; D72296. DR RefSeq; NP_228882.1; NC_000853.1. DR RefSeq; WP_010865261.1; NZ_CP011107.1. DR PDB; 2KKN; NMR; -; A=2-157. DR PDBsum; 2KKN; -. DR STRING; 243274.TM1076; -. DR DNASU; 897148; -. DR EnsemblBacteria; AAD36153; AAD36153; TM_1076. DR EnsemblBacteria; AGL50004; AGL50004; Tmari_1080. DR GeneID; 897148; -. DR KEGG; tma:TM1076; -. DR KEGG; tmi:THEMA_08975; -. DR KEGG; tmm:Tmari_1080; -. DR KEGG; tmw:THMA_1098; -. DR PATRIC; 23937081; VBITheMar51294_1089. DR eggNOG; ENOG4107XZY; Bacteria. DR eggNOG; COG0622; LUCA. DR KO; K07095; -. DR OMA; ACHGNND; -. DR OrthoDB; EOG6ZPT4Z; -. DR BioCyc; TMAR243274:GC6P-1105-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29. DR PANTHER; PTHR11124; PTHR11124; 1. DR Pfam; PF12850; Metallophos_2; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00040; yfcE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2KKN}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000256|RuleBase:RU362039}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 146 Metallophos_2. FT {ECO:0000259|Pfam:PF12850}. SQ SEQUENCE 157 AA; 17614 MW; D3A3F32C1DD66B34 CRC64; MKRFLLISDS HVPVRMASLP DEILNSLKEY DGVIGLGDYV DLDTVILLEK FSKEFYGVHG NMDYPDVKEH LPFSKVLLVE GVTIGMCHGW GAPWDLKDRL LKVFNEKPQV ILFGHTHEPE DTVKAGVRFL NPGSLAEGSY AVLELDGGEV RFELKTL // ID Q9S5Y1_THEMA Unreviewed; 393 AA. AC Q9S5Y1; G4FGM4; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 13-APR-2016, entry version 99. DE SubName: Full=Maltose ABC transporter, periplasmic maltose-binding protein {ECO:0000313|EMBL:AAD36901.1}; DE SubName: Full=Maltose/maltodextrin ABC transporter, substrate binding periplasmic protein MalE {ECO:0000313|EMBL:AGL50771.1}; GN OrderedLocusNames=TM_1839 {ECO:0000313|EMBL:AAD36901.1}; GN ORFNames=Tmari_1847 {ECO:0000313|EMBL:AGL50771.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36901.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36901.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36901.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50771.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50771.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36901.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50771.1; -; Genomic_DNA. DR PIR; B72204; B72204. DR RefSeq; NP_229635.1; NC_000853.1. DR RefSeq; WP_004082383.1; NC_000853.1. DR PDB; 2FNC; X-ray; 1.70 A; A=22-393. DR PDBsum; 2FNC; -. DR STRING; 243274.TM1839; -. DR TCDB; 3.A.1.1.22; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36901; AAD36901; TM_1839. DR EnsemblBacteria; AGL50771; AGL50771; Tmari_1847. DR GeneID; 897815; -. DR KEGG; tma:TM1839; -. DR KEGG; tmm:Tmari_1847; -. DR PATRIC; 23938667; VBITheMar51294_1860. DR eggNOG; ENOG4107FKK; Bacteria. DR eggNOG; COG2182; LUCA. DR KO; K10108; -. DR OMA; NIPAMAY; -. DR OrthoDB; EOG60SCM8; -. DR BioCyc; TMAR243274:GC6P-1890-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro. DR GO; GO:0004175; F:endopeptidase activity; IEA:InterPro. DR GO; GO:0005363; F:maltose transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR InterPro; IPR006060; Maltose-bd. DR InterPro; IPR000426; Proteasome_asu_N. DR PRINTS; PR00181; MALTOSEBP. DR SMART; SM00948; Proteasome_A_N; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2FNC}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 106 128 PROTEASOME_ALPHA_1. FT {ECO:0000259|SMART:SM00948}. SQ SEQUENCE 393 AA; 42987 MW; 419BC074FAC41A84 CRC64; MVKRLLVLML VVVSALVLSQ TKLTIWCSEK QVDILQKLGE EFKAKYGIPV EVQYVDFGSI KSKFLTAAPQ GQGADIIVGA HDWVGELAVN GLIEPIPNFS DLKNFYDTAL KAFSYGGKLY GVPYAMEAVA LIYNKDYVDS VPKTMDELIE KAKQIDEEYG GEVRGFIYDV ANFYFSAPFI LGYGGYVFKE TPQGLDVTDI GLANEGAVKG AKLIKRMIDE GVLTPGDNYG TMDSMFKEGL AAMIINGLWA IKSYKDAGIN YGVAPIPELE PGVPAKPFVG VQGFMINAKS PNKVIAMEFL TNFIARKETM YKIYLADPRL PARKDVLELV KDNPDVVAFT QSASMGTPMP NVPEMAPVWS AMGDALSIII NGQASVEDAL KEAVEKIKAQ IEK // ID Q9WYY7_THEMA Unreviewed; 204 AA. AC Q9WYY7; G4FDV4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35602.1}; GN OrderedLocusNames=TM_0517 {ECO:0000313|EMBL:AAD35602.1}; GN ORFNames=Tmari_0513 {ECO:0000313|EMBL:AGL49438.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35602.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35602.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35602.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49438.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49438.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35602.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49438.1; -; Genomic_DNA. DR PIR; C72365; C72365. DR RefSeq; NP_228327.1; NC_000853.1. DR RefSeq; WP_004081413.1; NZ_CP011107.1. DR STRING; 243274.TM0517; -. DR EnsemblBacteria; AAD35602; AAD35602; TM_0517. DR EnsemblBacteria; AGL49438; AGL49438; Tmari_0513. DR GeneID; 897564; -. DR KEGG; tma:TM0517; -. DR KEGG; tmi:THEMA_02090; -. DR KEGG; tmm:Tmari_0513; -. DR KEGG; tmw:THMA_0529; -. DR PATRIC; 23935939; VBITheMar51294_0524. DR eggNOG; ENOG4108E3X; Bacteria. DR eggNOG; ENOG41103JX; LUCA. DR OMA; FVIFLHY; -. DR OrthoDB; EOG6PCPXN; -. DR BioCyc; TMAR243274:GC6P-541-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 160 180 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 204 AA; 24332 MW; D777405FF6C276D3 CRC64; MKRVNMNLAW MGVVFSAMSS ILLLEYYREI LAGSPSYTLG TVTLFLSLIS TISLLIVYRQ WSVLLNINVL QTLRLAEQRS VNLNEKPFVP NWPYIAFIAF WFLEFLFAGI WFFSLLQLIF FVIFLHYLFE TIRKLQEIKI HLYRTLFNID YKPVIKERNV LSVFLLTLFT LGVYWLYLVV RLSREINEFL DMDDRIMRNL EVKS // ID Q9WY08_THEMA Unreviewed; 272 AA. AC Q9WY08; G4FH75; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 101. DE SubName: Full=Geranyltranstransferase {ECO:0000313|EMBL:AAD35254.1}; DE SubName: Full=Octaprenyl-diphosphate synthase / Dimethylallyltransferase / Geranyltranstransferase (Farnesyldiphosphate synthase) / Geranylgeranyl pyrophosphate synthetase {ECO:0000313|EMBL:AGL49085.1}; DE EC=2.5.1.- {ECO:0000313|EMBL:AGL49085.1}; DE EC=2.5.1.1 {ECO:0000313|EMBL:AGL49085.1}; DE EC=2.5.1.10 {ECO:0000313|EMBL:AGL49085.1}; DE EC=2.5.1.29 {ECO:0000313|EMBL:AGL49085.1}; GN OrderedLocusNames=TM_0161 {ECO:0000313|EMBL:AAD35254.1}; GN ORFNames=Tmari_0159 {ECO:0000313|EMBL:AGL49085.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35254.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35254.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35254.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49085.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49085.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. CC {ECO:0000256|RuleBase:RU004466}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35254.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49085.1; -; Genomic_DNA. DR PIR; G72410; G72410. DR RefSeq; NP_227976.1; NC_000853.1. DR RefSeq; WP_004082783.1; NZ_CP011107.1. DR PDB; 2FTZ; X-ray; 1.90 A; A=1-272. DR PDBsum; 2FTZ; -. DR STRING; 243274.TM0161; -. DR EnsemblBacteria; AAD35254; AAD35254; TM_0161. DR EnsemblBacteria; AGL49085; AGL49085; Tmari_0159. DR GeneID; 897000; -. DR KEGG; tma:TM0161; -. DR KEGG; tmi:THEMA_03995; -. DR KEGG; tmm:Tmari_0159; -. DR KEGG; tmw:THMA_0157; -. DR PATRIC; 23935170; VBITheMar51294_0162. DR eggNOG; ENOG4105CTB; Bacteria. DR eggNOG; COG0142; LUCA. DR KO; K13789; -. DR OMA; DFKPYMI; -. DR OrthoDB; EOG6TN43W; -. DR BioCyc; TMAR243274:GC6P-162-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004311; F:farnesyltranstransferase activity; IDA:CACAO. DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC. DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IDA:CACAO. DR Gene3D; 1.10.600.10; -; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR017446; Polyprenyl_synth-rel. DR PANTHER; PTHR12001; PTHR12001; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SUPFAM; SSF48576; SSF48576; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2FTZ}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU004466, KW ECO:0000313|EMBL:AAD35254.1}. FT MOD_RES 3 3 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 5 5 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 35 35 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 55 55 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 88 88 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 117 117 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 122 122 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 133 133 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 148 148 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 163 163 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 179 179 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 181 181 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 185 185 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 187 187 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 192 192 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 204 204 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 223 223 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 228 228 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 229 229 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 234 234 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 241 241 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 248 248 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 263 263 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. FT MOD_RES 266 266 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2FTZ}. SQ SEQUENCE 272 AA; 31024 MW; 24882CB92CD27AE8 CRC64; MKKEKVEERI REILRPGWDL LTEEAMLYSA TVGGKRIRPL LVLTLGEDLG VEEEKLLDVA VAVELFHTAS LIHDDLPPID NADFRRGKPS CHRTYGEDIA LLAGDGLFFL AFSQISKIGN SKIFEEFSET AYKLLLGEAM DVEFERRKME VSQEMVERMY AFKTGALFAF CFSAPFILKG KDHTKMKLLG EKFGVAFQIY DDLKDILGSF EKVGKDLGKD TEKVTLVKKV GIQKAREMAD KYYEEVLKGI ESEGLFRTLF LLKELKQMVE ER // ID Q9WYT9_THEMA Unreviewed; 122 AA. AC Q9WYT9; G4FE02; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE SubName: Full=Chemotaxis regulator-transmits chemoreceptor signals to flagelllar motor components CheY {ECO:0000313|EMBL:AGL49390.1}; DE SubName: Full=Response regulator {ECO:0000313|EMBL:AAD35552.1}; GN OrderedLocusNames=TM_0468 {ECO:0000313|EMBL:AAD35552.1}; GN ORFNames=Tmari_0465 {ECO:0000313|EMBL:AGL49390.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35552.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35552.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35552.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49390.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49390.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- INTERACTION: CC Q9WZV7:TM_0853; NbExp=4; IntAct=EBI-2464826, EBI-2464828; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35552.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49390.1; -; Genomic_DNA. DR PIR; D72374; D72374. DR RefSeq; NP_228278.1; NC_000853.1. DR RefSeq; WP_004081498.1; NZ_CP011107.1. DR PDB; 3DGE; X-ray; 2.80 A; C/D=1-122. DR PDB; 3DGF; X-ray; 2.00 A; C=1-122. DR PDB; 3GL9; X-ray; 1.80 A; A/B/C/D=1-122. DR PDB; 4JA2; X-ray; 1.79 A; A=1-122. DR PDB; 4JAS; X-ray; 3.00 A; B=1-122. DR PDB; 4JAV; X-ray; 3.10 A; C/D=1-122. DR PDBsum; 3DGE; -. DR PDBsum; 3DGF; -. DR PDBsum; 3GL9; -. DR PDBsum; 4JA2; -. DR PDBsum; 4JAS; -. DR PDBsum; 4JAV; -. DR DIP; DIP-54543N; -. DR STRING; 243274.TM0468; -. DR EnsemblBacteria; AAD35552; AAD35552; TM_0468. DR EnsemblBacteria; AGL49390; AGL49390; Tmari_0465. DR GeneID; 897499; -. DR KEGG; tma:TM0468; -. DR KEGG; tmi:THEMA_02350; -. DR KEGG; tmm:Tmari_0465; -. DR KEGG; tmw:THMA_0477; -. DR PATRIC; 23935833; VBITheMar51294_0475. DR eggNOG; ENOG4108ZC7; Bacteria. DR eggNOG; COG0784; LUCA. DR KO; K02485; -. DR KO; K03413; -. DR OMA; VMTKPFS; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; TMAR243274:GC6P-488-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR Pfam; PF00072; Response_reg; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3DGE, ECO:0000213|PDB:3DGF, KW ECO:0000213|PDB:3GL9, ECO:0000213|PDB:4JA2}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Magnesium {ECO:0000213|PDB:3GL9, ECO:0000213|PDB:4JA2, KW ECO:0000213|PDB:4JAS, ECO:0000213|PDB:4JAV}; KW Metal-binding {ECO:0000213|PDB:3GL9, ECO:0000213|PDB:4JA2, KW ECO:0000213|PDB:4JAS, ECO:0000213|PDB:4JAV}; KW Receptor {ECO:0000313|EMBL:AGL49390.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 120 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT METAL 10 10 Magnesium. {ECO:0000213|PDB:3GL9, FT ECO:0000213|PDB:4JA2, FT ECO:0000213|PDB:4JAS}. FT METAL 53 53 Magnesium. {ECO:0000213|PDB:3GL9, FT ECO:0000213|PDB:4JA2, FT ECO:0000213|PDB:4JAS}. FT METAL 55 55 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:3GL9, FT ECO:0000213|PDB:4JA2, FT ECO:0000213|PDB:4JAS}. SQ SEQUENCE 122 AA; 13829 MW; D946EB06B5F279E0 CRC64; MSKKVLLVDD SAVLRKIVSF NLKKEGYEVI EAENGQIALE KLSEFTPDLI VLDIMMPVMD GFTVLKKLQE KEEWKRIPVI VLTAKGGEED ESLALSLGAR KVMRKPFSPS QFIEEVKHLL NE // ID Q9X229_THEMA Unreviewed; 593 AA. AC Q9X229; G4FG90; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 92. DE SubName: Full=Phosphoglycerol transferase {ECO:0000313|EMBL:AGL50635.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36770.1}; GN OrderedLocusNames=TM_1703 {ECO:0000313|EMBL:AAD36770.1}; GN ORFNames=Tmari_1711 {ECO:0000313|EMBL:AGL50635.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36770.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36770.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36770.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50635.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50635.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36770.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50635.1; -; Genomic_DNA. DR PIR; A72221; A72221. DR RefSeq; NP_229503.1; NC_000853.1. DR RefSeq; WP_004082219.1; NZ_CP011107.1. DR STRING; 243274.TM1703; -. DR EnsemblBacteria; AAD36770; AAD36770; TM_1703. DR EnsemblBacteria; AGL50635; AGL50635; Tmari_1711. DR GeneID; 897887; -. DR KEGG; tma:TM1703; -. DR KEGG; tmi:THEMA_05725; -. DR KEGG; tmm:Tmari_1711; -. DR KEGG; tmw:THMA_1745; -. DR PATRIC; 23938380; VBITheMar51294_1720. DR eggNOG; ENOG4105E0M; Bacteria. DR eggNOG; COG1368; LUCA. DR OMA; KEDNPKN; -. DR OrthoDB; EOG6SR8X1; -. DR BioCyc; TMAR243274:GC6P-1751-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR012160; ltaS-like. DR InterPro; IPR000917; Sulfatase_N. DR Pfam; PF00884; Sulfatase; 1. DR PIRSF; PIRSF005091; Mmb_sulf_HI1246; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Manganese {ECO:0000256|PIRSR:PIRSR005091-2}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR005091-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL50635.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 44 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 71 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 113 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 120 139 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 202 492 Sulfatase. {ECO:0000259|Pfam:PF00884}. FT ACT_SITE 254 254 {ECO:0000256|PIRSR:PIRSR005091-1}. FT METAL 210 210 Manganese. FT {ECO:0000256|PIRSR:PIRSR005091-3}. FT METAL 254 254 Manganese. FT {ECO:0000256|PIRSR:PIRSR005091-3}. FT METAL 427 427 Manganese. FT {ECO:0000256|PIRSR:PIRSR005091-3}. FT METAL 428 428 Manganese. FT {ECO:0000256|PIRSR:PIRSR005091-3}. FT BINDING 367 367 Substrate. FT {ECO:0000256|PIRSR:PIRSR005091-2}. SQ SEQUENCE 593 AA; 67651 MW; 430525688F741560 CRC64; MSDYLLVVFL AAKIVLFYVP TLSSFSVSVV FSTAGWLMLL ILVFKGGHKL LYTVLSLLLF VDFLYFQNFG NLPSIKEVVL LPQVGDLGGE IKYFIDLYSL LFVADLPFVW FFFKENTKRA YSLSSLFVLV LSFTFLGAIH TSQNLQSKFV FNRYGVFDYH VQDIINLFVN KKEENNDLTV SSVRNETTKP SQKSFFGIGK GKNVIVVQME SLQNFVIGLE VNGQEVTPNI NSFLRDSGTV YFSSCYQQVG SGNTADAEFI VNTSLHTLGD SVVYEEYPVI NLPALPRIMK QNGYHTIAFH GNVGWFWNRE EVYKHIGFDE FVSLEDFQQD EVFGMGLADV SFFKQAVQKL RNYPQPFYAF LITISSHTPF VIPEEHRKLE LPEDIADTIV GHYLQAIHYA DEAFGVFIDE LKRAELYENS VIVLYGDHAG LYPFNREVKT KIPEILDREF SFEIALNIPF AIHIPGENIR RVVNVPGGQI DFLPTILNVM GINYREGFFM GQDLLNAKHG FAALRYHVPD GSFIDDNRVF IVSWDGRLDK STAIDRKNGT PQRYVEFLDG YVKAIQQIEA SRYFILRNCQ PLQKVAKDQT SSR // ID Q9WY83_THEMA Unreviewed; 341 AA. AC Q9WY83; G4FHF5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35332.1}; GN OrderedLocusNames=TM_0241 {ECO:0000313|EMBL:AAD35332.1}; GN ORFNames=Tmari_0239 {ECO:0000313|EMBL:AGL49165.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35332.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35332.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35332.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49165.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49165.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35332.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49165.1; -; Genomic_DNA. DR PIR; C72403; C72403. DR RefSeq; NP_228055.1; NC_000853.1. DR RefSeq; WP_004082943.1; NZ_CP011107.1. DR STRING; 243274.TM0241; -. DR EnsemblBacteria; AAD35332; AAD35332; TM_0241. DR EnsemblBacteria; AGL49165; AGL49165; Tmari_0239. DR GeneID; 897142; -. DR KEGG; tma:TM0241; -. DR KEGG; tmi:THEMA_03520; -. DR KEGG; tmm:Tmari_0239; -. DR KEGG; tmw:THMA_0248; -. DR PATRIC; 23935357; VBITheMar51294_0244. DR eggNOG; ENOG4108YRR; Bacteria. DR eggNOG; ENOG4111KC6; LUCA. DR OMA; DEEWMEK; -. DR OrthoDB; EOG63Z768; -. DR BioCyc; TMAR243274:GC6P-254-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032602; DUF4899. DR Pfam; PF16240; DUF4899; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 318 340 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 341 AA; 39589 MW; 60C36B8A551496CD CRC64; MDLYFVKFRV TSKLTSEIVQ GYFLGKLNQI PEYDFFVIPG RYARKYSVDL NLGFEDFLED FKAKKESALK EVLEASAITD EFFDFWLIQS RKQNLRLVGS EFFRLVESGD HEALRVFIAD LFREWSEKLE VEVVGVPLDY EDVSLEVVKE HFEELSTDEV FKLFQREDLR NLPEVFPVLD PLNGVTIREI DVEERIDFVI LNYGNEEFSE KFKRFLKEKF GTENVASLPG KVLSKEIVKT REGTLYLLKV EFEEGIIGKA IVSPNLKIKR GESRVKISDE EWMEKIGEML KEGEESKQEK LKLRNSPQPV QKTTSSDFLL ALVLALLVMG ILLILSYLLF S // ID Q9X156_THEMA Unreviewed; 594 AA. AC Q9X156; G4FF73; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 103. DE SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:AGL50266.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36406.1}; GN OrderedLocusNames=TM_1334 {ECO:0000313|EMBL:AAD36406.1}; GN ORFNames=Tmari_1342 {ECO:0000313|EMBL:AGL50266.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36406.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36406.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36406.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50266.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50266.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36406.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50266.1; -; Genomic_DNA. DR PIR; F72265; F72265. DR RefSeq; NP_229136.1; NC_000853.1. DR RefSeq; WP_004081533.1; NZ_CP011107.1. DR STRING; 243274.TM1334; -. DR EnsemblBacteria; AAD36406; AAD36406; TM_1334. DR EnsemblBacteria; AGL50266; AGL50266; Tmari_1342. DR GeneID; 898148; -. DR KEGG; tma:TM1334; -. DR KEGG; tmi:THEMA_07675; -. DR KEGG; tmm:Tmari_1342; -. DR KEGG; tmw:THMA_1358; -. DR PATRIC; 23937601; VBITheMar51294_1346. DR eggNOG; COG1032; LUCA. DR OMA; ENIFMVE; -. DR OrthoDB; EOG62C98V; -. DR BioCyc; TMAR243274:GC6P-1365-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 222 435 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 594 AA; 68905 MW; 8D256B90F62BB07A CRC64; MRTSLLYKIK EEERILPSKN LKGNEIIFIL AFPDIYKYGL PNLGIQTLYK ELYLRDDVAV DRYYTDEDQP FSFEYGFKLK DSDFIGISFQ YEGIVLNAFK ILKAGSIPLI NLLREENDPI IIGGGPVANY NPLPLSLVCD VIVLGEAEEA IHKIIDSYKV YRNVKRKRMK FLQAVSQIEG IYVPCIHGFF QTGMVKQTSP VDINEHPAHS IFVTKNTVYE ERVFSIEVRR GCTQRCRFCY MGHRLKPPRT LRWETFKKIV DLAIDQCNVE IIKLFYEGLE TRIVEHYLEY IIKKGGRVRI GSQRLEKLSK RIIEIAAISG QRKITVAPET SGRLRKVIGK HEIKDEEILE VVRISSLYGI PDFGLYFILA IPGETFEDLD KIADLIMKVR HQMNKLKNTD GRLEIGINPL YPKPFTPFQY VKLPSLKNIE DRFLYIVEKV KKEGFPVVIS NDVVDEKVEK RQKDENENES LVKFETTVFH PISLLQPMIS RGGLEIAFLL HYLHSKRFNT VSDLENLLNE FGINAAWYFE EYIDKYCPWK IQKTLISEDY LLKEYFKALN FISTDEECKL NCSQCFNRCI DISTTNYQGG MSNA // ID Q9X210_THEMA Unreviewed; 565 AA. AC Q9X210; G4FG69; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36749.1}; GN OrderedLocusNames=TM_1682 {ECO:0000313|EMBL:AAD36749.1}; GN ORFNames=Tmari_1690 {ECO:0000313|EMBL:AGL50614.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36749.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36749.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36749.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50614.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50614.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36749.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50614.1; -; Genomic_DNA. DR PIR; D72222; D72222. DR RefSeq; NP_229482.1; NC_000853.1. DR RefSeq; WP_004082198.1; NZ_CP011107.1. DR STRING; 243274.TM1682; -. DR EnsemblBacteria; AAD36749; AAD36749; TM_1682. DR EnsemblBacteria; AGL50614; AGL50614; Tmari_1690. DR GeneID; 897236; -. DR KEGG; tma:TM1682; -. DR KEGG; tmm:Tmari_1690; -. DR KEGG; tmw:THMA_1724; -. DR PATRIC; 23938338; VBITheMar51294_1699. DR eggNOG; ENOG4108IU7; Bacteria. DR eggNOG; COG2206; LUCA. DR OMA; KKHTIWG; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1730-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 41 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 383 518 HDc. {ECO:0000259|SMART:SM00471}. FT COILED 320 368 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 565 AA; 65088 MW; 9B886F5B78A0A698 CRC64; MAPRKLSDVI KDLVYKKNLI FIFLLSLVIA VFVFIVTYYI GKKDWFEKLT LVSNEWERTI DHYRDVLDFF ADRSKDFENP GTILEVLKLI REHFGDYSAY PIFATPDGNY YIYPLYTFPP DFDPRERPWY KAAAENPDSA VVTPPFTHRI LGVVTFGIVR AILDERGNLL GVLGIDIVPS KVMKDLLQPG MYVLSEDGTV LLQNGEIHVK LDPEDFESRD YGAKISVSGV AFFRKTGSTV FVIQVPLLVF LRNSLLHLGY VIGLAFIISF PIVRRVSKLI DRELRVPLEV FSKASKEYLR SRIFDLGGTS SNILEINQLI DEVSDMITII ESQREELEAS YEELEASYSE LQKMAQEIEE KSRAVEEAYE FFTYKLVDIV EGFDEPTGNH VRRVQELSKF FAEEMGLDED LVHKIYLYAP LHDIGKIKVP KEILNKKGKL TAEEWEIMKK HTIWGGELLS GRKELEVARN IALYHHESYD GTGYPFGLKD DEIPIEAQIV KIVDVYDALR SERPYKKALS HEEAVRVILE GDGRTSPSNF HPKLIEIFRE KHEKIKEIWE KTHGE // ID Q9WYF1_THEMA Unreviewed; 83 AA. AC Q9WYF1; G4FHM9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35403.1}; GN OrderedLocusNames=TM_0315 {ECO:0000313|EMBL:AAD35403.1}; GN ORFNames=Tmari_0313 {ECO:0000313|EMBL:AGL49239.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35403.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35403.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35403.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49239.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49239.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35403.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49239.1; -; Genomic_DNA. DR PIR; B72392; B72392. DR RefSeq; NP_228127.1; NC_000853.1. DR RefSeq; WP_004083053.1; NZ_CP011107.1. DR STRING; 243274.TM0315; -. DR EnsemblBacteria; AAD35403; AAD35403; TM_0315. DR EnsemblBacteria; AGL49239; AGL49239; Tmari_0313. DR GeneID; 897256; -. DR KEGG; tma:TM0315; -. DR KEGG; tmi:THEMA_03150; -. DR KEGG; tmm:Tmari_0313; -. DR KEGG; tmw:THMA_0322; -. DR PATRIC; 23935509; VBITheMar51294_0320. DR eggNOG; ENOG4107MR9; Bacteria. DR eggNOG; COG3462; LUCA. DR KO; K08982; -. DR OMA; DGAMEIL; -. DR OrthoDB; EOG6HQSV5; -. DR BioCyc; TMAR243274:GC6P-328-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR018649; SHOCT. DR Pfam; PF09851; SHOCT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 41 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 55 80 SHOCT. {ECO:0000259|Pfam:PF09851}. SQ SEQUENCE 83 AA; 10309 MW; 860F8A76833E5A0B CRC64; MCPFCFWSWG FWPWNWGGGV IMMIFWAVIL VFLFVFLFRW LGGERHERVE RTDRALEILK ERFARGEITE EEYERMKRKI QNE // ID Q9X150_THEMA Unreviewed; 238 AA. AC Q9X150; G4FHZ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 109. DE SubName: Full=ABC transporter involved in cytochrome c biogenesis, ATPase component CcmA {ECO:0000313|EMBL:AGL50258.1}; DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36399.1}; GN OrderedLocusNames=TM_1327 {ECO:0000313|EMBL:AAD36399.1}; GN ORFNames=Tmari_1334 {ECO:0000313|EMBL:AGL50258.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36399.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36399.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36399.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50258.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50258.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36399.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50258.1; -; Genomic_DNA. DR PIR; C72267; C72267. DR RefSeq; NP_229129.1; NC_000853.1. DR RefSeq; WP_004083331.1; NZ_CP011107.1. DR STRING; 243274.TM1327; -. DR EnsemblBacteria; AAD36399; AAD36399; TM_1327. DR EnsemblBacteria; AGL50258; AGL50258; Tmari_1334. DR GeneID; 898155; -. DR KEGG; tma:TM1327; -. DR KEGG; tmi:THEMA_07710; -. DR KEGG; tmm:Tmari_1334; -. DR KEGG; tmw:THMA_1351; -. DR PATRIC; 23937591; VBITheMar51294_1341. DR eggNOG; ENOG4108R5A; Bacteria. DR eggNOG; COG4555; LUCA. DR KO; K01990; -. DR OMA; AFAINGE; -. DR OrthoDB; EOG65J54C; -. DR BioCyc; TMAR243274:GC6P-1358-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD36399.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD36399.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 233 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 238 AA; 27110 MW; B25BEE6108EB24B4 CRC64; MLEVIDVWKK YPPKTQALRE VSFEAEEGSI TAVFGENGSG KTTLLKVIAS FLIPDRGKVL IDSVNIVEKP SFAVEKVSIS TGYERSFYYR LSVEENLKFF GMLNDLLGKT LKRETERVMK ELGLLECRKK RYMELSTGYK KRVDVARALM KKASIYIFDE PCSGVDLRTR LKIHEIMKRL KESGRIVIFA SHDLEDLKIA DRVIVLKKGE KVLEFSPKKE DLAAVLRGIL EIQAFPGD // ID Q9WZ32_THEMA Unreviewed; 182 AA. AC Q9WZ32; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35647.1}; GN OrderedLocusNames=TM_0562 {ECO:0000313|EMBL:AAD35647.1}; GN ORFNames=Tmari_0559 {ECO:0000313|EMBL:AGL49484.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35647.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35647.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35647.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49484.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49484.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35647.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49484.1; -; Genomic_DNA. DR PIR; A72361; A72361. DR RefSeq; NP_228372.1; NC_000853.1. DR RefSeq; WP_010865147.1; NC_000853.1. DR EnsemblBacteria; AAD35647; AAD35647; TM_0562. DR EnsemblBacteria; AGL49484; AGL49484; Tmari_0559. DR GeneID; 897623; -. DR KEGG; tma:TM0562; -. DR KEGG; tmm:Tmari_0559; -. DR PATRIC; 23936031; VBITheMar51294_0570. DR OMA; WKRRISK; -. DR OrthoDB; EOG6QZMQN; -. DR BioCyc; TMAR243274:GC6P-586-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 44 61 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 150 169 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 182 AA; 21186 MW; E66AD5DF805A7813 CRC64; MKRLKYLLLF FATFLFDNSG TPIPILTATA LISVGKLKIF PSFFTIYMGL LSWDTVTFFA GKKLKSVPFN LRWKFVQKIL VEFLNVYIFS EKILLPLCKF VPWVGKFTPF LAGYTGRNFP TLLIIWLGDL LYESTFFFSS LIAGRVFLKF SKILGIVLFA VVILVYLLWK RRISKDIVRH RE // ID Q9X158_THEMA Unreviewed; 390 AA. AC Q9X158; G4FF75; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=MFS general substrate transporter {ECO:0000313|EMBL:AGL50268.1}; DE SubName: Full=Permease, putative {ECO:0000313|EMBL:AAD36408.1}; GN OrderedLocusNames=TM_1336 {ECO:0000313|EMBL:AAD36408.1}; GN ORFNames=Tmari_1344 {ECO:0000313|EMBL:AGL50268.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36408.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36408.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36408.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50268.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50268.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36408.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50268.1; -; Genomic_DNA. DR PIR; H72265; H72265. DR RefSeq; NP_229138.1; NC_000853.1. DR RefSeq; WP_004081535.1; NZ_CP011107.1. DR STRING; 243274.TM1336; -. DR EnsemblBacteria; AAD36408; AAD36408; TM_1336. DR EnsemblBacteria; AGL50268; AGL50268; Tmari_1344. DR GeneID; 898146; -. DR KEGG; tma:TM1336; -. DR KEGG; tmi:THEMA_07665; -. DR KEGG; tmm:Tmari_1344; -. DR KEGG; tmw:THMA_1360; -. DR PATRIC; 23937605; VBITheMar51294_1348. DR eggNOG; ENOG410817I; Bacteria. DR eggNOG; COG0477; LUCA. DR OMA; PSSHWPE; -. DR OrthoDB; EOG6PCPZS; -. DR BioCyc; TMAR243274:GC6P-1367-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042891; P:antibiotic transport; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR022324; Bacilysin_exporter_BacE_put. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR PRINTS; PR01988; EXPORTERBACE. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 82 109 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 184 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 205 228 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248 268 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 280 298 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 304 325 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 337 356 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 362 385 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 4 390 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 390 AA; 43591 MW; 6CA9C540B6F90A8E CRC64; MNRNLLLFAS GSFVSLIGTR IYQVALAWWL YSKTGSSEYV GLFMISSFLP AIIVSPFAGT VVDRHSRRNM MVVMDILRGV LFMYLFLMEY FSELTMALLL IVTVLVSVFD SFFNPAVDSL LPDLVRKENL VRANSLYRLL KNLSKILGPA LGSLLLKVVG LAGVILINSL SFLISGIFEM FIKVEEKHLK KVSKERNMWQ DIKSALLYIR SVRFILVTIL VIAIMNFFTG SMHVLLPEHV SKLGKSEWVY GTLMSMLSFG GLIVTFLMAT IRTRASVKTL GLNLVGYGLA VFVFAMTGNH WLMFAMYFLI GIFQTLFNIN VITLLQLAIP EEMRGKIFSL ISAVSFSLLP VSYGFFGFLS SYVATAHIFI TTSMALIAGG VLISLQRFEG // ID Q9X0Q7_THEMA Unreviewed; 70 AA. AC Q9X0Q7; G4FEH1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:AAD36250.1}; GN OrderedLocusNames=TM_1175 {ECO:0000313|EMBL:AAD36250.1}; GN ORFNames=Tmari_1182 {ECO:0000313|EMBL:AGL50106.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36250.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36250.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36250.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50106.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50106.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36250.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50106.1; -; Genomic_DNA. DR PIR; B72286; B72286. DR RefSeq; NP_228980.1; NC_000853.1. DR RefSeq; WP_004080188.1; NZ_CP011107.1. DR STRING; 243274.TM1175; -. DR EnsemblBacteria; AAD36250; AAD36250; TM_1175. DR EnsemblBacteria; AGL50106; AGL50106; Tmari_1182. DR GeneID; 898311; -. DR KEGG; tma:TM1175; -. DR KEGG; tmi:THEMA_08460; -. DR KEGG; tmm:Tmari_1182; -. DR KEGG; tmw:THMA_1200; -. DR PATRIC; 23937290; VBITheMar51294_1193. DR eggNOG; ENOG410606H; Bacteria. DR eggNOG; COG1146; LUCA. DR OMA; DKCIQCY; -. DR OrthoDB; EOG60SCM3; -. DR BioCyc; TMAR243274:GC6P-1204-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF13187; Fer4_9; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 34 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 35 65 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 70 AA; 7440 MW; 8D855487EE02B286 CRC64; MAKNWYPVID YGKCTGCLTC VNFCPHGVYT AENGKPKVSN PDACVEFCKG CQKICPAGAI NYSAEVSADG // ID Q9WYI5_THEMA Unreviewed; 200 AA. AC Q9WYI5; G4FHR2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Transporter, LysE family {ECO:0000313|EMBL:AGL49273.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35436.1}; GN OrderedLocusNames=TM_0350 {ECO:0000313|EMBL:AAD35436.1}; GN ORFNames=Tmari_0348 {ECO:0000313|EMBL:AGL49273.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35436.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35436.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35436.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49273.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49273.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35436.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49273.1; -; Genomic_DNA. DR PIR; D72389; D72389. DR RefSeq; NP_228161.1; NC_000853.1. DR RefSeq; WP_004083139.1; NZ_CP011107.1. DR STRING; 243274.TM0350; -. DR EnsemblBacteria; AAD35436; AAD35436; TM_0350. DR EnsemblBacteria; AGL49273; AGL49273; Tmari_0348. DR GeneID; 897306; -. DR KEGG; tma:TM0350; -. DR KEGG; tmi:THEMA_02965; -. DR KEGG; tmm:Tmari_0348; -. DR KEGG; tmw:THMA_0358; -. DR PATRIC; 23935581; VBITheMar51294_0355. DR eggNOG; ENOG4108XW4; Bacteria. DR eggNOG; COG1280; LUCA. DR OMA; WWATVGA; -. DR OrthoDB; EOG60KN2X; -. DR BioCyc; TMAR243274:GC6P-364-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0006865; P:amino acid transport; IEA:InterPro. DR InterPro; IPR001123; LysE-type. DR Pfam; PF01810; LysE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 61 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 67 85 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 127 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 139 162 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 174 196 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 200 AA; 21720 MW; 500597E88D43B582 CRC64; MISIFFGSFL VGLSGAVAPG PLMMIAVYQS AKSWKNSIKL IFGHVVLEAF LVLLLVLGFQ WVLKSPLVTK VIGLLGGSFL AFMGVSQLTA IKGEISQVEK TDQKIPLPIT GALVSLSNPY FLLWWMSVGS AFLVKAQTSL LAGVTAFYFG HILSDILWYS LIGVFGNTIL KSSLIYKIVM TVTGLFLIGF GLFFVLDSLR // ID Q9WY47_THEMA Unreviewed; 233 AA. AC Q9WY47; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 105. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35296.1}; DE SubName: Full=Alkanesulfonates ABC transporter ATP-binding protein {ECO:0000313|EMBL:AGL49128.1}; GN OrderedLocusNames=TM_0204 {ECO:0000313|EMBL:AAD35296.1}; GN ORFNames=Tmari_0202 {ECO:0000313|EMBL:AGL49128.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35296.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35296.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35296.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49128.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49128.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35296.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49128.1; -; Genomic_DNA. DR PIR; F72405; F72405. DR RefSeq; NP_228019.1; NC_000853.1. DR RefSeq; WP_008193907.1; NZ_CP011107.1. DR STRING; 243274.TM0204; -. DR EnsemblBacteria; AAD35296; AAD35296; TM_0204. DR EnsemblBacteria; AGL49128; AGL49128; Tmari_0202. DR GeneID; 897074; -. DR KEGG; tma:TM0204; -. DR KEGG; tmm:Tmari_0202; -. DR KEGG; tmw:THMA_0211; -. DR PATRIC; 23935280; VBITheMar51294_0206. DR eggNOG; ENOG4105D7T; Bacteria. DR eggNOG; COG1116; LUCA. DR KO; K02049; -. DR OMA; TKMKVMD; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-217-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD35296.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD35296.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 8 219 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 233 AA; 27112 MW; 390BA4C0BC87E23A CRC64; MEEVEVILKV EGLRKDFNGV KVIENWGFSV GKGERVALLG PSGCGKTTFL RIVSGLEDYQ GKVKVFTDKI GYVFQEPRLI PWKTITENLM LIRRDTDRIA SLLEKVELKG FENHYPWQLS EGMKQRVNFV RALLVDPDLL LLDEPFDALD LKTKMKVMDL LVDLWQKRRF SIVFVTHNVK EAVFLSERIF LLSGRPSKIL DEVKLKEKAI DFTDEKLFRL EKMVIERLLN LLR // ID Q9X0A8_THEMA Unreviewed; 139 AA. AC Q9X0A8; G4FEY1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36093.1}; GN OrderedLocusNames=TM_1016 {ECO:0000313|EMBL:AAD36093.1}; GN ORFNames=Tmari_1019 {ECO:0000313|EMBL:AGL49943.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36093.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36093.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36093.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49943.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49943.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36093.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49943.1; -; Genomic_DNA. DR PIR; H72305; H72305. DR RefSeq; NP_228822.1; NC_000853.1. DR RefSeq; WP_004080518.1; NZ_CP011107.1. DR STRING; 243274.TM1016; -. DR DNASU; 898694; -. DR EnsemblBacteria; AAD36093; AAD36093; TM_1016. DR EnsemblBacteria; AGL49943; AGL49943; Tmari_1019. DR GeneID; 898694; -. DR KEGG; tma:TM1016; -. DR KEGG; tmi:THEMA_09275; -. DR KEGG; tmm:Tmari_1019; -. DR KEGG; tmw:THMA_1038; -. DR PATRIC; 23936961; VBITheMar51294_1029. DR eggNOG; ENOG4107A9Q; Bacteria. DR eggNOG; ENOG410Z877; LUCA. DR OMA; ILISIEC; -. DR OrthoDB; EOG65BDP4; -. DR BioCyc; TMAR243274:GC6P-1045-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 49 67 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 74 94 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 106 128 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 139 AA; 15467 MW; B3AB0B7BED8B8E66 CRC64; MYRDKIAKII GTVFSALTVL PLAIPVFLSL LVLVTRGKFL YDFFMPAELF VFTLVGGLGV IVVLALMKKD FRRLAVALSL ALLNLIVSQV YANVSGLAHG STELTGTHLF IVSTFIVLYH FFAFLVVFES FRSLKFLRS // ID Q9X219_THEMA Unreviewed; 247 AA. AC Q9X219; G4FG80; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267}; DE EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267}; GN OrderedLocusNames=TM_1693 {ECO:0000313|EMBL:AAD36760.1}; GN ORFNames=Tmari_1701 {ECO:0000313|EMBL:AGL50625.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36760.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36760.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36760.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50625.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50625.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CC CoA + 1,2-diacyl-sn-glycerol 3-phosphate. CC {ECO:0000256|RuleBase:RU361267}. CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity CC and may constitute the binding site for the phosphate moiety of CC the glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}. CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate CC acyltransferase family. {ECO:0000256|RuleBase:RU361267}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36760.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50625.1; -; Genomic_DNA. DR PIR; G72223; G72223. DR RefSeq; NP_229493.1; NC_000853.1. DR RefSeq; WP_004082209.1; NZ_CP011107.1. DR STRING; 243274.TM1693; -. DR DNASU; 897253; -. DR EnsemblBacteria; AAD36760; AAD36760; TM_1693. DR EnsemblBacteria; AGL50625; AGL50625; Tmari_1701. DR GeneID; 897253; -. DR KEGG; tma:TM1693; -. DR KEGG; tmi:THEMA_05775; -. DR KEGG; tmm:Tmari_1701; -. DR KEGG; tmw:THMA_1735; -. DR PATRIC; 23938360; VBITheMar51294_1710. DR eggNOG; ENOG41080U1; Bacteria. DR eggNOG; COG0204; LUCA. DR KO; K00655; -. DR OMA; HEPVDPK; -. DR OrthoDB; EOG6ZWJDH; -. DR BioCyc; TMAR243274:GC6P-1741-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0016411; F:acylglycerol O-acyltransferase activity; IBA:GO_Central. DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR004552; AGP_acyltrans. DR InterPro; IPR002123; Plipid/glycerol_acylTrfase. DR Pfam; PF01553; Acyltransferase; 1. DR SMART; SM00563; PlsC; 1. DR TIGRFAMs; TIGR00530; AGP_acyltrn; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|RuleBase:RU361267, KW ECO:0000313|EMBL:AGL50625.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361267}; KW Lipid metabolism {ECO:0000256|RuleBase:RU361267}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267}; KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU361267, KW ECO:0000313|EMBL:AGL50625.1}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 78 191 PlsC. {ECO:0000259|SMART:SM00563}. SQ SEQUENCE 247 AA; 28697 MW; 0F970D7AF7399CCB CRC64; MRKIRNLLLT LYFYFIATVY IVFYGGFVLF RSFLMRDREK ARKYVLKEIE KFGKRAFTWL FSDVVVEGSE NIPKDRNFIV VANHQSLMDI PLILGFVATG AFIAKEELRK IPGVNWYIRY LNGVFLDRKN PRRAVRALRE AIEKLKNGVT FIVFPEGTRS PDGKVLSFKK DSLMIAVKTG VPVLPVSIWG TYHLIPKGRW TFTPGKVFLK IHEPVDPKGF SSEEELRKYV EEVVKRGVEE LKARWSK // ID Q9X0P3_THEMA Unreviewed; 314 AA. AC Q9X0P3; G4FEI7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36235.1}; GN OrderedLocusNames=TM_1159 {ECO:0000313|EMBL:AAD36235.1}; GN ORFNames=Tmari_1166 {ECO:0000313|EMBL:AGL50090.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36235.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36235.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36235.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50090.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50090.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36235.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50090.1; -; Genomic_DNA. DR PIR; E72287; E72287. DR RefSeq; NP_228965.1; NC_000853.1. DR RefSeq; WP_004080216.1; NZ_CP011107.1. DR STRING; 243274.TM1159; -. DR EnsemblBacteria; AAD36235; AAD36235; TM_1159. DR EnsemblBacteria; AGL50090; AGL50090; Tmari_1166. DR GeneID; 898327; -. DR KEGG; tma:TM1159; -. DR KEGG; tmi:THEMA_08540; -. DR KEGG; tmm:Tmari_1166; -. DR KEGG; tmw:THMA_1184; -. DR PATRIC; 23937255; VBITheMar51294_1176. DR eggNOG; ENOG41071GI; Bacteria. DR eggNOG; ENOG410XQYB; LUCA. DR OMA; GYCLGGM; -. DR OrthoDB; EOG6WX4MS; -. DR BioCyc; TMAR243274:GC6P-1188-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 146 163 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 314 AA; 36022 MW; 0AE61CA9D538746E CRC64; MFDDVRIPSE YSLGYLHRGK KIRVSILKFD STYSRAEKGT DPVEVYIFSP KRKKQGSVMI LQGLGSQNVL YLIWMAHYLS RKGIEAILPV LPGNFTRVAE GSVSGKDYFS SDLDRMSRFW EHALTDLLSL LELLKVKKMW HERNCLFGYC LGGMIAVLLN ALSSDFKKTI IMMAGGDFAT LFWKSPTLSF VRRELKSGKG EEHGMTNEEN FYDVYRSDLE RLKEFSSVQE MLSSNIHPLL KLDPLAYAKF VDTSRIVMLE AMFDKALPKS TRDILWEHLG KPKRIKVPSS HVSWLPFQVL AARYIMKLLK EQSA // ID Q9WYY0_THEMA Unreviewed; 172 AA. AC Q9WYY0; G4FDW1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 102. DE SubName: Full=Iron-dependent transcriptional repressor, putative {ECO:0000313|EMBL:AAD35595.1}; GN OrderedLocusNames=TM_0510 {ECO:0000313|EMBL:AAD35595.1}; GN ORFNames=Tmari_0506 {ECO:0000313|EMBL:AGL49431.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35595.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35595.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35595.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49431.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49431.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35595.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49431.1; -; Genomic_DNA. DR PIR; D72368; D72368. DR RefSeq; NP_228320.1; NC_000853.1. DR RefSeq; WP_004081427.1; NZ_CP011107.1. DR STRING; 243274.TM0510; -. DR EnsemblBacteria; AAD35595; AAD35595; TM_0510. DR EnsemblBacteria; AGL49431; AGL49431; Tmari_0506. DR GeneID; 897554; -. DR KEGG; tma:TM0510; -. DR KEGG; tmi:THEMA_02125; -. DR KEGG; tmm:Tmari_0506; -. DR KEGG; tmw:THMA_0522; -. DR PATRIC; 23935925; VBITheMar51294_0517. DR eggNOG; ENOG4105KTY; Bacteria. DR eggNOG; COG1321; LUCA. DR OMA; CPYVLKQ; -. DR OrthoDB; EOG6M9F3P; -. DR BioCyc; TMAR243274:GC6P-534-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR001367; Fe_dep_repressor. DR InterPro; IPR022687; HTH_DTXR. DR InterPro; IPR022689; Iron_dep_repressor. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02742; Fe_dep_repr_C; 1. DR Pfam; PF01325; Fe_dep_repress; 1. DR SMART; SM00529; HTH_DTXR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF47979; SSF47979; 1. DR PROSITE; PS50944; HTH_DTXR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 9 70 HTH dtxR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50944}. SQ SEQUENCE 172 AA; 20268 MW; D53511C092B9B261 CRC64; MPRGRKKTLT PALEDYLAVI QEILQKQPAA RVSTIARKMG VSLPSVTNAM KRLAELGYVE YEKYGYITLT EKGKRRARSL RGSQNRLRNF FFYVMGIPSP TAEKLSRHFS HFLDTKTRER FKRFYDIMVN FDESKVQELK EFLEESRRLV NVREIPEEAR IMEEDEEEEA QP // ID Q9X1C2_THEMA Unreviewed; 50 AA. AC Q9X1C2; G4FFD8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36473.1}; GN OrderedLocusNames=TM_1402 {ECO:0000313|EMBL:AAD36473.1}; GN ORFNames=Tmari_1409 {ECO:0000313|EMBL:AGL50333.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36473.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36473.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36473.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50333.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50333.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36473.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50333.1; -; Genomic_DNA. DR PIR; C72257; C72257. DR RefSeq; NP_229203.1; NC_000853.1. DR RefSeq; WP_004081631.1; NZ_CP011107.1. DR STRING; 243274.TM1402; -. DR EnsemblBacteria; AAD36473; AAD36473; TM_1402. DR EnsemblBacteria; AGL50333; AGL50333; Tmari_1409. DR GeneID; 898074; -. DR KEGG; tma:TM1402; -. DR KEGG; tmi:THEMA_07305; -. DR KEGG; tmm:Tmari_1409; -. DR KEGG; tmw:THMA_1431; -. DR PATRIC; 23937750; VBITheMar51294_1414. DR OMA; VRIMFRS; -. DR OrthoDB; EOG6384S6; -. DR BioCyc; TMAR243274:GC6P-1439-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 30 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 50 AA; 6116 MW; 23CE905A44DBC927 CRC64; MERVRDFFVL LFCVLLFIYE FLALNVRIMF RSIKKKRSRE TTPGFKFPVL // ID Q9WXW6_THEMA Unreviewed; 387 AA. AC Q9WXW6; G4FH26; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Alcohol dehydrogenase Acetaldehyde dehydrogenase {ECO:0000313|EMBL:AGL49034.1}; DE EC=1.1.1.1 {ECO:0000313|EMBL:AGL49034.1}; DE EC=1.2.1.10 {ECO:0000313|EMBL:AGL49034.1}; DE SubName: Full=Alcohol dehydrogenase, iron-containing {ECO:0000313|EMBL:AAD35205.1}; GN OrderedLocusNames=TM_0111 {ECO:0000313|EMBL:AAD35205.1}; GN ORFNames=Tmari_0108 {ECO:0000313|EMBL:AGL49034.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35205.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35205.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35205.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49034.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49034.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35205.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49034.1; -; Genomic_DNA. DR PIR; F72416; F72416. DR RefSeq; NP_227927.1; NC_000853.1. DR RefSeq; WP_004082682.1; NZ_CP011107.1. DR STRING; 243274.TM0111; -. DR EnsemblBacteria; AAD35205; AAD35205; TM_0111. DR EnsemblBacteria; AGL49034; AGL49034; Tmari_0108. DR GeneID; 896938; -. DR KEGG; tma:TM0111; -. DR KEGG; tmi:THEMA_04250; -. DR KEGG; tmm:Tmari_0108; -. DR KEGG; tmw:THMA_0107; -. DR PATRIC; 23935062; VBITheMar51294_0109. DR eggNOG; ENOG4105C0A; Bacteria. DR eggNOG; COG1454; LUCA. DR KO; K00001; -. DR OMA; KADIEGW; -. DR OrthoDB; EOG6TFCQS; -. DR BioCyc; TMAR243274:GC6P-111-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-EC. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR InterPro; IPR001670; ADH_Fe. DR InterPro; IPR018211; ADH_Fe_CS. DR Pfam; PF00465; Fe-ADH; 1. DR PROSITE; PS00913; ADH_IRON_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49034.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 9 378 Fe-ADH. {ECO:0000259|Pfam:PF00465}. SQ SEQUENCE 387 AA; 42659 MW; F464ACB11A3A016A CRC64; MFKISFYLPT EIIFRVGAVD ELEERAKKLG KKALIVTGRS STKKTGLLQR VVDLLKKAGV ESFVFDKIVP NPISDHVDEA AEIVRKEKID FIIGLGGGSP IDSAKAISIT APNEGKFWDY VPVGGGKIPE KSIPVVAIPT THGTGTEADP FAVITNPQTK EKVGIGYRNT FPVLSLVDPE VMKTLPKDQT AYTSMDAFYH AIEAFLNVNA NPYSDVLALD AMKRIVTYLP VAYENGEDME ARTNLAWAST EAGITETLTG VIANHALEHG LSGFYPEITH GLGLCITGPY LFEYIFDHAY ERLAIVGREV FGVYETDDRK AGRLAIKKLR DFQEMFGLNK RLSELGVKKE DIPKMAETGY RILNGVVVVT PGNLTAKDME EIFNRCY // ID Q9WYY3_THEMA Unreviewed; 501 AA. AC Q9WYY3; G4FDV8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 118. DE SubName: Full=ComM protein {ECO:0000313|EMBL:AAD35598.1}; DE SubName: Full=MG(2+) chelatase family protein / ComM-related protein {ECO:0000313|EMBL:AGL49434.1}; GN OrderedLocusNames=TM_0513 {ECO:0000313|EMBL:AAD35598.1}; GN ORFNames=Tmari_0509 {ECO:0000313|EMBL:AGL49434.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35598.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35598.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35598.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49434.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49434.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35598.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49434.1; -; Genomic_DNA. DR PIR; G72368; G72368. DR RefSeq; NP_228323.1; NC_000853.1. DR RefSeq; WP_004081420.1; NZ_CP011107.1. DR STRING; 243274.TM0513; -. DR EnsemblBacteria; AAD35598; AAD35598; TM_0513. DR EnsemblBacteria; AGL49434; AGL49434; Tmari_0509. DR GeneID; 897557; -. DR KEGG; tma:TM0513; -. DR KEGG; tmi:THEMA_02110; -. DR KEGG; tmm:Tmari_0509; -. DR KEGG; tmw:THMA_0525; -. DR PATRIC; 23935931; VBITheMar51294_0520. DR eggNOG; ENOG4105C0P; Bacteria. DR eggNOG; COG0606; LUCA. DR KO; K07391; -. DR OMA; CRCTPDQ; -. DR OrthoDB; EOG6ZWJFW; -. DR BioCyc; TMAR243274:GC6P-537-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR001208; MCM_dom. DR InterPro; IPR004482; Mg_chelat-rel. DR InterPro; IPR025158; Mg_chelat-rel_C. DR InterPro; IPR000523; Mg_chelatse_chII_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR32039:SF7; PTHR32039:SF7; 1. DR Pfam; PF01078; Mg_chelatase; 1. DR Pfam; PF13335; Mg_chelatase_C; 1. DR PRINTS; PR01657; MCMFAMILY. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR00368; TIGR00368; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 212 391 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 501 AA; 56046 MW; 8F2A09F10FF46D4E CRC64; MNYNKLSSAT IQGIEAMKID VEVDFDNRSV FNDIDVVGLG DTAVKESRKR VKSAILNSGF SLPHGKYVVN LAPGDVRKEG SMLDLPIALC ILASTGIVQV SENILAIGEL SLNGEVKRVN GVLPVLLSLS EMFSGTVLIP KENEEEAKCV KELDIYAVES LRECVEFLRG DRTLKRIEYS GIENTNLEYE IDFSDVRDHE MVKRAVEIAV AGFHNILMVG NPGSGKTMIA KRIPTIFPPM SEEEILETSK VYSASGYPGI VKLRPFRAPH HTASTVSIIG GGTNPRPGEI SLAHNGVLFL DELPEFKRDV LEALRQPLEE GIVTVARAKF TVTYPARFML VGAMNPCPCG NLGDPKQPCV CSPRDIMRYR KKISGPLLDR MDLVINVPKL SFEEMMKKPE GEKSSSIRER VMKAREIQKR RFRDTHISCN SQMSHRMLRR FVQLDEKSED LLKRYVERYG LSGRKIDKVL KISRTIADLE GSNGVEMSHL AEALQYRFRE S // ID Q9X246_THEMA Unreviewed; 288 AA. AC Q9X246; G4FGA9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Permease of the drug/metabolite transporter (DMT) superfamily {ECO:0000313|EMBL:AGL50654.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36788.1}; GN OrderedLocusNames=TM_1722 {ECO:0000313|EMBL:AAD36788.1}; GN ORFNames=Tmari_1730 {ECO:0000313|EMBL:AGL50654.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36788.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36788.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36788.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50654.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50654.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36788.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50654.1; -; Genomic_DNA. DR PIR; F72219; F72219. DR RefSeq; NP_229521.1; NC_000853.1. DR RefSeq; WP_004082238.1; NZ_CP011107.1. DR STRING; 243274.TM1722; -. DR EnsemblBacteria; AAD36788; AAD36788; TM_1722. DR EnsemblBacteria; AGL50654; AGL50654; Tmari_1730. DR GeneID; 897231; -. DR KEGG; tma:TM1722; -. DR KEGG; tmi:THEMA_05630; -. DR KEGG; tmm:Tmari_1730; -. DR KEGG; tmw:THMA_1764; -. DR PATRIC; 23938420; VBITheMar51294_1740. DR eggNOG; ENOG4106KUD; Bacteria. DR eggNOG; COG0697; LUCA. DR OMA; FWGERIM; -. DR OrthoDB; EOG6X6RHW; -. DR BioCyc; TMAR243274:GC6P-1770-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 50 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 78 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 102 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 125 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 137 156 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 163 184 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 190 211 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 223 242 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248 267 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 4 126 EamA. {ECO:0000259|Pfam:PF00892}. FT DOMAIN 134 266 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 288 AA; 31785 MW; 48CCDC08B2DDF93D CRC64; MVKALFSLLF VAFIWGSTFP IQKIVLVGVS PTFYIAVRFF IAALVSYFLF GKGNVKYGSI LGTLLGIAYT TQTWGLTITT STKSGFITSM YIVFVPVFAY LLEREIPTIF QIVSFFAASL GLYMISGGIK DFNFGDFLTL ICAVSFALHV VLITMFSKRV KEVDLLFPQF LVVGILNLIL NFFWKNWNFT LPALGSAVFT ALAATILAIY LQAKYQKALG NNVSAIVFLG EPVFAAVVSY FMLGETMAGK QLLGAALLLI SMLFSSLERV KIVRDANQKG RDECEDSL // ID Q9X187_THEMA Unreviewed; 124 AA. AC Q9X187; G4FFA3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=DUF369 domain-containing protein {ECO:0000313|EMBL:AGL50298.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36437.1}; GN OrderedLocusNames=TM_1367 {ECO:0000313|EMBL:AAD36437.1}; GN ORFNames=Tmari_1374 {ECO:0000313|EMBL:AGL50298.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36437.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36437.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36437.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50298.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50298.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36437.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50298.1; -; Genomic_DNA. DR PIR; H72263; H72263. DR RefSeq; NP_229168.1; NC_000853.1. DR RefSeq; WP_004081563.1; NZ_CP011107.1. DR PDB; 1ZX8; X-ray; 1.90 A; A/B/C=1-124. DR PDB; 2KA0; NMR; -; A=1-124. DR PDBsum; 1ZX8; -. DR PDBsum; 2KA0; -. DR STRING; 243274.TM1367; -. DR EnsemblBacteria; AAD36437; AAD36437; TM_1367. DR EnsemblBacteria; AGL50298; AGL50298; Tmari_1374. DR GeneID; 898113; -. DR KEGG; tma:TM1367; -. DR KEGG; tmi:THEMA_07505; -. DR KEGG; tmm:Tmari_1374; -. DR KEGG; tmw:THMA_1392; -. DR PATRIC; 23937672; VBITheMar51294_1379. DR eggNOG; ENOG4105XI4; Bacteria. DR eggNOG; COG2164; LUCA. DR KO; K09143; -. DR OMA; DVAYWIP; -. DR OrthoDB; EOG6NPM9J; -. DR BioCyc; TMAR243274:GC6P-1400-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR029000; Cyclophilin-like_dom. DR InterPro; IPR025658; Cyclophilin_TM1367. DR InterPro; IPR007256; DUF369. DR Pfam; PF04126; Cyclophil_like; 1. DR PIRSF; PIRSF006456; UCP006456; 1. DR SUPFAM; SSF50891; SSF50891; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1ZX8, ECO:0000213|PDB:2KA0}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 120 Cyclophil_like. FT {ECO:0000259|Pfam:PF04126}. SQ SEQUENCE 124 AA; 13923 MW; A36BD56D38608156 CRC64; MRVELLFESG KCVIDLNEEY EVVKLLKEKI PFESVVNTWG EEIYFSTPVN VQKMENPREV VEIGDVGYWP PGKALCLFFG KTPMSDDKIQ PASAVNVIGK IVEGLEDLKK IKDGEKVAVR FASS // ID Q9X1R9_THEMA Unreviewed; 360 AA. AC Q9X1R9; G4FFX1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36650.1}; GN OrderedLocusNames=TM_1583 {ECO:0000313|EMBL:AAD36650.1}; GN ORFNames=Tmari_1591 {ECO:0000313|EMBL:AGL50515.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36650.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36650.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36650.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50515.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50515.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36650.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50515.1; -; Genomic_DNA. DR PIR; G72235; G72235. DR RefSeq; NP_229383.1; NC_000853.1. DR RefSeq; WP_004082012.1; NZ_CP011107.1. DR STRING; 243274.TM1583; -. DR EnsemblBacteria; AAD36650; AAD36650; TM_1583. DR EnsemblBacteria; AGL50515; AGL50515; Tmari_1591. DR GeneID; 897954; -. DR KEGG; tma:TM1583; -. DR KEGG; tmi:THEMA_06365; -. DR KEGG; tmm:Tmari_1591; -. DR KEGG; tmw:THMA_1618; -. DR PATRIC; 23938130; VBITheMar51294_1602. DR OMA; YASSKGD; -. DR OrthoDB; EOG6CP3S9; -. DR BioCyc; TMAR243274:GC6P-1624-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:InterPro. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:InterPro. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro. DR InterPro; IPR002695; AICARFT_IMPCHas. DR InterPro; IPR011607; MGS-like_dom. DR PANTHER; PTHR11692; PTHR11692; 1. DR SUPFAM; SSF52335; SSF52335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 360 AA; 41345 MW; 60ACCB7E1A235585 CRC64; MRILLSVSRF EDELIEILDR LDETYEIFAD NDCFEILKDR IPRIRPFERD DFDLLYLNWR DLPSEKREEK ILSTIDENRT LLFLKAIKNY REKLVVTTLE DLKLTFSEIE RAGDVSLQTR RYLLLKGLAH FLKVHSEVLE SLSDLFFIKD WKAIVLERLQ EGIKAPVSLL PVSIPPELVE DIGLASHLIR FLPQKACVLV KNGKIVYASS TGDLPEIEGG VFALKGVFRG EKKFDFILAE DFEGDVEGLR IKDLLHQEEG LVLLGASGYL REPVPTNDFT EVLSMHPVFD SCAVTKEGKL VLHVVELNRS DVINALEKID LSGTEVAFNF PISDEEKAEL KQKGVKKVSW IDSRRIWRRC // ID Q9X0T7_THEMA Unreviewed; 112 AA. AC Q9X0T7; G4FED6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Putative, Na(+) H(+) antiporter subunit C {ECO:0000313|EMBL:AGL50141.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36285.1}; GN OrderedLocusNames=TM_1210 {ECO:0000313|EMBL:AAD36285.1}; GN ORFNames=Tmari_1217 {ECO:0000313|EMBL:AGL50141.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36285.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36285.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36285.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50141.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50141.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36285.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50141.1; -; Genomic_DNA. DR PIR; H72280; H72280. DR RefSeq; NP_229015.1; NC_000853.1. DR RefSeq; WP_004080098.1; NZ_CP011107.1. DR STRING; 243274.TM1210; -. DR EnsemblBacteria; AAD36285; AAD36285; TM_1210. DR EnsemblBacteria; AGL50141; AGL50141; Tmari_1217. DR GeneID; 898274; -. DR KEGG; tma:TM1210; -. DR KEGG; tmi:THEMA_08280; -. DR KEGG; tmm:Tmari_1217; -. DR KEGG; tmw:THMA_1236; -. DR PATRIC; 23937362; VBITheMar51294_1228. DR eggNOG; ENOG4105MJ3; Bacteria. DR eggNOG; COG1006; LUCA. DR KO; K05567; -. DR OMA; HAGMIKP; -. DR OrthoDB; EOG6CK7RD; -. DR BioCyc; TMAR243274:GC6P-1240-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K. DR Pfam; PF00420; Oxidored_q2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 72 93 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 112 AA; 12212 MW; BDB50942324E6C91 CRC64; MIYVISILLA GIGIYGLLTQ KNLFKHLVSL TIIDTAVNLF IIALGYREGD APIYTDRVMN FSLNFVDPLP QALVLTAIVI GVGVLALGAS LLVRIKEKHS SLDLEEMKGV KE // ID Q9WXP9_THEMA Unreviewed; 359 AA. AC Q9WXP9; G4FGV9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 114. DE SubName: Full=Aminopeptidase P, putative {ECO:0000313|EMBL:AAD35136.1}; DE SubName: Full=Aminopeptidase YpdF (MP-, MA-, MS-, AP-, NP-specific) {ECO:0000313|EMBL:AGL48965.1}; GN OrderedLocusNames=TM_0042 {ECO:0000313|EMBL:AAD35136.1}; GN ORFNames=Tmari_0039 {ECO:0000313|EMBL:AGL48965.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35136.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35136.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35136.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48965.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48965.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the peptidase M24B family. CC {ECO:0000256|RuleBase:RU000590}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35136.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48965.1; -; Genomic_DNA. DR PIR; G72425; G72425. DR RefSeq; NP_227858.1; NC_000853.1. DR RefSeq; WP_004082509.1; NZ_CP011107.1. DR PDB; 2ZSG; X-ray; 1.65 A; A/B=1-359. DR PDBsum; 2ZSG; -. DR STRING; 243274.TM0042; -. DR MEROPS; M24.031; -. DR EnsemblBacteria; AAD35136; AAD35136; TM_0042. DR EnsemblBacteria; AGL48965; AGL48965; Tmari_0039. DR GeneID; 896866; -. DR KEGG; tma:TM0042; -. DR KEGG; tmi:THEMA_04590; -. DR KEGG; tmm:Tmari_0039; -. DR KEGG; tmw:THMA_0038; -. DR PATRIC; 23934924; VBITheMar51294_0040. DR eggNOG; ENOG4105DC7; Bacteria. DR eggNOG; COG0006; LUCA. DR KO; K01262; -. DR OMA; GEPNKEA; -. DR OrthoDB; EOG618QTW; -. DR BioCyc; TMAR243274:GC6P-42-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.350.10; -; 1. DR Gene3D; 3.90.230.10; -; 1. DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD. DR InterPro; IPR028980; Creatinase/Aminopeptidase_P_N. DR InterPro; IPR000587; Creatinase_N. DR InterPro; IPR000994; Pept_M24_structural-domain. DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS. DR Pfam; PF01321; Creatinase_N; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR SUPFAM; SSF53092; SSF53092; 1. DR SUPFAM; SSF55920; SSF55920; 1. DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2ZSG}; KW Aminopeptidase {ECO:0000313|EMBL:AAD35136.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD35136.1}; KW Metal-binding {ECO:0000256|RuleBase:RU000590}; KW Protease {ECO:0000313|EMBL:AAD35136.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 133 Creatinase_N. {ECO:0000259|Pfam:PF01321}. FT DOMAIN 140 343 Peptidase_M24. FT {ECO:0000259|Pfam:PF00557}. FT BINDING 275 275 Chloride 1. {ECO:0000213|PDB:2ZSG}. FT BINDING 279 279 Chloride 1. {ECO:0000213|PDB:2ZSG}. FT BINDING 342 342 Chloride 2. {ECO:0000213|PDB:2ZSG}. SQ SEQUENCE 359 AA; 39940 MW; 61314A77FA933A6D CRC64; MDRSERLIQL ISEEGIDAFL IMNIENSARA SSVYFSGFTG SFSIILISEN TRLLITDSRY TVQAKQETDF EVREVKGGDF IDVLKKTVND LKIKTIALEE ERVSLSLFRR ISSAFGDRKF IGIDDEVKQM RMVKDEGEIE KIKQAIEISE RAFLETVQQI RAGMTEKEIA ALLEYTMRKE GAEGVAFDTI VASGCRSALP HGKASDKVVE RGDVIVIDFG ATYENYCADI TRVVSIGEPS DEVKEVHSIV LEAQERALKI AKAGVTGKLL DSVAREFIRE KGYGEFFGHS LGHGIGLEVH EGPAISFRND SPLPENVVFT VEPGIYLEGK FGIRIEEDVV LKEQGCEILT TLPRSIFVV // ID Q9X0U3_THEMA Unreviewed; 368 AA. AC Q9X0U3; G4FED0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 100. DE SubName: Full=NADH dehydrogenase, 49 kDa subunit, putative {ECO:0000313|EMBL:AAD36291.1}; DE SubName: Full=NADH-ubiquinone oxidoreductase chain D {ECO:0000313|EMBL:AGL50147.1}; DE EC=1.6.5.3 {ECO:0000313|EMBL:AGL50147.1}; GN OrderedLocusNames=TM_1216 {ECO:0000313|EMBL:AAD36291.1}; GN ORFNames=Tmari_1223 {ECO:0000313|EMBL:AGL50147.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36291.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36291.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36291.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50147.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50147.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family. CC {ECO:0000256|RuleBase:RU003685}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36291.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50147.1; -; Genomic_DNA. DR PIR; F72281; F72281. DR RefSeq; NP_229021.1; NC_000853.1. DR RefSeq; WP_004080082.1; NZ_CP011107.1. DR STRING; 243274.TM1216; -. DR EnsemblBacteria; AAD36291; AAD36291; TM_1216. DR EnsemblBacteria; AGL50147; AGL50147; Tmari_1223. DR GeneID; 898268; -. DR KEGG; tma:TM1216; -. DR KEGG; tmi:THEMA_08250; -. DR KEGG; tmm:Tmari_1223; -. DR KEGG; tmw:THMA_1242; -. DR PATRIC; 23937374; VBITheMar51294_1234. DR eggNOG; ENOG4105CQV; Bacteria. DR eggNOG; COG0649; LUCA. DR KO; K00333; -. DR OMA; THYWYPD; -. DR OrthoDB; EOG62G5MP; -. DR BioCyc; TMAR243274:GC6P-1246-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR Gene3D; 1.10.645.10; -; 1. DR InterPro; IPR001135; NADH_Q_OxRdtase_suD. DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS. DR InterPro; IPR029014; NiFe_Hase-like. DR Pfam; PF00346; Complex1_49kDa; 1. DR SUPFAM; SSF56762; SSF56762; 1. DR PROSITE; PS00535; COMPLEX1_49K; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW NAD {ECO:0000256|RuleBase:RU003685}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003685, KW ECO:0000313|EMBL:AGL50147.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Ubiquinone {ECO:0000313|EMBL:AGL50147.1}. FT DOMAIN 118 368 Complex1_49kDa. FT {ECO:0000259|Pfam:PF00346}. SQ SEQUENCE 368 AA; 42045 MW; EF371E1D92B3C627 CRC64; MGETKLFFGP NHPGMHGNFS VHMYVEGDIV KKARPVPGFL HRGFEKLMER RYWYSNISLI PRICVPEPDI NEICYAMAIE KIAKVEVPER AQWIRMIVLE LARIANHIWT VGGIGGPLGL YTASHWGVAD RDRILDIFEA LSGARVYHMY IIPGGVRKNM TPKIEEMIWK TLDYIESRLP DYENLIFKNR IVHSRLRGRL ILTREQAVEM GVTGVGLRAT GVEYDIRKVD PYLFYDRVEF EVPTATDGDA FSRVYLKFKE IPQSIKIIRQ ALEKMPQADR VNVPIGRGNG LRRIVPKGMA YAHVESTRGE YGFFVVSDGK NKPYRVAVRG ASYPQGLYGI EKYLPGTRIE DVPIWLATMD VCAPEIDR // ID Q9WZ06_THEMA Unreviewed; 194 AA. AC Q9WZ06; G4FDT5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35621.1}; GN OrderedLocusNames=TM_0536 {ECO:0000313|EMBL:AAD35621.1}; GN ORFNames=Tmari_0533 {ECO:0000313|EMBL:AGL49458.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35621.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35621.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35621.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49458.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49458.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35621.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49458.1; -; Genomic_DNA. DR PIR; E72363; E72363. DR RefSeq; NP_228346.1; NC_000853.1. DR RefSeq; WP_004081369.1; NZ_CP011107.1. DR STRING; 243274.TM0536; -. DR EnsemblBacteria; AAD35621; AAD35621; TM_0536. DR EnsemblBacteria; AGL49458; AGL49458; Tmari_0533. DR GeneID; 897588; -. DR KEGG; tma:TM0536; -. DR KEGG; tmi:THEMA_01995; -. DR KEGG; tmm:Tmari_0533; -. DR KEGG; tmw:THMA_0549; -. DR PATRIC; 23935979; VBITheMar51294_0544. DR OMA; DLRFFDY; -. DR OrthoDB; EOG644ZPP; -. DR BioCyc; TMAR243274:GC6P-560-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 194 AA; 22863 MW; 407C23FC9EC4B62D CRC64; MKYILIKGLR FFDYPGGWLF FRKELDSAKL ELLNHVLRTF EGVFVFINLF SEEVDPIIAE KFIKDYIPQN SIVLDEIVDY LDVSVERRLD FSYPEFTSSP LSEKCECLVY DGERFERIDL SGFKVRLEEI SVFSELMEVP EESFTLLKGI LWDREVERIK NKRSVKFVGK ILKKKNRPKL DALLLEEIET GDET // ID Q9X065_THEMA Unreviewed; 41 AA. AC Q9X065; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36049.1}; GN OrderedLocusNames=TM_0970 {ECO:0000313|EMBL:AAD36049.1}; GN ORFNames=Tmari_0973 {ECO:0000313|EMBL:AGL49898.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36049.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36049.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36049.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49898.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49898.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36049.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49898.1; -; Genomic_DNA. DR PIR; G72312; G72312. DR RefSeq; NP_228778.1; NC_000853.1. DR RefSeq; WP_008193287.1; NZ_CP011107.1. DR STRING; 243274.TM0970; -. DR EnsemblBacteria; AAD36049; AAD36049; TM_0970. DR EnsemblBacteria; AGL49898; AGL49898; Tmari_0973. DR GeneID; 898712; -. DR KEGG; tma:TM0970; -. DR KEGG; tmm:Tmari_0973; -. DR KEGG; tmw:THMA_0993; -. DR PATRIC; 23936871; VBITheMar51294_0984. DR eggNOG; COG0675; LUCA. DR KO; K07496; -. DR OrthoDB; EOG6JTC9V; -. DR BioCyc; TMAR243274:GC6P-1000-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 40 OrfB_Zn_ribbon. FT {ECO:0000259|Pfam:PF07282}. SQ SEQUENCE 41 AA; 4586 MW; 7E52C021810E2023 CRC64; MPYGKFLSKL KYKADQVGIR VIEVLETHTS QTCSICGAVD R // ID Q9X0L7_THEMA Unreviewed; 412 AA. AC Q9X0L7; G4FEL5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36209.1}; GN OrderedLocusNames=TM_1133 {ECO:0000313|EMBL:AAD36209.1}; GN ORFNames=Tmari_1139 {ECO:0000313|EMBL:AGL50063.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36209.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36209.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36209.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50063.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50063.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36209.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50063.1; -; Genomic_DNA. DR PIR; A72290; A72290. DR RefSeq; NP_228939.1; NC_000853.1. DR RefSeq; WP_004080274.1; NZ_CP011107.1. DR STRING; 243274.TM1133; -. DR EnsemblBacteria; AAD36209; AAD36209; TM_1133. DR EnsemblBacteria; AGL50063; AGL50063; Tmari_1139. DR GeneID; 898631; -. DR KEGG; tma:TM1133; -. DR KEGG; tmi:THEMA_08680; -. DR KEGG; tmm:Tmari_1139; -. DR KEGG; tmw:THMA_1156; -. DR PATRIC; 23937201; VBITheMar51294_1149. DR eggNOG; ENOG4108R2I; Bacteria. DR eggNOG; COG1721; LUCA. DR OMA; EENHVIV; -. DR OrthoDB; EOG6P8TNH; -. DR BioCyc; TMAR243274:GC6P-1162-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR002881; DUF58. DR Pfam; PF01882; DUF58; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 33 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 189 276 DUF58. {ECO:0000259|Pfam:PF01882}. SQ SEQUENCE 412 AA; 48329 MW; 0AB5FE15E3FBF60E CRC64; MRVRKKPLVI LTIFSVAVWI LTQNNIFLLM VFFTATRWLD LLLTLKAIPK IKIERHITKT RLFVDEKAEM IYKIRYSGHL RISMKLNPSF SPVRFFKKDT EEVSLTPSSS EKLVFIFSFG TRGRKILKGF SIKIEDTFAT FSVEKEFNAE DEVIVFPEYV PIEFYKEALK ELLPGRKSPQ RLLEDNTMLK GLRDYNGEPM NRIHWKASAR YGRLLVKEHD HTALGRVKIF LDLNLPRDVQ LGEVWKELRR YYEEEAVRFV ASVVKDLKER HTPVELTVIG EEIWKNHDRD WVMDFELLAT VRGTDNSRFD TKSVLETVVF DPSDTVLLFC VHLTEQELPL LLRVRSQVSK LIVFVIPYGL RDPNTKPFRS YLLMRKDLLD LLEKVKLLEE NHVIVRGVRE NMTVQEVVES VP // ID Q9X0A5_THEMA Unreviewed; 158 AA. AC Q9X0A5; G4FEY5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36089.1}; GN OrderedLocusNames=TM_1012 {ECO:0000313|EMBL:AAD36089.1}; GN ORFNames=Tmari_1015 {ECO:0000313|EMBL:AGL49939.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36089.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36089.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36089.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49939.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49939.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36089.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49939.1; -; Genomic_DNA. DR PIR; D72305; D72305. DR RefSeq; NP_228818.1; NC_000853.1. DR RefSeq; WP_004080525.1; NZ_CP011107.1. DR PDB; 2EWR; X-ray; 1.60 A; A=1-158. DR PDB; 2FCL; X-ray; 1.20 A; A=1-157. DR PDB; 4HX0; X-ray; 1.87 A; A=1-158. DR PDBsum; 2EWR; -. DR PDBsum; 2FCL; -. DR PDBsum; 4HX0; -. DR STRING; 243274.TM1012; -. DR EnsemblBacteria; AAD36089; AAD36089; TM_1012. DR EnsemblBacteria; AGL49939; AGL49939; Tmari_1015. DR GeneID; 897701; -. DR KEGG; tma:TM1012; -. DR KEGG; tmi:THEMA_09295; -. DR KEGG; tmm:Tmari_1015; -. DR KEGG; tmw:THMA_1034; -. DR PATRIC; 23936953; VBITheMar51294_1025. DR eggNOG; ENOG4105UR3; Bacteria. DR eggNOG; ENOG4111NG7; LUCA. DR OMA; IHDIDIQ; -. DR OrthoDB; EOG6W7219; -. DR BioCyc; TMAR243274:GC6P-1041-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2EWR, ECO:0000213|PDB:2FCL, KW ECO:0000213|PDB:4HX0}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 158 AA; 18626 MW; 48DD5B5CCC8B9EE8 CRC64; MIRPEYLRVL RKIYDRLKNE KVNWVVTGSL SFALQGVPVE VHDIDIQTDE EGAYEIERIF SEFVSKKVRF SSTEKICSHF GELIIDGIKV EIMGDIRKRL EDGTWEDPVD LNKYKRFVET HGMKIPVLSL EYEYQAYLKL GRVEKAETLR KWLNERKG // ID Q9X0C1_THEMA Unreviewed; 80 AA. AC Q9X0C1; G4FEW7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Glutaredoxin {ECO:0000313|EMBL:AAD36108.1}; DE SubName: Full=Glutaredoxin-related protein {ECO:0000313|EMBL:AGL49959.1}; GN OrderedLocusNames=TM_1031 {ECO:0000313|EMBL:AAD36108.1}; GN ORFNames=Tmari_1035 {ECO:0000313|EMBL:AGL49959.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36108.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36108.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36108.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49959.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49959.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36108.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49959.1; -; Genomic_DNA. DR PIR; F72303; F72303. DR RefSeq; NP_228837.1; NC_000853.1. DR RefSeq; WP_004080491.1; NZ_CP011107.1. DR STRING; 243274.TM1031; -. DR EnsemblBacteria; AAD36108; AAD36108; TM_1031. DR EnsemblBacteria; AGL49959; AGL49959; Tmari_1035. DR GeneID; 897057; -. DR KEGG; tma:TM1031; -. DR KEGG; tmi:THEMA_09205; -. DR KEGG; tmm:Tmari_1035; -. DR KEGG; tmw:THMA_1053; -. DR PATRIC; 23936991; VBITheMar51294_1044. DR eggNOG; ENOG4107YE2; Bacteria. DR eggNOG; COG0695; LUCA. DR OMA; VYTTTTC; -. DR OrthoDB; EOG6Z3KS6; -. DR BioCyc; TMAR243274:GC6P-1060-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR011911; GlrX_YruB. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR014025; Glutaredoxin_subgr. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00462; Glutaredoxin; 1. DR PRINTS; PR00160; GLUTAREDOXIN. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR02196; GlrX_YruB; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 80 Glutaredoxin. FT {ECO:0000259|PROSITE:PS51354}. SQ SEQUENCE 80 AA; 9127 MW; B1802B9D3460262F CRC64; MQHLKIKIYT TPTCPYCRKA KEYFRSLGLK FKEVDVTKNP REAELMVKKT GQMGVPVIEI GNKIVIGFDK AKIDRLLGIS // ID Q9WZL8_THEMA Unreviewed; 254 AA. AC Q9WZL8; G4FD64; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:AGL49685.1}; DE EC=2.3.1.- {ECO:0000313|EMBL:AGL49685.1}; DE SubName: Full=Acyltransferase, putative {ECO:0000313|EMBL:AAD35841.1}; GN OrderedLocusNames=TM_0759 {ECO:0000313|EMBL:AAD35841.1}; GN ORFNames=Tmari_0760 {ECO:0000313|EMBL:AGL49685.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35841.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35841.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35841.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49685.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49685.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35841.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49685.1; -; Genomic_DNA. DR PIR; E72335; E72335. DR RefSeq; NP_228568.1; NC_000853.1. DR RefSeq; WP_004080944.1; NZ_CP011107.1. DR STRING; 243274.TM0759; -. DR EnsemblBacteria; AAD35841; AAD35841; TM_0759. DR EnsemblBacteria; AGL49685; AGL49685; Tmari_0760. DR GeneID; 898427; -. DR KEGG; tma:TM0759; -. DR KEGG; tmi:THEMA_00855; -. DR KEGG; tmm:Tmari_0760; -. DR KEGG; tmw:THMA_0778; -. DR PATRIC; 23936440; VBITheMar51294_0772. DR eggNOG; ENOG4105J5G; Bacteria. DR eggNOG; COG0110; LUCA. DR OMA; VMPRKIV; -. DR OrthoDB; EOG6VTK03; -. DR BioCyc; TMAR243274:GC6P-786-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 3. DR SUPFAM; SSF51161; SSF51161; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000313|EMBL:AAD35841.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35841.1}. SQ SEQUENCE 254 AA; 27484 MW; C14AA38DABD8FD11 CRC64; MSFISKGAKI GENLKIGRNV VIEDGVVIGN NVMIGHNVVI RDGTIVGDNC VIFDGTVLGK LPFKSAISAV TEEKEFPPLK IGNGVTIGAN CVIYRGSVLE DFVFVGDLVV IREDVKIGPY TVIGKGVTVE NRTTIGRYVK IETNAYITAL STIEDYCFIA PEVTFTNDNF LGRTEERKKF FKGPTLKKGA RIGANATILP GVVVGEDALV AAGSVVTRDV PDRKIVMGIP ARVVRDVPEE QLLDNQSYYK EESS // ID Q9X0J9_THEMA Unreviewed; 216 AA. AC Q9X0J9; G4FEN3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36191.1}; GN OrderedLocusNames=TM_1115 {ECO:0000313|EMBL:AAD36191.1}; GN ORFNames=Tmari_1121 {ECO:0000313|EMBL:AGL50045.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36191.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36191.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36191.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50045.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50045.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36191.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50045.1; -; Genomic_DNA. DR PIR; H72291; H72291. DR RefSeq; NP_228921.1; NC_000853.1. DR RefSeq; WP_004080308.1; NZ_CP011107.1. DR STRING; 243274.TM1115; -. DR DNASU; 898650; -. DR EnsemblBacteria; AAD36191; AAD36191; TM_1115. DR EnsemblBacteria; AGL50045; AGL50045; Tmari_1121. DR GeneID; 898650; -. DR KEGG; tma:TM1115; -. DR KEGG; tmi:THEMA_08770; -. DR KEGG; tmm:Tmari_1121; -. DR KEGG; tmw:THMA_1138; -. DR PATRIC; 23937165; VBITheMar51294_1131. DR eggNOG; ENOG4108E4K; Bacteria. DR eggNOG; ENOG41103JB; LUCA. DR OMA; VRKPGTY; -. DR OrthoDB; EOG6G20KD; -. DR BioCyc; TMAR243274:GC6P-1144-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 216 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006753493. SQ SEQUENCE 216 AA; 24637 MW; 029CC15755436CDF CRC64; MRRLLLIMLA LVVSSMFFAG FVDVYAYEGD PDNAKAFVSM GDSGHCNRHV WEIPMTLEVQ VAQWVHWNLT GTKWTWFVRK PGTYVANCIT ATLQSNSDLE ITFSGFDHLK YATGTSVNDT IEVEYAFGQQ VYSIPEDNWT PAPDLNSVEL LVPDSRVLHN GATYKLWNRI HVVRCNSAST YRDSGIIMLT LKNQKPWIDD EGNYADDLEK YVNNQR // ID Q9X2D6_THEMA Unreviewed; 124 AA. AC Q9X2D6; G4FGK3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36879.1}; GN OrderedLocusNames=TM_1816 {ECO:0000313|EMBL:AAD36879.1}; GN ORFNames=Tmari_1826 {ECO:0000313|EMBL:AGL50750.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36879.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36879.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36879.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50750.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50750.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36879.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50750.1; -; Genomic_DNA. DR PIR; C72206; C72206. DR RefSeq; NP_229613.1; NC_000853.1. DR RefSeq; WP_004082362.1; NZ_CP011107.1. DR PDB; 1O13; X-ray; 1.83 A; A=1-124. DR PDB; 1T3V; NMR; -; A=1-124. DR PDBsum; 1O13; -. DR PDBsum; 1T3V; -. DR STRING; 243274.TM1816; -. DR EnsemblBacteria; AAD36879; AAD36879; TM_1816. DR EnsemblBacteria; AGL50750; AGL50750; Tmari_1826. DR GeneID; 897351; -. DR KEGG; tma:TM1816; -. DR KEGG; tmi:THEMA_05115; -. DR KEGG; tmm:Tmari_1826; -. DR KEGG; tmw:THMA_1861; -. DR PATRIC; 23938619; VBITheMar51294_1836. DR eggNOG; ENOG4105VZY; Bacteria. DR eggNOG; COG1433; LUCA. DR OMA; GGIANML; -. DR OrthoDB; EOG6VXFD3; -. DR BioCyc; TMAR243274:GC6P-1867-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.30.420.130; -; 1. DR InterPro; IPR003731; Di-Nase_FeMo-co_biosynth. DR Pfam; PF02579; Nitro_FeMo-Co; 1. DR SUPFAM; SSF53146; SSF53146; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O13, ECO:0000213|PDB:1T3V}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 14 104 Nitro_FeMo-Co. FT {ECO:0000259|Pfam:PF02579}. SQ SEQUENCE 124 AA; 13625 MW; 5FF10C4ECBC24E13 CRC64; MIIAIPVSEN RGKDSPISEH FGRAPYFAFV KVKNNAIADI SVEENPLAQD HVHGAVPNFV KEKGAELVIV RGIGRRAIAA FEAMGVKVIK GASGTVEEVV NQYLSGQLKD SDYEVHDHHH HEHH // ID Q9X177_THEMA Unreviewed; 126 AA. AC Q9X177; G4FF92; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Sigma factor RpoE regulatory protein RseC {ECO:0000313|EMBL:AGL50287.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36427.1}; GN OrderedLocusNames=TM_1356 {ECO:0000313|EMBL:AAD36427.1}; GN ORFNames=Tmari_1363 {ECO:0000313|EMBL:AGL50287.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36427.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36427.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36427.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50287.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50287.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36427.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50287.1; -; Genomic_DNA. DR PIR; D72265; D72265. DR RefSeq; NP_229157.1; NC_000853.1. DR RefSeq; WP_004081552.1; NZ_CP011107.1. DR STRING; 243274.TM1356; -. DR EnsemblBacteria; AAD36427; AAD36427; TM_1356. DR EnsemblBacteria; AGL50287; AGL50287; Tmari_1363. DR GeneID; 898124; -. DR KEGG; tma:TM1356; -. DR KEGG; tmi:THEMA_07560; -. DR KEGG; tmm:Tmari_1363; -. DR KEGG; tmw:THMA_1381; -. DR PATRIC; 23937650; VBITheMar51294_1368. DR eggNOG; COG3086; LUCA. DR KO; K03803; -. DR OMA; MARETMV; -. DR OrthoDB; EOG60CWQ0; -. DR BioCyc; TMAR243274:GC6P-1389-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007359; SigmaE_reg_RseC_MucC. DR Pfam; PF04246; RseC_MucC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 68 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 111 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 126 AA; 14381 MW; CAB2EAF294E4530D CRC64; MYVREVKDGK VVVAKARTSA CGSCPAKNIC LSDNEIKLEI DWCGEDLKPG DEVVVDIPEY DPLKVSTLVY FLPLVIFAVT VITGYLFRLK DWVTFVLALG SVFAYYSLFR FRRKDRKPPR ILRKVS // ID Q9WZM4_THEMA Unreviewed; 265 AA. AC Q9WZM4; G4FD58; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 108. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35847.1}; GN OrderedLocusNames=TM_0765 {ECO:0000313|EMBL:AAD35847.1}; GN ORFNames=Tmari_0766 {ECO:0000313|EMBL:AGL49691.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35847.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35847.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35847.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49691.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49691.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35847.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49691.1; -; Genomic_DNA. DR PIR; C72336; C72336. DR RefSeq; NP_228574.1; NC_000853.1. DR RefSeq; WP_004080933.1; NZ_CP011107.1. DR STRING; 243274.TM0765; -. DR EnsemblBacteria; AAD35847; AAD35847; TM_0765. DR EnsemblBacteria; AGL49691; AGL49691; Tmari_0766. DR GeneID; 898433; -. DR KEGG; tma:TM0765; -. DR KEGG; tmm:Tmari_0766; -. DR KEGG; tmw:THMA_0784; -. DR PATRIC; 23936452; VBITheMar51294_0778. DR eggNOG; ENOG4105DVE; Bacteria. DR eggNOG; COG1131; LUCA. DR KO; K01990; -. DR OMA; PYLRVKE; -. DR OrthoDB; EOG6P5ZHH; -. DR BioCyc; TMAR243274:GC6P-792-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD35847.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD35847.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 217 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 265 AA; 30099 MW; 31AC8237F0B0838F CRC64; MMILRVKDLK KFYGEKAAVD GISFEVEKGE IFAILGPNGA GKTTTLKCIT GLRKKDSGEI ELNGTFTYLP EEKKLYPYLR VKEIIDLFKK IGKNFNEKNC LELLERFRID LNEKVTNLSH GMRTILYLSL VLSENVDLYI LDEPTWGLDP IVRNEILDRI RSLTFEGKSV LYTSHVLAEV EKIADRVAIM KEGKIILTGN LDDIKSSYGL VVSRENLNGY LLKTLKSGEK VYLVKKEEAP EGVKIEDAAF EDIFEAIVRG EINDR // ID Q9X002_THEMA Unreviewed; 160 AA. AC Q9X002; G4FCS5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35981.1}; GN OrderedLocusNames=TM_0900 {ECO:0000313|EMBL:AAD35981.1}; GN ORFNames=Tmari_0902 {ECO:0000313|EMBL:AGL49827.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35981.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35981.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35981.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49827.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49827.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35981.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49827.1; -; Genomic_DNA. DR PIR; C72318; C72318. DR RefSeq; NP_228708.1; NC_000853.1. DR RefSeq; WP_004080669.1; NZ_CP011107.1. DR STRING; 243274.TM0900; -. DR EnsemblBacteria; AAD35981; AAD35981; TM_0900. DR EnsemblBacteria; AGL49827; AGL49827; Tmari_0902. DR GeneID; 898574; -. DR KEGG; tma:TM0900; -. DR KEGG; tmi:THEMA_00135; -. DR KEGG; tmm:Tmari_0902; -. DR KEGG; tmw:THMA_0922; -. DR PATRIC; 23936731; VBITheMar51294_0914. DR eggNOG; ENOG4105Q8Y; Bacteria. DR eggNOG; ENOG4111X55; LUCA. DR OMA; KPVEFRI; -. DR OrthoDB; EOG6TN46H; -. DR BioCyc; TMAR243274:GC6P-930-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 160 AA; 18373 MW; A0454983576BEFAD CRC64; MTIAYLDSRK IEGKFIGGLL SVDERGIPVE FKYTDPVVPN ELQKILYGSS IDTYLKGELI AKTLLKKMEK KPDFVFVRDP ELLEVDDRLL LIVERTEKVE TPTRVSEEEV LLPFKGSSVK IVGKISDEDM KKLADLLETF DVMEPFQRLE RALEYLCSEK // ID Q9WYL8_THEMA Unreviewed; 336 AA. AC Q9WYL8; G4FHU8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE RecName: Full=Transport permease protein {ECO:0000256|RuleBase:RU361157}; GN OrderedLocusNames=TM_0387 {ECO:0000313|EMBL:AAD35472.1}; GN ORFNames=Tmari_0385 {ECO:0000313|EMBL:AGL49310.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35472.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35472.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35472.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49310.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49310.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU361157}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU361157}. CC -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family. CC {ECO:0000256|RuleBase:RU361157}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-2 domain. CC {ECO:0000256|RuleBase:RU361157}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35472.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49310.1; -; Genomic_DNA. DR PIR; C72384; C72384. DR RefSeq; NP_228197.1; NC_000853.1. DR RefSeq; WP_004083210.1; NZ_CP011107.1. DR STRING; 243274.TM0387; -. DR EnsemblBacteria; AAD35472; AAD35472; TM_0387. DR EnsemblBacteria; AGL49310; AGL49310; Tmari_0385. DR GeneID; 897365; -. DR KEGG; tma:TM0387; -. DR KEGG; tmi:THEMA_02785; -. DR KEGG; tmm:Tmari_0385; -. DR KEGG; tmw:THMA_0394; -. DR PATRIC; 23935657; VBITheMar51294_0393. DR eggNOG; ENOG4107Z66; Bacteria. DR eggNOG; COG0842; LUCA. DR KO; K01992; -. DR OMA; FPLMFLV; -. DR OrthoDB; EOG60KN2B; -. DR BioCyc; TMAR243274:GC6P-401-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR InterPro; IPR013525; ABC_2_trans. DR InterPro; IPR000412; ABC_2_transport. DR Pfam; PF01061; ABC2_membrane; 1. DR PRINTS; PR00164; ABC2TRNSPORT. DR PROSITE; PS51012; ABC_TM2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU361157}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU361157}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU361157}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361157}; KW Transport {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 20 40 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 141 164 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 185 212 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 218 244 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 256 275 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 309 332 Helical. {ECO:0000256|RuleBase:RU361157}. FT DOMAIN 3 298 ABC2_membrane. FT {ECO:0000259|Pfam:PF01061}. SQ SEQUENCE 336 AA; 38103 MW; 2D3904E58683B934 CRC64; MSEFLALFSA MWKESWRDKI STFFSIAFPV MFLLIFGFLF GGSGNSVKTA VVTVDYDLSD FGDVYTSLEE LKGYYHEVAV VEKERIIFIR NTTDEYYQSL LDSWEISLKN KVTRLLNGLN PVIMVKKEVL KTARELTSFD YTLTGVIAVS LLSIGLFGTV DVFSRYRERG FLKRLKATPV GNFSFVFGLI SARMFYGILS TALIMLLGTL IFKASYELNV FLFLISVVSS VLSFIALGAL ISILFKKSDV ATDAAVILFT IMMFLTGVYF PVSFLPDYLR VVSYFLPVKY GVELIRYSLG FEIFPFSRYL ITAVIMFLAG LMFVFYTASL VLRKED // ID Q9WXZ8_THEMA Unreviewed; 182 AA. AC Q9WXZ8; G4FH65; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Ribosomal protein L32p-like protein {ECO:0000313|EMBL:AGL49075.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35244.1}; GN OrderedLocusNames=TM_0151 {ECO:0000313|EMBL:AAD35244.1}; GN ORFNames=Tmari_0149 {ECO:0000313|EMBL:AGL49075.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35244.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35244.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35244.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49075.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49075.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35244.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49075.1; -; Genomic_DNA. DR PIR; E72412; E72412. DR RefSeq; NP_227966.1; NC_000853.1. DR RefSeq; WP_004082764.1; NZ_CP011107.1. DR STRING; 243274.TM0151; -. DR EnsemblBacteria; AAD35244; AAD35244; TM_0151. DR EnsemblBacteria; AGL49075; AGL49075; Tmari_0149. DR GeneID; 896987; -. DR KEGG; tma:TM0151; -. DR KEGG; tmi:THEMA_04045; -. DR KEGG; tmm:Tmari_0149; -. DR KEGG; tmw:THMA_0147; -. DR PATRIC; 23935146; VBITheMar51294_0150. DR eggNOG; ENOG4105VAT; Bacteria. DR eggNOG; COG1399; LUCA. DR KO; K07040; -. DR OMA; SEEFEFC; -. DR OrthoDB; EOG68Q0V3; -. DR BioCyc; TMAR243274:GC6P-152-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR InterPro; IPR003772; DUF177. DR Pfam; PF02620; DUF177; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Ribonucleoprotein {ECO:0000313|EMBL:AGL49075.1}; KW Ribosomal protein {ECO:0000313|EMBL:AGL49075.1}. SQ SEQUENCE 182 AA; 20901 MW; A25C8A02814C7390 CRC64; MNWKVELSEI EKKKRFFLEG IFDKDGIELD VGFCRFLEPV QVKMVVAKTK DGFTVGGYVH TAVEHPCARC LEPARVEIRG VIEALYLPES MRKNVKEEKL ESLKNIIYYH ETEFDLSERI IEAIVVAIPE KVLCKPDCKG LCPYCGANLN EEPDHKCDKI PVVDSRFEIL AELKNKLKNE EV // ID Q9X204_THEMA Unreviewed; 277 AA. AC Q9X204; G4FG63; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36743.1}; GN OrderedLocusNames=TM_1676 {ECO:0000313|EMBL:AAD36743.1}; GN ORFNames=Tmari_1684 {ECO:0000313|EMBL:AGL50608.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36743.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36743.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36743.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50608.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50608.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36743.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50608.1; -; Genomic_DNA. DR PIR; B72226; B72226. DR RefSeq; NP_229476.1; NC_000853.1. DR RefSeq; WP_004082192.1; NZ_CP011107.1. DR STRING; 243274.TM1676; -. DR EnsemblBacteria; AAD36743; AAD36743; TM_1676. DR EnsemblBacteria; AGL50608; AGL50608; Tmari_1684. DR GeneID; 897264; -. DR KEGG; tma:TM1676; -. DR KEGG; tmi:THEMA_05860; -. DR KEGG; tmm:Tmari_1684; -. DR KEGG; tmw:THMA_1718; -. DR PATRIC; 23938326; VBITheMar51294_1693. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR OMA; QWTELKE; -. DR OrthoDB; EOG6SV57W; -. DR BioCyc; TMAR243274:GC6P-1724-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 195 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 277 AA; 32570 MW; F8F5D215954A835D CRC64; MYLKRYKWIF LVVAMLIFFG VAFVQIHYQK KLERYQLEVF KIIVQRSVDL VSSGYFQWTE LKEAIEKNDE EFIEEAFEEI KSLDPYIKEI KILNQPPDFE EEYYRVESDG ERLWALFKIY DSMGEEMIAD RTAYVEWNVA GILNSIGASV EFRKGGKKTF WGLEYRSKFG NKWFAVSFWS SLGGFSIILI IHSIFVRSIL KFHYETEGLE RMIKIIDKKD HYTALHSEYT SRIAVLLGKK LGLNKKELKE LGIAGRLHDR TPTTQAIPLQ GDSKWLL // ID Q9X132_THEMA Unreviewed; 144 AA. AC Q9X132; G4FE44; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36380.1}; GN OrderedLocusNames=TM_1306 {ECO:0000313|EMBL:AAD36380.1}; GN ORFNames=Tmari_1313 {ECO:0000313|EMBL:AGL50237.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36380.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36380.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36380.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50237.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50237.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36380.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50237.1; -; Genomic_DNA. DR PIR; D72270; D72270. DR RefSeq; NP_229110.1; NC_000853.1. DR RefSeq; WP_004079914.1; NZ_CP011107.1. DR STRING; 243274.TM1306; -. DR DNASU; 898176; -. DR EnsemblBacteria; AAD36380; AAD36380; TM_1306. DR EnsemblBacteria; AGL50237; AGL50237; Tmari_1313. DR GeneID; 898176; -. DR KEGG; tma:TM1306; -. DR KEGG; tmi:THEMA_07810; -. DR KEGG; tmm:Tmari_1313; -. DR KEGG; tmw:THMA_1331; -. DR PATRIC; 23937552; VBITheMar51294_1322. DR eggNOG; ENOG41063IW; Bacteria. DR eggNOG; ENOG410Y412; LUCA. DR KO; K01992; -. DR OMA; FIAFIFH; -. DR OrthoDB; EOG6DJZ36; -. DR BioCyc; TMAR243274:GC6P-1337-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR InterPro; IPR013525; ABC_2_trans. DR Pfam; PF01061; ABC2_membrane; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 24 48 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 74 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 130 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 2 101 ABC2_membrane. FT {ECO:0000259|Pfam:PF01061}. SQ SEQUENCE 144 AA; 16348 MW; BE7ED1DE3F0963CB CRC64; MEAAVVVAYS YFVLKLEFAI SNPVMFACSF LILVLSFIST SFVFATLLTL SKNAFSWMST IQYPVYFISG MLFPIDILPK WIRVISSFLP ISWSVTLMRD SFEVGSAGKD LIFNALLLTL FYFLLGHVLF KKIERKSRAE GELV // ID Q9X0E1_THEMA Unreviewed; 233 AA. AC Q9X0E1; G4FEU7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36128.1}; GN OrderedLocusNames=TM_1051 {ECO:0000313|EMBL:AAD36128.1}; GN ORFNames=Tmari_1055 {ECO:0000313|EMBL:AGL49979.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36128.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36128.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36128.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49979.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49979.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36128.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49979.1; -; Genomic_DNA. DR PIR; E72301; E72301. DR RefSeq; NP_228857.1; NC_000853.1. DR RefSeq; WP_004080457.1; NZ_CP011107.1. DR STRING; 243274.TM1051; -. DR EnsemblBacteria; AAD36128; AAD36128; TM_1051. DR EnsemblBacteria; AGL49979; AGL49979; Tmari_1055. DR GeneID; 897089; -. DR KEGG; tma:TM1051; -. DR KEGG; tmi:THEMA_09105; -. DR KEGG; tmm:Tmari_1055; -. DR KEGG; tmw:THMA_1073; -. DR PATRIC; 23937031; VBITheMar51294_1064. DR eggNOG; ENOG4105Y2K; Bacteria. DR eggNOG; ENOG4112D06; LUCA. DR OMA; FEEFDYE; -. DR OrthoDB; EOG6S7XX7; -. DR BioCyc; TMAR243274:GC6P-1080-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR SUPFAM; SSF55186; SSF55186; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 13 34 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 233 AA; 26840 MW; 9656C561F05F790C CRC64; MARITLSDGQ SRFLFWLIVV IFGVAIALLS WNIYLKFQLR NVKVEIVEIK PVELKIPEEI EESFSVTPPP TPLLVEFEEF DYEKLRDEMA DFVSEDQVVS SFVVKKEDAL RIIRRSGLPY LISPVSTDTY SVVLLGEFED FSQVAQRSLY GVFVITTLSE SLSKELAYDL RVAGYPSYVY AFQKLDKKYY SVVVGAFPTL RLAEDYFEKL NWEDIMKRVK VNRPGYAGRL ISP // ID Q9X020_THEMA Unreviewed; 661 AA. AC Q9X020; G4FF72; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AAD35999.1}; GN OrderedLocusNames=TM_0918 {ECO:0000313|EMBL:AAD35999.1}; GN ORFNames=Tmari_0920 {ECO:0000313|EMBL:AGL49845.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35999.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35999.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35999.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49845.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49845.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35999.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49845.1; -; Genomic_DNA. DR PIR; G72316; G72316. DR RefSeq; NP_228726.1; NC_000853.1. DR RefSeq; WP_004080644.1; NZ_CP011107.1. DR STRING; 243274.TM0918; -. DR EnsemblBacteria; AAD35999; AAD35999; TM_0918. DR EnsemblBacteria; AGL49845; AGL49845; Tmari_0920. DR GeneID; 898592; -. DR KEGG; tma:TM0918; -. DR KEGG; tmi:THEMA_00045; -. DR KEGG; tmm:Tmari_0920; -. DR KEGG; tmw:THMA_0940; -. DR PATRIC; 23936767; VBITheMar51294_0932. DR eggNOG; ENOG4105C8Q; Bacteria. DR eggNOG; COG0840; LUCA. DR KO; K03406; -. DR OMA; TIINEVQ; -. DR OrthoDB; EOG6CK7NC; -. DR BioCyc; TMAR243274:GC6P-948-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR004089; MCPsignal_dom. DR Pfam; PF00015; MCPsignal; 1. DR SMART; SM00304; HAMP; 1. DR SMART; SM00283; MA; 1. DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1. DR PROSITE; PS50885; HAMP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 152 174 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 285 307 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 304 356 HAMP. {ECO:0000259|PROSITE:PS50885}. FT DOMAIN 375 611 Methyl-accepting transducer. FT {ECO:0000259|PROSITE:PS50111}. SQ SEQUENCE 661 AA; 72211 MW; 463A65CD195FEAB8 CRC64; MTLRAKVFLV ILVVLAGLLV SFYLIYQSVS GAVVETVKKN ATVQIQVLSN YFAEKLNKYV ERAVALTQSM EAQLLDTYSM ASNMVKLVKE ASNTLIAGIT IEEMTGSGYI AKADGLEQID SSSTIYQKYM DLVKNSQNPY LVTSDVFEGK PALVVLAPLG AFGAGTLGAV GYVIDLSQNK NFWRTVAEGG KLGESGYGLL VTSDGKVLIH KDMGNFMKDV KELGGFEKAF EEAKKGGEKY VEYEYNGEKK YTVWEKVPGY DFYIFSTGYL DELLAEGRKA TLGTIVTYVV FGGVIFAVLF VSMMPVVKRM RQQVEKVKRF GEGDLTVEFE AKGEDELTQI EESLKEAVLS LKEMIVSIIE AAKELSGASE EIKVLSEESH KMSENLHEEA KKILDEANNM SSALTEVTSG VEEVAASAQN ISKITQDLTE RSEAVTKAAR EGTERVEAVG GVINKLKGSA ERQRDYLREL VDSAKTIGEI VDTISSIAEQ TNLLALNAAI EAARAGEAGR GFAVVADEIR KLAEESQRAT EDIAKMLSSL RTTIEHVENG SKEMFEGVDE IAVMGEEVTK RFREILGRIE EINSMIENTA ATAQEQGAAA EEMASAMDNV TKIVEGVVES LNRMESLIED QTTSAAKVSQ AAERLSELSE QLSTLVQKFK V // ID Q9X2G6_THEMA Unreviewed; 1010 AA. AC Q9X2G6; G4FGP3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 98. DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:AGL50790.1}; DE EC=3.2.1.24 {ECO:0000313|EMBL:AGL50790.1}; DE SubName: Full=Alpha-mannosidase, putative {ECO:0000313|EMBL:AAD36913.1}; GN OrderedLocusNames=TM_1851 {ECO:0000313|EMBL:AAD36913.1}; GN ORFNames=Tmari_1866 {ECO:0000313|EMBL:AGL50790.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36913.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36913.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36913.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50790.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50790.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36913.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50790.1; -; Genomic_DNA. DR PIR; D72203; D72203. DR RefSeq; NP_229647.1; NC_000853.1. DR RefSeq; WP_004082402.1; NZ_CP011107.1. DR STRING; 243274.TM1851; -. DR CAZy; GH38; Glycoside Hydrolase Family 38. DR EnsemblBacteria; AAD36913; AAD36913; TM_1851. DR EnsemblBacteria; AGL50790; AGL50790; Tmari_1866. DR GeneID; 897181; -. DR KEGG; tma:TM1851; -. DR KEGG; tmi:THEMA_04915; -. DR KEGG; tmm:Tmari_1866; -. DR KEGG; tmw:THMA_1901; -. DR PATRIC; 23938691; VBITheMar51294_1872. DR eggNOG; ENOG4105C8I; Bacteria. DR eggNOG; COG0383; LUCA. DR HOGENOM; HOG000048425; -. DR KO; K01191; -. DR OMA; GTWVQLP; -. DR OrthoDB; EOG6038T2; -. DR BioCyc; TMAR243274:GC6P-1902-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006013; P:mannose metabolic process; IBA:GO_Central. DR GO; GO:0006517; P:protein deglycosylation; IBA:GO_Central. DR Gene3D; 1.20.1270.50; -; 1. DR Gene3D; 3.20.110.10; -; 1. DR InterPro; IPR011013; Gal_mutarotase_SF_dom. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR027291; Glyco_hydro_38/57_N. DR InterPro; IPR011682; Glyco_hydro_38_C. DR InterPro; IPR015341; Glyco_hydro_38_cen. DR InterPro; IPR000602; Glyco_hydro_38_N. DR InterPro; IPR028995; Glyco_hydro_57/38_cen. DR Pfam; PF09261; Alpha-mann_mid; 1. DR Pfam; PF01074; Glyco_hydro_38; 1. DR Pfam; PF07748; Glyco_hydro_38C; 1. DR SMART; SM00872; Alpha-mann_mid; 1. DR SUPFAM; SSF74650; SSF74650; 1. DR SUPFAM; SSF88688; SSF88688; 1. DR SUPFAM; SSF88713; SSF88713; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000313|EMBL:AGL50790.1}; KW Hydrolase {ECO:0000313|EMBL:AGL50790.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 513 586 Alpha-mann_mid. FT {ECO:0000259|SMART:SM00872}. SQ SEQUENCE 1010 AA; 117949 MW; B52ED9C793FB81DC CRC64; MKGRLWRMLS EIVPYTVLRR ERIESWIFSD DAVERIVDPS FEWDFSSAPV RFRKELEPFS VAGEQRAYLK LWFGGETLVL IDGKPYGEIN EYHRMLNITP LADGKPHTIE AQVMPRGLFG KPEKPVFTEA FFIVVDEALM KVVKTLELTI KTAEVIEDES LSKKLLDISE EFLSKVWIPR DTGTYLMTAL EDPGIKDEIK NTWNTPEFKE FTGVKLPEEL RNQILEEFEK FKEKLDRIRK NHPGFGTIHL VGHAHIDYAW LWPVEETKRK ILRTFANSVL LSKLYPEFVY TQSSAQMYED LKQNSPELFE EVRKLVEEGR WEPVGGMWVE SDCNVPSIES LVRQFYYGQK FFEREFGKKS KVCWLPDVFG FSWVLPQILK EAGIKYFVTT KLNWNDTNEF PYDLCRWRGI DGSEVIYFSF KNPNEGYNGK IDPDTVYKTW KNFRQKDLTN RVLLSFGHGD GGGGPTEEML ENYEVLKDFP GLPHLEMGTV EEFFKKVEID EELPVWDGEL YLELHRGTYT SQFRTKKLHK EAEDSLYLAE LISAFTDKDF SDEIDELWKI LLRNEFHDIL PGSSIKEVYE DTEKELRHVI EKSKDIVIES LKVLSSENKD VLTILNASSF PKKCLFFLNE DLAISFEGEA LLKQKTHDGR YVYFIDREIP PFTKVELKVR KATSEETPSE LRETNIMENE FLRVHVNDDG TIQIYDKELD RYVFEEKGNI LKLHKNIPAY WDNWDIAENV EKTGYTLRAK NIEKIESGPV REVIRVEHES EGSRITQHYI LYRKSRRLDI ETKVDWHTRR ALLRAYFPTT VLSRKARFDI SGGFIERPTH RNTSFEQARF EVPFHRWMDL SQTDFGVSIL NDGKYGGSVH QGIMALSLIK AGIFPDFLCD EGEHTFTYSV YVHPGDSLRD VVKESEDLNR SFIVHRGVLN LPSPLLEISP QNFRLTSLRR VKDKIVLRLV EIFGTSGKLS IKLPWHGEIY QTNVLEEKKQ KVTFPVVYHP FKIYTFVVEG // ID Q9WXM5_THEMA Unreviewed; 607 AA. AC Q9WXM5; G4FGS6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 116. DE SubName: Full=NADP-reducing hydrogenase, subunit C {ECO:0000313|EMBL:AAD35104.1}; GN OrderedLocusNames=TM_0010 {ECO:0000313|EMBL:AAD35104.1}; GN ORFNames=Tmari_0007 {ECO:0000313|EMBL:AGL48933.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35104.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35104.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35104.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48933.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48933.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35104.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48933.1; -; Genomic_DNA. DR PIR; D72430; D72430. DR RefSeq; NP_227826.1; NC_000853.1. DR RefSeq; WP_004082447.1; NZ_CP011107.1. DR STRING; 243274.TM0010; -. DR EnsemblBacteria; AAD35104; AAD35104; TM_0010. DR EnsemblBacteria; AGL48933; AGL48933; Tmari_0007. DR GeneID; 896819; -. DR KEGG; tma:TM0010; -. DR KEGG; tmi:THEMA_04750; -. DR KEGG; tmm:Tmari_0007; -. DR KEGG; tmw:THMA_0006; -. DR PATRIC; 23934860; VBITheMar51294_0008. DR eggNOG; ENOG4107EEP; Bacteria. DR eggNOG; COG1145; LUCA. DR eggNOG; COG1894; LUCA. DR KO; K00335; -. DR OMA; MSTIKYF; -. DR OrthoDB; EOG6W9XGK; -. DR BioCyc; TMAR243274:GC6P-10-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IBA:GO_Central. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS. DR InterPro; IPR011538; Nuo51_FMN-bd. DR InterPro; IPR019575; Nuop51_4Fe4S-bd. DR InterPro; IPR019554; Soluble_ligand-bd. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF01512; Complex1_51K; 1. DR Pfam; PF00037; Fer4; 2. DR Pfam; PF10589; NADH_4Fe-4S; 1. DR Pfam; PF10531; SLBB; 1. DR SMART; SM00928; NADH_4Fe-4S; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. DR PROSITE; PS00645; COMPLEX1_51K_2; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|RuleBase:RU003429, ECO:0000256|SAAS:SAAS00445598}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|RuleBase:RU003429, ECO:0000256|SAAS:SAAS00445598}; KW Iron-sulfur {ECO:0000256|RuleBase:RU003429, KW ECO:0000256|SAAS:SAAS00445598}; KW Metal-binding {ECO:0000256|RuleBase:RU003429, KW ECO:0000256|SAAS:SAAS00445598}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 539 568 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 569 598 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 607 AA; 66081 MW; 00EFE7AA56D26F64 CRC64; MPLTTNTILI CAGGACISAG EKSVKDAFEE ELRKYGLDEV VRVIETGCMG ACTLGPIAVI YPESVFYQKL TPDAAREIVE EHILKGRIVE KYLYKASEGK PVPRVHEEVP FFKKQVRIVT RNLGVIDPTK IEEYIARDGY FALAKALQMK PEDVIKEIKD SGLRGRGGAG FPTGLKWELA ARQKAEKKFV VCNADEGDPG AFMDRSVLEG DPHAVIEGMA IAAYAIGAQK GFVYVRAEYP LAIERLNIAL NQAREYGFLG GNIMGTDFSF DIEIRIGAGA FVCGEETALM ASIEGERGQP KVKPPYPVEK GLWGYPTVIN NVETLANVPW IIRNGAKEFR KYGTENSPGT KVFALAGKVK NTGLVEVPMG ITLRELIYEI GGGIAGDKKL KAIQTGGPSG GCIPAEYVDT PVDFESLQKL GAIMGSGGMI VMDEDDCMVD VARFFLEFTV EESCGKCTPC REGTKKMLEI LEKITSGEGT EEDIEELEKL AHVVKDTSLC GLGQTAPNPV LSTLRYFRDE YLAHVKEKRC PSKKCKALIS YVIDPEKCVG CTACARVCPV QCISGQVRQP HVIDQAECVR CGSCIEVCRF GAISKVTPAL PVEEAVE // ID Q9X019_THEMA Unreviewed; 309 AA. AC Q9X019; G4FCQ9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Phosphate permease, putative {ECO:0000313|EMBL:AAD35998.1}; DE SubName: Full=Putative low-affinity inorganic phosphate transporter {ECO:0000313|EMBL:AGL49844.1}; GN OrderedLocusNames=TM_0917 {ECO:0000313|EMBL:AAD35998.1}; GN ORFNames=Tmari_0919 {ECO:0000313|EMBL:AGL49844.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35998.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35998.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35998.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49844.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49844.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35998.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49844.1; -; Genomic_DNA. DR PIR; F72316; F72316. DR RefSeq; NP_228725.1; NC_000853.1. DR RefSeq; WP_004080645.1; NZ_CP011107.1. DR STRING; 243274.TM0917; -. DR EnsemblBacteria; AAD35998; AAD35998; TM_0917. DR EnsemblBacteria; AGL49844; AGL49844; Tmari_0919. DR GeneID; 898591; -. DR KEGG; tma:TM0917; -. DR KEGG; tmi:THEMA_00050; -. DR KEGG; tmm:Tmari_0919; -. DR KEGG; tmw:THMA_0939; -. DR PATRIC; 23936765; VBITheMar51294_0931. DR eggNOG; ENOG4107WWA; Bacteria. DR eggNOG; COG0306; LUCA. DR KO; K03306; -. DR OMA; ANVFGPF; -. DR OrthoDB; EOG6NWBS7; -. DR BioCyc; TMAR243274:GC6P-947-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central. DR InterPro; IPR001204; Phos_transporter. DR PANTHER; PTHR11101; PTHR11101; 1. DR Pfam; PF01384; PHO4; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 91 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 127 150 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 162 180 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 200 221 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 282 304 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 309 AA; 32199 MW; 613DF1F9D8BCEF7B CRC64; MFVLLLPSLF LGWSLGANDA ANVFGPFVGS GLIPYRKATI VASIFVILGS VLGGARGLQN ISSLSTSDLL LSSIAVLSGA LTVTIMTKLG IPVSTSQAVV GGIIGANVTV MGIGGIDFSA LTKILTVWFL TPVGAFFLSL IFYPVLSFLF RKIPSIQIQD RVIKISAWII GAYGAFSLGA NNVANVTGVF AGKILTIEQA AFLGGISIAI GILTYSKNVM LTVGKNLIEL DHFTSLIAVL SQAMVVWIFS LIGIHVSSSQ AIVGAVLGAG YSKGMNLGNK KVLIKILSGW FLTPAVSGTL SFLLTSLIK // ID Q9X262_THEMA Unreviewed; 140 AA. AC Q9X262; G4FGC6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 88. DE RecName: Full=Mini-ribonuclease 3 {ECO:0000256|HAMAP-Rule:MF_01468}; DE Short=Mini-3 {ECO:0000256|HAMAP-Rule:MF_01468}; DE Short=Mini-RNase 3 {ECO:0000256|HAMAP-Rule:MF_01468}; DE EC=3.1.26.- {ECO:0000256|HAMAP-Rule:MF_01468}; DE AltName: Full=Mini-RNase III {ECO:0000256|HAMAP-Rule:MF_01468}; GN Name=mrnC {ECO:0000256|HAMAP-Rule:MF_01468}; GN OrderedLocusNames=TM_1740 {ECO:0000313|EMBL:AAD36805.1}; GN ORFNames=Tmari_1748 {ECO:0000313|EMBL:AGL50672.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36805.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36805.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36805.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50672.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50672.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Involved in correct processing of both the 5' and 3' CC ends of 23S rRNA precursor. Processes 30S rRNA precursor CC transcript even in absence of ribonuclease 3 (Rnc); Rnc processes CC 30S rRNA into smaller rRNA precursors. {ECO:0000256|HAMAP- CC Rule:MF_01468}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01468}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01468}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01468}. CC -!- SIMILARITY: Belongs to the MrnC RNase family. {ECO:0000256|HAMAP- CC Rule:MF_01468}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36805.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50672.1; -; Genomic_DNA. DR PIR; C72218; C72218. DR RefSeq; NP_229538.1; NC_000853.1. DR RefSeq; WP_004082263.1; NZ_CP011107.1. DR STRING; 243274.TM1740; -. DR EnsemblBacteria; AAD36805; AAD36805; TM_1740. DR EnsemblBacteria; AGL50672; AGL50672; Tmari_1748. DR GeneID; 897119; -. DR KEGG; tma:TM1740; -. DR KEGG; tmi:THEMA_05535; -. DR KEGG; tmm:Tmari_1748; -. DR KEGG; tmw:THMA_1782; -. DR PATRIC; 23938456; VBITheMar51294_1758. DR eggNOG; ENOG4105KEB; Bacteria. DR eggNOG; COG1939; LUCA. DR KO; K11145; -. DR OMA; CAERDSK; -. DR OrthoDB; EOG6W45XT; -. DR BioCyc; TMAR243274:GC6P-1788-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1520.10; -; 1. DR HAMAP; MF_01468; RNase_Mini_III; 1. DR InterPro; IPR008226; Mini3_fam. DR InterPro; IPR000999; RNase_III_dom. DR Pfam; PF00636; Ribonuclease_3; 1. DR PIRSF; PIRSF005520; UCP005520; 1. DR SMART; SM00535; RIBOc; 1. DR SUPFAM; SSF69065; SSF69065; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01468}; KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_01468}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01468}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01468}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01468}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01468}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01468}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_01468}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01468}. FT DOMAIN 2 131 RNase III. {ECO:0000259|SMART:SM00535}. FT ACT_SITE 24 24 {ECO:0000256|HAMAP-Rule:MF_01468}. SQ SEQUENCE 140 AA; 16409 MW; 84B63229C549676B CRC64; MEKLFRFEAE PEKLPPAVLA YLGDAVLELI FRSRFTGDYR MSVIHERVKE HTSKHGQAWM LENIWNLLDE REQEIVKRAM NSKAAKRHGN DPTYRKSTGF EALIGYLFLK REFDRIEELL RVVMDLESLR KKNPGGSAQE // ID Q9WZI3_THEMA Unreviewed; 309 AA. AC Q9WZI3; G4FD99; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Inner membrane protein YrbG, predicted calcium/sodium:proton antiporter {ECO:0000313|EMBL:AGL49650.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35806.1}; GN OrderedLocusNames=TM_0724 {ECO:0000313|EMBL:AAD35806.1}; GN ORFNames=Tmari_0725 {ECO:0000313|EMBL:AGL49650.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35806.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35806.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35806.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49650.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49650.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35806.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49650.1; -; Genomic_DNA. DR PIR; B72342; B72342. DR RefSeq; NP_228533.1; NC_000853.1. DR RefSeq; WP_004081007.1; NZ_CP011107.1. DR STRING; 243274.TM0724; -. DR EnsemblBacteria; AAD35806; AAD35806; TM_0724. DR EnsemblBacteria; AGL49650; AGL49650; Tmari_0725. DR GeneID; 898391; -. DR KEGG; tma:TM0724; -. DR KEGG; tmi:THEMA_01040; -. DR KEGG; tmm:Tmari_0725; -. DR KEGG; tmw:THMA_0740; -. DR PATRIC; 23936368; VBITheMar51294_0737. DR eggNOG; ENOG4105FEU; Bacteria. DR eggNOG; COG0530; LUCA. DR KO; K07301; -. DR OMA; EQMAELP; -. DR OrthoDB; EOG6H4K73; -. DR BioCyc; TMAR243274:GC6P-750-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0008273; F:calcium, potassium:sodium antiporter activity; IBA:GO_Central. DR GO; GO:0030955; F:potassium ion binding; IBA:GO_Central. DR GO; GO:0031402; F:sodium ion binding; IBA:GO_Central. DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GOC. DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central. DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GOC. DR InterPro; IPR004481; K/Na/Ca-exchanger. DR InterPro; IPR004837; NaCa_Exmemb. DR PANTHER; PTHR10846; PTHR10846; 1. DR Pfam; PF01699; Na_Ca_ex; 2. DR TIGRFAMs; TIGR00367; TIGR00367; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 89 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 101 118 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 124 143 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 163 180 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 200 218 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 230 254 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 266 282 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 289 306 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 2 143 Na_Ca_ex. {ECO:0000259|Pfam:PF01699}. FT DOMAIN 166 306 Na_Ca_ex. {ECO:0000259|Pfam:PF01699}. SQ SEQUENCE 309 AA; 33125 MW; BF7DCB3532B41984 CRC64; MAFLLTALGI AILVIGANWL VTGASSLALT LGISKLIVGL SVVAFGTSLP ELVSSLVSAS KGYSSIAISN VVGSNIANVG LCLGLAAVLR AVPVKRSTVR SEIPFMILAT ISFISLFLKN YYLSWHDGVV FLSFMVIFMY YLITSAKEVV EEELEEIKPQ KSVAVSLLMI VGGILALWFG GDLAIENAVK IAETFGLSQA FIGLTVIAVG TSLPELVVSI VSTAKKESDI LVGNIVGSNV FNILLILGVS SFFGRLTVDV NYSVDLWFLF ITSALLLVFA VSRRRISRFE GAVFLIIYSV YVYFVVLRG // ID Q9X1Q9_THEMA Unreviewed; 603 AA. AC Q9X1Q9; G4FFW1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 91. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36640.1}; GN OrderedLocusNames=TM_1573 {ECO:0000313|EMBL:AAD36640.1}; GN ORFNames=Tmari_1581 {ECO:0000313|EMBL:AGL50505.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36640.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36640.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36640.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50505.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50505.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36640.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50505.1; -; Genomic_DNA. DR PIR; F72237; F72237. DR RefSeq; NP_229373.1; NC_000853.1. DR RefSeq; WP_004081993.1; NZ_CP011107.1. DR STRING; 243274.TM1573; -. DR EnsemblBacteria; AAD36640; AAD36640; TM_1573. DR EnsemblBacteria; AGL50505; AGL50505; Tmari_1581. DR GeneID; 897959; -. DR KEGG; tma:TM1573; -. DR KEGG; tmi:THEMA_06415; -. DR KEGG; tmm:Tmari_1581; -. DR KEGG; tmw:THMA_1608; -. DR PATRIC; 23938108; VBITheMar51294_1591. DR eggNOG; ENOG4107X7R; Bacteria. DR eggNOG; COG1520; LUCA. DR OMA; WKIDLEA; -. DR OrthoDB; EOG6P5Z9H; -. DR BioCyc; TMAR243274:GC6P-1614-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.140.10.10; -; 1. DR InterPro; IPR025666; PQQ-like_dom. DR InterPro; IPR018391; PQQ_beta_propeller_repeat. DR InterPro; IPR002372; PQQ_repeat. DR InterPro; IPR027295; Quinoprotein_ADH-like_fam. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR InterPro; IPR017986; WD40_repeat_dom. DR Pfam; PF13360; PQQ_2; 1. DR Pfam; PF13570; PQQ_3; 1. DR SMART; SM00564; PQQ; 7. DR SUPFAM; SSF50978; SSF50978; 2. DR SUPFAM; SSF50998; SSF50998; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 603 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972314. SQ SEQUENCE 603 AA; 68048 MW; D1C7EEF487532C2D CRC64; MWRKIVFFCI LLASYLFSAQ LMVVQGNLAS LVEVEGDYLK KNLEIVFPFS PLDGVVVSDT AYFATGNALL EYNLKSKEII RSLKIPAKKL KWNDERLVVI CEKEVLLLDP VSFKYSKISF QQSVSDVDFY EGYLLVSHGK YVSLTKNSEE IWKIEAEAEI NKISVNKEKK AFAALTSDGT IFLVDLENVL APKVVFFSKF EEAEDLEWIE DFLIVFFRNK VITMNAAKLT SPRAFKEYIA SGNTTSVVKL QDSILFTKGN DLYRVGVFSL KKIGTAQRVF PVLAQGEMYT PGDLIWQLNL EAEVRSSPVI FENLLVVADV EGIVHAISMS GGKLWSYRTG FVITAPPRVF MERIYVTSWD NFLYAISQNG QLVWKIDLEA DVSKPFEVNS YGIYLATDSG EVYFIDHDSS IVWRFKDEEW ISTGVTVDEN GVVYFGTSRS LYSLYSNGSL RWKTRTGYLL TMKPIIIDRY VITGSNSGWL LCVNRTNGNV VWKKKLPLSL NSQLSAFGDT VFVNAEDGIY SIDLSGNVKR IISASTPSPV AVSKEGYVYF VSEGVLYSFT LDGKRRWERK VGESTVEPVV GEERVVVVTR SGNLYCFFDS VHP // ID Q9X0H3_THEMA Unreviewed; 222 AA. AC Q9X0H3; G4FER1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 88. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36164.1}; GN OrderedLocusNames=TM_1087 {ECO:0000313|EMBL:AAD36164.1}; GN ORFNames=Tmari_1091 {ECO:0000313|EMBL:AGL50015.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36164.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36164.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36164.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50015.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50015.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36164.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50015.1; -; Genomic_DNA. DR PIR; G72297; G72297. DR RefSeq; NP_228893.1; NC_000853.1. DR RefSeq; WP_004080389.1; NZ_CP011107.1. DR STRING; 243274.TM1087; -. DR MEROPS; S54.027; -. DR DNASU; 897088; -. DR EnsemblBacteria; AAD36164; AAD36164; TM_1087. DR EnsemblBacteria; AGL50015; AGL50015; Tmari_1091. DR GeneID; 897088; -. DR KEGG; tma:TM1087; -. DR KEGG; tmi:THEMA_08920; -. DR KEGG; tmm:Tmari_1091; -. DR KEGG; tmw:THMA_1109; -. DR PATRIC; 23937103; VBITheMar51294_1100. DR eggNOG; ENOG4107S6E; Bacteria. DR eggNOG; COG0705; LUCA. DR OMA; MGHIRFL; -. DR OrthoDB; EOG6P335V; -. DR BioCyc; TMAR243274:GC6P-1116-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. DR Gene3D; 1.20.1540.10; -; 1. DR InterPro; IPR002610; Peptidase_S54_rhomboid. DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom. DR PANTHER; PTHR22936; PTHR22936; 1. DR Pfam; PF01694; Rhomboid; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 15 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 91 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 129 148 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 160 181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 193 212 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 66 214 Rhomboid. {ECO:0000259|Pfam:PF01694}. SQ SEQUENCE 222 AA; 25929 MW; 727793AEC17C6E50 CRC64; MFPLYDVLPS RKKPYVTIAL ILINVVVFVY ELMLNDRELL LFMYRYGLVP ARYTVERVKE ALGFSLLPFI THMFLHGGFW HILGNMWFLW IFGDNTEDEM GHVGYTLFYL SAGIFAALTQ FVFTLHSTTP MVGASGAVSG VMGAYFVLFP YSRIVTLFPI FFFLTLVEIP AFYYLMIWFF IQVLNGLVGS YGIAWWAHIG GFVYGMIWGY ILRMRRIHRY RY // ID Q9X1V5_THEMA Unreviewed; 121 AA. AC Q9X1V5; G4FG09; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|SAAS:SAAS00088523}; DE EC=1.11.1.15 {ECO:0000256|SAAS:SAAS00088503}; GN OrderedLocusNames=TM_1620 {ECO:0000313|EMBL:AAD36687.1}; GN ORFNames=Tmari_1629 {ECO:0000313|EMBL:AGL50553.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36687.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36687.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36687.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1P8C} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), AND DISULFIDE BONDS. RA Kim Y., Joachimiak A., Brunzelle J.S., Korolev S.V., Edwards A., RA Xu X., Savchenko A.; RT "Crystal Structure Analysis of Thermotoga maritima protein TM1620 RT (APC4843)."; RL Submitted (MAY-2003) to the PDB data bank. RN [3] {ECO:0000213|PDB:1VKE} RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS), AND DISULFIDE BONDS. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of carboxymuconolactone decarboxylase family RT protein possibly involved in antioxidative response (TM1620) from RT Thermotoga maritima at 1.56 A resolution."; RL Submitted (MAY-2004) to the PDB data bank. RN [4] {ECO:0000313|EMBL:AGL50553.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50553.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity. CC Required for the reduction of the AhpC active site cysteine CC residues and for the regeneration of the AhpC enzyme activity. CC {ECO:0000256|SAAS:SAAS00088543}. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC {ECO:0000256|SAAS:SAAS00088505}. CC -!- SIMILARITY: Belongs to the AhpD family. CC {ECO:0000256|SAAS:SAAS00571262}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36687.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50553.1; -; Genomic_DNA. DR PIR; F72232; F72232. DR RefSeq; NP_229420.1; NC_000853.1. DR RefSeq; WP_004082088.1; NZ_CP011107.1. DR PDB; 1P8C; X-ray; 2.30 A; A/B/C/D/E/F=1-121. DR PDB; 1VKE; X-ray; 1.56 A; A/B/C/D/E/F=1-121. DR PDBsum; 1P8C; -. DR PDBsum; 1VKE; -. DR SMR; Q9X1V5; 2-120. DR STRING; 243274.TM1620; -. DR PeroxiBase; 4560; TmaCMD. DR EnsemblBacteria; AAD36687; AAD36687; TM_1620. DR EnsemblBacteria; AGL50553; AGL50553; Tmari_1629. DR GeneID; 897931; -. DR KEGG; tma:TM1620; -. DR KEGG; tmi:THEMA_06145; -. DR KEGG; tmm:Tmari_1629; -. DR KEGG; tmw:THMA_1661; -. DR PATRIC; 23938214; VBITheMar51294_1639. DR eggNOG; ENOG4107YV4; Bacteria. DR eggNOG; COG0599; LUCA. DR OMA; RIFNLDT; -. DR OrthoDB; EOG6X3W8C; -. DR BioCyc; TMAR243274:GC6P-1666-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC. DR Gene3D; 1.20.1290.10; -; 1. DR InterPro; IPR029032; AhpD-like. DR InterPro; IPR004675; AhpD_core. DR InterPro; IPR003779; CMD-like. DR Pfam; PF02627; CMD; 1. DR SUPFAM; SSF69118; SSF69118; 1. DR TIGRFAMs; TIGR00778; ahpD_dom; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1P8C, ECO:0000213|PDB:1VKE}; KW Antioxidant {ECO:0000256|SAAS:SAAS00461132}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00461175}; KW Lyase {ECO:0000313|EMBL:AGL50553.1}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00461184}; KW Peroxidase {ECO:0000256|SAAS:SAAS00461184}; KW Redox-active center {ECO:0000256|SAAS:SAAS00461089}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 26 102 CMD. {ECO:0000259|Pfam:PF02627}. FT DISULFID 59 62 {ECO:0000213|PDB:1P8C, FT ECO:0000213|PDB:1VKE}. SQ SEQUENCE 121 AA; 13789 MW; 256A16A2F49A4548 CRC64; MEYKKFVEAR RELNEKVLSR GTLNTKRFFN LDSAVYRPGK LDVKTKELMG LVASTVLRCD DCIRYHLVRC VQEGASDEEI FEALDIALVV GGSIVIPHLR RAVGFLEELR EMEKNGETIS L // ID Q9WXT4_THEMA Unreviewed; 322 AA. AC Q9WXT4; G4FGZ4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Iron(III) ABC transporter, permease protein {ECO:0000313|EMBL:AAD35173.1}; DE SubName: Full=Vitamin B12 ABC transporter, permease component BtuC {ECO:0000313|EMBL:AGL49002.1}; GN OrderedLocusNames=TM_0079 {ECO:0000313|EMBL:AAD35173.1}; GN ORFNames=Tmari_0076 {ECO:0000313|EMBL:AGL49002.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35173.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35173.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35173.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49002.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49002.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. FecCD subfamily. CC {ECO:0000256|SAAS:SAAS00535775}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35173.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49002.1; -; Genomic_DNA. DR PIR; G72421; G72421. DR RefSeq; NP_227895.1; NC_000853.1. DR RefSeq; WP_004082603.1; NZ_CP011107.1. DR STRING; 243274.TM0079; -. DR EnsemblBacteria; AAD35173; AAD35173; TM_0079. DR EnsemblBacteria; AGL49002; AGL49002; Tmari_0076. DR GeneID; 896905; -. DR KEGG; tma:TM0079; -. DR KEGG; tmi:THEMA_04410; -. DR KEGG; tmm:Tmari_0076; -. DR KEGG; tmw:THMA_0075; -. DR PATRIC; 23934998; VBITheMar51294_0077. DR eggNOG; ENOG4105EHG; Bacteria. DR eggNOG; COG0609; LUCA. DR KO; K02015; -. DR OMA; ISWIYRI; -. DR OrthoDB; EOG61ZTDC; -. DR BioCyc; TMAR243274:GC6P-79-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR029022; ABC_BtuC-like. DR InterPro; IPR000522; ABC_transptr_permAse. DR PANTHER; PTHR30472; PTHR30472; 1. DR Pfam; PF01032; FecCD; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00417415}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00417415, KW ECO:0000256|SAAS:SAAS00417419, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00417419, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00417419, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00417373}. FT TRANSMEM 50 70 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 82 101 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 107 130 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 142 164 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 187 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 234 257 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 269 287 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 299 318 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 322 AA; 34972 MW; F934A0BFDECB2444 CRC64; MRKLVFPILI LSFLLGIFFG SVPLDPLEVL GVLFGLKENP GVERILSLRI PRVLASFLVG AGLSIVGNSF QNLLKNPLVD PYLLGISSGA SFGTVVSFYL AETLGISWIY RIPLLSFGFS MIASLLTLLI ARKEGRFPVT TIVLSGVVVS TLFSSLTYMT IVLLKRNVTT ISMWLFGSFS GSTWEDVLFY LMVVIPFLLY SLIFSKHLNA MALGEEEAFI LGVSVERLKV VTFLFGNLIT AFLVSRSGVI GFVGLIVPHI SRYLVGPNFL KSVLSSLIVG GVLLTLCDTA ARTFFSPTEL PVGVVTALIG APFLAFLMKR GV // ID Q9WZR3_THEMA Unreviewed; 1065 AA. AC Q9WZR3; G4FD18; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35888.1}; GN OrderedLocusNames=TM_0806 {ECO:0000313|EMBL:AAD35888.1}; GN ORFNames=Tmari_0807 {ECO:0000313|EMBL:AGL49732.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35888.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35888.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35888.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49732.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49732.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35888.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49732.1; -; Genomic_DNA. DR PIR; G72330; G72330. DR RefSeq; NP_228615.1; NC_000853.1. DR RefSeq; WP_004080857.1; NZ_CP011107.1. DR STRING; 243274.TM0806; -. DR EnsemblBacteria; AAD35888; AAD35888; TM_0806. DR EnsemblBacteria; AGL49732; AGL49732; Tmari_0807. DR GeneID; 898474; -. DR KEGG; tma:TM0806; -. DR KEGG; tmi:THEMA_00620; -. DR KEGG; tmm:Tmari_0807; -. DR KEGG; tmw:THMA_0825; -. DR PATRIC; 23936532; VBITheMar51294_0818. DR eggNOG; ENOG4108GKU; Bacteria. DR eggNOG; COG3307; LUCA. DR OMA; GWNNFKR; -. DR OrthoDB; EOG6VMTFM; -. DR BioCyc; TMAR243274:GC6P-833-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007016; O-antigen_ligase-related. DR Pfam; PF04932; Wzy_C; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 29 48 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 160 183 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 195 213 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 219 237 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 257 274 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 365 385 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 397 416 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 422 442 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 454 473 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 495 522 {ECO:0000256|SAM:Coils}. FT COILED 547 584 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1065 AA; 123498 MW; 9255270C2F3199D0 CRC64; MEILFYVMYV VVALFSSRKL TYEFSVPKYA LITVFLSVMF SMVLMKILRK EKLEIRFNMA HVAFFAFAIS ALLSTINVYR DNPVYFRYSF DIAIYVLLMF FTSIFISNFF VTKERIKRFL TVSVALAGFI AFDALLNFYG GVDVFLGSVG SPFSRATVKA TIGNVNFVSN FLSLNLPLAI YLIASADFKR KEASVIKVIA SVSALLMVSG ILVSQTRSLY VANIISLCIF VAFYMIFRKK KVSEETDREV LNMSKTLMTF VLIASIVLVV LYNLPTPLNG YGMVSPAGRI QAVAEVSSWH ERLLSWFSSI YQWRTHKILG TGIGTYQILT INYMGDVIED HPILMYGWNN FKRTHNDYLQ VLGEMGIVGF ASVVFLALSL GILFFKIIRR IAVRDDLLLF LALASSFITF MMHSAFSFPA HLLPNGFLVM TVASIAVGGY FYGGKKAEIQ RKKAVVFGTI VLLVGVVSAY LKWNYFISEV YFKWGNSAYL SIRKVEEDMA KLDNYEQQVK TAMEELSSLS GRYSYLKPDE FKKFVESQNL PVKPSNLEIE RLRLETIQKE SQKLQNALQQ IASYRNQLTN QKIELYRKAK EYFLKSVQVN KAYGRSYFYL ASLATSEYRI DELKAKLKTK EDYNAFFEQN FDEYQKVIFP DVKKTDLTFL ENASLSTIND LGEDNLITAQ VLLDSVSLYL SSLKSFNERN TYRGLATRYV GLHQIMKILF SKAQDDLTQK AFAELASKYF DSFTNYAKLT VKILPGAWNR FPDWKHYDLR KAVAGQDIYR YFATKAAEAQ PLTVQKNREF LFHLAKREIW AVESMNKAGV WGVPDGVLDF LHAMPFEYVS SNNRQEALFA SEDVLKIYNE SYRNAKESIS MYESRAEKTF ESVLEELKEY LESNLGKEYA NQFEKLFKDL FESFKNLNWL SINVQEMNKF ISEKNYTYKL NPWAELLVER MKNFENYMKQ RNVEASRISE VLSRIYNDLY ELRDVLVFER YIRFLEHYRL ILNDARNFLR TLEKVYSVAS DEEWKMILED WSVNLWNDEK FETKEQVLER LKKSEEFLKT IEEGL // ID Q9WXR3_THEMA Unreviewed; 338 AA. AC Q9WXR3; G4FGX2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 128. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35151.1}; DE SubName: Full=Xylose-regulated ABC transporter, ATP-binding protein 2 {ECO:0000313|EMBL:AGL48980.1}; GN OrderedLocusNames=TM_0057 {ECO:0000313|EMBL:AAD35151.1}; GN ORFNames=Tmari_0054 {ECO:0000313|EMBL:AGL48980.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35151.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35151.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35151.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48980.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48980.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35151.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48980.1; -; Genomic_DNA. DR PIR; B72424; B72424. DR RefSeq; NP_227873.1; NC_000853.1. DR RefSeq; WP_004082545.1; NZ_CP011107.1. DR STRING; 243274.TM0057; -. DR TCDB; 3.A.1.5.29; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35151; AAD35151; TM_0057. DR EnsemblBacteria; AGL48980; AGL48980; Tmari_0054. DR GeneID; 896881; -. DR KEGG; tma:TM0057; -. DR KEGG; tmi:THEMA_04520; -. DR KEGG; tmm:Tmari_0054; -. DR KEGG; tmw:THMA_0053; -. DR PATRIC; 23934954; VBITheMar51294_0055. DR eggNOG; ENOG4108JQ7; Bacteria. DR eggNOG; COG4608; LUCA. DR KO; K02032; -. DR OMA; MEKCALE; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-57-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35151.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35151.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 4 258 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 338 AA; 38139 MW; 5E9A081C3AC94506 CRC64; MKLLEVKGLK KYFPLTKGFF KKVVGYVRAV DDVSFDIKQG ETLALVGESG CGKTTTAKSI LRAIDPTDGD VILHLDGKDV NIAKLSRDEL KPYRRYMQMI FQNPYTSLNP RMKVKEIVGE PLLVNGIAKG KELEDRVAEL LKAVGLRPEY MIRYPHAFSG GQRQRIVIAR AIALRPKLVV CDEPTSALDV SIRAQILNLL MDLQEEFALT YLFITHDLSV VEHISDRVAV MYLGKIVELS STEEIFENPK HPYTETLLRS VPKPDPDLRE ELVPIEGEVP NPANPPSGCY FHPRCPYAKS ICKEEYPEFR NLGTEDNPHY VACHFAESLK LRGVKITL // ID Q9WZG1_THEMA Unreviewed; 88 AA. AC Q9WZG1; G4FDC7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 84. DE SubName: Full=Flagellar biosynthesis protein FliQ {ECO:0000313|EMBL:AAD35779.1}; GN OrderedLocusNames=TM_0697 {ECO:0000313|EMBL:AAD35779.1}; GN ORFNames=Tmari_0697 {ECO:0000313|EMBL:AGL49622.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35779.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35779.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35779.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49622.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49622.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35779.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49622.1; -; Genomic_DNA. DR PIR; G72345; G72345. DR RefSeq; NP_228506.1; NC_000853.1. DR RefSeq; WP_004081052.1; NZ_CP011107.1. DR STRING; 243274.TM0697; -. DR EnsemblBacteria; AAD35779; AAD35779; TM_0697. DR EnsemblBacteria; AGL49622; AGL49622; Tmari_0697. DR GeneID; 898364; -. DR KEGG; tma:TM0697; -. DR KEGG; tmi:THEMA_01180; -. DR KEGG; tmm:Tmari_0697; -. DR KEGG; tmw:THMA_0712; -. DR PATRIC; 23936312; VBITheMar51294_0709. DR eggNOG; ENOG41084BY; Bacteria. DR eggNOG; COG1987; LUCA. DR KO; K02420; -. DR OMA; FNQIQNM; -. DR OrthoDB; EOG6CS09R; -. DR BioCyc; TMAR243274:GC6P-723-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR002191; Bac_export_3. DR InterPro; IPR006305; FliQ. DR Pfam; PF01313; Bac_export_3; 1. DR PIRSF; PIRSF004669; FliQ; 1. DR PRINTS; PR00952; TYPE3IMQPROT. DR TIGRFAMs; TIGR01402; fliQ; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AAD35779.1}; KW Cilium {ECO:0000313|EMBL:AAD35779.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35779.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 39 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 70 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 88 AA; 10089 MW; D7B92BB71AC9B790 CRC64; MTIEVFLDIM KSGISLLLEI IVPPLVVSLI VGLVISIFQA VTQIHEQTLM FAPRIIVLFL TILFLSGWMA QKILDFFSEM LQKYFQMI // ID Q9WZM7_THEMA Unreviewed; 471 AA. AC Q9WZM7; G4FD54; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 112. DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:AAD35851.1}; DE SubName: Full=Phosphomannomutase / Phosphoglucomutase {ECO:0000313|EMBL:AGL49695.1}; DE EC=5.4.2.2 {ECO:0000313|EMBL:AGL49695.1}; DE EC=5.4.2.8 {ECO:0000313|EMBL:AGL49695.1}; GN OrderedLocusNames=TM_0769 {ECO:0000313|EMBL:AAD35851.1}; GN ORFNames=Tmari_0770 {ECO:0000313|EMBL:AGL49695.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35851.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35851.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35851.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49695.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49695.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000256|RuleBase:RU004326, ECO:0000256|SAAS:SAAS00551227}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35851.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49695.1; -; Genomic_DNA. DR PIR; G72336; G72336. DR RefSeq; NP_228578.1; NC_000853.1. DR RefSeq; WP_004080925.1; NZ_CP011107.1. DR STRING; 243274.TM0769; -. DR EnsemblBacteria; AAD35851; AAD35851; TM_0769. DR EnsemblBacteria; AGL49695; AGL49695; Tmari_0770. DR GeneID; 898437; -. DR KEGG; tma:TM0769; -. DR KEGG; tmi:THEMA_00805; -. DR KEGG; tmm:Tmari_0770; -. DR KEGG; tmw:THMA_0788; -. DR PATRIC; 23936460; VBITheMar51294_0782. DR eggNOG; ENOG4105D6M; Bacteria. DR eggNOG; COG1109; LUCA. DR KO; K01840; -. DR OMA; SVLICEM; -. DR OrthoDB; EOG6103ZG; -. DR BioCyc; TMAR243274:GC6P-796-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC. DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.30.310.50; -; 1. DR Gene3D; 3.40.120.10; -; 3. DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I. DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III. DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II. DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III. DR InterPro; IPR005843; A-D-PHexomutase_C. DR InterPro; IPR016066; A-D-PHexomutase_CS. DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF. DR Pfam; PF02878; PGM_PMM_I; 1. DR Pfam; PF02879; PGM_PMM_II; 1. DR Pfam; PF02880; PGM_PMM_III; 1. DR Pfam; PF00408; PGM_PMM_IV; 1. DR PRINTS; PR00509; PGMPMM. DR SUPFAM; SSF53738; SSF53738; 3. DR SUPFAM; SSF55957; SSF55957; 1. DR PROSITE; PS00710; PGM_PMM; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000313|EMBL:AGL49695.1}; KW Magnesium {ECO:0000256|RuleBase:RU004326, KW ECO:0000256|SAAS:SAAS00436074}; KW Metal-binding {ECO:0000256|RuleBase:RU004326, KW ECO:0000256|SAAS:SAAS00436123}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 135 PGM_PMM_I. {ECO:0000259|Pfam:PF02878}. FT DOMAIN 154 249 PGM_PMM_II. {ECO:0000259|Pfam:PF02879}. FT DOMAIN 256 373 PGM_PMM_III. {ECO:0000259|Pfam:PF02880}. FT DOMAIN 380 459 PGM_PMM_IV. {ECO:0000259|Pfam:PF00408}. SQ SEQUENCE 471 AA; 52981 MW; D32526B31FF2DD43 CRC64; MILFGTGGIR GVMRKGEFDE ETVKRASLST ALWLKEKGQK SVVIAYDTRK NSKEFAELAG RVFAGEGIEA YVFPEPTPTP VLSFAVRYMK TGGGVVITAS HNPPEYNGYK VYTWDGVQAI PEYTNEITEI YKKVDLSHVK EGEIKFVPPE VKESYIKAVL EIVSNLPMKT DLDIAYSPLH GTGANYVPEV LKRLGFKVRL VEEQMKPDPN FSTVPTPNPE EDEALVLLNK KGATLGLATD PDCDRVGVVF KGRRLTGNQV GVLLTDFLLD HVKVENPLVI KTIVTTDMVR PICEEKGAFL EETPTGFKFI GHLIEEHTKK GDRNFVFGFE ESCGYLAGNH ARDKDGVVGS VLSAVAFSNY DPYEKLEELY QKYGYYMEKL INFKFEDVDR AVEIYRSLKN YDGIIDYSKG YGNVIPNETI AFVFEKSRIF VRPSGTEPKL KVYIHVRGDT REEAEELMKE SESKIKEILK L // ID Q9X0W5_THEMA Unreviewed; 648 AA. AC Q9X0W5; G4FEA9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=DNA helicase {ECO:0000256|SAAS:SAAS00553569}; DE EC=3.6.4.12 {ECO:0000256|SAAS:SAAS00553569}; GN OrderedLocusNames=TM_1238 {ECO:0000313|EMBL:AAD36313.1}; GN ORFNames=Tmari_1244 {ECO:0000313|EMBL:AGL50168.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36313.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36313.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36313.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50168.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50168.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|SAAS:SAAS00553768}. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000256|SAAS:SAAS00597767}. CC -!- SIMILARITY: Contains uvrD-like helicase ATP-binding domain. CC {ECO:0000256|SAAS:SAAS00553567}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36313.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50168.1; -; Genomic_DNA. DR PIR; G72279; G72279. DR RefSeq; NP_229043.1; NC_000853.1. DR RefSeq; WP_004080037.1; NZ_CP011107.1. DR STRING; 243274.TM1238; -. DR EnsemblBacteria; AAD36313; AAD36313; TM_1238. DR EnsemblBacteria; AGL50168; AGL50168; Tmari_1244. DR GeneID; 898246; -. DR KEGG; tma:TM1238; -. DR KEGG; tmi:THEMA_08145; -. DR KEGG; tmm:Tmari_1244; -. DR KEGG; tmw:THMA_1263; -. DR PATRIC; 23937416; VBITheMar51294_1255. DR eggNOG; ENOG4105C4R; Bacteria. DR eggNOG; COG0210; LUCA. DR KO; K03657; -. DR OMA; PAFTIHD; -. DR OrthoDB; EOG64N9TW; -. DR BioCyc; TMAR243274:GC6P-1268-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 4. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR000212; DNA_helicase_UvrD/REP. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR PANTHER; PTHR11070; PTHR11070; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1. DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS00493105, KW ECO:0000313|EMBL:AAD36313.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Helicase {ECO:0000256|SAAS:SAAS00493105, ECO:0000313|EMBL:AAD36313.1}; KW Hydrolase {ECO:0000256|SAAS:SAAS00493105, KW ECO:0000313|EMBL:AAD36313.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00493105, KW ECO:0000313|EMBL:AAD36313.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 17 303 UvrD-like helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51198}. FT DOMAIN 302 562 UvrD-like helicase C-terminal. FT {ECO:0000259|PROSITE:PS51217}. SQ SEQUENCE 648 AA; 75843 MW; 4274FFE319250280 CRC64; MKEYRIRPRE ANLSFLEDLD EEQRRAVVES EGRCIVIAGP GSGKTRVITY KIAYLLANGV DPSRILLVTF TRAAAREMVE RAKAVTGREL SEMLAGTFHH VCNHFLRKYA PYVGLERNYS ILDREDAESL MRHARSKYLE RKSKEERKNF PQPSVLMAIY SYMKNTLKSL RESIVVKNPK FLDLKEEISE IFDLYEQEKR SQNVVDYEDL LFYAYRLFEE NKEIRDREAE RFLWILVDEF QDTNYVQYKI VEHLSSKHGN ILAVGDDAQS IYSFRGARYE NVEDFIRVPG TKIFKIQTNY RSTESIVKFI NAMLPRKSVP KELKPVKKDG MKPVVVKTWD RYEEARFVSQ RILELIEEGF KPEEIAVLYR SHSHSLELQM ELVRSRIDFR VLSGPRFTES AHVKDVLSFL RIVQNPRDKS AWLRAAKLFY GIGDRTASKI ADLASAYVEE GLDPFQELKK VSFSGEYSRF IDILDQIRKL DSPGEMIERV LSSFYSEYLE ARYPDFRERE MDLERLVEIA SRYTSLESFL TDLAVTENVE IEREISQKEG KVTLTTVHQA KGLEWRVVFV ISVNPGDFPN YFAISEGNLD EEERIFYVAI TRAKEQLYIS YQVTGTSYPY RGNRFIMRSG ENFIDRIPLE LVEFWEVK // ID Q9X1Y3_THEMA Unreviewed; 422 AA. AC Q9X1Y3; G4FG39; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:AGL50583.1}; DE EC=3.2.1.1 {ECO:0000313|EMBL:AGL50583.1}; DE SubName: Full=Alpha-amylase, putative {ECO:0000313|EMBL:AAD36717.1}; GN OrderedLocusNames=TM_1650 {ECO:0000313|EMBL:AAD36717.1}; GN ORFNames=Tmari_1659 {ECO:0000313|EMBL:AGL50583.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36717.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36717.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36717.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50583.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50583.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36717.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50583.1; -; Genomic_DNA. DR PIR; G72227; G72227. DR RefSeq; NP_229450.1; NC_000853.1. DR RefSeq; WP_004082154.1; NZ_CP011107.1. DR STRING; 243274.TM1650; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblBacteria; AAD36717; AAD36717; TM_1650. DR EnsemblBacteria; AGL50583; AGL50583; Tmari_1659. DR GeneID; 897916; -. DR KEGG; tma:TM1650; -. DR KEGG; tmi:THEMA_05995; -. DR KEGG; tmm:Tmari_1659; -. DR KEGG; tmw:THMA_1691; -. DR PATRIC; 23938274; VBITheMar51294_1669. DR eggNOG; ENOG4105EP6; Bacteria. DR eggNOG; COG0366; LUCA. DR KO; K01176; -. DR OMA; IYSGQEY; -. DR OrthoDB; EOG6M0T1W; -. DR BioCyc; TMAR243274:GC6P-1696-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR015902; Glyco_hydro_13. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10357; PTHR10357; 1. DR Pfam; PF00128; Alpha-amylase; 2. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000313|EMBL:AGL50583.1}; KW Hydrolase {ECO:0000313|EMBL:AGL50583.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 422 AA; 50188 MW; D08C1ACA8695A9C4 CRC64; MNFKRLIIYE AFARAYPGEK GKKFDSLIKD LERLKGMGIN TVWLMPIHPT GIEGRKGTLG SPYAIRDYYE IDPLIGTKDD FKRFVKRAHE LNMYVLMDMV LNHAAADNVL VREHPEWFLR DEKGNPTRKV PDWTDIVDFD YSNGELRKYM INMMKYWVEE FDVDGFRCDV AGLVPLDFWL QARKELDPVK RLIWLSETHD PYMYQAFDIT YDYDGYYKFR DFIEGRGSLR EYVDFLRMQD HMYPRGYIKM RFLENHDQPR IAKFIEEDSL VHWIAFLFTF KGVPLVHNGQ EYGLKEDVDI FNEYTLPFPM EENRISILHR KLAHYRYGTS VFSEGEMLFV KNDQPEKVIS YLWRYENRYI LCMLNPLLEN TKVTLDFSGI WESACIHSKN VFNDEIVRVP VKNSRATVEI GKEPLILSFV LY // ID Q9S5X3_THEMA Unreviewed; 129 AA. AC Q9S5X3; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 11-MAY-2016, entry version 81. DE SubName: Full=Putative transposase {ECO:0000313|EMBL:AGL49703.1}; DE SubName: Full=Transposase {ECO:0000313|EMBL:AAD35859.1}; GN OrderedLocusNames=TM_0777 {ECO:0000313|EMBL:AAD35859.1}; GN ORFNames=Tmari_0778 {ECO:0000313|EMBL:AGL49703.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35859.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35859.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35859.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49703.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49703.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35859.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49703.1; -; Genomic_DNA. DR PIR; B72332; B72332. DR RefSeq; NP_228586.1; NC_000853.1. DR RefSeq; WP_010865201.1; NZ_CP011107.1. DR STRING; 243274.TM0777; -. DR EnsemblBacteria; AAD35859; AAD35859; TM_0777. DR EnsemblBacteria; AGL49703; AGL49703; Tmari_0778. DR GeneID; 898445; -. DR KEGG; tma:TM0777; -. DR KEGG; tmi:THEMA_00765; -. DR KEGG; tmm:Tmari_0778; -. DR KEGG; tmw:THMA_0796; -. DR PATRIC; 23936476; VBITheMar51294_0790. DR eggNOG; ENOG4108VIJ; Bacteria. DR eggNOG; COG1943; LUCA. DR KO; K07491; -. DR OMA; INVIKGA; -. DR OrthoDB; EOG6PP9P5; -. DR BioCyc; TMAR243274:GC6P-804-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR Gene3D; 3.30.70.1290; -; 1. DR InterPro; IPR002686; Transposase_17. DR Pfam; PF01797; Y1_Tnp; 1. DR SMART; SM01321; Y1_Tnp; 1. DR SUPFAM; SSF143422; SSF143422; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 129 AA; 15118 MW; 7E5AFB5783223FD0 CRC64; MHIKKTRWSH YNLNYHFVWI PKYRRKILVG SIAEELERIL RNTAKQHGIE ILALSIQPDH VHLFVSAPPR FSPAEIANLF KGVSARKLLE KFPELRTKEG LWARSYYVGT AGDVSEETIR RYIEECQDV // ID Q9WY31_THEMA Unreviewed; 143 AA. AC Q9WY31; G4FHA2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 85. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35280.1}; GN OrderedLocusNames=TM_0188 {ECO:0000313|EMBL:AAD35280.1}; GN ORFNames=Tmari_0186 {ECO:0000313|EMBL:AGL49112.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35280.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35280.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35280.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49112.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49112.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35280.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49112.1; -; Genomic_DNA. DR PIR; D72406; D72406. DR RefSeq; NP_228003.1; NC_000853.1. DR RefSeq; WP_004082829.1; NZ_CP011107.1. DR SMR; Q9WY31; 3-133. DR STRING; 243274.TM0188; -. DR DNASU; 897036; -. DR EnsemblBacteria; AAD35280; AAD35280; TM_0188. DR EnsemblBacteria; AGL49112; AGL49112; Tmari_0186. DR GeneID; 897036; -. DR KEGG; tma:TM0188; -. DR KEGG; tmi:THEMA_03825; -. DR KEGG; tmm:Tmari_0186; -. DR KEGG; tmw:THMA_0190; -. DR PATRIC; 23935236; VBITheMar51294_0190. DR eggNOG; ENOG4108R96; Bacteria. DR eggNOG; COG1720; LUCA. DR OMA; CRLEIFE; -. DR OrthoDB; EOG60SCKQ; -. DR BioCyc; TMAR243274:GC6P-195-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.40.30.70; -; 1. DR InterPro; IPR023370; TsaA-like. DR InterPro; IPR023368; UPF0066_cons_site. DR Pfam; PF01980; UPF0066; 1. DR SUPFAM; SSF118196; SSF118196; 1. DR TIGRFAMs; TIGR00104; tRNA_TsaA; 1. DR PROSITE; PS01318; TSAA_1; 1. DR PROSITE; PS51668; TSAA_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 134 TsaA-like. {ECO:0000259|PROSITE:PS51668}. SQ SEQUENCE 143 AA; 16461 MW; EEDBFE2AA6736819 CRC64; MFLLKQIGVI RSPFKSPSEC PFQGRFSQER FTIELFPEYE EGLKDIETCT HLIVLYWLDR ANRDRLIAIP PFDKREHGVF ATRSPHRPNP IGFSVVKLLE VRGRELVVEG LDAVDGTPVV DIKPYSSKID CVENARIGWF EEV // ID Q9X046_THEMA Unreviewed; 332 AA. AC Q9X046; G4FF41; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 98. DE SubName: Full=Ribose operon repressor {ECO:0000313|EMBL:AGL49876.1}; DE SubName: Full=Transcriptional regulator, LacI family {ECO:0000313|EMBL:AAD36030.1}; GN OrderedLocusNames=TM_0949 {ECO:0000313|EMBL:AAD36030.1}; GN ORFNames=Tmari_0951 {ECO:0000313|EMBL:AGL49876.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36030.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36030.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36030.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49876.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49876.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains HTH lacI-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00590899}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36030.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49876.1; -; Genomic_DNA. DR PIR; H72313; H72313. DR RefSeq; NP_228757.1; NC_000853.1. DR RefSeq; WP_004080613.1; NZ_CP011107.1. DR STRING; 243274.TM0949; -. DR EnsemblBacteria; AAD36030; AAD36030; TM_0949. DR EnsemblBacteria; AGL49876; AGL49876; Tmari_0951. DR GeneID; 898686; -. DR KEGG; tma:TM0949; -. DR KEGG; tmi:THEMA_09600; -. DR KEGG; tmm:Tmari_0951; -. DR KEGG; tmw:THMA_0972; -. DR PATRIC; 23936829; VBITheMar51294_0963. DR eggNOG; ENOG4105ETE; Bacteria. DR eggNOG; COG1609; LUCA. DR KO; K02529; -. DR OMA; LWAVIIS; -. DR OrthoDB; EOG6SJJMM; -. DR BioCyc; TMAR243274:GC6P-979-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR000843; Tscrpt_reg_HTH_LacI. DR Pfam; PF00356; LacI; 1. DR SMART; SM00354; HTH_LACI; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF53822; SSF53822; 1. DR PROSITE; PS00356; HTH_LACI_1; 1. DR PROSITE; PS50932; HTH_LACI_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00590989}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00590865}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00590865}. FT DOMAIN 5 59 HTH lacI-type DNA-binding. FT {ECO:0000259|PROSITE:PS50932}. SQ SEQUENCE 332 AA; 37566 MW; F137AB6E78F5D631 CRC64; MKRRPTINDV AKLAGVSIST VSRYLKDPSQ VSEKLGERIR EAIKKLGYKP NKIAQGLRTG DSKMIGFIVP DITNPAFLTI VKGAEDFLRK KGYSFIIGGT DHKSKDEVVI LESFIFHNVD GVIVTCTGYE NKALKELIER YHLKLVFVDR RYPGIDAPYI GVDNFGGVAR MVDYLVETGH RSFAYLCGDM TSTAKERLEG FLDRMKKYKI KDYQVLYGEF TFESGYKLTK RLSKIPDAII AGNDLMAFGV IEALKERGLV VPEDVSVTGF DDMFFSKYYK PSLTTVRQDL YEMGKQAGKV LFALISGKKI RKKEYILPTE IVIRDSVKER RA // ID Q9WY99_THEMA Unreviewed; 402 AA. AC Q9WY99; G4FHH5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 84. DE RecName: Full=Phosphate transporter {ECO:0000256|RuleBase:RU363058}; GN OrderedLocusNames=TM_0261 {ECO:0000313|EMBL:AAD35349.1}; GN ORFNames=Tmari_0259 {ECO:0000313|EMBL:AGL49185.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35349.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35349.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35349.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49185.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49185.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU363058}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363058}. CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) CC (TC 2.A.20) family. {ECO:0000256|RuleBase:RU363058}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35349.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49185.1; -; Genomic_DNA. DR PIR; D72400; D72400. DR RefSeq; NP_228074.1; NC_000853.1. DR RefSeq; WP_004082965.1; NZ_CP011107.1. DR STRING; 243274.TM0261; -. DR EnsemblBacteria; AAD35349; AAD35349; TM_0261. DR EnsemblBacteria; AGL49185; AGL49185; Tmari_0259. DR GeneID; 897171; -. DR KEGG; tma:TM0261; -. DR KEGG; tmi:THEMA_03420; -. DR KEGG; tmm:Tmari_0259; -. DR KEGG; tmw:THMA_0268; -. DR PATRIC; 23935399; VBITheMar51294_0265. DR eggNOG; ENOG4105CJ3; Bacteria. DR eggNOG; COG0306; LUCA. DR KO; K03306; -. DR OMA; FFTIKGI; -. DR OrthoDB; EOG6NWBS7; -. DR BioCyc; TMAR243274:GC6P-274-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central. DR InterPro; IPR001204; Phos_transporter. DR PANTHER; PTHR11101; PTHR11101; 1. DR Pfam; PF01384; PHO4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363058}; KW Phosphate transport {ECO:0000256|RuleBase:RU363058}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363058}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363058}; KW Transport {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 42 60 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 81 102 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 108 125 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 132 153 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 173 191 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 203 221 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 284 303 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 375 396 Helical. {ECO:0000256|RuleBase:RU363058}. SQ SEQUENCE 402 AA; 42694 MW; 0B2AB69767CED5F3 CRC64; MTILIIAGIL GFIMAFSIGA NDVANSMATA VGARAITVRQ AALIAMFLEF LGAVMFGSHV SQTIVKGIVE VEKVQPVELM YGALSALIAA SFWILIATNW GYPVSTTHSI VGGMMGFGLV AVGINGVNWK TFLFIVLSWV VSPVLGGLIS FVMFKLISLS VFHTKNPKKS STVAIPFFIS LAIFTMISLF VKKTLKQPLS ESFLLGIAFS LVTFFVVHFA VRKLINEKKD VYDAVENVFK RAQILTSCYV SFSHGANDVA NAAGPVAAVM IVASTGVVPK TVEIPFLALL LGGIGISLGV FFLGQKVMET VGEKITTLTN SRGFTVDFST ATTVLLASSL GLPISTTHVV VGAVTGVGFA RGLEMVNVGV LKNIVISWLL IVPTVAATSA AVYWVLKLIL KF // ID Q9X1E0_THEMA Unreviewed; 379 AA. AC Q9X1E0; G4FFF8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 87. DE SubName: Full=Sporulation stage II, protein E {ECO:0000313|EMBL:AGL50353.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36493.1}; GN OrderedLocusNames=TM_1423 {ECO:0000313|EMBL:AAD36493.1}; GN ORFNames=Tmari_1429 {ECO:0000313|EMBL:AGL50353.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36493.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36493.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36493.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50353.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50353.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36493.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50353.1; -; Genomic_DNA. DR PIR; D72256; D72256. DR RefSeq; NP_229223.1; NC_000853.1. DR RefSeq; WP_004081668.1; NZ_CP011107.1. DR STRING; 243274.TM1423; -. DR EnsemblBacteria; AAD36493; AAD36493; TM_1423. DR EnsemblBacteria; AGL50353; AGL50353; Tmari_1429. DR GeneID; 898052; -. DR KEGG; tma:TM1423; -. DR KEGG; tmi:THEMA_07200; -. DR KEGG; tmm:Tmari_1429; -. DR KEGG; tmw:THMA_1453; -. DR PATRIC; 23937794; VBITheMar51294_1435. DR eggNOG; ENOG4105CY7; Bacteria. DR eggNOG; ENOG410XPBR; LUCA. DR OMA; KIVCGGT; -. DR OrthoDB; EOG64FKCZ; -. DR BioCyc; TMAR243274:GC6P-1461-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR InterPro; IPR001932; PPM-type_phosphatase_dom. DR Pfam; PF07228; SpoIIE; 1. DR SUPFAM; SSF81606; SSF81606; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 30 219 PPM-type phosphatase. FT {ECO:0000259|Pfam:PF07228}. SQ SEQUENCE 379 AA; 42367 MW; 9B6B39141CEC24B0 CRC64; MLTCDVFFAS KNKKGEEVCG DSIKVKRESE KIVVSVSDGL GSGIKASILS TLTATIASTM LMNGLPVTDV FRTILATLPI CRVRKISYSN LCSVVCDFKN NTCTVVEYEF PVVMLFKGER RVFPEKQGLE IEGKKVFVWQ FRSEAGTLLL LATDGLSQAG MGTDLFPLGF GVENIEKEMK HLLKNHVSPE NIVRHFVKLA EKLDQEVRGD DTLVACLNFR EKRILNLFVG PPEDRKKDEE YVRTFLSLPG KKIVCGGTTG QIFERVTGKK VEIDLYTLSE NSPPVGYMEG IDLMTEGIVT LTQVFRYLEG QSEELGYGAK FIVKSLLEAD EINFFVGRAI NPAHQNPLFS HDISLKFRLV KDIAQILREK GKIVNVQYC // ID Q9X0N6_THEMA Unreviewed; 323 AA. AC Q9X0N6; G4FEJ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 123. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36228.1}; DE SubName: Full=Oligopeptide transport ATP-binding protein OppD {ECO:0000313|EMBL:AGL50083.1}; GN OrderedLocusNames=TM_1152 {ECO:0000313|EMBL:AAD36228.1}; GN ORFNames=Tmari_1159 {ECO:0000313|EMBL:AGL50083.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36228.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36228.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36228.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50083.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50083.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36228.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50083.1; -; Genomic_DNA. DR PIR; D72289; D72289. DR RefSeq; NP_228958.1; NC_000853.1. DR RefSeq; WP_004080229.1; NZ_CP011107.1. DR STRING; 243274.TM1152; -. DR DNASU; 898334; -. DR EnsemblBacteria; AAD36228; AAD36228; TM_1152. DR EnsemblBacteria; AGL50083; AGL50083; Tmari_1159. DR GeneID; 898334; -. DR KEGG; tma:TM1152; -. DR KEGG; tmi:THEMA_08580; -. DR KEGG; tmm:Tmari_1159; -. DR KEGG; tmw:THMA_1176; -. DR PATRIC; 23937241; VBITheMar51294_1169. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR KO; K02031; -. DR OMA; EDHFVEM; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1181-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36228.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36228.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 4 252 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 323 AA; 36032 MW; 9C77249A226546AC CRC64; MKVLELKNVS VRYKTGEKTV NAVENVSFHL EKGETLGLVG ESGCGKSTLG FSIMRLLPKG TKIDGSIKIE GIDISSLSDE EMRQIRGSKV AMIFQDPMTS LNPILRIEDH FVEMILTHRP ELSKEDAREL AAKALEDVGI NRNRLKDYPF QFSGGMRQRV MIALSIVLNP AVLIADEPTT SLDVIVQAQI MELLEKLTKE HRTAMILITH DMGLVAEAAD RIGVMYAGHL VELASKERIF TNPLHPYTVG LLRSIPNTDV NDKELRYIPG SPPDLSNPPE GCRFAPRCEK AMKICWEKEP PEFEIDGTRV KCWLYGGDQN GTD // ID Q9WYD5_THEMA Unreviewed; 344 AA. AC Q9WYD5; G4FHL3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 96. DE SubName: Full=Putative xyloglucan oligosaccharides-responsive regulator, LacI family {ECO:0000313|EMBL:AGL49223.1}; DE SubName: Full=Transcriptional regulator, LacI family {ECO:0000313|EMBL:AAD35387.1}; GN OrderedLocusNames=TM_0299 {ECO:0000313|EMBL:AAD35387.1}; GN ORFNames=Tmari_0297 {ECO:0000313|EMBL:AGL49223.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35387.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35387.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35387.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49223.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49223.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains HTH lacI-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00590899}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35387.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49223.1; -; Genomic_DNA. DR PIR; C72395; C72395. DR RefSeq; NP_228111.1; NC_000853.1. DR RefSeq; WP_004083018.1; NC_023151.1. DR STRING; 243274.TM0299; -. DR DNASU; 897224; -. DR EnsemblBacteria; AAD35387; AAD35387; TM_0299. DR EnsemblBacteria; AGL49223; AGL49223; Tmari_0297. DR GeneID; 897224; -. DR KEGG; tma:TM0299; -. DR KEGG; tmi:THEMA_03230; -. DR KEGG; tmm:Tmari_0297; -. DR PATRIC; 23935477; VBITheMar51294_0304. DR eggNOG; ENOG4105ETE; Bacteria. DR eggNOG; COG1609; LUCA. DR KO; K02529; -. DR OMA; HERVERY; -. DR OrthoDB; EOG6SJJMM; -. DR BioCyc; TMAR243274:GC6P-312-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR000843; Tscrpt_reg_HTH_LacI. DR Pfam; PF00356; LacI; 1. DR SMART; SM00354; HTH_LACI; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF53822; SSF53822; 1. DR PROSITE; PS50932; HTH_LACI_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00590989}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00590865}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00590865}. FT DOMAIN 4 58 HTH lacI-type DNA-binding. FT {ECO:0000259|PROSITE:PS50932}. SQ SEQUENCE 344 AA; 38875 MW; DE511C1AE330880A CRC64; MKKATLKDIA EYFGVSISTV SRALSGKPGV SSELREKILE KAREIGYTPN LMALGLKKGN TRTVGVLIPE LSANFFADIV SSIEKSLFHL GYRLILCSTD DDPVKEREHL QLLLDQKVEG ILSAPVNVKE NKDIYNSIIN HFKIPVVFFD RLVEGVDSDF VISDNREGME ILVNYLVKHG HKKIGLIHPL RGSFTGEERL KGFLLFKDSI EIREEWIRDG RSSEQGGYES FLRIMTSQER PTAIVIGNNL MTLGVLKAAK ELNIKIPEDI SLVSFDDAYW NEIFDPPITC VRQDPQQIGL IAATILLDRM KNRKKPSPRM QVVLKVKFVE RSSVRTIKTL KDFS // ID Q9X0X8_THEMA Unreviewed; 311 AA. AC Q9X0X8; G4FE97; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 116. DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|RuleBase:RU004370, ECO:0000256|SAAS:SAAS00245445}; DE EC=6.3.3.1 {ECO:0000256|RuleBase:RU004370, ECO:0000256|SAAS:SAAS00245411}; GN OrderedLocusNames=TM_1251 {ECO:0000313|EMBL:AAD36326.1}; GN ORFNames=Tmari_1256 {ECO:0000313|EMBL:AGL50180.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36326.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36326.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36326.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50180.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50180.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: ATP + 2-(formamido)-N(1)-(5-phospho-D- CC ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole. {ECO:0000256|RuleBase:RU004370, CC ECO:0000256|SAAS:SAAS00088371}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 2/2. CC {ECO:0000256|SAAS:SAAS00088385}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00245373}. CC -!- SIMILARITY: Belongs to the AIR synthase family. CC {ECO:0000256|RuleBase:RU004370, ECO:0000256|SAAS:SAAS00571239}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36326.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50180.1; -; Genomic_DNA. DR PIR; E72277; E72277. DR RefSeq; NP_229056.1; NC_000853.1. DR RefSeq; WP_004080012.1; NZ_CP011107.1. DR STRING; 243274.TM1251; -. DR EnsemblBacteria; AAD36326; AAD36326; TM_1251. DR EnsemblBacteria; AGL50180; AGL50180; Tmari_1256. DR GeneID; 898232; -. DR KEGG; tma:TM1251; -. DR KEGG; tmi:THEMA_08080; -. DR KEGG; tmm:Tmari_1256; -. DR KEGG; tmw:THMA_1276; -. DR PATRIC; 23937442; VBITheMar51294_1267. DR eggNOG; ENOG4105CXB; Bacteria. DR eggNOG; COG0150; LUCA. DR KO; K01933; -. DR OMA; EVAGWDC; -. DR OrthoDB; EOG61CM1V; -. DR BioCyc; TMAR243274:GC6P-1282-MONOMER; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR004733; PurM_cligase. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR00878; purM; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS00461058}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00461019}; KW Ligase {ECO:0000256|RuleBase:RU004370, ECO:0000256|SAAS:SAAS00461036, KW ECO:0000313|EMBL:AAD36326.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00461058}; KW Purine biosynthesis {ECO:0000256|SAAS:SAAS00461072}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 50 151 AIRS. {ECO:0000259|Pfam:PF00586}. FT DOMAIN 162 303 AIRS_C. {ECO:0000259|Pfam:PF02769}. SQ SEQUENCE 311 AA; 34481 MW; B1DB93938B13B40F CRC64; MKYTYREAGV DVERGESFAK TIKSAVKLPE WVMKEPTGYA SILTITTPPV VVTADGIGTK LILHRKHGTW RYAAEDLVGM NYNDLVCVGA RPVAFLDYLG VERISEEHES FIKELVNVLD SVDVKLVGGE TAEMPDVYRG DWDAVGFAVG VLEKRIPVDK IKEGDVIVGI PSSGFHSNGW SLIRRIIKEE SIKIEELPFE LLKGTRIYRE VIELFDLVKG IAHVTGGGVV RALKRVLGKL GAHVSLPKRD FVDWILKYVD FNEAVNTFNM GVGMFLIVEK QKVDEVLARV DGTVVGKVSS DWRIEYGGEG G // ID Q9WZL7_THEMA Unreviewed; 387 AA. AC Q9WZL7; G4FD65; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=Flagellin {ECO:0000256|RuleBase:RU362073}; GN OrderedLocusNames=TM_0758 {ECO:0000313|EMBL:AAD35840.1}; GN ORFNames=Tmari_0759 {ECO:0000313|EMBL:AGL49684.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35840.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35840.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35840.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49684.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49684.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Flagellin is the subunit protein which polymerizes to CC form the filaments of bacterial flagella. CC {ECO:0000256|RuleBase:RU362073, ECO:0000256|SAAS:SAAS00588713}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362073}. CC Bacterial flagellum {ECO:0000256|RuleBase:RU362073}. CC -!- SIMILARITY: Belongs to the bacterial flagellin family. CC {ECO:0000256|RuleBase:RU362073, ECO:0000256|SAAS:SAAS00588699}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35840.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49684.1; -; Genomic_DNA. DR PIR; D72335; D72335. DR RefSeq; NP_228567.1; NC_000853.1. DR RefSeq; WP_004080946.1; NZ_CP011107.1. DR SMR; Q9WZL7; 348-386. DR STRING; 243274.TM0758; -. DR EnsemblBacteria; AAD35840; AAD35840; TM_0758. DR EnsemblBacteria; AGL49684; AGL49684; Tmari_0759. DR GeneID; 898426; -. DR KEGG; tma:TM0758; -. DR KEGG; tmi:THEMA_00860; -. DR KEGG; tmm:Tmari_0759; -. DR KEGG; tmw:THMA_0777; -. DR PATRIC; 23936438; VBITheMar51294_0771. DR eggNOG; ENOG4105I03; Bacteria. DR eggNOG; COG1344; LUCA. DR KO; K02406; -. DR OMA; GGITFKW; -. DR OrthoDB; EOG6M9DVB; -. DR BioCyc; TMAR243274:GC6P-785-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009420; C:bacterial-type flagellum filament; IEA:InterPro. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR Gene3D; 1.20.1330.10; -; 2. DR InterPro; IPR001492; Flagellin. DR InterPro; IPR001029; Flagellin_D0/D1. DR Pfam; PF00700; Flagellin_C; 1. DR Pfam; PF00669; Flagellin_N; 1. DR PRINTS; PR00207; FLAGELLIN. PE 3: Inferred from homology; KW Bacterial flagellum {ECO:0000256|RuleBase:RU362073, KW ECO:0000256|SAAS:SAAS00482835}; KW Cell projection {ECO:0000313|EMBL:AAD35840.1}; KW Cilium {ECO:0000313|EMBL:AAD35840.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35840.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Secreted {ECO:0000256|RuleBase:RU362073}. FT DOMAIN 3 139 Flagellin_D0/D1. FT {ECO:0000259|Pfam:PF00669}. FT DOMAIN 303 386 Flagellin_D0/D1. FT {ECO:0000259|Pfam:PF00700}. SQ SEQUENCE 387 AA; 41688 MW; 34828810C8E6EB7A CRC64; MRINHNISAL NAWRNISQTQ YSMSKTLERL SSGLRINRAG DDAAGLAISE KMRGQIKGLN MAIKNAQDAI SLIQTAEGAL TEVHSILQRM RELAVQAASD TNTDVDREQI QKEIDQLREE IDRIARTTEF NTKKLLDGKL ESFRSQVDAK VVTGGNINVQ LGSVSSAAVE GTYVIEVGQF NGAETSELDV KITLFTAGGY STTVVTITVG SATVGNINFT WDTDVLSIND FGGALPKNEV VDSAVVRVEA IYTSASQLIF QIGANEGHNM VAGIDDMSAA ALGLTTVSLD VTTQDAAERA IMVVDAAIHR VSTARAALGA VQNRLEHTIS NLGVAAENLT AAESRIRDAD MAKEMMEFTK QQILLQSSMA MLAQSNTLPQ NVLQLMR // ID Q9X241_THEMA Unreviewed; 204 AA. AC Q9X241; G4FGA3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=PASTA domain-containing protein {ECO:0000313|EMBL:AGL50648.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36782.1}; GN OrderedLocusNames=TM_1716 {ECO:0000313|EMBL:AAD36782.1}; GN ORFNames=Tmari_1724 {ECO:0000313|EMBL:AGL50648.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36782.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36782.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36782.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50648.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50648.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36782.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50648.1; -; Genomic_DNA. DR PIR; H72218; H72218. DR RefSeq; NP_229515.1; NC_000853.1. DR RefSeq; WP_004082232.1; NZ_CP011107.1. DR STRING; 243274.TM1716; -. DR EnsemblBacteria; AAD36782; AAD36782; TM_1716. DR EnsemblBacteria; AGL50648; AGL50648; Tmari_1724. DR GeneID; 897312; -. DR KEGG; tma:TM1716; -. DR KEGG; tmi:THEMA_05660; -. DR KEGG; tmm:Tmari_1724; -. DR KEGG; tmw:THMA_1758; -. DR PATRIC; 23938408; VBITheMar51294_1734. DR eggNOG; ENOG41087C3; Bacteria. DR eggNOG; COG2815; LUCA. DR OMA; QKKIVPR; -. DR OrthoDB; EOG6B8XHP; -. DR BioCyc; TMAR243274:GC6P-1764-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005543; PASTA_dom. DR Pfam; PF03793; PASTA; 1. DR SMART; SM00740; PASTA; 3. DR PROSITE; PS51178; PASTA; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 26 85 PASTA. {ECO:0000259|PROSITE:PS51178}. FT DOMAIN 88 148 PASTA. {ECO:0000259|PROSITE:PS51178}. FT DOMAIN 151 203 PASTA. {ECO:0000259|PROSITE:PS51178}. SQ SEQUENCE 204 AA; 22882 MW; 63D2121A278D483D CRC64; MRVFLGIIIG IVVGGLFFLF TMKFYQSQYS TVPDVVGLSG TEACERLKTS GLFCDKSSSE TVVDTYPRAG SRVKKGRTVN LYYENPQKKI VPRLSQLNFP VAEEILKRLG WNYETVYFPF GTEKDRVLAT YPKEGQIYNG KLILLIDTGE KESYFLVENF VGKKVDELKD DPRVLLLGTG DTVVAQYPPE GSIATKVILI LGEE // ID Q9WXV7_THEMA Unreviewed; 359 AA. AC Q9WXV7; G4FH17; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Basic membrane protein {ECO:0000313|EMBL:AAD35196.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL49025.1}; GN OrderedLocusNames=TM_0102 {ECO:0000313|EMBL:AAD35196.1}; GN ORFNames=Tmari_0099 {ECO:0000313|EMBL:AGL49025.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35196.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35196.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35196.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49025.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49025.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35196.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49025.1; -; Genomic_DNA. DR PIR; F72418; F72418. DR RefSeq; NP_227918.1; NC_000853.1. DR RefSeq; WP_004082657.1; NZ_CP011107.1. DR STRING; 243274.TM0102; -. DR EnsemblBacteria; AAD35196; AAD35196; TM_0102. DR EnsemblBacteria; AGL49025; AGL49025; Tmari_0099. DR GeneID; 896929; -. DR KEGG; tma:TM0102; -. DR KEGG; tmi:THEMA_04295; -. DR KEGG; tmm:Tmari_0099; -. DR KEGG; tmw:THMA_0098; -. DR PATRIC; 23935044; VBITheMar51294_0100. DR eggNOG; ENOG4105DIH; Bacteria. DR eggNOG; COG1744; LUCA. DR KO; K07335; -. DR OMA; GYNTAMQ; -. DR OrthoDB; EOG6Z9B3D; -. DR BioCyc; TMAR243274:GC6P-102-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:InterPro. DR InterPro; IPR003760; Bmp. DR InterPro; IPR028082; Peripla_BP_I. DR Pfam; PF02608; Bmp; 1. DR SUPFAM; SSF53822; SSF53822; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 20 340 Bmp. {ECO:0000259|Pfam:PF02608}. SQ SEQUENCE 359 AA; 39335 MW; EAF2A32262CFC274 CRC64; MRKFLVISLM IFAVALFGFK VIMVTDVGGL GDKSFNDGTW AGIKQAAEEL GIEAKVIQSY EQSDYIPNLS KAAEEADLVF AVGFMMTNDL FKVAKQYPDT YFVGIDITPP EGQILPNVLT FTFKEQEAAF LVGYVAAAMT KTGMVGFVGG IPIPPVERFR YGYEAGIKTY SVLHKKNVKI LRGYTQDFED PKKGKDLAMS QFAEGADIVF HASGACGNGV IEAAREKFSA LAGSDKLVDL IDYYTTNGKG FFAIGVDMDQ DYMAPGAVLT SAMKRVDVAS YYGVVWAYEG TFEGGHRVLG ISEDAVGISP MKYTKGLVPN RVIAELLYLE KLMKEGTLKV PETQEELDAF EVPQIEFPF // ID Q9WY11_THEMA Unreviewed; 264 AA. AC Q9WY11; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35257.1}; GN OrderedLocusNames=TM_0164 {ECO:0000313|EMBL:AAD35257.1}; GN ORFNames=Tmari_0162 {ECO:0000313|EMBL:AGL49088.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35257.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35257.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35257.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49088.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49088.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35257.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49088.1; -; Genomic_DNA. DR PIR; B72411; B72411. DR RefSeq; NP_227979.1; NC_000853.1. DR RefSeq; WP_010865064.1; NZ_CP011107.1. DR STRING; 243274.TM0164; -. DR DNASU; 897003; -. DR EnsemblBacteria; AAD35257; AAD35257; TM_0164. DR EnsemblBacteria; AGL49088; AGL49088; Tmari_0162. DR GeneID; 897003; -. DR KEGG; tma:TM0164; -. DR KEGG; tmi:THEMA_03980; -. DR KEGG; tmm:Tmari_0162; -. DR KEGG; tmw:THMA_0160; -. DR PATRIC; 23935176; VBITheMar51294_0165. DR eggNOG; ENOG4105D4H; Bacteria. DR eggNOG; COG2035; LUCA. DR KO; K08974; -. DR OMA; LIWSFFF; -. DR OrthoDB; EOG6V7BKJ; -. DR BioCyc; TMAR243274:GC6P-165-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007163; DUF368. DR Pfam; PF04018; DUF368; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 79 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 122 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 162 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 168 193 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 205 222 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 234 254 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 264 AA; 29043 MW; 23BB506AAC6F6C80 CRC64; MKVWFFFSGV LMGIANVVPG VSGGTIAVLM GVYEKLIESV NSFFHGNSRS LKVLIPVGAG VLVGVFGIAR FLEIFLSKYP VPTHFFFLGL IIVSFVKTKE YFSIKPVNIF FVLLGMFLIF MLHFSGETTA KESMFLLVLG GFVAATAMVV PGISGSLILL IFGVYDHVLY LVSHLIIGEL LIFSIGVVAG ILVSVKIMNF LLKRFREETY SFIGGMILAS LYEVLPKKMN TNVVLPSVLS LVLSLTLGFF LLYIEKKLSV TQKL // ID Q9X064_THEMA Unreviewed; 94 AA. AC Q9X064; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Archaeal ATPase, fused to C-terminal DUF234 domain protein {ECO:0000313|EMBL:AGL49896.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36048.1}; GN OrderedLocusNames=TM_0969 {ECO:0000313|EMBL:AAD36048.1}; GN ORFNames=Tmari_0971 {ECO:0000313|EMBL:AGL49896.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36048.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36048.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36048.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49896.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49896.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36048.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49896.1; -; Genomic_DNA. DR PIR; F72312; F72312. DR RefSeq; NP_228777.1; NC_000853.1. DR RefSeq; WP_010865227.1; NZ_CP011107.1. DR STRING; 243274.TM0969; -. DR EnsemblBacteria; AAD36048; AAD36048; TM_0969. DR EnsemblBacteria; AGL49896; AGL49896; Tmari_0971. DR GeneID; 898708; -. DR KEGG; tma:TM0969; -. DR KEGG; tmm:Tmari_0971; -. DR KEGG; tmw:THMA_0992; -. DR PATRIC; 23936869; VBITheMar51294_0983. DR eggNOG; ENOG4105EM3; Bacteria. DR eggNOG; ENOG410XSDB; LUCA. DR OrthoDB; EOG6P06XW; -. DR BioCyc; TMAR243274:GC6P-999-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.1350.10; -; 1. DR InterPro; IPR004256; DUF234_ATPase_C. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR Pfam; PF03008; DUF234; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 38 DUF234. {ECO:0000259|Pfam:PF03008}. SQ SEQUENCE 94 AA; 10877 MW; 98F35F6E915FA730 CRC64; MYVCKHCGSA MNKDVEIDIV GIKGNTLYVG ECKWSNKKID VRVLDRLRSK VPYLLKDLQV DNLSVVYYLF SRSGFDGLKE TEEVKLVELK DLFR // ID Q9X0S8_THEMA Unreviewed; 606 AA. AC Q9X0S8; G4FEE5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE RecName: Full=Arabinogalactan endo-beta-1,4-galactanase {ECO:0000256|RuleBase:RU361192}; DE EC=3.2.1.89 {ECO:0000256|RuleBase:RU361192}; GN OrderedLocusNames=TM_1201 {ECO:0000313|EMBL:AAD36276.1}; GN ORFNames=Tmari_1208 {ECO:0000313|EMBL:AGL50132.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36276.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36276.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36276.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50132.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50132.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: The enzyme specifically hydrolyzes (1->4)- CC beta-D-galactosidic linkages in type I arabinogalactans. CC {ECO:0000256|RuleBase:RU361192}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 53 family. CC {ECO:0000256|RuleBase:RU361192}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36276.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50132.1; -; Genomic_DNA. DR PIR; G72282; G72282. DR RefSeq; NP_229006.1; NC_000853.1. DR RefSeq; WP_004080113.1; NZ_CP011107.1. DR PDB; 2XOM; X-ray; 0.95 A; A=461-606. DR PDB; 2XON; X-ray; 1.40 A; A/L=461-606. DR PDBsum; 2XOM; -. DR PDBsum; 2XON; -. DR STRING; 243274.TM1201; -. DR CAZy; GH53; Glycoside Hydrolase Family 53. DR EnsemblBacteria; AAD36276; AAD36276; TM_1201. DR EnsemblBacteria; AGL50132; AGL50132; Tmari_1208. DR GeneID; 898283; -. DR KEGG; tma:TM1201; -. DR KEGG; tmi:THEMA_08325; -. DR KEGG; tmm:Tmari_1208; -. DR KEGG; tmw:THMA_1227; -. DR PATRIC; 23937344; VBITheMar51294_1219. DR eggNOG; ENOG4106FKC; Bacteria. DR eggNOG; COG3867; LUCA. DR KO; K01224; -. DR OMA; TGWLEWK; -. DR OrthoDB; EOG6H4K5M; -. DR BioCyc; TMAR243274:GC6P-1231-MONOMER; -. DR BRENDA; 3.2.1.89; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031218; F:arabinogalactan endo-1,4-beta-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0015926; F:glucosidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR011081; Big_4. DR InterPro; IPR011683; Glyco_hydro_53. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF07532; Big_4; 1. DR Pfam; PF07745; Glyco_hydro_53; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2XOM, ECO:0000213|PDB:2XON}; KW Calcium {ECO:0000213|PDB:2XOM, ECO:0000213|PDB:2XON}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361192}; KW Hydrolase {ECO:0000256|RuleBase:RU361192}; KW Metal-binding {ECO:0000213|PDB:2XOM, ECO:0000213|PDB:2XON}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 30 375 Glyco_hydro_53. FT {ECO:0000259|Pfam:PF07745}. FT DOMAIN 393 446 Big_4. {ECO:0000259|Pfam:PF07532}. FT REGION 506 508 Galactose binding. {ECO:0000213|PDB:2XOM, FT ECO:0000213|PDB:2XON}. FT METAL 469 469 Calcium; via carbonyl oxygen. FT {ECO:0000213|PDB:2XOM, FT ECO:0000213|PDB:2XON}. FT METAL 471 471 Calcium. {ECO:0000213|PDB:2XOM, FT ECO:0000213|PDB:2XON}. FT METAL 500 500 Calcium. {ECO:0000213|PDB:2XOM, FT ECO:0000213|PDB:2XON}. FT METAL 503 503 Calcium; via carbonyl oxygen. FT {ECO:0000213|PDB:2XOM, FT ECO:0000213|PDB:2XON}. FT METAL 598 598 Calcium. {ECO:0000213|PDB:2XOM, FT ECO:0000213|PDB:2XON}. FT BINDING 497 497 Galactose. {ECO:0000213|PDB:2XOM, FT ECO:0000213|PDB:2XON}. FT BINDING 563 563 Galactose. {ECO:0000213|PDB:2XON}. FT BINDING 594 594 Galactose. {ECO:0000213|PDB:2XOM, FT ECO:0000213|PDB:2XON}. SQ SEQUENCE 606 AA; 68620 MW; 0A4C121D93ABCB00 CRC64; MRGVLFVLMI SSMAFGLIVN PVENLREDFI FGMDVSMLYE IEQLGGKYFE NGVEKDCLEI LKNHGINWIR LRVWNDPRDE NGNPLGGGNC DYLKMTEIAK RAKNLGMKVL LDFHYSDWWA DPGKQNKPKE WEYLHGELLE RAVYSYTKLV LNHMRRNGAL PDMVQVGNEV NNGFLWPDGK ISGEGAGGFD GFTRLLKAAI KAVREVDPDI KIVIHLAEGG NNSLFRWFFD EITRRNVDFD VIGVSYYPYW HGTLEDLKNN LYDIATRYNK DVLVVETAYA WTLEDGDGYP NIFNGEEMEL TGGYKATVQG QATFLRDLIE VVNSVPNGHG LGIFYWEGDW IPVRGAGWKT GEGNPWDNQA MFDFSGNALP SLNVFKLVKT SSPVEIAIKE ILPVEVTTNL GEVPKFPDAV KVLFSDDSIR SLPVEWNFDS ALVEESGVYK VEGYIKDIDR KIFATLTVKG SRNYLKNPGF ETGEFSPWRV SGDKKAVKVV KANPSSNAHQ GEYAVNFWLD ESFSFELSQE VELPAGVYRV GFWTHGEKGV KIALKVSDYG GNERSVEVET TGWLEWKNPE IRNIKVETGR IKITVSVEGR AGDWGFIDDF YLFREE // ID Q9X075_THEMA Unreviewed; 117 AA. AC Q9X075; G4FF15; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36059.1}; GN OrderedLocusNames=TM_0980 {ECO:0000313|EMBL:AAD36059.1}; GN ORFNames=Tmari_0983 {ECO:0000313|EMBL:AGL49908.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36059.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36059.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36059.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49908.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49908.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36059.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49908.1; -; Genomic_DNA. DR PIR; A72310; A72310. DR RefSeq; NP_228788.1; NC_000853.1. DR RefSeq; WP_004080584.1; NZ_CP011107.1. DR STRING; 243274.TM0980; -. DR EnsemblBacteria; AAD36059; AAD36059; TM_0980. DR EnsemblBacteria; AGL49908; AGL49908; Tmari_0983. DR GeneID; 898726; -. DR KEGG; tma:TM0980; -. DR KEGG; tmi:THEMA_09450; -. DR KEGG; tmm:Tmari_0983; -. DR KEGG; tmw:THMA_1002; -. DR PATRIC; 23936889; VBITheMar51294_0993. DR eggNOG; ENOG4105GSP; Bacteria. DR eggNOG; COG2923; LUCA. DR KO; K07236; -. DR OMA; SIWVNEA; -. DR OrthoDB; EOG6QCDC5; -. DR BioCyc; TMAR243274:GC6P-1010-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.1260.10; -; 1. DR InterPro; IPR027396; DsrEFH-like. DR SUPFAM; SSF75169; SSF75169; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 117 AA; 13466 MW; 83F5CE72A86BB9FF CRC64; MKKLLFVAYQ SPVGSVWVNE AFRTAFGMYG EDLEPNVLLI EEASVALSKN TKPEMLGLLP LSICHKYIKR YGTKVYAVKQ HLEKYRVKEL DENFGAEVID EANLPEFLHS FDYVIFM // ID Q9X1P6_THEMA Unreviewed; 202 AA. AC Q9X1P6; G4FFU8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Formiminotetrahydrofolate cyclodeaminase {ECO:0000313|EMBL:AGL50492.1}; DE EC=4.3.1.4 {ECO:0000313|EMBL:AGL50492.1}; DE SubName: Full=Serine cycle enzyme, putative {ECO:0000313|EMBL:AAD36626.1}; GN OrderedLocusNames=TM_1560 {ECO:0000313|EMBL:AAD36626.1}; GN ORFNames=Tmari_1568 {ECO:0000313|EMBL:AGL50492.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36626.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36626.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36626.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50492.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50492.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36626.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50492.1; -; Genomic_DNA. DR PIR; C72240; C72240. DR RefSeq; NP_229360.1; NC_000853.1. DR RefSeq; WP_004081967.1; NZ_CP011107.1. DR PDB; 1O5H; X-ray; 2.80 A; A/B=1-202. DR PDBsum; 1O5H; -. DR STRING; 243274.TM1560; -. DR EnsemblBacteria; AAD36626; AAD36626; TM_1560. DR EnsemblBacteria; AGL50492; AGL50492; Tmari_1568. DR GeneID; 897966; -. DR KEGG; tma:TM1560; -. DR KEGG; tmi:THEMA_06480; -. DR KEGG; tmm:Tmari_1568; -. DR KEGG; tmw:THMA_1595; -. DR PATRIC; 23938082; VBITheMar51294_1578. DR eggNOG; ENOG410908R; Bacteria. DR eggNOG; COG3404; LUCA. DR OMA; TIGKEKY; -. DR OrthoDB; EOG6T1WR9; -. DR BioCyc; TMAR243274:GC6P-1601-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030412; F:formimidoyltetrahydrofolate cyclodeaminase activity; IEA:UniProtKB-EC. DR GO; GO:0044237; P:cellular metabolic process; IEA:InterPro. DR InterPro; IPR007044; Cyclodeamin/CycHdrlase. DR Pfam; PF04961; FTCD_C; 1. DR SUPFAM; SSF101262; SSF101262; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O5H}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000313|EMBL:AGL50492.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 177 FTCD_C. {ECO:0000259|Pfam:PF04961}. FT COILED 169 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 202 AA; 22713 MW; 56E7EFB671B949AF CRC64; MEVERLSLKE FCDMVAERKP TPGGGAVGSV VGAMACALAE MVANFTRKKK GYEDVEPEME RIVEAMEEAR LKLFDLAKKD MEAFEKVMKA YKSSEGELQN ALKEAASVPM DVIRVMKDLA HELEKLAEFG NKNLASDTLN AADLCHAVFQ VEKVNVLINL KEISDETFRK NMLEELEEQE AQIEGCYQRV KKMLEGIVWS SK // ID Q9X1A0_THEMA Unreviewed; 222 AA. AC Q9X1A0; G4FFB6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE RecName: Full=Ribosomal RNA small subunit methyltransferase E {ECO:0000256|PIRNR:PIRNR015601}; DE EC=2.1.1.193 {ECO:0000256|PIRNR:PIRNR015601}; GN OrderedLocusNames=TM_1380 {ECO:0000313|EMBL:AAD36450.1}; GN ORFNames=Tmari_1387 {ECO:0000313|EMBL:AGL50311.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36450.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36450.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36450.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50311.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50311.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Specifically methylates the N3 position of the uracil CC ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully CC assembled 30S ribosomal subunit. {ECO:0000256|PIRNR:PIRNR015601}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(1498) in 16S CC rRNA = S-adenosyl-L-homocysteine + N(3)-methyluracil(1498) in 16S CC rRNA. {ECO:0000256|PIRNR:PIRNR015601}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR015601}. CC -!- SIMILARITY: Belongs to the RNA methyltransferase RsmE family. CC {ECO:0000256|PIRNR:PIRNR015601}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36450.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50311.1; -; Genomic_DNA. DR PIR; E72261; E72261. DR RefSeq; NP_229181.1; NC_000853.1. DR RefSeq; WP_004081578.1; NZ_CP011107.1. DR PDB; 1Z85; X-ray; 2.12 A; A/B=1-222. DR PDBsum; 1Z85; -. DR STRING; 243274.TM1380; -. DR DNASU; 898098; -. DR EnsemblBacteria; AAD36450; AAD36450; TM_1380. DR EnsemblBacteria; AGL50311; AGL50311; Tmari_1387. DR GeneID; 898098; -. DR KEGG; tma:TM1380; -. DR KEGG; tmi:THEMA_07425; -. DR KEGG; tmm:Tmari_1387; -. DR KEGG; tmw:THMA_1407; -. DR PATRIC; 23937702; VBITheMar51294_1392. DR eggNOG; ENOG41083JB; Bacteria. DR eggNOG; COG1385; LUCA. DR KO; K09761; -. DR OMA; EREAHHM; -. DR OrthoDB; EOG6FJNHQ; -. DR BioCyc; TMAR243274:GC6P-1415-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR006700; rRNA_ssu_MeTrfase-E. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF04452; Methyltrans_RNA; 1. DR PIRSF; PIRSF015601; MTase_slr0722; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00046; TIGR00046; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1Z85}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR015601}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR015601, KW ECO:0000313|EMBL:AGL50311.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW rRNA processing {ECO:0000256|PIRNR:PIRNR015601}; KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR015601}; KW Transferase {ECO:0000256|PIRNR:PIRNR015601, KW ECO:0000313|EMBL:AGL50311.1}. FT REGION 84 85 Chloride 2 binding. FT {ECO:0000213|PDB:1Z85}. FT REGION 115 118 Chloride 3 binding. FT {ECO:0000213|PDB:1Z85}. FT BINDING 116 116 Chloride 4; via amide nitrogen. FT {ECO:0000213|PDB:1Z85}. FT BINDING 177 177 Chloride 1; via amide nitrogen. FT {ECO:0000213|PDB:1Z85}. SQ SEQUENCE 222 AA; 25098 MW; 6C155250D5408DFA CRC64; MPHLFYGTAQ NGEVIFDERE AHHMRVVRLK EGDVIEATDG NGFSYTCILK SLKKKTAAAK IVKVEEKEKE PTEKLSVVVP IGRWERTRFL IEKCVELGVD EIFFHKFERS QHEISLDKAK IVVREAAKQC KRYLFPKVSF LEKLEFSGNV ITLDLDASQN LLDANLEGSI TVVVGPEGGF SEKERELLRS STTIVSLGKK ILRFETAAIL TVGYIALKKQ KI // ID Q9WZS3_THEMA Unreviewed; 142 AA. AC Q9WZS3; G4FD08; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 108. DE SubName: Full=Transcriptional regulator, MarR family {ECO:0000313|EMBL:AGL49742.1}; DE SubName: Full=Transcriptional regulator, putative, Mar family {ECO:0000313|EMBL:AAD35898.1}; GN OrderedLocusNames=TM_0816 {ECO:0000313|EMBL:AAD35898.1}; GN ORFNames=Tmari_0817 {ECO:0000313|EMBL:AGL49742.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35898.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35898.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35898.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49742.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49742.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 3 HTH marR-type DNA-binding domains. CC {ECO:0000256|RuleBase:RU000702}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35898.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49742.1; -; Genomic_DNA. DR PIR; C72329; C72329. DR RefSeq; NP_228625.1; NC_000853.1. DR RefSeq; WP_004080846.1; NZ_CP011107.1. DR PDB; 2ETH; X-ray; 2.30 A; A/B=1-142. DR PDBsum; 2ETH; -. DR STRING; 243274.TM0816; -. DR EnsemblBacteria; AAD35898; AAD35898; TM_0816. DR EnsemblBacteria; AGL49742; AGL49742; Tmari_0817. DR GeneID; 898484; -. DR KEGG; tma:TM0816; -. DR KEGG; tmi:THEMA_00570; -. DR KEGG; tmm:Tmari_0817; -. DR KEGG; tmw:THMA_0835; -. DR PATRIC; 23936552; VBITheMar51294_0828. DR eggNOG; ENOG41083H6; Bacteria. DR eggNOG; COG1846; LUCA. DR OMA; LAGICED; -. DR OrthoDB; EOG6PS5VV; -. DR BioCyc; TMAR243274:GC6P-843-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR000835; HTH_MarR-typ. DR InterPro; IPR023187; Tscrpt_reg_MarR-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01047; MarR; 1. DR PRINTS; PR00598; HTHMARR. DR SMART; SM00347; HTH_MARR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS01117; HTH_MARR_1; 1. DR PROSITE; PS50995; HTH_MARR_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2ETH}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487313}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487138}; KW Transcription regulation {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487138}. FT DOMAIN 3 135 HTH marR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50995}. SQ SEQUENCE 142 AA; 16387 MW; 0D36B87FD206C0DC CRC64; MDALEIFKTL FSLVMRFSSY LPSNEEISDM KTTELYAFLY VALFGPKKMK EIAEFLSTTK SNVTNVVDSL EKRGLVVREM DPVDRRTYRV VLTEKGKEIF GEILSNFESL LKSVLEKFSE EDFKVVSEGF NRMVEALSRE GR // ID Q9WXU8_THEMA Unreviewed; 127 AA. AC Q9WXU8; G4FH08; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35187.1}; GN OrderedLocusNames=TM_0093 {ECO:0000313|EMBL:AAD35187.1}; GN ORFNames=Tmari_0090 {ECO:0000313|EMBL:AGL49016.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35187.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35187.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35187.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49016.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49016.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35187.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49016.1; -; Genomic_DNA. DR PIR; E72417; E72417. DR RefSeq; NP_227909.1; NC_000853.1. DR RefSeq; WP_004082636.1; NZ_CP011107.1. DR STRING; 243274.TM0093; -. DR EnsemblBacteria; AAD35187; AAD35187; TM_0093. DR EnsemblBacteria; AGL49016; AGL49016; Tmari_0090. DR GeneID; 896920; -. DR KEGG; tma:TM0093; -. DR KEGG; tmi:THEMA_04340; -. DR KEGG; tmm:Tmari_0090; -. DR KEGG; tmw:THMA_0089; -. DR PATRIC; 23935026; VBITheMar51294_0091. DR OMA; WRITVEP; -. DR OrthoDB; EOG651SX3; -. DR BioCyc; TMAR243274:GC6P-93-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 127 AA; 14409 MW; AA9C8BE4D4B3FF0B CRC64; MNIIEVLIVI AISLMIMGFF IPTLMFKLGK DHQAVAFKVM TIRMIEKTSR NGLLIIEDNG KIVTYDPHKN EKKIYEFPFI FLSKVAVDGE DITFKNGFVS TAGTVYGDGW WITVEPVTGR MRLYGGR // ID Q9WXZ9_THEMA Unreviewed; 215 AA. AC Q9WXZ9; G4FH66; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Transcriptional regulators of sugar metabolism {ECO:0000313|EMBL:AGL49076.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35245.1}; GN OrderedLocusNames=TM_0152 {ECO:0000313|EMBL:AAD35245.1}; GN ORFNames=Tmari_0150 {ECO:0000313|EMBL:AGL49076.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35245.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35245.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35245.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49076.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49076.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35245.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49076.1; -; Genomic_DNA. DR PIR; F72412; F72412. DR RefSeq; NP_227967.1; NC_000853.1. DR RefSeq; WP_004082766.1; NZ_CP011107.1. DR EnsemblBacteria; AAD35245; AAD35245; TM_0152. DR EnsemblBacteria; AGL49076; AGL49076; Tmari_0150. DR GeneID; 896988; -. DR KEGG; tma:TM0152; -. DR KEGG; tmm:Tmari_0150; -. DR KEGG; tmw:THMA_0148; -. DR PATRIC; 23935148; VBITheMar51294_0151. DR eggNOG; ENOG4108VZ1; Bacteria. DR eggNOG; ENOG410ZXQV; LUCA. DR OMA; AFERIKM; -. DR OrthoDB; EOG6G20PF; -. DR BioCyc; TMAR243274:GC6P-153-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.10420; -; 1. DR InterPro; IPR024185; FTHF_cligase-like. DR InterPro; IPR003741; LUD_dom. DR InterPro; IPR009501; UCP020269. DR Pfam; PF02589; DUF162; 1. DR PIRSF; PIRSF020269; DUF1121; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 17 208 DUF162. {ECO:0000259|Pfam:PF02589}. SQ SEQUENCE 215 AA; 24473 MW; 1636F7B6700D7139 CRC64; MSLREELWLW KKEKLAEHVA NNLRKKKHEV WIARDREEIL ERVKELIPEG ATVSAGGSLT LADTGVIELL RSGRYNFLDR AAAKTREEVE EIYRKSFWAD YYFTSVNAIT EDGKLVFLDG NGNRVAAVVF GPKNVVVIAS VNKVVKDVEE ARERLRYISP MNSKRLNLET PCTKTGFCAD CSSPQRICDY FLVVESGVRQ PGRFKVILTL EDFGL // ID Q9WYR3_THEMA Unreviewed; 423 AA. AC Q9WYR3; G4FHZ1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=N-Acetyl-D-glucosamine ABC transport system, sugar-binding protein {ECO:0000313|EMBL:AGL49354.1}; DE SubName: Full=Sugar ABC transporter, periplasmic sugar-binding protein, putative {ECO:0000313|EMBL:AAD35517.1}; GN OrderedLocusNames=TM_0432 {ECO:0000313|EMBL:AAD35517.1}; GN ORFNames=Tmari_0429 {ECO:0000313|EMBL:AGL49354.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35517.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35517.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35517.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49354.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49354.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35517.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49354.1; -; Genomic_DNA. DR PIR; C72376; C72376. DR RefSeq; NP_228242.1; NC_000853.1. DR RefSeq; WP_004083321.1; NZ_CP011107.1. DR STRING; 243274.TM0432; -. DR EnsemblBacteria; AAD35517; AAD35517; TM_0432. DR EnsemblBacteria; AGL49354; AGL49354; Tmari_0429. DR GeneID; 897445; -. DR KEGG; tma:TM0432; -. DR KEGG; tmi:THEMA_02565; -. DR KEGG; tmm:Tmari_0429; -. DR KEGG; tmw:THMA_0438; -. DR PATRIC; 23935749; VBITheMar51294_0438. DR eggNOG; ENOG4105NGE; Bacteria. DR eggNOG; COG1653; LUCA. DR KO; K17241; -. DR OMA; EPWTWEE; -. DR OrthoDB; EOG6K9QD2; -. DR BioCyc; TMAR243274:GC6P-447-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR006059; SBP_1_dom. DR Pfam; PF01547; SBP_bac_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 423 AA; 48009 MW; 6EE706190A28C7E1 CRC64; MRKLAVVLLI SLILLPVLAS AVKLTIYCGG GTERKGLEAL VAEYKKLNPD VDFEIIDISY SSYMQKISLA VMSGDVPDLM TITYPFAPEL RKYLIDLDPY IEKYLGITPK EYEDAFYNVV KPYIKDENGK IKYVPLHFTV QGLWVNVDYF EKAGIPFPPL GGREEPWTWE EFVEVLRKVK EANNLPYAMS MQYSAERIAN YLAIRGAKVL DENLNLVLDK DPKAIKALED FVNLFKENLC VPAEWVSGQS ADNDFYGGVT AVYWAGSWET LDALSVEGKR FLPAYLPKDE YCFGVEGGRF FGAFKTGDKK KEEEAAKFAL WAGWKGKGYD IYLKTTLHLS AYKDHKVDYG VPIMESVQKV FGYLAANAPE WIVTVRANPV WSRLYDPLRK QISLVIAGQQ DLQTALKNIR AEYERIVEEL GIK // ID Q9X1J8_THEMA Unreviewed; 406 AA. AC Q9X1J8; G4FFP7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=DUF1015 domain-containing protein {ECO:0000313|EMBL:AGL50442.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36577.1}; GN OrderedLocusNames=TM_1510 {ECO:0000313|EMBL:AAD36577.1}; GN ORFNames=Tmari_1518 {ECO:0000313|EMBL:AGL50442.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36577.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36577.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36577.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50442.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50442.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36577.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50442.1; -; Genomic_DNA. DR PIR; G72244; G72244. DR RefSeq; NP_229310.1; NC_000853.1. DR RefSeq; WP_004081856.1; NZ_CP011107.1. DR STRING; 243274.TM1510; -. DR EnsemblBacteria; AAD36577; AAD36577; TM_1510. DR EnsemblBacteria; AGL50442; AGL50442; Tmari_1518. DR GeneID; 897991; -. DR KEGG; tma:TM1510; -. DR KEGG; tmi:THEMA_06750; -. DR KEGG; tmm:Tmari_1518; -. DR KEGG; tmw:THMA_1542; -. DR PATRIC; 23937978; VBITheMar51294_1527. DR eggNOG; ENOG4105CGQ; Bacteria. DR eggNOG; COG4198; LUCA. DR OMA; EPVFFAY; -. DR OrthoDB; EOG60W7TW; -. DR BioCyc; TMAR243274:GC6P-1550-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR008323; UCP033563. DR Pfam; PF06245; DUF1015; 1. DR PIRSF; PIRSF033563; UCP033563; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 406 AA; 47815 MW; D9F97024A9C73ED0 CRC64; MEIKPFRGFR PREEIAEKFV AKPYDVVSFL EAKETIKNNP FSFLRVTRVE AETHEIEMDP TPEDMEKARR NLEKFIEDGI LIQEEKEAFY IYRQRMGDHI QTGIVALFPV EEYKKGRIKK HELTRKKKEE ERVQHILKTR AHTGQVFLFY RAFEEFDRKL SEIADSQEPV YRIRDDLDVI HEFFVVKNEN EVNEIKKLFE RVEELYIADG HHRAAAAARV SDILDEKIGK GPHNYFMATA FPHNQLRIFD YNRVVKSQLT PEELLEKLQE KFETYRSYKV PARPSREHEI TMYVGNRKWY ALIPKRVPED VVESLDVNIL QREVLEPIFG ISNPREDERI DFVGGIKGLC ELERMVDKGE FDVAFAMYPV NIETLMKVSD EGKIMPPKST WFEPKLLSGL VVHVFG // ID Q9WZ14_THEMA Unreviewed; 244 AA. AC Q9WZ14; G4FDS7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 119. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35629.1}; GN OrderedLocusNames=TM_0544 {ECO:0000313|EMBL:AAD35629.1}; GN ORFNames=Tmari_0541 {ECO:0000313|EMBL:AGL49466.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35629.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35629.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35629.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49466.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49466.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35629.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49466.1; -; Genomic_DNA. DR PIR; E72364; E72364. DR RefSeq; NP_228354.1; NC_000853.1. DR RefSeq; WP_004081352.1; NZ_CP011107.1. DR PDB; 1VPL; X-ray; 2.10 A; A=1-244. DR PDBsum; 1VPL; -. DR STRING; 243274.TM0544; -. DR EnsemblBacteria; AAD35629; AAD35629; TM_0544. DR EnsemblBacteria; AGL49466; AGL49466; Tmari_0541. DR GeneID; 897598; -. DR KEGG; tma:TM0544; -. DR KEGG; tmi:THEMA_01955; -. DR KEGG; tmm:Tmari_0541; -. DR KEGG; tmw:THMA_0557; -. DR PATRIC; 23935995; VBITheMar51294_0552. DR eggNOG; ENOG4108TAD; Bacteria. DR eggNOG; COG1131; LUCA. DR KO; K01990; -. DR OMA; VYGNQKS; -. DR OrthoDB; EOG65J54C; -. DR BioCyc; TMAR243274:GC6P-568-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VPL}; KW ATP-binding {ECO:0000313|EMBL:AAD35629.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD35629.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 234 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT REGION 39 43 Sulfate 2 binding. FT {ECO:0000213|PDB:1VPL}. FT BINDING 12 12 Sulfate 1. {ECO:0000213|PDB:1VPL}. FT BINDING 56 56 Sulfate 1. {ECO:0000213|PDB:1VPL}. SQ SEQUENCE 244 AA; 27129 MW; 41C345711BAF5EBF CRC64; MGAVVVKDLR KRIGKKEILK GISFEIEEGE IFGLIGPNGA GKTTTLRIIS TLIKPSSGIV TVFGKNVVEE PHEVRKLISY LPEEAGAYRN MQGIEYLRFV AGFYASSSSE IEEMVERATE IAGLGEKIKD RVSTYSKGMV RKLLIARALM VNPRLAILDE PTSGLDVLNA REVRKILKQA SQEGLTILVS SHNMLEVEFL CDRIALIHNG TIVETGTVEE LKERYKAQNI EEVFEEVVKC SENF // ID Q9WZB4_THEMA Unreviewed; 176 AA. AC Q9WZB4; G4FDH8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35730.1}; GN OrderedLocusNames=TM_0646 {ECO:0000313|EMBL:AAD35730.1}; GN ORFNames=Tmari_0646 {ECO:0000313|EMBL:AGL49571.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35730.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35730.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35730.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49571.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49571.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35730.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49571.1; -; Genomic_DNA. DR PIR; E72351; E72351. DR RefSeq; NP_228455.1; NC_000853.1. DR RefSeq; WP_004081152.1; NZ_CP011107.1. DR STRING; 243274.TM0646; -. DR EnsemblBacteria; AAD35730; AAD35730; TM_0646. DR EnsemblBacteria; AGL49571; AGL49571; Tmari_0646. DR GeneID; 897751; -. DR KEGG; tma:TM0646; -. DR KEGG; tmi:THEMA_01435; -. DR KEGG; tmm:Tmari_0646; -. DR KEGG; tmw:THMA_0661; -. DR PATRIC; 23936206; VBITheMar51294_0656. DR eggNOG; ENOG4105Z8Y; Bacteria. DR eggNOG; COG4741; LUCA. DR OMA; PADARFI; -. DR OrthoDB; EOG6K9QJZ; -. DR BioCyc; TMAR243274:GC6P-671-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR019287; Hday_junct_resolvase-rel_dom. DR InterPro; IPR028300; Holliday_junct_resolvase-rel. DR Pfam; PF10107; Endonuc_Holl; 1. DR PIRSF; PIRSF014735; UCP014735; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 21 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 15 172 Endonuc_Holl. {ECO:0000259|Pfam:PF10107}. SQ SEQUENCE 176 AA; 21195 MW; D5768886C85A08FB CRC64; MTVLIIVILI IVVFILTRNL LKMSREIQEL RGKIESNAMK MFEEWKKSEW ELQRRVLEAN LKREYEVKFQ EWKMEEEKRI REDAINKSKS VIMGQVTEHL IPFFPEFRYN PKDARFIGTP VDFVVFDGLS EGNLRRIVFV EVKTGKTGNL NTRERQVRDV VEKREVYWEK LHYRGE // ID Q9X252_THEMA Unreviewed; 403 AA. AC Q9X252; G4FGB5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Outer membrane protein {ECO:0000313|EMBL:AAD36794.1}; DE SubName: Full=S-layer domain protein {ECO:0000313|EMBL:AGL50661.1}; GN OrderedLocusNames=TM_1729 {ECO:0000313|EMBL:AAD36794.1}; GN ORFNames=Tmari_1737 {ECO:0000313|EMBL:AGL50661.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36794.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36794.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36794.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50661.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50661.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36794.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50661.1; -; Genomic_DNA. DR PIR; H72216; H72216. DR RefSeq; NP_229527.1; NC_000853.1. DR RefSeq; WP_004082244.1; NZ_CP011107.1. DR STRING; 243274.TM1729; -. DR EnsemblBacteria; AAD36794; AAD36794; TM_1729. DR EnsemblBacteria; AGL50661; AGL50661; Tmari_1737. DR GeneID; 897874; -. DR KEGG; tma:TM1729; -. DR KEGG; tmi:THEMA_05590; -. DR KEGG; tmm:Tmari_1737; -. DR KEGG; tmw:THMA_1771; -. DR PATRIC; 23938434; VBITheMar51294_1747. DR eggNOG; ENOG4105QZY; Bacteria. DR eggNOG; ENOG4111ZAU; LUCA. DR OMA; GTFQGNQ; -. DR OrthoDB; EOG6FV856; -. DR BioCyc; TMAR243274:GC6P-1777-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR001119; SLH_dom. DR Pfam; PF00395; SLH; 1. DR PROSITE; PS51272; SLH; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 403 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006753485. FT TRANSMEM 381 400 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 17 80 SLH (S-layer homology). FT {ECO:0000259|PROSITE:PS51272}. FT COILED 143 170 {ECO:0000256|SAM:Coils}. FT COILED 264 357 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 403 AA; 43716 MW; 659421A7585D4604 CRC64; MKKLLVFVLM LGAFVGISQQ FKDVPVNHWA YEAVMEMSKL GVLTGMPDGT FQGNSYLTRY QAAVAFYRLY NILKQPSADV SGLINKVSTL EDLVSTALMK VQNLSDNFGG VTSDLETLKN DVANLKATLV DLKNLRVEVM SQVQSQSDEL QSLDAKVNEA LSKIAALESK LSGDFVNKDY VDSKIAQTVS KLSDLEGRLS AVETKTANLE ALVRNSEASL KDYVEKTLKS YTDTLDQKLS ELSASVEKNN TALSGEIGNL KVLVSKLQSD LETQQKTARA LDARVSVLEG QITTVNSRVE SLEKRVSQVE SAVDKVNSLE RSMGAVTARV TKVEEEVKNL NQSNAELSQK VDEVVSSKPW MEDVNSVSAT LSKKISDVQT MALAGVAIGI VGVIIGFVMG SGK // ID Q9WZF7_THEMA Unreviewed; 90 AA. AC Q9WZF7; G4FDD1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35775.1}; GN OrderedLocusNames=TM_0693 {ECO:0000313|EMBL:AAD35775.1}; GN ORFNames=Tmari_0693 {ECO:0000313|EMBL:AGL49618.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35775.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35775.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35775.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49618.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49618.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35775.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49618.1; -; Genomic_DNA. DR PIR; C72345; C72345. DR RefSeq; NP_228502.1; NC_000853.1. DR RefSeq; WP_004081063.1; NZ_CP011107.1. DR PDB; 2FZT; X-ray; 2.05 A; A/B=1-78. DR PDB; 2G42; X-ray; 2.28 A; A/B=1-78. DR PDBsum; 2FZT; -. DR PDBsum; 2G42; -. DR STRING; 243274.TM0693; -. DR EnsemblBacteria; AAD35775; AAD35775; TM_0693. DR EnsemblBacteria; AGL49618; AGL49618; Tmari_0693. DR GeneID; 898360; -. DR KEGG; tma:TM0693; -. DR KEGG; tmi:THEMA_01200; -. DR KEGG; tmm:Tmari_0693; -. DR KEGG; tmw:THMA_0708; -. DR PATRIC; 23936304; VBITheMar51294_0705. DR OMA; TRGDTIG; -. DR OrthoDB; EOG61CM4H; -. DR BioCyc; TMAR243274:GC6P-719-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2FZT, ECO:0000213|PDB:2G42}; KW Calcium {ECO:0000213|PDB:2G42}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000213|PDB:2G42}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT METAL 18 18 Calcium. {ECO:0000213|PDB:2G42}. FT METAL 21 21 Calcium. {ECO:0000213|PDB:2G42}. SQ SEQUENCE 90 AA; 10683 MW; 8FDC2107AB957A68 CRC64; MNIDEIERKI DEAIEKEDYE TLLSLLNKRK ELMEGLPKDK LSEILEKDRK RLEIIEKRKT ALFQEINVIR EARSSLQKNI WTRGDTLGRG // ID Q9WZ98_THEMA Unreviewed; 346 AA. AC Q9WZ98; G4FDJ3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 98. DE SubName: Full=Nucleotide sugar epimerase, putative {ECO:0000313|EMBL:AAD35714.1}; DE SubName: Full=UDP-glucose 4-epimerase {ECO:0000313|EMBL:AGL49556.1}; DE EC=5.1.3.2 {ECO:0000313|EMBL:AGL49556.1}; GN OrderedLocusNames=TM_0630 {ECO:0000313|EMBL:AAD35714.1}; GN ORFNames=Tmari_0631 {ECO:0000313|EMBL:AGL49556.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35714.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35714.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35714.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49556.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49556.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35714.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49556.1; -; Genomic_DNA. DR PIR; C72353; C72353. DR RefSeq; NP_228439.1; NC_000853.1. DR RefSeq; WP_004081172.1; NZ_CP011107.1. DR STRING; 243274.TM0630; -. DR EnsemblBacteria; AAD35714; AAD35714; TM_0630. DR EnsemblBacteria; AGL49556; AGL49556; Tmari_0631. DR GeneID; 897726; -. DR KEGG; tma:TM0630; -. DR KEGG; tmm:Tmari_0631; -. DR KEGG; tmw:THMA_0646; -. DR PATRIC; 23936173; VBITheMar51294_0640. DR eggNOG; COG0451; LUCA. DR OMA; FAFHLAC; -. DR OrthoDB; EOG69GZPD; -. DR BioCyc; TMAR243274:GC6P-655-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000313|EMBL:AGL49556.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 16 255 Epimerase. {ECO:0000259|Pfam:PF01370}. SQ SEQUENCE 346 AA; 39119 MW; FA011CB4B32DEFEC CRC64; MMGKTEYLDY YSGKRVLVTG GAGAVGSNLV RRLLDLGAFV IVIDNLSSGY TWLLPQDAPN LLFIEGDITN DVDLKRVFNE EPEIIFHLAA FFANQNSVDY PEKDLWVNGF GTLKLLEYTR IYGKVERFVY ASSGCSIYPS DAPMPFKEDL PISSWMSTPY QITKALGELY CNYFYKMYDI PITKARFFNS FGPGEVPGQY RNVIPNFIYW AMLGKPLPIT GTGEETRDFT YVGDIVDGLL RMGYYREAIG EAFNLAAGRE VKIKYLAEKV NELTGNTAGI VFKPRRKWDT KPRMLASNEK AKKVLGFNPD PDFDGRLAET VEWFKQNWEL IKKSAEFGPG VSSAVR // ID Q9X0P2_THEMA Unreviewed; 227 AA. AC Q9X0P2; G4FEI9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 109. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36234.1}; GN OrderedLocusNames=TM_1158 {ECO:0000313|EMBL:AAD36234.1}; GN ORFNames=Tmari_1165 {ECO:0000313|EMBL:AGL50089.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36234.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36234.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36234.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50089.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50089.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36234.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50089.1; -; Genomic_DNA. DR PIR; D72287; D72287. DR RefSeq; NP_228964.1; NC_000853.1. DR RefSeq; WP_004080220.1; NZ_CP011107.1. DR PDB; 1O1Y; X-ray; 1.70 A; A=2-227. DR PDBsum; 1O1Y; -. DR STRING; 243274.TM1158; -. DR EnsemblBacteria; AAD36234; AAD36234; TM_1158. DR EnsemblBacteria; AGL50089; AGL50089; Tmari_1165. DR GeneID; 898328; -. DR KEGG; tma:TM1158; -. DR KEGG; tmi:THEMA_08550; -. DR KEGG; tmm:Tmari_1165; -. DR KEGG; tmw:THMA_1182; -. DR PATRIC; 23937253; VBITheMar51294_1175. DR eggNOG; ENOG41082JW; Bacteria. DR eggNOG; COG0518; LUCA. DR OMA; REIGWAP; -. DR OrthoDB; EOG63FW50; -. DR BioCyc; TMAR243274:GC6P-1187-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O1Y}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 194 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. SQ SEQUENCE 227 AA; 26900 MW; BA9A539CFA4D6DC8 CRC64; MRVLAIRHVE IEDLGMMEDI FREKNWSFDY LDTPKGEKLE RPLEEYSLVV LLGGYMGAYE EEKYPFLKYE FQLIEEILKK EIPFLGICLG SQMLAKVLGA SVYRGKNGEE IGWYFVEKVS DNKFFREFPD RLRVFQWHGD TFDLPRRATR VFTSEKYENQ GFVYGKAVGL QFHIEVGART MKRWIEAYKD ELEKKKIDPR LLLETAEREE KVLKGLLRSL LERMVES // ID Q9WYV6_THEMA Unreviewed; 94 AA. AC Q9WYV6; G4FDY4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=UPF0045 protein {ECO:0000313|EMBL:AGL49408.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35571.1}; GN OrderedLocusNames=TM_0486 {ECO:0000313|EMBL:AAD35571.1}; GN ORFNames=Tmari_0483 {ECO:0000313|EMBL:AGL49408.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35571.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35571.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35571.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49408.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49408.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35571.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49408.1; -; Genomic_DNA. DR PIR; E72369; E72369. DR RefSeq; NP_228296.1; NC_000853.1. DR RefSeq; WP_004081480.1; NZ_CP011107.1. DR PDB; 1VK8; X-ray; 1.80 A; A/B/C/D=1-94. DR PDBsum; 1VK8; -. DR STRING; 243274.TM0486; -. DR EnsemblBacteria; AAD35571; AAD35571; TM_0486. DR EnsemblBacteria; AGL49408; AGL49408; Tmari_0483. DR GeneID; 897525; -. DR KEGG; tma:TM0486; -. DR KEGG; tmi:THEMA_02240; -. DR KEGG; tmm:Tmari_0483; -. DR KEGG; tmw:THMA_0499; -. DR PATRIC; 23935877; VBITheMar51294_0493. DR eggNOG; ENOG41085GA; Bacteria. DR eggNOG; COG0011; LUCA. DR OMA; KKAHIVA; -. DR OrthoDB; EOG69PQ9Q; -. DR BioCyc; TMAR243274:GC6P-510-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.30.70.930; -; 1. DR InterPro; IPR029756; MTH1187/YkoF-like. DR InterPro; IPR002767; Thiamine_BP. DR Pfam; PF01910; Thiamine_BP; 1. DR SUPFAM; SSF89957; SSF89957; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VK8}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 6 93 Thiamine_BP. {ECO:0000259|Pfam:PF01910}. SQ SEQUENCE 94 AA; 10805 MW; 85FBC953ED8D77EB CRC64; MPKVTVSIKV VPAVEDGRLH EVIDRAIEKI SSWGMKYEVG PSNTTVEGEF EEIMDRVKEL ARYLEQFAKR FVLQLDIDYK AGGITIEEKV SKYR // ID Q9X2C4_THEMA Unreviewed; 156 AA. AC Q9X2C4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36867.1}; GN OrderedLocusNames=TM_1804 {ECO:0000313|EMBL:AAD36867.1}; GN ORFNames=Tmari_1815 {ECO:0000313|EMBL:AGL50739.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36867.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36867.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36867.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50739.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50739.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36867.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50739.1; -; Genomic_DNA. DR PIR; A72208; A72208. DR RefSeq; NP_229601.1; NC_000853.1. DR RefSeq; WP_008194418.1; NZ_CP011107.1. DR STRING; 243274.TM1804; -. DR DNASU; 897152; -. DR EnsemblBacteria; AAD36867; AAD36867; TM_1804. DR EnsemblBacteria; AGL50739; AGL50739; Tmari_1815. DR GeneID; 897152; -. DR KEGG; tma:TM1804; -. DR KEGG; tmi:THEMA_05170; -. DR KEGG; tmm:Tmari_1815; -. DR KEGG; tmw:THMA_1850; -. DR PATRIC; 23938597; VBITheMar51294_1825. DR OMA; VPNPGYV; -. DR OrthoDB; EOG6NPM81; -. DR BioCyc; TMAR243274:GC6P-1855-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 48 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 77 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 89 108 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 120 140 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 156 AA; 17646 MW; 37F9D90833F8056C CRC64; MHVKKVTYGG LVSALVVLLL YIGNFTKSKI FFAALSSVFT GVLVELFGIG SVPIIIAVNV LVFLLVPNPG YVLLFFVLSF YGFLRKKPIL IRFLYLNAST LLLVFVASKF FNAELPDVSF SLYVLGFLGV QVAFFVYDYL YNRILQELLR IIRRKN // ID Q9WY88_THEMA Unreviewed; 224 AA. AC Q9WY88; G4FHG0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE RecName: Full=Electron transport complex subunit G {ECO:0000256|HAMAP-Rule:MF_00479}; GN OrderedLocusNames=TM_0246 {ECO:0000313|EMBL:AAD35337.1}; GN ORFNames=Tmari_0244 {ECO:0000313|EMBL:AGL49170.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35337.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35337.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35337.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49170.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49170.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000256|HAMAP-Rule:MF_00479}. CC -!- SUBUNIT: Composed of six subunits. {ECO:0000256|HAMAP- CC Rule:MF_00479}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00479}. CC -!- SIMILARITY: Belongs to the RnfG family. {ECO:0000256|HAMAP- CC Rule:MF_00479}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35337.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49170.1; -; Genomic_DNA. DR PIR; G72398; G72398. DR RefSeq; NP_228060.1; NC_000853.1. DR RefSeq; WP_004082950.1; NZ_CP011107.1. DR PDB; 3DCZ; X-ray; 1.65 A; A=30-224. DR PDBsum; 3DCZ; -. DR STRING; 243274.TM0246; -. DR EnsemblBacteria; AAD35337; AAD35337; TM_0246. DR EnsemblBacteria; AGL49170; AGL49170; Tmari_0244. DR GeneID; 897153; -. DR KEGG; tma:TM0246; -. DR KEGG; tmi:THEMA_03495; -. DR KEGG; tmm:Tmari_0244; -. DR KEGG; tmw:THMA_0253; -. DR PATRIC; 23935367; VBITheMar51294_0249. DR eggNOG; ENOG4108XPW; Bacteria. DR eggNOG; COG4659; LUCA. DR KO; K03612; -. DR OMA; NAMYKFL; -. DR OrthoDB; EOG6W19H8; -. DR BioCyc; TMAR243274:GC6P-259-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR HAMAP; MF_00479; RsxG_RnfG; 1. DR InterPro; IPR010209; Elect_transpt_RnfG/RsxG. DR InterPro; IPR007329; FMN-bd. DR Pfam; PF04205; FMN_bind; 1. DR SMART; SM00900; FMN_bind; 1. DR TIGRFAMs; TIGR01947; rnfG; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3DCZ}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00479}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00479}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00479}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00479}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00479}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00479}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00479}. FT TRANSMEM 9 29 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00479}. FT DOMAIN 110 219 FMN_bind. {ECO:0000259|SMART:SM00900}. FT REGION 100 102 Acetate binding. {ECO:0000213|PDB:3DCZ}. FT REGION 204 206 Sulfate 2 binding. FT {ECO:0000213|PDB:3DCZ}. FT BINDING 206 206 Sulfate 1. {ECO:0000213|PDB:3DCZ}. SQ SEQUENCE 224 AA; 24397 MW; DA409A9AED3D85B9 CRC64; MKDILKTGLI LMVFTAISGL FLGLVYVGVK GKIQEADNAA KLSAIKFVLK DPLTGDYLVD EKEIEEIVKK TGIETVVLKE YKEGVVLGPL YEFVTKDGRN AYVLSGYAPG FGGNVTVVAC FIKTEDGFML NSVRVIDYSQ ETPGLGAKIG EESIQRRFFP VPPEGLKNGL RVDKDAGLPK GSPEELKKQG IVKVSDVMTG ATITPRAVVT ALNLMYRYLE EVSK // ID Q9WZ01_THEMA Unreviewed; 579 AA. AC Q9WZ01; G4FDU0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein {ECO:0000313|EMBL:AAD35616.1}; DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein OppA {ECO:0000313|EMBL:AGL49453.1}; GN OrderedLocusNames=TM_0531 {ECO:0000313|EMBL:AAD35616.1}; GN ORFNames=Tmari_0528 {ECO:0000313|EMBL:AGL49453.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35616.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35616.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35616.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49453.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49453.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35616.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49453.1; -; Genomic_DNA. DR PIR; A72367; A72367. DR RefSeq; NP_228341.1; NC_000853.1. DR RefSeq; WP_004081378.1; NZ_CP011107.1. DR STRING; 243274.TM0531; -. DR EnsemblBacteria; AAD35616; AAD35616; TM_0531. DR EnsemblBacteria; AGL49453; AGL49453; Tmari_0528. DR GeneID; 897583; -. DR KEGG; tma:TM0531; -. DR KEGG; tmi:THEMA_02020; -. DR KEGG; tmm:Tmari_0528; -. DR KEGG; tmw:THMA_0544; -. DR PATRIC; 23935969; VBITheMar51294_0539. DR eggNOG; ENOG4107QRA; Bacteria. DR eggNOG; COG0747; LUCA. DR KO; K02035; -. DR OMA; PDQYVRF; -. DR OrthoDB; EOG6384GZ; -. DR BioCyc; TMAR243274:GC6P-555-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GOC. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 83 467 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. SQ SEQUENCE 579 AA; 66509 MW; 65F6BB9D27F71081 CRC64; MRRFLGIFLM IAAVALFAEL SPFAQFETYI GAEFTGQYGG VLVVPTLSGP RTCNNVVAQE TSSRDVIARF MASMIELDNY ARIHPALAES WELIQNEDGS MEIVWHLRKG VKWSDGTPFT ADDVVFTIND VYFNPDIPND MQDLFADNWP VAEKLDDYTV KTTLKETYRL AVRYIGGIPI FPKHLAEPYV KEGKFKEFWT VDAINKGEIV GLGPFIPVEY VPDQYVRFVK NPYYWKYDKE GKQLPYLDGI IFKIIPTQDA QRLAFENGEV DVYGPRGTEY AELKAMAREK DWVVGIGGPN FGTTFISFNW NAPDPVKRKW FRNDFFRRAV AYAIDKQSMI DTLYNGLAVE QWGPISQAAT VYYDESVLRK YPYNLDLART MLKLGGFKWD ENGQLLDSEG NPVKFIIMTN AGNQIREGMG NIITEALKKL GMDVTFAPID FNTLVQKLVV NGDWEAVIIG LTGSDEPQGG ANVWRIKGSL HFWNYHPEVK DFVDPNDYYL PDWEKEIDRI FEENVKILDQ QKVVDMFREF QRLVSEHIPL IYTTQQLYLY AYSNKLHNVE PTAFGGVWGW NQDCVWKEQ // ID Q9X0M6_THEMA Unreviewed; 219 AA. AC Q9X0M6; G4FEK6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:AGL50072.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36218.1}; GN OrderedLocusNames=TM_1142 {ECO:0000313|EMBL:AAD36218.1}; GN ORFNames=Tmari_1148 {ECO:0000313|EMBL:AGL50072.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36218.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36218.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36218.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50072.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50072.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36218.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50072.1; -; Genomic_DNA. DR PIR; B72291; B72291. DR RefSeq; NP_228948.1; NC_000853.1. DR RefSeq; WP_004080260.1; NZ_CP011107.1. DR STRING; 243274.TM1142; -. DR DNASU; 898622; -. DR EnsemblBacteria; AAD36218; AAD36218; TM_1142. DR EnsemblBacteria; AGL50072; AGL50072; Tmari_1148. DR GeneID; 898622; -. DR KEGG; tma:TM1142; -. DR KEGG; tmi:THEMA_08635; -. DR KEGG; tmm:Tmari_1148; -. DR KEGG; tmw:THMA_1165; -. DR PATRIC; 23937219; VBITheMar51294_1158. DR eggNOG; ENOG4105JXG; Bacteria. DR eggNOG; COG2143; LUCA. DR OMA; SSPSCVY; -. DR OrthoDB; EOG65XN32; -. DR BioCyc; TMAR243274:GC6P-1171-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF13098; Thioredoxin_2; 1. DR SUPFAM; SSF52833; SSF52833; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 31 135 Thioredoxin. {ECO:0000259|Pfam:PF13098}. SQ SEQUENCE 219 AA; 25273 MW; 2983BE228EDCB457 CRC64; MKRFLIITIL ALSVFSLALT LDDAYRLANI TQRKLIMMFS SPTCYYCNLF KKEVFPKEDF QEILIPNFVF VELYATDEKT TLFAKEVLGE ESVSYRDLFA GFGVRGTPTF FFFKGKEGLG YLPGYVDKDN FIKILKYVAQ ELKEDFQTYL KKDDPFVGEP LIIEIFKEDA DFVLEKDENA VKVDTVPNEV RRDRIYVTDS PDVAKTLQEK GALRVLLAK // ID Q9WYS3_THEMA Unreviewed; 427 AA. AC Q9WYS3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Putative uronate isomerase {ECO:0000313|EMBL:AGL49364.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35527.1}; GN OrderedLocusNames=TM_0442 {ECO:0000313|EMBL:AAD35527.1}; GN ORFNames=Tmari_0439 {ECO:0000313|EMBL:AGL49364.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35527.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35527.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35527.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49364.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49364.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35527.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49364.1; -; Genomic_DNA. DR PIR; E72377; E72377. DR RefSeq; NP_228252.1; NC_000853.1. DR RefSeq; WP_010865122.1; NZ_CP011107.1. DR PDB; 4NAR; X-ray; 2.39 A; A=1-427. DR PDBsum; 4NAR; -. DR STRING; 243274.TM0442; -. DR EnsemblBacteria; AAD35527; AAD35527; TM_0442. DR EnsemblBacteria; AGL49364; AGL49364; Tmari_0439. DR GeneID; 897457; -. DR KEGG; tma:TM0442; -. DR KEGG; tmi:THEMA_02515; -. DR KEGG; tmm:Tmari_0439; -. DR KEGG; tmw:THMA_0448; -. DR PATRIC; 23935769; VBITheMar51294_0448. DR eggNOG; ENOG4105QUH; Bacteria. DR eggNOG; COG3875; LUCA. DR OMA; IYAPHIT; -. DR OrthoDB; EOG6MM1HW; -. DR BioCyc; TMAR243274:GC6P-457-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR InterPro; IPR018657; DUF2088. DR Pfam; PF09861; DUF2088; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4NAR}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000313|EMBL:AGL49364.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 21 183 DUF2088. {ECO:0000259|Pfam:PF09861}. FT BINDING 41 41 Acetate. {ECO:0000213|PDB:4NAR}. FT BINDING 41 41 Sulfate 1. {ECO:0000213|PDB:4NAR}. FT BINDING 72 72 Sulfate 2. {ECO:0000213|PDB:4NAR}. FT BINDING 150 150 Acetate; via amide nitrogen. FT {ECO:0000213|PDB:4NAR}. FT BINDING 154 154 Sulfate 1. {ECO:0000213|PDB:4NAR}. FT BINDING 161 161 Acetate; via amide nitrogen. FT {ECO:0000213|PDB:4NAR}. FT BINDING 164 164 Sulfate 1. {ECO:0000213|PDB:4NAR}. FT BINDING 180 180 Sulfate 2. {ECO:0000213|PDB:4NAR}. FT BINDING 283 283 Sulfate 2. {ECO:0000213|PDB:4NAR}. FT BINDING 287 287 Sulfate 1. {ECO:0000213|PDB:4NAR}. FT BINDING 341 341 Sulfate 3. {ECO:0000213|PDB:4NAR}. SQ SEQUENCE 427 AA; 49054 MW; 7833914BB6170312 CRC64; MTVYLEGDPL TEEKIKEGLS KLVEDLGKVK KVLVVHTDYT RVDFTHLVAK NLYRFLLERG LKEFHTLNAS GTHRTMKIEE FEKKLGISRN ERRVFFHNHE FFNPEALAFV GTLPAGFVSE MTEGDLEEEI PIKVNRLLFE DFDAIFFING TVPHESTGFS GGLKIVIPGI ASTEVVDTFH WAAVLMGIPK LIGTVDNPAR KIINRASEMI FEKIKARSFT LNMVYEEEEE VIPRALYIDE GYEGFLRAYE KACELSSQLH VKYIDRPLRR AVQVIGEEYD EVWTAGKGSY KLQRPGVMAK GGQIIIYAPH IKRFHSNPQM DKWIREIGYH CKDYVKWYLK KHPDFNKNVA AHVINVRGAG TFDPETGKEE FEFDVILATS IPEDECRAVN LGYMDPSKIK KEDFMDEDSL WIVPGGKYLY DLKERRG // ID G4FEX7_THEMA Unreviewed; 422 AA. AC G4FEX7; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-MAR-2016, entry version 36. DE SubName: Full=Major facilitator superfamily MFS_1 {ECO:0000313|EMBL:AGL49947.1}; DE SubName: Full=Permease, putative {ECO:0000313|EMBL:AAD36098.1}; GN OrderedLocusNames=TM_1021 {ECO:0000313|EMBL:AAD36098.1}; GN ORFNames=Tmari_1023 {ECO:0000313|EMBL:AGL49947.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36098.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36098.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36098.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49947.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49947.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36098.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49947.1; -; Genomic_DNA. DR PIR; D72302; D72302. DR RefSeq; NP_228827.1; NC_000853.1. DR RefSeq; WP_004080510.1; NZ_CP011107.1. DR STRING; 243274.TM1021; -. DR EnsemblBacteria; AAD36098; AAD36098; TM_1021. DR EnsemblBacteria; AGL49947; AGL49947; Tmari_1023. DR GeneID; 898616; -. DR KEGG; tma:TM1021; -. DR KEGG; tmm:Tmari_1023; -. DR KEGG; tmw:THMA_1042; -. DR eggNOG; ENOG4105DNH; Bacteria. DR eggNOG; ENOG410XR3C; LUCA. DR OMA; RIFSIFN; -. DR BioCyc; TMAR243274:GC6P-1050-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 114 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 126 148 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 154 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 217 237 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 252 272 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 284 304 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 310 336 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 357 378 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 384 402 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 2 406 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 422 AA; 46051 MW; 88806D6745364570 CRC64; MAVIFILILM VLLNADQMVM SPNIGAIEQE FNITDAQIGL VASSFTVIGA LVSLVWGYLA DRYSRKNLLI YSILVGEIPC LMSAFSRSYG ELFFWRALTG IGVGASFPIV YSMIGDMFDE VKRGKVVALI SSAISIGSVL GMIVGGFLGP KYGWRVPFIA VSVPNIFFAV LSIFVLKEPK RGAFEKGIGE LVQSGYEYPK APKLSDYAKL VKVKTNLLLF FQGIAGTIPW GAIPYFLVEF FRRERGLSVE TATLVFLVFG LGNIVGIILG GLWGASIYAK SRPFLPLFCS ITTALGTFFT VMTLDYMGSL LVLMLLGFIA SFTASLTGPN VKFMLLNVNE PQERGRIFSI FNLTDSLGTG FGKFAGGVMS VALGSLGAAL KVSAYFWLIC AVLLFVLVFY FAKDVERLQK TMIELAKNSQ TR // ID Q9X1A9_THEMA Unreviewed; 248 AA. AC Q9X1A9; G4FFC5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 104. DE SubName: Full=Ubiquinone/menaquinone biosynthesis methyltransferase-related protein {ECO:0000313|EMBL:AAD36459.1}; GN OrderedLocusNames=TM_1389 {ECO:0000313|EMBL:AAD36459.1}; GN ORFNames=Tmari_1396 {ECO:0000313|EMBL:AGL50320.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36459.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36459.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36459.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50320.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50320.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36459.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50320.1; -; Genomic_DNA. DR PIR; F72262; F72262. DR RefSeq; NP_229190.1; NC_000853.1. DR RefSeq; WP_004081594.1; NZ_CP011107.1. DR PDB; 2AVN; X-ray; 2.35 A; A/B=1-248. DR PDBsum; 2AVN; -. DR STRING; 243274.TM1389; -. DR EnsemblBacteria; AAD36459; AAD36459; TM_1389. DR EnsemblBacteria; AGL50320; AGL50320; Tmari_1396. DR GeneID; 898089; -. DR KEGG; tma:TM1389; -. DR KEGG; tmi:THEMA_07380; -. DR KEGG; tmm:Tmari_1396; -. DR KEGG; tmw:THMA_1416; -. DR PATRIC; 23937720; VBITheMar51294_1401. DR eggNOG; ENOG41082XR; Bacteria. DR eggNOG; COG0500; LUCA. DR OMA; YDSMYET; -. DR OrthoDB; EOG61307W; -. DR BioCyc; TMAR243274:GC6P-1424-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2AVN}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Methyltransferase {ECO:0000313|EMBL:AAD36459.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD36459.1}; KW Ubiquinone {ECO:0000313|EMBL:AAD36459.1}. FT DOMAIN 47 137 Methyltransf_11. FT {ECO:0000259|Pfam:PF08241}. FT BINDING 156 156 Phosphate; via amide nitrogen. FT {ECO:0000213|PDB:2AVN}. FT BINDING 214 214 Phosphate. {ECO:0000213|PDB:2AVN}. SQ SEQUENCE 248 AA; 28811 MW; 8ECDD400113CD011 CRC64; MKLRSWEFYD RIARAYDSMY ETPKWKLYHR LIGSFLEEYL KNPCRVLDLG GGTGKWSLFL QERGFEVVLV DPSKEMLEVA REKGVKNVVE AKAEDLPFPS GAFEAVLALG DVLSYVENKD KAFSEIRRVL VPDGLLIATV DNFYTFLQQM IEKDAWDQIT RFLKTQTTSV GTTLFSFNSY AFKPEDLDSL EGFETVDIRG IGVMEYPDER ISEREETIFR LEQELSRDRN IIWKADHIFF VLKKKRGA // ID Q9WYB7_THEMA Unreviewed; 484 AA. AC Q9WYB7; G4FHJ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 98. DE SubName: Full=Alpha-L-arabinofuranosidase {ECO:0000313|EMBL:AAD35369.1}; DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:AGL49205.1}; DE EC=3.2.1.55 {ECO:0000313|EMBL:AGL49205.1}; GN OrderedLocusNames=TM_0281 {ECO:0000313|EMBL:AAD35369.1}; GN ORFNames=Tmari_0279 {ECO:0000313|EMBL:AGL49205.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35369.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35369.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35369.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49205.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49205.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35369.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49205.1; -; Genomic_DNA. DR PIR; G72395; G72395. DR RefSeq; NP_228093.1; NC_000853.1. DR RefSeq; WP_004082990.1; NZ_CP011107.1. DR PDB; 3UG3; X-ray; 1.80 A; A/B/C/D/E/F=1-484. DR PDB; 3UG4; X-ray; 2.15 A; A/B/C/D/E/F=1-484. DR PDB; 3UG5; X-ray; 2.30 A; A/B/C/D/E/F=1-484. DR PDB; 4ATW; X-ray; 3.00 A; A/B/C/D/E/F=2-482. DR PDBsum; 3UG3; -. DR PDBsum; 3UG4; -. DR PDBsum; 3UG5; -. DR PDBsum; 4ATW; -. DR STRING; 243274.TM0281; -. DR CAZy; GH51; Glycoside Hydrolase Family 51. DR EnsemblBacteria; AAD35369; AAD35369; TM_0281. DR EnsemblBacteria; AGL49205; AGL49205; Tmari_0279. DR GeneID; 897198; -. DR KEGG; tma:TM0281; -. DR KEGG; tmi:THEMA_03320; -. DR KEGG; tmm:Tmari_0279; -. DR KEGG; tmw:THMA_0288; -. DR PATRIC; 23935441; VBITheMar51294_0286. DR eggNOG; ENOG4105CZZ; Bacteria. DR eggNOG; COG3534; LUCA. DR KO; K01209; -. DR OMA; ARNTMEN; -. DR OrthoDB; EOG6SJJF9; -. DR BioCyc; TMAR243274:GC6P-294-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC. DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR010720; Alpha-L-AF_C. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF06964; Alpha-L-AF_C; 1. DR SMART; SM00813; Alpha-L-AF_C; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3UG3, ECO:0000213|PDB:3UG4, KW ECO:0000213|PDB:3UG5, ECO:0000213|PDB:4ATW}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000313|EMBL:AGL49205.1}; KW Hydrolase {ECO:0000313|EMBL:AGL49205.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 280 475 Alpha-L-AF_C. FT {ECO:0000259|SMART:SM00813}. FT DISULFID 306 476 {ECO:0000213|PDB:4ATW}. SQ SEQUENCE 484 AA; 55268 MW; 27A39D32CA949B8C CRC64; MSYRIVVDPK EVVKPISRHI YGHFTEHLGR CIYGGIYEEG SPLSDERGFR KDVLEAVKRI KVPNLRWPGG NFVSNYHWED GIGPKDQRPV RFDLAWQQEE TNRFGTDEFI EYCREIGAEP YISINMGTGT LDEALHWLEY CNGKGNTYYA QLRRKYGHPE PYNVKFWGIG NEMYGEWQVG HMTADEYARA AKEYTKWMKV FDPTIKAIAV GCDDPIWNLR VLQEAGDVID FISYHFYTGS DDYYETVSTV YLLKERLIGV KKLIDMVDTA RKRGVKIALD EWNVWYRVSD NKLEEPYDLK DGIFACGVLV LLQKMSDIVP LANLAQLVNA LGAIHTEKDG LILTPVYKAF ELIVNHSGEK LVKTHVESET YNIEGVMFIN KMPFSVENAP FLDAAASISE DGKKLFIAVV NYRKEDALKV PIRVEGLGQK KATVYTLTGP DVNARNTMEN PNVVDITSET ITVDTEFEHT FKPFSCSVIE VELE // ID Q9WYB4_THEMA Unreviewed; 294 AA. AC Q9WYB4; G4FHJ2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE SubName: Full=Putative arabinoside ABC transporter, permease component 1 {ECO:0000313|EMBL:AGL49202.1}; DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35366.1}; GN OrderedLocusNames=TM_0278 {ECO:0000313|EMBL:AAD35366.1}; GN ORFNames=Tmari_0276 {ECO:0000313|EMBL:AGL49202.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35366.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35366.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35366.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49202.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49202.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35366.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49202.1; -; Genomic_DNA. DR PIR; D72395; D72395. DR RefSeq; NP_228090.1; NC_000853.1. DR RefSeq; WP_004082985.1; NZ_CP011107.1. DR STRING; 243274.TM0278; -. DR TCDB; 3.A.1.1.37; the atp-binding cassette (abc) superfamily. DR DNASU; 897195; -. DR EnsemblBacteria; AAD35366; AAD35366; TM_0278. DR EnsemblBacteria; AGL49202; AGL49202; Tmari_0276. DR GeneID; 897195; -. DR KEGG; tma:TM0278; -. DR KEGG; tmi:THEMA_03335; -. DR KEGG; tmm:Tmari_0276; -. DR KEGG; tmw:THMA_0285; -. DR PATRIC; 23935435; VBITheMar51294_0283. DR eggNOG; ENOG4105HS6; Bacteria. DR eggNOG; COG1175; LUCA. DR KO; K02025; -. DR OMA; LAWKFAF; -. DR OrthoDB; EOG68WR86; -. DR BioCyc; TMAR243274:GC6P-291-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 34 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 72 91 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 103 122 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 149 175 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 196 218 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 257 279 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 66 278 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 294 AA; 33219 MW; 5AE1ACDB1FF6C267 CRC64; MRKRIVPWLM VLPVLALFLA MTIYPFGFMI WASFRDYDLS KSAETHFIGL SNYFQIFRDS TAIESMKFTA KLLSIAVPVE LVLGVLIAFL IRGVKGEKII RSSLLIPMMI PPAVSGVAWK MLYNFAFGPV NWFLSLFGVP KISWLGDPFY AQLGIIIIDV WQWTPFIFLM IYAGLQSIPQ DLIDAARVDG ADWGRVFLHV EFPLLRPLIL VALVLRIIDC LKTFDIVFMT TWGGPGSATH TYSFYIYKVG ISFGWNIGYA SALSVLLLIV AIVLVNVVFR LVRMRQQLGF GGEE // ID Q9WYF6_THEMA Unreviewed; 67 AA. AC Q9WYF6; G4FHN4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Heavy metal binding protein {ECO:0000313|EMBL:AAD35408.1}; GN OrderedLocusNames=TM_0320 {ECO:0000313|EMBL:AAD35408.1}; GN ORFNames=Tmari_0318 {ECO:0000313|EMBL:AGL49244.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35408.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35408.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35408.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49244.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49244.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35408.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49244.1; -; Genomic_DNA. DR PIR; G72392; G72392. DR RefSeq; NP_228132.1; NC_000853.1. DR RefSeq; WP_004083068.1; NZ_CP011107.1. DR PDB; 2KYZ; NMR; -; A=1-67. DR PDBsum; 2KYZ; -. DR STRING; 243274.TM0320; -. DR DNASU; 897262; -. DR EnsemblBacteria; AAD35408; AAD35408; TM_0320. DR EnsemblBacteria; AGL49244; AGL49244; Tmari_0318. DR GeneID; 897262; -. DR KEGG; tma:TM0320; -. DR KEGG; tmi:THEMA_03125; -. DR KEGG; tmm:Tmari_0318; -. DR KEGG; tmw:THMA_0327; -. DR PATRIC; 23935519; VBITheMar51294_0325. DR eggNOG; ENOG410681U; Bacteria. DR eggNOG; ENOG410XUQ1; LUCA. DR OMA; YPVESYQ; -. DR OrthoDB; EOG6742RM; -. DR BioCyc; TMAR243274:GC6P-333-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR InterPro; IPR017969; Heavy-metal-associated_CS. DR InterPro; IPR006121; HMA_dom. DR Pfam; PF00403; HMA; 1. DR SUPFAM; SSF55008; SSF55008; 1. DR PROSITE; PS01047; HMA_1; 1. DR PROSITE; PS50846; HMA_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2KYZ}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 63 HMA. {ECO:0000259|PROSITE:PS50846}. SQ SEQUENCE 67 AA; 7853 MW; 3CCAF7A84E461987 CRC64; MRYVLYVPDI SCNHCKMRIS KALEELGVKN YEVSVEEKKV VVETENLDSV LKKLEEIDYP VESYQEV // ID Q9WZQ7_THEMA Unreviewed; 314 AA. AC Q9WZQ7; G4FD24; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 106. DE SubName: Full=Enoyl-[acyl-carrier-protein] reductase [FMN] {ECO:0000313|EMBL:AGL49726.1}; DE EC=1.3.1.9 {ECO:0000313|EMBL:AGL49726.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35882.1}; GN OrderedLocusNames=TM_0800 {ECO:0000313|EMBL:AAD35882.1}; GN ORFNames=Tmari_0801 {ECO:0000313|EMBL:AGL49726.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35882.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35882.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35882.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49726.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49726.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35882.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49726.1; -; Genomic_DNA. DR PIR; A72335; A72335. DR RefSeq; NP_228609.1; NC_000853.1. DR RefSeq; WP_004080864.1; NZ_CP011107.1. DR PDB; 3BO9; X-ray; 2.71 A; A/B=1-314. DR PDBsum; 3BO9; -. DR STRING; 243274.TM0800; -. DR EnsemblBacteria; AAD35882; AAD35882; TM_0800. DR EnsemblBacteria; AGL49726; AGL49726; Tmari_0801. DR GeneID; 898468; -. DR KEGG; tma:TM0800; -. DR KEGG; tmm:Tmari_0801; -. DR KEGG; tmw:THMA_0819; -. DR PATRIC; 23936520; VBITheMar51294_0812. DR eggNOG; ENOG4105EA8; Bacteria. DR eggNOG; COG2070; LUCA. DR KO; K02371; -. DR OMA; KECNVHP; -. DR OrthoDB; EOG6K9QD1; -. DR BioCyc; TMAR243274:GC6P-827-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC. DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR017569; Enoyl_ACP_red-II_put. DR InterPro; IPR004136; NMO. DR Pfam; PF03060; NMO; 2. DR TIGRFAMs; TIGR03151; enACPred_II; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3BO9}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49726.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 80 NMO. {ECO:0000259|Pfam:PF03060}. FT DOMAIN 83 299 NMO. {ECO:0000259|Pfam:PF03060}. FT REGION 193 194 Phosphate binding. FT {ECO:0000213|PDB:3BO9}. FT BINDING 143 143 Phosphate. {ECO:0000213|PDB:3BO9}. FT BINDING 280 280 Phosphate. {ECO:0000213|PDB:3BO9}. SQ SEQUENCE 314 AA; 33673 MW; 3321EBCF7647D9B8 CRC64; MTVRTRVTDL LEIEHPILMG GMAWAGTPTL AAAVSEAGGL GIIGSGAMKP DDLRKAISEL RQKTDKPFGV NIILVSPWAD DLVKVCIEEK VPVVTFGAGN PTKYIRELKE NGTKVIPVVA SDSLARMVER AGADAVIAEG MESGGHIGEV TTFVLVNKVS RSVNIPVIAA GGIADGRGMA AAFALGAEAV QMGTRFVASV ESDVHPVYKE KIVKASIRDT VVTGAKLGHP ARVLRTPFAR KIQEMEFENP MQAEEMLVGS LRRAVVEGDL ERGSFMVGQS AGLIDEIKPV KQIIEDILKE FKETVEKLRG YIEE // ID Q9X0R0_THEMA Unreviewed; 279 AA. AC Q9X0R0; G4FEG8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Acetyltransferase-related protein {ECO:0000313|EMBL:AAD36253.1}; DE SubName: Full=Ribosomal-protein-S18p-alanine acetyltransferase {ECO:0000313|EMBL:AGL50109.1}; DE EC=2.3.1.- {ECO:0000313|EMBL:AGL50109.1}; GN OrderedLocusNames=TM_1178 {ECO:0000313|EMBL:AAD36253.1}; GN ORFNames=Tmari_1185 {ECO:0000313|EMBL:AGL50109.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36253.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36253.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36253.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50109.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50109.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36253.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50109.1; -; Genomic_DNA. DR PIR; E72286; E72286. DR RefSeq; NP_228983.1; NC_000853.1. DR RefSeq; WP_004080182.1; NZ_CP011107.1. DR STRING; 243274.TM1178; -. DR EnsemblBacteria; AAD36253; AAD36253; TM_1178. DR EnsemblBacteria; AGL50109; AGL50109; Tmari_1185. DR GeneID; 898308; -. DR KEGG; tma:TM1178; -. DR KEGG; tmi:THEMA_08445; -. DR KEGG; tmm:Tmari_1185; -. DR KEGG; tmw:THMA_1203; -. DR PATRIC; 23937296; VBITheMar51294_1196. DR eggNOG; ENOG4108U2R; Bacteria. DR eggNOG; COG0456; LUCA. DR OMA; NWQREPI; -. DR OrthoDB; EOG661H8F; -. DR BioCyc; TMAR243274:GC6P-1207-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031248; C:protein acetyltransferase complex; IBA:GO_Central. DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IBA:GO_Central. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000313|EMBL:AGL50109.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL50109.1}. FT DOMAIN 1 153 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 279 AA; 32396 MW; 0F71EB0D43006C86 CRC64; MTIKKASEVS VIDLVNLVNE IFKDYAVPVN WDVYNFNLDV RENSISLDDS FVFFENDVPV GFILLCIRKD RGRIDSMGVI KPKRGTGLAD MILKHALEHL MWKGVKSVVL EVVADDQRAV RFYEKNGFKK RRELYSYFFD RRIDGTGSVK FFETDEKRIH MYALKARTDF KRNPNWQREC TTLLLADGRY RMERASWRDG EGYLVWGETP QSVFIVDAFA LRGSMDEFIR ECVDHIQKES GKTAVTCTAV PEDDPLSRSL EVNGFQRVLV QYEMELKLS // ID Q9X1V7_THEMA Unreviewed; 154 AA. AC Q9X1V7; G4FG11; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36689.1}; GN OrderedLocusNames=TM_1622 {ECO:0000313|EMBL:AAD36689.1}; GN ORFNames=Tmari_1631 {ECO:0000313|EMBL:AGL50555.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36689.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36689.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36689.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50555.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50555.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36689.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50555.1; -; Genomic_DNA. DR PIR; H72232; H72232. DR RefSeq; NP_229422.1; NC_000853.1. DR RefSeq; WP_004082092.1; NZ_CP011107.1. DR PDB; 1VR8; X-ray; 1.75 A; A=25-154. DR PDBsum; 1VR8; -. DR STRING; 243274.TM1622; -. DR EnsemblBacteria; AAD36689; AAD36689; TM_1622. DR EnsemblBacteria; AGL50555; AGL50555; Tmari_1631. DR GeneID; 897930; -. DR KEGG; tma:TM1622; -. DR KEGG; tmi:THEMA_06135; -. DR KEGG; tmm:Tmari_1631; -. DR KEGG; tmw:THMA_1663; -. DR PATRIC; 23938218; VBITheMar51294_1641. DR eggNOG; ENOG4106FKE; Bacteria. DR eggNOG; ENOG410Y3SN; LUCA. DR OMA; LPNMGKF; -. DR OrthoDB; EOG6KHG0W; -. DR BioCyc; TMAR243274:GC6P-1668-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR021636; DUF3242. DR Pfam; PF11586; DUF3242; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VR8}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 154 AA; 17843 MW; 983013F73543A6F6 CRC64; MRRSLFLVVV LLMLSSCTLI KIVVPPEAYS LDTAIFVLET RDYRLSDVKE IDSYGDVEMK GKVAVFETEY GPVFLYVYKG EEAKKIWKKL NGRAGFVSIR SVLDLPNMGK FSTVSNGKKI VAWWRKNWLF IVEGKNGVEE FVKHVYRVYE EMKQ // ID Q9WY09_THEMA Unreviewed; 771 AA. AC Q9WY09; G4FH76; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Alpha/beta-Hydrolase {ECO:0000313|EMBL:AGL49086.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35255.1}; GN OrderedLocusNames=TM_0162 {ECO:0000313|EMBL:AAD35255.1}; GN ORFNames=Tmari_0160 {ECO:0000313|EMBL:AGL49086.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35255.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35255.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35255.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49086.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49086.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35255.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49086.1; -; Genomic_DNA. DR PIR; H72410; H72410. DR RefSeq; NP_227977.1; NC_000853.1. DR RefSeq; WP_004082785.1; NZ_CP011107.1. DR STRING; 243274.TM0162; -. DR EnsemblBacteria; AAD35255; AAD35255; TM_0162. DR EnsemblBacteria; AGL49086; AGL49086; Tmari_0160. DR GeneID; 897001; -. DR KEGG; tma:TM0162; -. DR KEGG; tmi:THEMA_03990; -. DR KEGG; tmm:Tmari_0160; -. DR KEGG; tmw:THMA_0158; -. DR PATRIC; 23935172; VBITheMar51294_0163. DR eggNOG; ENOG4108PU6; Bacteria. DR eggNOG; ENOG410ZMSF; LUCA. DR OMA; LYRVEFA; -. DR OrthoDB; EOG6GJBPH; -. DR BioCyc; TMAR243274:GC6P-163-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 2. DR InterPro; IPR029058; AB_hydrolase. DR SUPFAM; SSF53474; SSF53474; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49086.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 16 35 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 771 AA; 87499 MW; EBB5D3781852AA1D CRC64; MSFLKKLLEI VLKRKILFFT LVFISITVFF LLIFFQKEGS LKIGKEGAES GFINLRVEIP PGAFGKQKVL KITRLSDEER KLYPDVFVGD LYRVEFADGV DEFALKPIRL KYYFDAKYLR GENYNNLTFA YATEDGGYRI IPGSMIGKDE RGYYVEAFTY HLSVFGVVLR SAGFQKHGIR LLREAVNSSG PAVLLVPGED PTFEGVVKDN NIWETIFPDR TIMTYEYALY EPRSLAYSEM YRSFIEKEGR RSFIDFESDF LSQEILKYSQ YEFDILAHGT GGLIVLRMLQ RHPEVNNVRK VVLLSTPVQG TNVVNPLYFS SIFYGKDPEV LEDIFGIEWT KLKMLTLHIR NLIDTLGEVV QEILPDSQLV KELGGFSRND VEIVSICGDT PPYGVDVSGT ELERFYPEFV KGRGDGFVSI QSCRVGKVEQ LSGNFYDLYS REENVAYIRE LLKYEVQVFS GFRSDDYEEY LPSKNPELSE ESAQKVVEVK ETEGTEFPVL PVNILFENFL ERIRSLELSS YLSGALVGKE VYIATESGVF AWDKKVLDKK IEFFKKIEDY ASFVGEGDIF IIDNIGIKKY APFPLVGDIS DALITRNAII YARVVPGGVR YYLFRNGAEK LIATSPGTTV RMKSENGNYL LITDGEVVAI GSDFKEKGRV LSSLFGEKVK IVDASFKDDA FYILLNDGSI AFVSSSRSET KNYGLAVPKK VLNFQGRILV VYDGVILDLS AGKAQRFDRG IIDVFPGNES LFIVFDEKVR VSVEEWWLSK D // ID Q9X0Z0_THEMA Unreviewed; 275 AA. AC Q9X0Z0; G4FE85; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE SubName: Full=Phosphate ABC transporter, permease protein {ECO:0000313|EMBL:AAD36337.1}; DE SubName: Full=Phosphate transport system permease protein PstC {ECO:0000313|EMBL:AGL50192.1}; GN OrderedLocusNames=TM_1263 {ECO:0000313|EMBL:AAD36337.1}; GN ORFNames=Tmari_1268 {ECO:0000313|EMBL:AGL50192.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36337.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36337.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36337.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50192.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50192.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36337.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50192.1; -; Genomic_DNA. DR PIR; B72276; B72276. DR RefSeq; NP_229068.1; NC_000853.1. DR RefSeq; WP_004079995.1; NZ_CP011107.1. DR STRING; 243274.TM1263; -. DR DNASU; 898220; -. DR EnsemblBacteria; AAD36337; AAD36337; TM_1263. DR EnsemblBacteria; AGL50192; AGL50192; Tmari_1268. DR GeneID; 898220; -. DR KEGG; tma:TM1263; -. DR KEGG; tmm:Tmari_1268; -. DR KEGG; tmw:THMA_1288; -. DR PATRIC; 23937466; VBITheMar51294_1279. DR eggNOG; ENOG4105C8U; Bacteria. DR eggNOG; COG0573; LUCA. DR KO; K02037; -. DR OMA; NDHIEAS; -. DR OrthoDB; EOG6TJ81W; -. DR BioCyc; TMAR243274:GC6P-1294-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GOC. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 50 78 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 99 119 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 131 151 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 199 216 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 243 265 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 56 266 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 275 AA; 29508 MW; 187E8959D5ABB4DF CRC64; MIVALSGTGI LALFLLVFFL IREAWPALVE IGGELFTSIY WYPTADPPEY GMLAMIAGTL LLTAFSSAVL LPLGYLIAFF LHTYAKDFEK NLIRTTVEFL AGTPSVIIGL FVLLYIAPIL LNFDVWSTEN FLLASIGLIL TALPYTVSLS LEALDSVDVA LEESALALGA TRFTTVFKVT TRAALPGILN AFVLTVNRVV GETMIVLMAG GGAAIIPRSF FDPVKPLTAA IASEIGEVAV GSMHYHVLFA AGVILLVISL VLTGLSRYIS GRQTR // ID Q9X2A9_THEMA Unreviewed; 101 AA. AC Q9X2A9; G4FGH6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36852.1}; GN OrderedLocusNames=TM_1789 {ECO:0000313|EMBL:AAD36852.1}; GN ORFNames=Tmari_1798 {ECO:0000313|EMBL:AGL50722.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36852.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36852.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36852.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50722.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50722.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36852.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50722.1; -; Genomic_DNA. DR PIR; H72211; H72211. DR RefSeq; NP_229586.1; NC_000853.1. DR RefSeq; WP_004082335.1; NZ_CP011107.1. DR STRING; 243274.TM1789; -. DR EnsemblBacteria; AAD36852; AAD36852; TM_1789. DR EnsemblBacteria; AGL50722; AGL50722; Tmari_1798. DR GeneID; 897840; -. DR KEGG; tma:TM1789; -. DR KEGG; tmi:THEMA_05250; -. DR KEGG; tmm:Tmari_1798; -. DR KEGG; tmw:THMA_1834; -. DR PATRIC; 23938565; VBITheMar51294_1809. DR OMA; LYEVPAT; -. DR OrthoDB; EOG6KT2SC; -. DR BioCyc; TMAR243274:GC6P-1840-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 101 AA; 11675 MW; 5F3BDD64B96B7660 CRC64; MIFVGDVSTL DMCRRDHAGE IKLKDVLTKN EGLQRLQKLR WWYLYEVPAT IAGLAVPAAK RVKTELKTPS DLWILIDNKW LVFHIEAEKK PIKRSEPSTS Q // ID Q9X1A1_THEMA Unreviewed; 129 AA. AC Q9X1A1; G4FFB7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36451.1}; GN OrderedLocusNames=TM_1381 {ECO:0000313|EMBL:AAD36451.1}; GN ORFNames=Tmari_1388 {ECO:0000313|EMBL:AGL50312.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36451.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36451.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36451.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50312.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50312.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36451.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50312.1; -; Genomic_DNA. DR PIR; F72261; F72261. DR RefSeq; NP_229182.1; NC_000853.1. DR RefSeq; WP_004081579.1; NZ_CP011107.1. DR STRING; 243274.TM1381; -. DR EnsemblBacteria; AAD36451; AAD36451; TM_1381. DR EnsemblBacteria; AGL50312; AGL50312; Tmari_1388. DR GeneID; 898097; -. DR KEGG; tma:TM1381; -. DR KEGG; tmi:THEMA_07420; -. DR KEGG; tmm:Tmari_1388; -. DR KEGG; tmw:THMA_1408; -. DR PATRIC; 23937704; VBITheMar51294_1393. DR eggNOG; ENOG4105XBM; Bacteria. DR eggNOG; ENOG41124Q9; LUCA. DR OMA; VKYEHEL; -. DR OrthoDB; EOG66B453; -. DR BioCyc; TMAR243274:GC6P-1416-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 129 AA; 15516 MW; AF1FDB4EAC007E54 CRC64; MKKGEKILSF VKQEKELIED YRKSLHDVKR SDEVGDVFIE FALKFLEKVL EDFKPEEYTE DIAFEPEKES YTLSERLKER IGEDLLKKSD LPAILQRFCE MAAHRWKQLK ADEEKTDFFK RPGHEMRRD // ID Q9X2E2_THEMA Unreviewed; 308 AA. AC Q9X2E2; G4FGK9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=FtsH protease activity modulator HflK {ECO:0000313|EMBL:AAD36885.1}; DE SubName: Full=HflK protein {ECO:0000313|EMBL:AGL50756.1}; GN OrderedLocusNames=TM_1822 {ECO:0000313|EMBL:AAD36885.1}; GN ORFNames=Tmari_1832 {ECO:0000313|EMBL:AGL50756.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36885.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36885.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36885.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50756.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50756.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36885.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50756.1; -; Genomic_DNA. DR PIR; A72207; A72207. DR RefSeq; NP_229619.1; NC_000853.1. DR RefSeq; WP_004082368.1; NZ_CP011107.1. DR STRING; 243274.TM1822; -. DR EnsemblBacteria; AAD36885; AAD36885; TM_1822. DR EnsemblBacteria; AGL50756; AGL50756; Tmari_1832. DR GeneID; 897422; -. DR KEGG; tma:TM1822; -. DR KEGG; tmi:THEMA_05085; -. DR KEGG; tmm:Tmari_1832; -. DR KEGG; tmw:THMA_1867; -. DR PATRIC; 23938631; VBITheMar51294_1842. DR eggNOG; ENOG4107VGJ; Bacteria. DR eggNOG; COG0330; LUCA. DR KO; K04088; -. DR OMA; DKEREIN; -. DR OrthoDB; EOG6J48MH; -. DR BioCyc; TMAR243274:GC6P-1873-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR001107; Band_7. DR InterPro; IPR010201; HflK. DR InterPro; IPR001972; Stomatin_fam. DR PANTHER; PTHR10264; PTHR10264; 2. DR PANTHER; PTHR10264:SF51; PTHR10264:SF51; 2. DR Pfam; PF01145; Band_7; 1. DR PRINTS; PR00721; STOMATIN. DR SMART; SM00244; PHB; 1. DR SUPFAM; SSF117892; SSF117892; 1. DR TIGRFAMs; TIGR01933; hflK; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD36885.1}; KW Protease {ECO:0000313|EMBL:AAD36885.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 19 198 PHB. {ECO:0000259|SMART:SM00244}. FT COILED 190 217 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 308 AA; 34778 MW; ADE03603E5101A9D CRC64; MRKYVWIVVF IVLGIYFLTG VYQVGPSEVA LLKTFGRFTS VVPSGIHYHL PYPIQSHVTV DVTTVRKIEI GFRSIQRGER ISYQSVPQEA IMITGDNNLV SVEAVVQYRV KDPVAYAFNI TEADSIVRFT TESVLREKVA MRSIDDVLTS GRDEIGFKTA QMLQEILDSY NCGIKVENVY LQEVVPPDPV VDAFDDVNNA RQDKERLINE ARKYANDVVP KAQGQAQEIL RQAEAYAQEV YLKALGEAKR FEEVLEEYSK APDITRKRML LDALQSLLEK SENKVFFVGN GDSLNILNIS DLLKGMGK // ID Q9X0G2_THEMA Unreviewed; 476 AA. AC Q9X0G2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Rhamnulokinase {ECO:0000313|EMBL:AGL50001.1}; DE EC=2.7.1.5 {ECO:0000313|EMBL:AGL50001.1}; DE SubName: Full=Sugar kinase {ECO:0000313|EMBL:AAD36150.1}; GN OrderedLocusNames=TM_1073 {ECO:0000313|EMBL:AAD36150.1}; GN ORFNames=Tmari_1077 {ECO:0000313|EMBL:AGL50001.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36150.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36150.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36150.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50001.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50001.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36150.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50001.1; -; Genomic_DNA. DR PIR; C72299; C72299. DR RefSeq; NP_228879.1; NC_000853.1. DR RefSeq; WP_010865260.1; NZ_CP011107.1. DR STRING; 243274.TM1073; -. DR EnsemblBacteria; AAD36150; AAD36150; TM_1073. DR EnsemblBacteria; AGL50001; AGL50001; Tmari_1077. DR GeneID; 898732; -. DR KEGG; tma:TM1073; -. DR KEGG; tmi:THEMA_08995; -. DR KEGG; tmm:Tmari_1077; -. DR KEGG; tmw:THMA_1095; -. DR PATRIC; 23937075; VBITheMar51294_1086. DR eggNOG; ENOG4105DET; Bacteria. DR eggNOG; COG1070; LUCA. DR KO; K00848; -. DR OMA; HETREWT; -. DR OrthoDB; EOG6K9QGW; -. DR BioCyc; TMAR243274:GC6P-1102-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central. DR GO; GO:0008993; F:rhamnulokinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR GO; GO:0019301; P:rhamnose catabolic process; IBA:GO_Central. DR InterPro; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000313|EMBL:AAD36150.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD36150.1}. FT DOMAIN 6 236 FGGY_N. {ECO:0000259|Pfam:PF00370}. FT DOMAIN 246 429 FGGY_C. {ECO:0000259|Pfam:PF02782}. SQ SEQUENCE 476 AA; 54058 MW; EEB95AF922DA8DE4 CRC64; MAVKVLSIDL GATNGKIYEV ELKDRLTVKE IKRFRTEGTF LPGKDREHFV WNLPGFYEEI KGVLEASDAQ SVGVDTWGVD FALLDENGRL VSLPYHYRDV RTKGVMKKAF EVVPKDEIFQ RTGIQFMEIN TLYQLYSMVL SNDPFLKTTK HLLMIPDVFN FWLSGEMVSE YTIASTSQCY SVPDGEWAYD LLEKLSIPTE IFPKVVPPGT ILGKCRVKKG INVIATACHD TASAVVAVPL EGEGIYISSG TWFLVGTELE RPLLSKEALE RNFTNEGGYG KIRFLKNATG MWLLEECNRI WKKDYSEIIE SVRNVPGFQA FLDPDREEFL HPGNMPERIR NYLERTGQKI LERIGEISRL IFESLAFNCR WIVEQIKELT GKRYGKIHVV GGAVRNDLLM SFIASATGKT VVAGPVDATP IGNALVQLIT LGAIANINEA RKIVKESFEL KTFEPKNPEL WSEKYEEWRR YKGMRV // ID Q9WYG5_THEMA Unreviewed; 434 AA. AC Q9WYG5; G4FHP3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Exoenzymes regulatory protein aepA {ECO:0000313|EMBL:AGL49253.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35417.1}; GN OrderedLocusNames=TM_0330 {ECO:0000313|EMBL:AAD35417.1}; GN ORFNames=Tmari_0328 {ECO:0000313|EMBL:AGL49253.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35417.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35417.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35417.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49253.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49253.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35417.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49253.1; -; Genomic_DNA. DR PIR; D72390; D72390. DR RefSeq; NP_228141.1; NC_000853.1. DR RefSeq; WP_004083093.1; NZ_CP011107.1. DR STRING; 243274.TM0330; -. DR EnsemblBacteria; AAD35417; AAD35417; TM_0330. DR EnsemblBacteria; AGL49253; AGL49253; Tmari_0328. DR GeneID; 897281; -. DR KEGG; tma:TM0330; -. DR KEGG; tmi:THEMA_03070; -. DR KEGG; tmm:Tmari_0328; -. DR KEGG; tmw:THMA_0338; -. DR PATRIC; 23935541; VBITheMar51294_0335. DR eggNOG; ENOG410825R; Bacteria. DR eggNOG; COG1574; LUCA. DR KO; K07047; -. DR OMA; HSDDFHG; -. DR OrthoDB; EOG6CS03W; -. DR BioCyc; TMAR243274:GC6P-344-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR Gene3D; 2.30.40.10; -; 2. DR InterPro; IPR013108; Amidohydro_3. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF07969; Amidohydro_3; 1. DR SUPFAM; SSF51338; SSF51338; 2. DR SUPFAM; SSF51556; SSF51556; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 34 424 Amidohydro_3. {ECO:0000259|Pfam:PF07969}. SQ SEQUENCE 434 AA; 49561 MW; A79CA827A70F8BEB CRC64; MIIKGALVWS GKEFVQKDLF VENGEFVEKS SEPVIDAKGY FLVPGFVDSH AHVVGTGFSK LSVQFNDWDE LFERDLTSEV VVGRGWFEEP DGSVVERLDR IEAPVFLIRR CGHKAFLNKK AMEVLGVEER YLVENLEKIY EYVFKEKIAE FYRVGEEEFL KHGVTFVQSD DLYGVSVERL LSIIKHSRIR LFEKLKPKDL KPEHFGDLNK RVHVKGVKVF MDGSLGAKTA LISGEYDDGT QGVQLLTEEK LEELARFCDE HDLILNVHAI GDSAVSLVLD VLERHRGHRI IHAQFVQEKD LQRVKNTTFS VQPHFFFEDQ PLLKKVKVNA LHYPFYRMFK AGVSISFSSD SPVSPCDPKY IAEHALKMGF SREETFYLMT EAGASQVGIK TGKIEAGYRA DFCLYERNPL LFEDDPIAVF VEGEKIYEKN GSSH // ID Q9X1M3_THEMA Unreviewed; 441 AA. AC Q9X1M3; G4FFS5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 102. DE SubName: Full=Mg-protoporphyrin IX monomethyl ester oxidative cyclase-related protein {ECO:0000313|EMBL:AAD36604.1}; DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:AGL50469.1}; GN OrderedLocusNames=TM_1537 {ECO:0000313|EMBL:AAD36604.1}; GN ORFNames=Tmari_1545 {ECO:0000313|EMBL:AGL50469.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36604.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36604.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36604.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50469.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50469.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36604.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50469.1; -; Genomic_DNA. DR PIR; E72242; E72242. DR RefSeq; NP_229337.1; NC_000853.1. DR RefSeq; WP_004081919.1; NZ_CP011107.1. DR STRING; 243274.TM1537; -. DR EnsemblBacteria; AAD36604; AAD36604; TM_1537. DR EnsemblBacteria; AGL50469; AGL50469; Tmari_1545. DR GeneID; 897385; -. DR KEGG; tma:TM1537; -. DR KEGG; tmi:THEMA_06600; -. DR KEGG; tmm:Tmari_1545; -. DR KEGG; tmw:THMA_1571; -. DR PATRIC; 23938034; VBITheMar51294_1555. DR eggNOG; ENOG4105EPH; Bacteria. DR eggNOG; COG1032; LUCA. DR KO; K04034; -. DR OMA; AMSKAGC; -. DR OrthoDB; EOG647TTV; -. DR BioCyc; TMAR243274:GC6P-1577-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR PROSITE; PS51332; B12_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 135 B12-binding. FT {ECO:0000259|PROSITE:PS51332}. SQ SEQUENCE 441 AA; 51039 MW; D096EC15A46A04D8 CRC64; MRVLLINPYS GGYYYRLGAV YPPLGLMYIS SSLKRKGHSV ALIDMNVEKF DLERFNFRDY DVVGISADTV RFPVVERIAK KAKAQNVTVV MGGPHATAYY HEILQKGLCD YVVLGEGERA FSDLVESIAS NEKYPLIPGV AYMKDGEVIA LPSRFLENLD DLPFPDREKV HLYRTKFAGE RATSLITSRG CPFNCEFCSA SQFMGRRIRW RSIENVIDEL KILKKLGYGS VIFFDDNFTI NPKRVVNLCE EMMRKDLRFK WWAFSRADEL LGREDMVEAM SKAGCRMLFI GFESANDEVL EEYGKNLKSD IAFDVMKLLK KYKVDVFASF VIGALKDTRK TIEKTVKFAK KLKASIVQFS ILTPYPGTAL FEKLKHLIFE KDWRKFDGTH LVFKHPNFSP KELRRLFIKA YYAVYTSPRL IFRRGIPFLV RLLFYREAYF L // ID Q9WZ83_THEMA Unreviewed; 116 AA. AC Q9WZ83; G4FDK7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Nucleotidyltransferase {ECO:0000313|EMBL:AGL49539.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35699.1}; GN OrderedLocusNames=TM_0614 {ECO:0000313|EMBL:AAD35699.1}; GN ORFNames=Tmari_0614 {ECO:0000313|EMBL:AGL49539.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35699.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35699.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35699.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49539.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49539.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35699.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49539.1; -; Genomic_DNA. DR PIR; B72356; B72356. DR RefSeq; NP_228424.1; NC_000853.1. DR RefSeq; WP_004081204.1; NZ_CP011107.1. DR STRING; 243274.TM0614; -. DR EnsemblBacteria; AAD35699; AAD35699; TM_0614. DR EnsemblBacteria; AGL49539; AGL49539; Tmari_0614. DR GeneID; 897697; -. DR KEGG; tma:TM0614; -. DR KEGG; tmi:THEMA_01595; -. DR KEGG; tmm:Tmari_0614; -. DR KEGG; tmw:THMA_0630; -. DR PATRIC; 23936141; VBITheMar51294_0624. DR eggNOG; ENOG4106CNH; Bacteria. DR eggNOG; COG1708; LUCA. DR KO; K07076; -. DR OMA; LSEYKQM; -. DR OrthoDB; EOG69WFP8; -. DR BioCyc; TMAR243274:GC6P-639-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49539.1}. FT DOMAIN 27 100 NTP_transf_2. {ECO:0000259|Pfam:PF01909}. SQ SEQUENCE 116 AA; 13407 MW; D31759EABC956632 CRC64; MLKRSSDSAK IFYPEYKREK VLGIIRNSLP QLLKKLPVRL VVLFGSYAKG NFTVFSDVDL LVVYEDPFRE DAYKIVKRTI KLKGLEPHVY SLSEYKQMEK TISKMIEGGV VVYKAL // ID Q9X0Z3_THEMA Unreviewed; 82 AA. AC Q9X0Z3; G4FE82; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36341.1}; GN OrderedLocusNames=TM_1266 {ECO:0000313|EMBL:AAD36341.1}; GN ORFNames=Tmari_1271 {ECO:0000313|EMBL:AGL50195.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36341.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36341.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36341.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50195.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50195.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36341.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50195.1; -; Genomic_DNA. DR PIR; A72274; A72274. DR RefSeq; NP_229071.1; NC_000853.1. DR RefSeq; WP_004079987.1; NZ_CP011107.1. DR PDB; 2NZC; X-ray; 1.95 A; A/B/C/D=1-82. DR PDBsum; 2NZC; -. DR STRING; 243274.TM1266; -. DR EnsemblBacteria; AAD36341; AAD36341; TM_1266. DR EnsemblBacteria; AGL50195; AGL50195; Tmari_1271. DR GeneID; 898217; -. DR KEGG; tma:TM1266; -. DR KEGG; tmi:THEMA_08005; -. DR KEGG; tmm:Tmari_1271; -. DR KEGG; tmw:THMA_1291; -. DR PATRIC; 23937472; VBITheMar51294_1282. DR eggNOG; ENOG41084A3; Bacteria. DR eggNOG; ENOG410ZXK0; LUCA. DR OMA; EIIVGRM; -. DR OrthoDB; EOG6VQPXS; -. DR BioCyc; TMAR243274:GC6P-1297-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR023860; FeFe-hyd_TM1266. DR TIGRFAMs; TIGR03959; hyd_TM1266; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2NZC}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT BINDING 23 23 Phosphate. {ECO:0000213|PDB:2NZC}. FT BINDING 36 36 Phosphate. {ECO:0000213|PDB:2NZC}. SQ SEQUENCE 82 AA; 9462 MW; 9299898BD7394194 CRC64; MEKRFYILTI VVEDREKAYR QVNELLHNFS EDILLRVGYP VREENMAIIF LVLKTDNDTI GALSGKLGQI SGVRVKTVPL KR // ID Q9WYC0_THEMA Unreviewed; 506 AA. AC Q9WYC0; G4FHJ8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE SubName: Full=Alternative Ribulokinase {ECO:0000313|EMBL:AGL49208.1}; DE EC=2.7.1.16 {ECO:0000313|EMBL:AGL49208.1}; DE SubName: Full=Sugar kinase, FGGY family {ECO:0000313|EMBL:AAD35372.1}; GN OrderedLocusNames=TM_0284 {ECO:0000313|EMBL:AAD35372.1}; GN ORFNames=Tmari_0282 {ECO:0000313|EMBL:AGL49208.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35372.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35372.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35372.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49208.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49208.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the FGGY kinase family. CC {ECO:0000256|RuleBase:RU003733}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35372.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49208.1; -; Genomic_DNA. DR PIR; B72396; B72396. DR RefSeq; NP_228096.1; NC_000853.1. DR RefSeq; WP_004082994.1; NZ_CP011107.1. DR STRING; 243274.TM0284; -. DR EnsemblBacteria; AAD35372; AAD35372; TM_0284. DR EnsemblBacteria; AGL49208; AGL49208; Tmari_0282. DR GeneID; 897202; -. DR KEGG; tma:TM0284; -. DR KEGG; tmi:THEMA_03305; -. DR KEGG; tmm:Tmari_0282; -. DR KEGG; tmw:THMA_0291; -. DR PATRIC; 23935447; VBITheMar51294_0289. DR eggNOG; ENOG4105CMG; Bacteria. DR eggNOG; COG1070; LUCA. DR KO; K00854; -. DR OMA; SDLWMQI; -. DR OrthoDB; EOG6S52KR; -. DR BioCyc; TMAR243274:GC6P-297-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central. DR GO; GO:0008741; F:ribulokinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000256|SAAS:SAAS00430777, KW ECO:0000313|EMBL:AAD35372.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU003733, KW ECO:0000256|SAAS:SAAS00430777, ECO:0000313|EMBL:AAD35372.1}. FT DOMAIN 2 248 FGGY_N. {ECO:0000259|Pfam:PF00370}. FT DOMAIN 261 454 FGGY_C. {ECO:0000259|Pfam:PF02782}. SQ SEQUENCE 506 AA; 56750 MW; E011F35DD4AED355 CRC64; MYLIGSDIGT QGTKSVIVNE KGEVLAEAFR EYEVITPKPN WAEQWPDVWV KAVFETVKEV VEKSGVSKKE IAGIAISGLY GGSGIPVDRN MQPLRPCLIW MDRRAVKETE WVKQNVPKEK LFEITGNYVD SYFGFTKIMW IRNNEPEIWE KIYKFITPKD YVIYQMTGEV VIDYSSAGNL GGVFDIRKLT WSKEMCDVLG IPIEFLPERI VKSSDVVGRV TKEASELCGL LEGTPVVAGG IDAPVAQLSA GALEEGEHVA MVGTSTCWGT VHDGSKLAFG LVNYPYVVYD TERIYTFGGS ATTGALARWF KEQFGESETI VGERTGISPY QLFDKEVANI PAGSEGIIVL PYFMGERSPI WDPTARGVFF GVTLYHKRAH LYRALMEGGA YALRHNMEEG LKAGLKLNDE CWIVGGVSKS SVWVKIFADV TGFKMRQVAS LVEAPYGDAF LAGLGTGVID KPERIKEWVK YRDPVEPDPE NKKIYDRYYE IYRELYERTK DLMARL // ID Q9WZ77_THEMA Unreviewed; 236 AA. AC Q9WZ77; G4FDL1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Putative preQ0 transporter {ECO:0000313|EMBL:AGL49533.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35693.1}; GN OrderedLocusNames=TM_0608 {ECO:0000313|EMBL:AAD35693.1}; GN ORFNames=Tmari_0608 {ECO:0000313|EMBL:AGL49533.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35693.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35693.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35693.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49533.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49533.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35693.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49533.1; -; Genomic_DNA. DR PIR; D72355; D72355. DR RefSeq; NP_228418.1; NC_000853.1. DR RefSeq; WP_004081219.1; NZ_CP011107.1. DR STRING; 243274.TM0608; -. DR EnsemblBacteria; AAD35693; AAD35693; TM_0608. DR EnsemblBacteria; AGL49533; AGL49533; Tmari_0608. DR GeneID; 897689; -. DR KEGG; tma:TM0608; -. DR KEGG; tmi:THEMA_01625; -. DR KEGG; tmm:Tmari_0608; -. DR KEGG; tmw:THMA_0624; -. DR PATRIC; 23936131; VBITheMar51294_0619. DR eggNOG; ENOG4108PKW; Bacteria. DR eggNOG; COG1738; LUCA. DR KO; K09125; -. DR OMA; EDWAHEH; -. DR OrthoDB; EOG60CWR6; -. DR BioCyc; TMAR243274:GC6P-633-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003744; DUF165. DR Pfam; PF02592; Vut_1; 1. DR TIGRFAMs; TIGR00697; TIGR00697; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 50 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 87 110 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 122 144 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 202 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 236 AA; 27124 MW; 8848B1E74C6958F1 CRC64; MLVNWMFLGL EYLVGVLLVF FAIRFFGLKG MYALGAILVL YMNVAVLKAY ELFPGVQLYA GVFLGPFFVT LIAIVTEVYG YREAQKLVAV GFFAQVVFLV GMLIALGYIP SSEDWAHEHM KALFLPVWRT TLFSWLAFVV SGIFKARFQD FLKRTKGLFG KHLWLRDNTA TKLAQLVDNV IFFYGALTGY FSLRTITVFL IWTTLFEWLF DYLDTWVVVK GVGWMLNSSE PYLQKE // ID Q9WY80_THEMA Unreviewed; 180 AA. AC Q9WY80; G4FHF2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35329.1}; GN OrderedLocusNames=TM_0238 {ECO:0000313|EMBL:AAD35329.1}; GN ORFNames=Tmari_0236 {ECO:0000313|EMBL:AGL49162.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35329.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35329.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35329.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49162.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49162.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35329.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49162.1; -; Genomic_DNA. DR PIR; H72402; H72402. DR RefSeq; NP_228052.1; NC_000853.1. DR RefSeq; WP_004082938.1; NZ_CP011107.1. DR STRING; 243274.TM0238; -. DR EnsemblBacteria; AAD35329; AAD35329; TM_0238. DR EnsemblBacteria; AGL49162; AGL49162; Tmari_0236. DR GeneID; 897138; -. DR KEGG; tma:TM0238; -. DR KEGG; tmi:THEMA_03535; -. DR KEGG; tmm:Tmari_0236; -. DR KEGG; tmw:THMA_0245; -. DR PATRIC; 23935351; VBITheMar51294_0241. DR eggNOG; ENOG41066G0; Bacteria. DR eggNOG; ENOG4112AKR; LUCA. DR OMA; WKDREIV; -. DR OrthoDB; EOG6QK4TB; -. DR BioCyc; TMAR243274:GC6P-251-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR029017; Enolase_N-like. DR SUPFAM; SSF54826; SSF54826; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 180 AA; 21216 MW; C4F4596A7624F2B3 CRC64; MILTYHLEKW KDREIVKVEL MEDEFKGGST IVPERSLGEH YKIFVAVLEE YEGILKEAKS SQIFGLFERL EAHFPEHPKV LFSLSCAMLE LFSRRYGVRL EEMFDLPDFE PEELDFPSGD FLIFPEMIGH VLRVMGFMSA MRSFGERVYL VVREYPDSNT NFIVDLLKKL SDGFIEEKWR // ID Q9X038_THEMA Unreviewed; 304 AA. AC Q9X038; G4FF50; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 104. DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028}; DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028}; GN OrderedLocusNames=TM_0940 {ECO:0000313|EMBL:AAD36021.1}; GN ORFNames=Tmari_0942 {ECO:0000313|EMBL:AGL49867.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36021.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36021.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36021.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49867.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49867.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil. CC {ECO:0000256|RuleBase:RU362028}. CC -!- CATALYTIC ACTIVITY: RNA uridine = RNA pseudouridine. CC {ECO:0000256|RuleBase:RU362028}. CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family. CC {ECO:0000256|RuleBase:RU362028}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36021.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49867.1; -; Genomic_DNA. DR PIR; D72316; D72316. DR RefSeq; NP_228748.1; NC_000853.1. DR RefSeq; WP_004080622.1; NZ_CP011107.1. DR STRING; 243274.TM0940; -. DR EnsemblBacteria; AAD36021; AAD36021; TM_0940. DR EnsemblBacteria; AGL49867; AGL49867; Tmari_0942. DR GeneID; 898615; -. DR KEGG; tma:TM0940; -. DR KEGG; tmi:THEMA_09650; -. DR KEGG; tmm:Tmari_0942; -. DR KEGG; tmw:THMA_0962; -. DR PATRIC; 23936811; VBITheMar51294_0954. DR eggNOG; ENOG4105EI2; Bacteria. DR eggNOG; COG0564; LUCA. DR KO; K06179; -. DR OMA; FAIVNDQ; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; TMAR243274:GC6P-970-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR006225; PsdUridine_synth_RluC/D. DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00005; rluA_subfam; 1. DR PROSITE; PS01129; PSI_RLU; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000256|RuleBase:RU362028}; KW Lyase {ECO:0000313|EMBL:AGL49867.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 12 92 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 304 AA; 35750 MW; F5AE2B1418DE0443 CRC64; MRMEVTRENF YRRLDKFLRN QLKDVPLSVI YKLIRKGKVY VNRKRVKDPS FDLEEGDVVE LRYVNLENLP KRSEKKDLTP VPMKLDVLYE DDHYLVLNKP PNIAIHPGKG VHVATLIEGL LYYGQEKGFS PFLVHRLDKE TSGLLVVAKN REAARILTEL FKGRNIEKEY VTLVRGVPEN NMKITIPLDG QEAVSEIVSV KPLKDVSLLR VKIHTGRKHQ IRRHLSQIGF PVVGDDTYGD RHFNREFRKR YGLKRQFLHS YRMKFIDPWT EEEKDFRAPL PDDLLSVLNL LEERSDEWLE EFLS // ID Q9X0K2_THEMA Unreviewed; 368 AA. AC Q9X0K2; G4FEN0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36194.1}; GN OrderedLocusNames=TM_1118 {ECO:0000313|EMBL:AAD36194.1}; GN ORFNames=Tmari_1124 {ECO:0000313|EMBL:AGL50048.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36194.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36194.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36194.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50048.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50048.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36194.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50048.1; -; Genomic_DNA. DR PIR; C72292; C72292. DR RefSeq; NP_228924.1; NC_000853.1. DR RefSeq; WP_004080302.1; NZ_CP011107.1. DR STRING; 243274.TM1118; -. DR TCDB; 9.B.161.1.1; the putative beta barrrel porin-6 (bbp6) family. DR EnsemblBacteria; AAD36194; AAD36194; TM_1118. DR EnsemblBacteria; AGL50048; AGL50048; Tmari_1124. DR GeneID; 898646; -. DR KEGG; tma:TM1118; -. DR KEGG; tmi:THEMA_08755; -. DR KEGG; tmm:Tmari_1124; -. DR KEGG; tmw:THMA_1141; -. DR PATRIC; 23937171; VBITheMar51294_1134. DR eggNOG; ENOG4108E5B; Bacteria. DR eggNOG; ENOG41103IN; LUCA. DR OMA; QPIAYSK; -. DR OrthoDB; EOG6K13PT; -. DR BioCyc; TMAR243274:GC6P-1147-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.40.160.10; -; 1. DR InterPro; IPR023614; Porin_dom. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 368 AA; 41967 MW; 79CD3A67A64E8A65 CRC64; MKWSLMIFLI LAVATVFSES MIMYQFVMAE VKESTGTGVS LEELYLSTDE SSEGSIHYSS DTVELKLFPL SIKVKFPVIR DSYRILSKPW ILTVLGKPAV VRVGREEILT VTQGMTTVQE MYLSITPQQL DKKSVLSEIE MKLDGAHLRT KLWISQEDFQ PIAYSKFKTD EKEHRMIVFC RSLVVEKPPE EKVFVAGNVS GLEEFMGKEE EERSEESFIL LSSHPEARVS LWLNKNIHFS ASFPDGLLIE TKLFGEELKL GAIYWRFRYL GVGFSDRTSV GNLSLSAGVY ALFDFTKFSG ILWWGRGDLK LNRFSASLSF RSHWTLEETP WEVSLSAGYD LSKNITVLLG VTYDSTNYKI FVGVRYSF // ID Q9WYD8_THEMA Unreviewed; 289 AA. AC Q9WYD8; G4FHL6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35390.1}; DE SubName: Full=Xyloglucan ABC transport system, permease protein 2 {ECO:0000313|EMBL:AGL49226.1}; GN OrderedLocusNames=TM_0302 {ECO:0000313|EMBL:AAD35390.1}; GN ORFNames=Tmari_0300 {ECO:0000313|EMBL:AGL49226.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35390.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35390.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35390.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49226.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49226.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35390.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49226.1; -; Genomic_DNA. DR PIR; C72393; C72393. DR RefSeq; NP_228114.1; NC_000853.1. DR RefSeq; WP_004083025.1; NZ_CP011107.1. DR STRING; 243274.TM0302; -. DR TCDB; 3.A.1.5.30; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35390; AAD35390; TM_0302. DR EnsemblBacteria; AGL49226; AGL49226; Tmari_0300. DR GeneID; 897229; -. DR KEGG; tma:TM0302; -. DR KEGG; tmm:Tmari_0300; -. DR KEGG; tmw:THMA_0309; -. DR PATRIC; 23935483; VBITheMar51294_0307. DR eggNOG; COG1173; LUCA. DR KO; K02034; -. DR OMA; RRHLWPA; -. DR OrthoDB; EOG6WX4NQ; -. DR BioCyc; TMAR243274:GC6P-315-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 20 39 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 80 104 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 111 132 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 138 157 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 202 222 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 256 276 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 76 270 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 289 AA; 32657 MW; 065FE6975C46CF80 CRC64; MKRILRLFFD MWEDLRFKYA VTVLTALVLL SILSIFSPYD PYKWYVLPTN QPPSLEHILG TDGKGQDIFW LLTFSLKNSL ILATIAAVFS RIIAITIGML SGYLGGTTDR ILMALTDTFM VMPVFPLLLL LSSLIKNYLS LPILGLIIGV FGWAGDARVI RSMILSLRER EFVVTSKFSG MRTFEVVFGD FVPYLIPVIS GGFIGSMMGA IGFEIVLAIL GFTRVEIPTL GSMFHWMINF QAMLLGYWWW VLTPIVTAVF LFTALYTLSL SINEYLDPRT RMQRIGAVK // ID Q9X0M3_THEMA Unreviewed; 239 AA. AC Q9X0M3; G4FEK9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 127. DE SubName: Full=Branched chain amino acid ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36215.1}; DE SubName: Full=Branched-chain amino acid transport ATP-binding protein LivF {ECO:0000313|EMBL:AGL50069.1}; GN OrderedLocusNames=TM_1139 {ECO:0000313|EMBL:AAD36215.1}; GN ORFNames=Tmari_1145 {ECO:0000313|EMBL:AGL50069.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36215.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36215.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36215.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50069.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50069.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36215.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50069.1; -; Genomic_DNA. DR PIR; G72290; G72290. DR RefSeq; NP_228945.1; NC_000853.1. DR RefSeq; WP_004080267.1; NZ_CP011107.1. DR PDB; 1JI0; X-ray; 2.00 A; A=1-239. DR PDBsum; 1JI0; -. DR STRING; 243274.TM1139; -. DR EnsemblBacteria; AAD36215; AAD36215; TM_1139. DR EnsemblBacteria; AGL50069; AGL50069; Tmari_1145. DR GeneID; 898625; -. DR KEGG; tma:TM1139; -. DR KEGG; tmi:THEMA_08650; -. DR KEGG; tmm:Tmari_1145; -. DR KEGG; tmw:THMA_1162; -. DR PATRIC; 23937213; VBITheMar51294_1155. DR eggNOG; ENOG4108IV0; Bacteria. DR eggNOG; COG0410; LUCA. DR KO; K01996; -. DR OMA; EVGHILF; -. DR OrthoDB; EOG6QK4RR; -. DR BioCyc; TMAR243274:GC6P-1168-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015658; F:branched-chain amino acid transmembrane transporter activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR030660; ABC_branched_ATPase_LivF/BraG. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR PIRSF; PIRSF039137; ABC_branched_ATPase; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1JI0}; KW ATP-binding {ECO:0000213|PDB:1JI0, ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD36215.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000213|PDB:1JI0, KW ECO:0000256|RuleBase:RU363033, ECO:0000313|EMBL:AAD36215.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 6 238 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT NP_BIND 41 46 ATP. {ECO:0000213|PDB:1JI0}. FT BINDING 15 15 ATP. {ECO:0000213|PDB:1JI0}. FT BINDING 87 87 ATP. {ECO:0000213|PDB:1JI0}. FT BINDING 164 164 ATP. {ECO:0000213|PDB:1JI0}. SQ SEQUENCE 239 AA; 26191 MW; D4AA24A0A38AECD8 CRC64; MSDIVLEVQS LHVYYGAIHA IKGIDLKVPR GQIVTLIGAN GAGKTTTLSA IAGLVRAQKG KIIFNGQDIT NKPAHVINRM GIALVPEGRR IFPELTVYEN LMMGAYNRKD KEGIKRDLEW IFSLFPRLKE RLKQLGGTLS GGEQQMLAIG RALMSRPKLL MMDEPSLGLA PILVSEVFEV IQKINQEGTT ILLVEQNALG ALKVAHYGYV LETGQIVLEG KASELLDNEM VRKAYLGVA // ID Q9WYV5_THEMA Unreviewed; 250 AA. AC Q9WYV5; G4FDY5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE SubName: Full=ABC transporter, permease protein, cysTW family {ECO:0000313|EMBL:AAD35570.1}; DE SubName: Full=Hydroxymethylpyrimidine ABC transporter, transmembrane component {ECO:0000313|EMBL:AGL49407.1}; GN OrderedLocusNames=TM_0485 {ECO:0000313|EMBL:AAD35570.1}; GN ORFNames=Tmari_0482 {ECO:0000313|EMBL:AGL49407.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35570.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35570.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35570.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49407.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49407.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35570.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49407.1; -; Genomic_DNA. DR PIR; D72369; D72369. DR RefSeq; NP_228295.1; NC_000853.1. DR RefSeq; WP_004081481.1; NZ_CP011107.1. DR STRING; 243274.TM0485; -. DR DNASU; 897524; -. DR EnsemblBacteria; AAD35570; AAD35570; TM_0485. DR EnsemblBacteria; AGL49407; AGL49407; Tmari_0482. DR GeneID; 897524; -. DR KEGG; tma:TM0485; -. DR KEGG; tmi:THEMA_02245; -. DR KEGG; tmm:Tmari_0482; -. DR KEGG; tmw:THMA_0498; -. DR PATRIC; 23935875; VBITheMar51294_0492. DR eggNOG; ENOG4105Y36; Bacteria. DR eggNOG; COG0600; LUCA. DR OMA; IGAFWIN; -. DR OrthoDB; EOG6GR3CZ; -. DR BioCyc; TMAR243274:GC6P-509-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 51 76 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 88 112 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 118 137 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 181 202 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 214 232 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 52 232 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 250 AA; 28138 MW; A491D22692EEBB5C CRC64; MKRRYRSTAK WLFFIALIFV WEFSKVPQYL LPKPSSIVLE GLSQWKILMD HSLYTILEAF SGLVIGLVLG VGLAVLMDLF QTVKEVMYPI LIISQAIPIV AVAPLVIIWF GLGVGTKIGI VAFVTLFPVA LNTLEGFRTI DQDALDLFKV MKATKIQIYR YLVLPHTLPY VLSGLKISAT YAVVSAVIGE WLGAEKGLGI YMIRAMNTFR ADRLFLSVIV VVLLSVVVFK IADILSRKLT PWFEERRLVQ // ID Q9X1D1_THEMA Unreviewed; 245 AA. AC Q9X1D1; G4FFE7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Helicase-related protein {ECO:0000313|EMBL:AAD36482.1}; DE SubName: Full=Putative ATP-dependent helicase {ECO:0000313|EMBL:AGL50342.1}; GN OrderedLocusNames=TM_1411 {ECO:0000313|EMBL:AAD36482.1}; GN ORFNames=Tmari_1418 {ECO:0000313|EMBL:AGL50342.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36482.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36482.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36482.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50342.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50342.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36482.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50342.1; -; Genomic_DNA. DR PIR; D72258; D72258. DR RefSeq; NP_229212.1; NC_000853.1. DR RefSeq; WP_004081644.1; NZ_CP011107.1. DR STRING; 243274.TM1411; -. DR EnsemblBacteria; AAD36482; AAD36482; TM_1411. DR EnsemblBacteria; AGL50342; AGL50342; Tmari_1418. DR GeneID; 898065; -. DR KEGG; tma:TM1411; -. DR KEGG; tmi:THEMA_07260; -. DR KEGG; tmm:Tmari_1418; -. DR KEGG; tmw:THMA_1440; -. DR PATRIC; 23937768; VBITheMar51294_1423. DR eggNOG; COG1112; LUCA. DR OrthoDB; EOG6QP0XR; -. DR BioCyc; TMAR243274:GC6P-1448-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR InterPro; IPR022622; DUF3492. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF11997; DUF3492; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD36482.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Helicase {ECO:0000313|EMBL:AAD36482.1}; KW Hydrolase {ECO:0000313|EMBL:AAD36482.1}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD36482.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 73 DUF3492. {ECO:0000259|Pfam:PF11997}. SQ SEQUENCE 245 AA; 28205 MW; D45A92970C178E44 CRC64; MRVGLIAEGT YPYITGGVSS WIQTLISNLP EFEFEIYHLR PDSKKREVRY KIPKNVVRIH EVNIFGDFDP EIPEEANLSA LTEITKAIVL SPKNVLVFID TKNRSDRFER QRKDSPSREN PLEAQIVKEV VEKLLSMGVK EDWIGIITPY DDQVNLIREL IEAKVEVHSV DGFQGREKEV IIISFVRSNK NGEIGFLEDL RRLNVSLTRA KRKLIATGDS STLSVHPTYR RFVEFVKKKG TYVIF // ID Q9WZR9_THEMA Unreviewed; 271 AA. AC Q9WZR9; G4FD12; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE SubName: Full=Chitobiose ABC transport system, permease protein 2 {ECO:0000313|EMBL:AGL49738.1}; DE SubName: Full=Sugar ABC transporter, permease protein, putative {ECO:0000313|EMBL:AAD35894.1}; GN OrderedLocusNames=TM_0812 {ECO:0000313|EMBL:AAD35894.1}; GN ORFNames=Tmari_0813 {ECO:0000313|EMBL:AGL49738.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35894.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35894.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35894.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49738.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49738.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35894.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49738.1; -; Genomic_DNA. DR PIR; E72331; E72331. DR RefSeq; NP_228621.1; NC_000853.1. DR RefSeq; WP_004080850.1; NZ_CP011107.1. DR STRING; 243274.TM0812; -. DR EnsemblBacteria; AAD35894; AAD35894; TM_0812. DR EnsemblBacteria; AGL49738; AGL49738; Tmari_0813. DR GeneID; 898480; -. DR KEGG; tma:TM0812; -. DR KEGG; tmi:THEMA_00590; -. DR KEGG; tmm:Tmari_0813; -. DR KEGG; tmw:THMA_0831; -. DR PATRIC; 23936544; VBITheMar51294_0824. DR eggNOG; ENOG4105EX2; Bacteria. DR eggNOG; COG0395; LUCA. DR KO; K17246; -. DR OMA; LARIDFK; -. DR OrthoDB; EOG693GR8; -. DR BioCyc; TMAR243274:GC6P-839-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 7 28 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 67 91 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 103 127 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 133 153 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 236 257 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 68 256 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 271 AA; 30733 MW; D79C557FC0E5CEFA CRC64; MPKIRKVLTY VVLVLFSLLS VWPFYWIAKT SFEAGGNVYK YPPSLIPYPA TFSNYVGAWK TVKLGNYYLN TIIIAGFGTL LNVLFSLMVA YPLARIDFKG KQLVLFLILL PMMIPVQNTL IVNYLTLRKL GLLNTYTGVI LPQAVTIFGI FMMRQAYLSI PKSFEDAARI DGAGELYIWW KIITPLIKPD IATLVVFQVI TWWDNFLWPL IVLSDSNKYP LSVALVYLNS TFQVNFRYTA AGIVLAILPV VLLFIFAQRY IINAIAGGVK Y // ID Q9X0K3_THEMA Unreviewed; 349 AA. AC Q9X0K3; G4FEM9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36195.1}; GN OrderedLocusNames=TM_1119 {ECO:0000313|EMBL:AAD36195.1}; GN ORFNames=Tmari_1125 {ECO:0000313|EMBL:AGL50049.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36195.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36195.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36195.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50049.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50049.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36195.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50049.1; -; Genomic_DNA. DR PIR; D72292; D72292. DR RefSeq; NP_228925.1; NC_000853.1. DR RefSeq; WP_004080300.1; NZ_CP011107.1. DR STRING; 243274.TM1119; -. DR EnsemblBacteria; AAD36195; AAD36195; TM_1119. DR EnsemblBacteria; AGL50049; AGL50049; Tmari_1125. DR GeneID; 898645; -. DR KEGG; tma:TM1119; -. DR KEGG; tmi:THEMA_08750; -. DR KEGG; tmm:Tmari_1125; -. DR KEGG; tmw:THMA_1142; -. DR PATRIC; 23937173; VBITheMar51294_1135. DR eggNOG; ENOG4106AX5; Bacteria. DR eggNOG; COG3629; LUCA. DR OMA; ICIPETD; -. DR OrthoDB; EOG632D30; -. DR BioCyc; TMAR243274:GC6P-1148-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR005158; BTAD. DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor. DR InterPro; IPR011990; TPR-like_helical_dom. DR Pfam; PF03704; BTAD; 1. DR SMART; SM01043; BTAD; 1. DR SUPFAM; SSF46894; SSF46894; 1. DR SUPFAM; SSF48452; SSF48452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 102 234 BTAD. {ECO:0000259|SMART:SM01043}. SQ SEQUENCE 349 AA; 41128 MW; EEEBE4F6750C33A6 CRC64; MSIFVKTFGG TRVIKDNDIV SARDWPSQKA FALFRYLIFR RNEEVSVEEI YNLFWEDMDD TFAKSNLNTT LHIIRKTTGI TSEELFVKGD LCCFFPGGEI TIDADIFEEC HRNLMKATSD AEREKLLKRM FEIYTGPFLV EDIFAEWVQE IREIYESWYS DVLKELFKLY LSKKDYDAAL EMVNAYFQRE PYDEDMYYRA IEVLLKKGDI TRAKRVYDKL SSHLMEIGIK PRLKFDDFLS KRDSEFMLNG NKAVVVDEKL FERFLFLESR RREKSFVLVE VKLTDKSIST EDVSQRVASQ LRKGDVITFS GETIRILFHC PEQRRPTMEK RVVDALEKVG VKKGQYEIS // ID Q9WXS6_THEMA Unreviewed; 625 AA. AC Q9WXS6; G4FGY6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein {ECO:0000313|EMBL:AAD35165.1}; DE SubName: Full=Xylobiose ABC transport system, sugar-binding protein {ECO:0000313|EMBL:AGL48994.1}; GN OrderedLocusNames=TM_0071 {ECO:0000313|EMBL:AAD35165.1}; GN ORFNames=Tmari_0068 {ECO:0000313|EMBL:AGL48994.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35165.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35165.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35165.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48994.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48994.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35165.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48994.1; -; Genomic_DNA. DR PIR; G72420; G72420. DR RefSeq; NP_227887.1; NC_000853.1. DR RefSeq; WP_004082579.1; NZ_CP011107.1. DR STRING; 243274.TM0071; -. DR TCDB; 3.A.1.5.13; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35165; AAD35165; TM_0071. DR EnsemblBacteria; AGL48994; AGL48994; Tmari_0068. DR GeneID; 896896; -. DR KEGG; tma:TM0071; -. DR KEGG; tmi:THEMA_04450; -. DR KEGG; tmm:Tmari_0068; -. DR KEGG; tmw:THMA_0067; -. DR PATRIC; 23934982; VBITheMar51294_0069. DR eggNOG; ENOG4106IG1; Bacteria. DR eggNOG; COG0747; LUCA. DR KO; K02035; -. DR OMA; NYPGAEN; -. DR OrthoDB; EOG63JR4Z; -. DR BioCyc; TMAR243274:GC6P-71-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GOC. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 625 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006753468. FT DOMAIN 76 511 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. SQ SEQUENCE 625 AA; 71885 MW; E0177E3F5B2B32FB CRC64; MKKFLVVLFV VSMFSLFFAQ LPPNIPRNET FIAQVLTGRA ANPTNFNVWT GWVWQDRGIQ NLLLEPLWYV DFATGKIISA LAESLPTYNS DFTELTIKLR KGVYWSDGEP FTADDVVFTI ETIMSTPAFG YHQELVNEVE SVEKLDDYTV KIKLKRPNAR FHAYFIDRWG GIRPMPKHVF EKVEDPVNFE FNPPVGTGPY VLHSVDPGGY WTLWQRREDW ERTPTGMLFG MPQPKYVLFI DYGSPEKQVL AMAQHQLDEA ILTIEALKAV LNRVKTARAW RKNFPWTVNN DPCVTGFVFN TAKEPFNNIE VRWALTLAID IVEYAANAFD GAVTLSPIHI PLSTAYYNWY FTRLEDWLKN YEIDLGNGEK FKPYDPEAGL RLAEYAKKRG YSVPDSPEII KRTFGPGWWK YAPDVAAKLL EKNGFYRDKN GKWHLPNGDL WQITIIAPTN PSDPAYRNAF ALSQAWKKFG IDAVVQTSEN ANSFGAEGNF DVHTAWPAAE PWGGHPDLYR TLYPFHSEYV VPIGEDAPWG NYCRWSDPRL DKIIEELKNT PWGNTQKLIE LGTEALKIIV EGLPSVPTFN YPGVIAWDEY YWTNYPGAEN PYTQPYQHWP NFKYMLPFLK PTGRK // ID Q9WZU5_THEMA Unreviewed; 456 AA. AC Q9WZU5; G4FCY3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=S-layer-like array protein {ECO:0000313|EMBL:AAD35923.1}; GN OrderedLocusNames=TM_0841 {ECO:0000313|EMBL:AAD35923.1}; GN ORFNames=Tmari_0843 {ECO:0000313|EMBL:AGL49768.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35923.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35923.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35923.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49768.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49768.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35923.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49768.1; -; Genomic_DNA. DR PIR; B72326; B72326. DR RefSeq; NP_228650.1; NC_000853.1. DR RefSeq; WP_004080789.1; NZ_CP011107.1. DR STRING; 243274.TM0841; -. DR EnsemblBacteria; AAD35923; AAD35923; TM_0841. DR EnsemblBacteria; AGL49768; AGL49768; Tmari_0843. DR GeneID; 898512; -. DR KEGG; tma:TM0841; -. DR KEGG; tmi:THEMA_00435; -. DR KEGG; tmm:Tmari_0843; -. DR KEGG; tmw:THMA_0862; -. DR PATRIC; 23936608; VBITheMar51294_0854. DR eggNOG; ENOG4108Q5A; Bacteria. DR eggNOG; ENOG4111FAP; LUCA. DR OMA; GYREETR; -. DR OrthoDB; EOG66TG2M; -. DR BioCyc; TMAR243274:GC6P-870-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR Gene3D; 2.60.40.1120; -; 1. DR InterPro; IPR013784; Carb-bd-like_fold. DR InterPro; IPR014766; CarboxyPept_regulatory_dom. DR InterPro; IPR025493; DUF4384. DR InterPro; IPR013229; PEGA. DR Pfam; PF14326; DUF4384; 1. DR Pfam; PF08308; PEGA; 4. DR SUPFAM; SSF49452; SSF49452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 46 125 DUF4384. {ECO:0000259|Pfam:PF14326}. FT DOMAIN 179 244 PEGA. {ECO:0000259|Pfam:PF08308}. FT DOMAIN 247 313 PEGA. {ECO:0000259|Pfam:PF08308}. FT DOMAIN 316 385 PEGA. {ECO:0000259|Pfam:PF08308}. FT DOMAIN 389 447 PEGA. {ECO:0000259|Pfam:PF08308}. SQ SEQUENCE 456 AA; 51807 MW; 0A282CB9742FF010 CRC64; MRRYVFLLLI LVSMVAFSFE AKSIIIVPEK PYFTVDVWLN KPEGSVYEVG ERIEIFVKSS RDAYILIYDI NAQGKVTLIF PNKYESDNFV RANEIKKIPS KSTYSLRVSP PYGKEYIQVI ASTRPIPIFN QLKELGTTRA FPTLSDNVEE YVQKKLKPYL TGEWVSDLTY FYVGRAPAFG TLIVDSTPPG MTVYIDGSYK GKTPVTVSVD EGTHYVTVYF ENYTFYKEVY VGRNQTVKVI ATLPLAQLSL SSSPSGASVY LNGVYQGKTP LTLNLSPGNY TVTFRKEGYR EETRNITLSA GETRSVYVTL KPAQSSLKLR TDPSGVDVYI DGRYVGTTDQ NGLNLILDPG MYEVKLEKEG YETDRFTVNL APGEEKEIFR RLEKRVVFSE VRIETEPSGA TIYLNGYYHG ETPITLYVQA GTYEITIVKP GYRTIVKTIT FDDEEEYFKF IMNRIE // ID Q9WYJ5_THEMA Unreviewed; 116 AA. AC Q9WYJ5; G4FHS2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 88. DE SubName: Full=MazG-related protein {ECO:0000313|EMBL:AAD35447.1}; GN OrderedLocusNames=TM_0360 {ECO:0000313|EMBL:AAD35447.1}; GN ORFNames=Tmari_0358 {ECO:0000313|EMBL:AGL49283.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35447.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35447.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35447.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49283.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49283.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35447.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49283.1; -; Genomic_DNA. DR PIR; H72386; H72386. DR RefSeq; NP_228171.1; NC_000853.1. DR RefSeq; WP_004083161.1; NZ_CP011107.1. DR PDB; 2YXH; X-ray; 2.00 A; A/B=1-116. DR PDBsum; 2YXH; -. DR STRING; 243274.TM0360; -. DR EnsemblBacteria; AAD35447; AAD35447; TM_0360. DR EnsemblBacteria; AGL49283; AGL49283; Tmari_0358. DR GeneID; 897318; -. DR KEGG; tma:TM0360; -. DR KEGG; tmi:THEMA_02915; -. DR KEGG; tmm:Tmari_0358; -. DR KEGG; tmw:THMA_0368; -. DR PATRIC; 23935601; VBITheMar51294_0365. DR eggNOG; ENOG41071HC; Bacteria. DR eggNOG; COG1694; LUCA. DR KO; K02428; -. DR OMA; EKCPWLE; -. DR OrthoDB; EOG67X1VS; -. DR BioCyc; TMAR243274:GC6P-374-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central. DR GO; GO:0046061; P:dATP catabolic process; IBA:GO_Central. DR GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central. DR GO; GO:0046076; P:dTTP catabolic process; IBA:GO_Central. DR GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central. DR GO; GO:0046047; P:TTP catabolic process; IBA:GO_Central. DR GO; GO:0046052; P:UTP catabolic process; IBA:GO_Central. DR InterPro; IPR004518; MazG_cat. DR InterPro; IPR011551; NTP_PyrPHydrolase_MazG. DR PANTHER; PTHR30522:SF0; PTHR30522:SF0; 1. DR Pfam; PF03819; MazG; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2YXH}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Magnesium {ECO:0000213|PDB:2YXH}; KW Metal-binding {ECO:0000213|PDB:2YXH}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 22 95 MazG. {ECO:0000259|Pfam:PF03819}. FT COILED 21 44 {ECO:0000256|SAM:Coils}. FT METAL 34 34 Magnesium. {ECO:0000213|PDB:2YXH}. FT METAL 37 37 Magnesium. {ECO:0000213|PDB:2YXH}. FT METAL 53 53 Magnesium. {ECO:0000213|PDB:2YXH}. FT METAL 56 56 Magnesium. {ECO:0000213|PDB:2YXH}. SQ SEQUENCE 116 AA; 13574 MW; A82659DBAA63215A CRC64; MVERLLEIIE RSLRKCPWLE KQSIETLLEA LASEIEEVAE AVKKNDLANL EEEIGDLIYD ALLVAAVAQR DYGIDLESAI QKVVEKISHR KPWLFWEEKI SLEEAEKIWK ERKKKI // ID Q9X2H0_THEMA Unreviewed; 418 AA. AC Q9X2H0; G4FGP7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Multiple sugar ABC transporter, substrate-binding protein {ECO:0000313|EMBL:AGL50794.1}; DE SubName: Full=Sugar ABC transporter, periplasmic sugar-binding protein, putative {ECO:0000313|EMBL:AAD36917.1}; GN OrderedLocusNames=TM_1855 {ECO:0000313|EMBL:AAD36917.1}; GN ORFNames=Tmari_1870 {ECO:0000313|EMBL:AGL50794.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36917.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36917.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36917.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50794.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50794.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36917.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50794.1; -; Genomic_DNA. DR PIR; H72203; H72203. DR RefSeq; NP_229651.1; NC_000853.1. DR RefSeq; WP_004082406.1; NZ_CP011107.1. DR STRING; 243274.TM1855; -. DR EnsemblBacteria; AAD36917; AAD36917; TM_1855. DR EnsemblBacteria; AGL50794; AGL50794; Tmari_1870. DR GeneID; 898528; -. DR KEGG; tma:TM1855; -. DR KEGG; tmi:THEMA_04895; -. DR KEGG; tmm:Tmari_1870; -. DR KEGG; tmw:THMA_1905; -. DR PATRIC; 23938699; VBITheMar51294_1876. DR eggNOG; ENOG4105EYZ; Bacteria. DR eggNOG; COG1653; LUCA. DR KO; K02027; -. DR OMA; HQYVLPI; -. DR OrthoDB; EOG6FRCSD; -. DR BioCyc; TMAR243274:GC6P-1906-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 418 AA; 48387 MW; 88D90A0ED6D41FFD CRC64; MWKRVLLFML VVLSVFAFAE VKKIVFWTAP NPNQETFWKE LVEKWNAEHP DVQIEWSVIP AAGSSEEAIL NAIAAGNAPD ICTNIFSGFA AQLAEELDVL VAFDEEFGEE FWKLVDARKM RGILEGWKLN GHYYVIPIYS NPMLFWWRGD LLKELGYDKP PRTYSEIYEL AKKWVVPKEK YVIRAVAGRN WWDRWFDFIT FYYAASGGKP YIENGKAVFN NEYGKAVAEF IYTLFKNGWT AVDLGQDPFE NGTILGQLMG PWHLNYTKEH YPEVYPHIVM TPPPVPDNYP EDKPIYTFAD TKGLVMFEHC KYKKEAFEFI KWVFSNAQND ARWIELTRMP PAREDLGTNP VFAEYMKDPY FAKIAEAVAY AVPPAMITNT IDVQNAMTTY LMEPLMYLKA TPEEALKQAV KEINALLW // ID Q9X1J5_THEMA Unreviewed; 324 AA. AC Q9X1J5; G4FFP4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 79. DE SubName: Full=PhoH-related protein {ECO:0000313|EMBL:AAD36574.1}; DE SubName: Full=Phosphate starvation-inducible protein PhoH, predicted ATPase {ECO:0000313|EMBL:AGL50439.1}; GN OrderedLocusNames=TM_1507 {ECO:0000313|EMBL:AAD36574.1}; GN ORFNames=Tmari_1515 {ECO:0000313|EMBL:AGL50439.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36574.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36574.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36574.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50439.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50439.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36574.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50439.1; -; Genomic_DNA. DR PIR; D72244; D72244. DR RefSeq; NP_229307.1; NC_000853.1. DR RefSeq; WP_004081850.1; NZ_CP011107.1. DR SMR; Q9X1J5; 114-316. DR STRING; 243274.TM1507; -. DR EnsemblBacteria; AAD36574; AAD36574; TM_1507. DR EnsemblBacteria; AGL50439; AGL50439; Tmari_1515. DR GeneID; 897489; -. DR KEGG; tma:TM1507; -. DR KEGG; tmm:Tmari_1515; -. DR KEGG; tmw:THMA_1539; -. DR PATRIC; 23937972; VBITheMar51294_1524. DR eggNOG; ENOG4105C9A; Bacteria. DR eggNOG; COG1702; LUCA. DR KO; K06217; -. DR OMA; TEFEYLV; -. DR OrthoDB; EOG6F81S0; -. DR BioCyc; TMAR243274:GC6P-1547-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003714; PhoH. DR Pfam; PF02562; PhoH; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 113 316 PhoH. {ECO:0000259|Pfam:PF02562}. SQ SEQUENCE 324 AA; 36910 MW; 9604C78256DD593E CRC64; MEVEITITVR KVRIPEDVAV LEIFGQYDKR ARYLKKLFNV EFAVRDSEIL IKGMDEKSVD AAHRVLDEII SITRDGHLLD WTEFEYLVER VSNSESVKEV YSNNSKGLII GKKVKPKTLG QKKYLEAVEK NDVVFVIGPA GTGKTYLAVA VALDYLKMGK VNRIILTRPA VEAGEKLGYL PGDLSEKVEP YLRPLYDAII DITSPDKFNS YRERGIIEIV PLAYMRGRTL NNSFIILDEA QNTTYQQMKM FLTRLGFNSK AVITGDITQV DIEKEKSGLI ECQKILEGIS GIEFVYLNES DVVRHPLVKK IIKAYEEYER SRKS // ID Q9X1H6_THEMA Unreviewed; 170 AA. AC Q9X1H6; G4FFK1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Cob(I)alamin adenosyltransferase {ECO:0000313|EMBL:AAD36533.1}; DE EC=2.5.1.17 {ECO:0000313|EMBL:AGL50396.1}; GN OrderedLocusNames=TM_1465 {ECO:0000313|EMBL:AAD36533.1}; GN ORFNames=Tmari_1472 {ECO:0000313|EMBL:AGL50396.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36533.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36533.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36533.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50396.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50396.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36533.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50396.1; -; Genomic_DNA. DR PIR; B72252; B72252. DR RefSeq; NP_229265.1; NC_000853.1. DR RefSeq; WP_004081762.1; NZ_CP011107.1. DR STRING; 243274.TM1465; -. DR EnsemblBacteria; AAD36533; AAD36533; TM_1465. DR EnsemblBacteria; AGL50396; AGL50396; Tmari_1472. DR GeneID; 898015; -. DR KEGG; tma:TM1465; -. DR KEGG; tmi:THEMA_06985; -. DR KEGG; tmm:Tmari_1472; -. DR KEGG; tmw:THMA_1496; -. DR PATRIC; 23937884; VBITheMar51294_1480. DR eggNOG; ENOG41068B1; Bacteria. DR eggNOG; COG2109; LUCA. DR KO; K19221; -. DR OMA; IKHYYKK; -. DR OrthoDB; EOG6GN76J; -. DR BioCyc; TMAR243274:GC6P-1504-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008817; F:cob(I)yrinic acid a,c-diamide adenosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003724; CblAdoTrfase_CobA. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF02572; CobA_CobO_BtuR; 1. DR PIRSF; PIRSF015617; Adensltrnsf_CobA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00708; cobA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD36533.1}. SQ SEQUENCE 170 AA; 18987 MW; 6B3CBC60E2AECC8C CRC64; MKGYIHVYTG NGKGKTTAAL GLATRAACAG LKVFFGQFLK GRETSELKIS EFLPNFEIVQ YGTPEFIVGN PSEEQIKKAK SGLADAKERL VSEKYDVVVL DELCVAIHLG LFSKEEIEDL LNVKPENVEL VITGRYAPEW LIEKADLVTE MKEVKHYYQK GVVARKGIEY // ID Q9X0V8_THEMA Unreviewed; 832 AA. AC Q9X0V8; G4FEB5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Alpha-mannosidase-related protein {ECO:0000313|EMBL:AAD36306.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL50162.1}; GN OrderedLocusNames=TM_1231 {ECO:0000313|EMBL:AAD36306.1}; GN ORFNames=Tmari_1238 {ECO:0000313|EMBL:AGL50162.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36306.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36306.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36306.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50162.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50162.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36306.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50162.1; -; Genomic_DNA. DR PIR; H72278; H72278. DR RefSeq; NP_229036.1; NC_000853.1. DR RefSeq; WP_004080050.1; NZ_CP011107.1. DR STRING; 243274.TM1231; -. DR CAZy; GH38; Glycoside Hydrolase Family 38. DR EnsemblBacteria; AAD36306; AAD36306; TM_1231. DR EnsemblBacteria; AGL50162; AGL50162; Tmari_1238. DR GeneID; 898253; -. DR KEGG; tma:TM1231; -. DR KEGG; tmi:THEMA_08175; -. DR KEGG; tmm:Tmari_1238; -. DR KEGG; tmw:THMA_1257; -. DR PATRIC; 23937404; VBITheMar51294_1249. DR eggNOG; ENOG4107VTQ; Bacteria. DR eggNOG; COG0383; LUCA. DR KO; K01191; -. DR OMA; LREYWME; -. DR OrthoDB; EOG6N0HF2; -. DR BioCyc; TMAR243274:GC6P-1261-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central. DR GO; GO:0006013; P:mannose metabolic process; IBA:GO_Central. DR GO; GO:0006517; P:protein deglycosylation; IBA:GO_Central. DR Gene3D; 3.20.110.10; -; 1. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR027291; Glyco_hydro_38/57_N. DR InterPro; IPR000602; Glyco_hydro_38_N. DR InterPro; IPR028995; Glyco_hydro_57/38_cen. DR Pfam; PF01074; Glyco_hydro_38; 1. DR SUPFAM; SSF88688; SSF88688; 1. DR SUPFAM; SSF88713; SSF88713; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 217 Glyco_hydro_38. FT {ECO:0000259|Pfam:PF01074}. SQ SEQUENCE 832 AA; 96627 MW; EFF0B33D0C81A01B CRC64; MKVKVVVHNH WDREWFTSSE VTSKWLKEVF FRVKELVQKN PEFVYVLDGQ TAAVEDLLVY HPDLEEDLRE LVRSGRLLVG PYYIQIDWRI PGEASILKNF EIGEKDTNRF GRRMNAGWLL DSFGHISQEP QLHRIFGIEK VFLWRGISFE NDGISQEFFW KGSDGTAVQG VFLVGGYRNL YNLKETQDIA EKRLKHEVEK LAKFSRSGEI LLLDGYDIDL SPEDPKDYLN VEIVSPEEFP ERFPENAPTL SGELLSGRYA CVFPGTLSTR AYLKLESDLV EKLLKMNDLL SVLNGEELSD LFWRDYLKTL AHDNSCGVCA DPVHEKMERT YRNVYFLVKS SVESRLRHLV ERLGLEKGTY ALSLSPFSYN HHFCDGERTF LLKTNGAGLF KTEVADEKKE VKELTWENEY YRAYFEGDGT LVLNNRKAGV LKLFKEDGDA YTTSVEETDF SISLEKMRTV LQTKHSMVVE LERTIRSSQC LIETKERVIF DETPLVKWRI ALKIKGKNYK LSMVYETGSG EIFAKMPFDV VKRKEKDSYL LPETPPEELK GILLAARETG EVREFPFQGF VSVWSEESSK TILARGLREY WMEEGKVHVT LSRSVEWIAK EVKNRVGDAG PMMYVPGAKC EGVFTVDLAF MELPVHPRSE EFFRWYLLFD NPPLLLDVEA DGTEKEKTFF FSSLPWAGVK DRYHLWVYNP YLEEIEGLRP LQIGEKSIES LSEKQCFVSR LNILNFPEFP VVSVEKNPEG EVIEFLKETL SSLEDEITNL EGKDDPRSKH RLFSLLRTKK EIELSLQYLI DVEKTARELN ELRMKRRTYD YVVELFESEE RE // ID Q9WYT8_THEMA Unreviewed; 445 AA. AC Q9WYT8; G4FE03; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE SubName: Full=Regulatory protein, putative {ECO:0000313|EMBL:AAD35551.1}; DE SubName: Full=Serine phosphatase RsbU, regulator of sigma subunit {ECO:0000313|EMBL:AGL49389.1}; GN OrderedLocusNames=TM_0467 {ECO:0000313|EMBL:AAD35551.1}; GN ORFNames=Tmari_0464 {ECO:0000313|EMBL:AGL49389.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35551.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35551.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35551.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49389.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49389.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35551.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49389.1; -; Genomic_DNA. DR PIR; C72374; C72374. DR RefSeq; NP_228277.1; NC_000853.1. DR RefSeq; WP_004081499.1; NZ_CP011107.1. DR STRING; 243274.TM0467; -. DR EnsemblBacteria; AAD35551; AAD35551; TM_0467. DR EnsemblBacteria; AGL49389; AGL49389; Tmari_0464. DR GeneID; 897498; -. DR KEGG; tma:TM0467; -. DR KEGG; tmi:THEMA_02355; -. DR KEGG; tmm:Tmari_0464; -. DR KEGG; tmw:THMA_0476; -. DR PATRIC; 23935831; VBITheMar51294_0474. DR eggNOG; ENOG4107SGM; Bacteria. DR eggNOG; COG2208; LUCA. DR KO; K07315; -. DR OMA; NEREICE; -. DR OrthoDB; EOG66QKXZ; -. DR BioCyc; TMAR243274:GC6P-487-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.60.40.10; -; 1. DR InterPro; IPR029016; GAF_dom-like. DR InterPro; IPR001932; PPM-type_phosphatase_dom. DR Pfam; PF07228; SpoIIE; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SUPFAM; SSF55781; SSF55781; 1. DR SUPFAM; SSF81606; SSF81606; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 228 438 PPM-type phosphatase. FT {ECO:0000259|SMART:SM00331}. FT COILED 184 213 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 445 AA; 50919 MW; 4B20D879D129F589 CRC64; MNEREICERI AEILNLEHDC SKGIDDLLKI LEYEINEYRK SLEEQAMFME AQIEELSRSY EEISTLLEIS EIFGTFEFPL NLQDKLEKVI RLLRNVIKFE SYLVHLESEL TVGDLNREEI EPEIGNPEKT VLIEPGKSEK FSNLLFVPIK GNKYYGYVCF VGKEDGGVFT AGDRKIAEMT ARYIASALDR LDFLKKEIER ERLEEQLNIA RQIQTNLLPR KIPEIGFVEA DACSQPAVQV GGDYYDFFVS QEKRFLTVVG DVAGKSVPAA LLMSAVRSYL KVLVTTCPDL EKLVNRLNTI LCEDMTNDRF VTMAFIEISP DGTLNLINAG HNPVYFLHKG ELVKIEASAI PIGITEWEYK KHTIHLKPDT FVISYSDGLT EARNEAGEEF GYERLEKILR EFKGETPAEL LEALRKRVKS FMGDAQQHDD MTIVVLKYKG QQEVE // ID Q9X1Z4_THEMA Unreviewed; 396 AA. AC Q9X1Z4; G4FG55; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:AGL50599.1}; DE EC=3.5.1.16 {ECO:0000313|EMBL:AGL50599.1}; DE SubName: Full=Succinyl-diaminopimelate desuccinylase, putative {ECO:0000313|EMBL:AAD36733.1}; GN OrderedLocusNames=TM_1666 {ECO:0000313|EMBL:AAD36733.1}; GN ORFNames=Tmari_1675 {ECO:0000313|EMBL:AGL50599.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36733.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36733.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36733.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50599.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50599.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36733.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50599.1; -; Genomic_DNA. DR PIR; H72224; H72224. DR RefSeq; NP_229466.1; NC_000853.1. DR RefSeq; WP_004082184.1; NZ_CP011107.1. DR STRING; 243274.TM1666; -. DR EnsemblBacteria; AAD36733; AAD36733; TM_1666. DR EnsemblBacteria; AGL50599; AGL50599; Tmari_1675. DR GeneID; 896862; -. DR KEGG; tma:TM1666; -. DR KEGG; tmi:THEMA_05915; -. DR KEGG; tmm:Tmari_1675; -. DR KEGG; tmw:THMA_1707; -. DR PATRIC; 23938306; VBITheMar51294_1685. DR eggNOG; ENOG4105C9Y; Bacteria. DR eggNOG; COG0624; LUCA. DR KO; K01439; -. DR OMA; KSILWFK; -. DR OrthoDB; EOG60651W; -. DR BioCyc; TMAR243274:GC6P-1712-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC. DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro. DR Gene3D; 3.30.70.360; -; 1. DR InterPro; IPR010182; ArgE/DapE. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR SUPFAM; SSF55031; SSF55031; 1. DR TIGRFAMs; TIGR01910; DapE-ArgE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50599.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 193 302 M20_dimer. {ECO:0000259|Pfam:PF07687}. SQ SEQUENCE 396 AA; 44198 MW; 159F2A15FB9EF481 CRC64; MEITKRIEEL REEMVESLKK FISINSVNPA FGGPGEKEKA DWLEGLLRDF GFEVDRCDVR DDRGIWRSNI VAKIPGKNRE KTLWIVTHID TVPPGDLSLW ETDPFVPVVK DGKVYGRGAE DNGGSMIASI YAGKALIDLG ITPEYNFGLA LVADEEAGSE YGIQYLIEKG LFSPEDMFLV PDAGNEKGDF IEIAEKSILW FKVMVNGKQG HASRPQTTEN ALRKGAHLIT EIDEALHRKY SDRDELFDEP LSTFEPTRAE KTVDNVNTVP GRFVFYFDCR VLPRYNLDEV LSIVKSILDG RGAELEVVVK QPAPEPTPPD SELVVKLSNV LRSLRGLEAK VGGIGGGTCA AFFRKKGWPA VVWSTIDETA HQPNEYRRIS HMVEDAKVFA LLGTER // ID Q9X0H7_THEMA Unreviewed; 276 AA. AC Q9X0H7; G4FEQ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36168.1}; GN OrderedLocusNames=TM_1092 {ECO:0000313|EMBL:AAD36168.1}; GN ORFNames=Tmari_1097 {ECO:0000313|EMBL:AGL50021.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36168.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36168.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36168.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50021.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50021.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36168.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50021.1; -; Genomic_DNA. DR PIR; C72298; C72298. DR RefSeq; NP_228898.1; NC_000853.1. DR RefSeq; WP_004080369.1; NZ_CP011107.1. DR STRING; 243274.TM1092; -. DR DNASU; 898673; -. DR EnsemblBacteria; AAD36168; AAD36168; TM_1092. DR EnsemblBacteria; AGL50021; AGL50021; Tmari_1097. DR GeneID; 898673; -. DR KEGG; tma:TM1092; -. DR KEGG; tmi:THEMA_08890; -. DR KEGG; tmm:Tmari_1097; -. DR KEGG; tmw:THMA_1115; -. DR PATRIC; 23937115; VBITheMar51294_1106. DR OMA; GLWARSQ; -. DR OrthoDB; EOG6HJ24C; -. DR BioCyc; TMAR243274:GC6P-1121-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 276 AA; 31882 MW; 4D530F15C8B65986 CRC64; MFENILWKMV KKRLIPKRKI SRVHRSRKGV KRVVCVAFPL DQMFKSADDF IDALMEILQE DLPFVDLLIF PRLTGNLLAG VSPIRIENFE KLDPFYTDLL RYISKGLDVP IVAPGVETFR TSPDVLVIEN GEVLHRYTLR ERFAVADFGE WYAAVLRKED TLSSKALRPL VEKNVFAFIH FDLETEENDW WKEKKGLWAR SQSLEVFGIK VSPRGTFLGK TYRGKSYVSA PIPLTPNLTG FLRQDCGVKM SVDLELDLLK GKRHRIDTVK HILFRG // ID Q9X0T9_THEMA Unreviewed; 626 AA. AC Q9X0T9; G4FED4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=NADH dehydrogenase, putative {ECO:0000313|EMBL:AAD36287.1}; DE SubName: Full=NADH-ubiquinone oxidoreductase chain M {ECO:0000313|EMBL:AGL50143.1}; DE EC=1.6.5.3 {ECO:0000313|EMBL:AGL50143.1}; GN OrderedLocusNames=TM_1212 {ECO:0000313|EMBL:AAD36287.1}; GN ORFNames=Tmari_1219 {ECO:0000313|EMBL:AGL50143.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36287.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36287.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36287.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50143.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50143.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000320}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU000320}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36287.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50143.1; -; Genomic_DNA. DR PIR; B72281; B72281. DR RefSeq; NP_229017.1; NC_000853.1. DR RefSeq; WP_004080094.1; NZ_CP011107.1. DR STRING; 243274.TM1212; -. DR EnsemblBacteria; AAD36287; AAD36287; TM_1212. DR EnsemblBacteria; AGL50143; AGL50143; Tmari_1219. DR GeneID; 898272; -. DR KEGG; tma:TM1212; -. DR KEGG; tmi:THEMA_08270; -. DR KEGG; tmm:Tmari_1219; -. DR KEGG; tmw:THMA_1238; -. DR PATRIC; 23937366; VBITheMar51294_1230. DR eggNOG; ENOG4108JPZ; Bacteria. DR eggNOG; COG0651; LUCA. DR KO; K00342; -. DR OMA; TWPILSV; -. DR OrthoDB; EOG6ZH2D5; -. DR BioCyc; TMAR243274:GC6P-1242-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR InterPro; IPR001750; ND/Mrp_mem. DR Pfam; PF00361; Proton_antipo_M; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50143.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Ubiquinone {ECO:0000313|EMBL:AGL50143.1}. FT TRANSMEM 6 21 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 28 48 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 68 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 115 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 121 138 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 150 172 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 192 217 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 229 253 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 273 291 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 298 318 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 330 349 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 370 391 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 403 423 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 444 465 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 506 526 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 607 624 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 117 415 Proton_antipo_M. FT {ECO:0000259|Pfam:PF00361}. SQ SEQUENCE 626 AA; 70410 MW; AEA3E1756A87B66A CRC64; MALGLLPLVL LTLSIFIYLV SKMSWKMGAL LNFLAGLFTI LYVFTLKVGT FEKLDLFGLN IQFEWTNVSF YFSFVSLLVI VSVMLFSTKW LETQKYRASY NMFLLMVTAG SLGVFMAADL ITLYVFWEIA VLSSLLIVPM EKKEARKAVV VYAVMSAVGT YAFLYGTFLA YQRYGTLNIH GIAQGMLNDT SIGFKMAVFL LLSAAGIAKS GIFPLHIWLR ETHGLAPNAF SSVLSGQFIK LGNYIFLLVL SVIPSLKVFS EVTVYSGIPL PNYILIALGN VSIVIGTLMA IKQDDMKMLM AYSSVANGGY ILIGIGTMDP LGFEGGMFHI FNHAVASAVI FMAFAAVIYR TKTQKISEMG GLIHKMPVTF LVYLFSIISL AGIPPMSGFI SKWMIYQALV RKGMFITAFL AFFGSIGSFL YVFRPLAGVF LGQLPRKYRD VKEAPAVMLT PMVLLVLISF FLGVWPFPIL QAIEKIRVDL DVAPSFKISD PENWLVKGFA GSWNPVLVFG LFLVGFIVAY ILYSLFPRPK KVDLLAPHRE EGTPINIYTG GEFIYNPDLY HYNTKFYAGF ERMYEKHPSW EKLLKMFGKL FHDAGEWIHS WFFEPSSSAY TFWVVVTLLL VFWVRW // ID Q9X1L6_THEMA Unreviewed; 285 AA. AC Q9X1L6; G4FFR8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Electron transfer flavoprotein, beta subunit {ECO:0000313|EMBL:AAD36597.1}; GN OrderedLocusNames=TM_1530 {ECO:0000313|EMBL:AAD36597.1}; GN ORFNames=Tmari_1538 {ECO:0000313|EMBL:AGL50462.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36597.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36597.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36597.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50462.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50462.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36597.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50462.1; -; Genomic_DNA. DR PIR; F72241; F72241. DR RefSeq; NP_229330.1; NC_000853.1. DR RefSeq; WP_004081902.1; NZ_CP011107.1. DR STRING; 243274.TM1530; -. DR EnsemblBacteria; AAD36597; AAD36597; TM_1530. DR EnsemblBacteria; AGL50462; AGL50462; Tmari_1538. DR GeneID; 897981; -. DR KEGG; tma:TM1530; -. DR KEGG; tmi:THEMA_06635; -. DR KEGG; tmm:Tmari_1538; -. DR KEGG; tmw:THMA_1564; -. DR PATRIC; 23938020; VBITheMar51294_1548. DR eggNOG; ENOG4105BZJ; Bacteria. DR eggNOG; COG2086; LUCA. DR KO; K03521; -. DR OMA; REALCMG; -. DR OrthoDB; EOG6Z9B4C; -. DR BioCyc; TMAR243274:GC6P-1570-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR014730; ETF_a/b_N. DR InterPro; IPR012255; ETF_b. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR21294; PTHR21294; 1. DR Pfam; PF01012; ETF; 1. DR PIRSF; PIRSF000090; Beta-ETF; 1. DR SMART; SM00893; ETF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 22 219 ETF. {ECO:0000259|SMART:SM00893}. SQ SEQUENCE 285 AA; 31575 MW; E94E3D0DD98E3F20 CRC64; MNVVVCIKQV PDTTNVRIDR KTNNLVREGV PSIINPDDER ALELASQLKE KFGATVYVIT MGPPQAKEAL KDAIAFGLDE AVHLSDRTFA GADTLATTYT LYWGIKKIEE RIGKIDLILT GKQAVDGDTG QVGPGLATRF GYALGAYVVR IEEIDPEKKE MVIVRRLDQG FEKIRLKLPA VLTITDELNK PRYADLPNLI RAIRYEPIVW THKDLGLDPK KCGFFGSPTR VVSTNIPPAR KGGDIISKNE DPEVAAEKLI EALKKFEAVR LVEALKPVLE GEKDE // ID Q9X0T3_THEMA Unreviewed; 82 AA. AC Q9X0T3; G4FEE0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Na(+) H(+) antiporter subunit F {ECO:0000313|EMBL:AGL50137.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36281.1}; GN OrderedLocusNames=TM_1206 {ECO:0000313|EMBL:AAD36281.1}; GN ORFNames=Tmari_1213 {ECO:0000313|EMBL:AGL50137.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36281.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36281.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36281.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50137.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50137.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36281.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50137.1; -; Genomic_DNA. DR PIR; D72280; D72280. DR RefSeq; NP_229011.1; NC_000853.1. DR RefSeq; WP_004080106.1; NZ_CP011107.1. DR STRING; 243274.TM1206; -. DR EnsemblBacteria; AAD36281; AAD36281; TM_1206. DR EnsemblBacteria; AGL50137; AGL50137; Tmari_1213. DR GeneID; 898278; -. DR KEGG; tma:TM1206; -. DR KEGG; tmi:THEMA_08300; -. DR KEGG; tmm:Tmari_1213; -. DR KEGG; tmw:THMA_1232; -. DR PATRIC; 23937354; VBITheMar51294_1224. DR eggNOG; ENOG41084EI; Bacteria. DR eggNOG; COG2212; LUCA. DR KO; K05570; -. DR OMA; RTIYIDI; -. DR OrthoDB; EOG693GW3; -. DR BioCyc; TMAR243274:GC6P-1236-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015075; F:ion transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR007208; MrpF/PhaF-like. DR Pfam; PF04066; MrpF_PhaF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 51 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 78 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 82 AA; 9090 MW; 55D2B15BB48E8BFD CRC64; MSLLFFVLVG AGVLLSFIRV IIGPTSSDRV AALDTMNVML TGLIVFLAYV FDRAIYLDIA LVYALLSFLE TIIVSRYLEG RK // ID Q9X0Y3_THEMA Unreviewed; 577 AA. AC Q9X0Y3; G4FE92; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 121. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36339.1}; GN OrderedLocusNames=TM_1256 {ECO:0000313|EMBL:AAD36339.1}; GN ORFNames=Tmari_1261 {ECO:0000313|EMBL:AGL50185.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36339.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36339.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36339.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50185.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50185.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36339.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50185.1; -; Genomic_DNA. DR PIR; C72275; C72275. DR RefSeq; NP_229061.1; NC_000853.1. DR RefSeq; WP_004080006.1; NZ_CP011107.1. DR STRING; 243274.TM1256; -. DR DNASU; 898227; -. DR EnsemblBacteria; AAD36339; AAD36339; TM_1256. DR EnsemblBacteria; AGL50185; AGL50185; Tmari_1261. DR GeneID; 898227; -. DR KEGG; tma:TM1256; -. DR KEGG; tmm:Tmari_1261; -. DR KEGG; tmw:THMA_1281; -. DR PATRIC; 23937452; VBITheMar51294_1272. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K06147; -. DR OMA; FRLTIIA; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1287-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0034040; F:lipid-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0006869; P:lipid transport; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD36339.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD36339.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 18 39 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 77 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 154 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 160 182 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 247 268 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 280 301 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 19 303 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 336 571 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 577 AA; 65813 MW; C7644B50AC943A72 CRC64; MKTSSILVDF LKRNWHKYLL GVLSLIAVDL LQVYIPRVIG KIVDMLNTET MNFDTLKIML FWVMAAASGM FIGRFFWRFF LGGTARKFFL ETSNKMFSKL LSLTPGFFDR MKSGELMARF TNDLSLLRRV LGQGAILFFD SFIMIVMVFF FMIGNVGWKL SWISFAPLLL LAPVSMSFGR LIHRKVSEVQ RSFSELSGFT EETISSVRIV KSFSVEDVSF KIFENRALKN YEDTLSAIKV SSVFRPLINL IASTAFFLAL LYGGRAVING KISLGDFIAF NSYLGMLVWP MMAYGFMVDL FQRGRAAMRR LDTIFTAQPE VKEPEKPIRI DHFESFEVRN LTYRYPGTER EVLKNVTMKI NRGEMIGIAG SVGSGKSTIA KLLVKLYPVE RGKIFINGVD INDVSSENIR SIVTLVPQET FLFSDTVRNN ITVGLENVDE KKIEEVTKLA AVYDDIMSFP EKFDTIVGER GVTLSGGQKQ RITIARALIR DFEVYIFDDC LSAVDPETEE RIIDSIRKGM KGKTIVVITH RLKVLKNADR IYVLHEGRVI EEGTHEELMI RDGMYSRMYR KQLIEEG // ID Q9WY24_THEMA Unreviewed; 189 AA. AC Q9WY24; G4FH94; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35273.1}; GN OrderedLocusNames=TM_0180 {ECO:0000313|EMBL:AAD35273.1}; GN ORFNames=Tmari_0178 {ECO:0000313|EMBL:AGL49104.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35273.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35273.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35273.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49104.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49104.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35273.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49104.1; -; Genomic_DNA. DR PIR; G72407; G72407. DR RefSeq; NP_227995.1; NC_000853.1. DR RefSeq; WP_004082815.1; NZ_CP011107.1. DR STRING; 243274.TM0180; -. DR EnsemblBacteria; AAD35273; AAD35273; TM_0180. DR EnsemblBacteria; AGL49104; AGL49104; Tmari_0178. DR GeneID; 897027; -. DR KEGG; tma:TM0180; -. DR KEGG; tmi:THEMA_03875; -. DR KEGG; tmm:Tmari_0178; -. DR KEGG; tmw:THMA_0181; -. DR PATRIC; 23935216; VBITheMar51294_0181. DR OMA; DVTLWVI; -. DR OrthoDB; EOG6J1DDX; -. DR BioCyc; TMAR243274:GC6P-186-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 189 AA; 20470 MW; 1AF4F2C2CFBAA5C0 CRC64; MKRVLIWSAL ITAGILVLIS GCIPVPIPID LGNLGIEPQV FEIPAGSSST LETTSASFTV KAEDVKNAQQ KAGVPGTVHF HNIEVSGKIT VEGDLRFVGF IRFALEEPSS TPTTGDVTIR IDTSQESEYS FPISADDSDA LRTALNRINN GEDVTLWVIF GQNEYESTTG ATVTVTITNV RLWVTWTAW // ID Q9X1G0_THEMA Unreviewed; 529 AA. AC Q9X1G0; G4FFI3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 84. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36516.1}; GN OrderedLocusNames=TM_1448 {ECO:0000313|EMBL:AAD36516.1}; GN ORFNames=Tmari_1454 {ECO:0000313|EMBL:AGL50378.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36516.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36516.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36516.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50378.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50378.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36516.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50378.1; -; Genomic_DNA. DR PIR; D72253; D72253. DR RefSeq; NP_229247.1; NC_000853.1. DR RefSeq; WP_004081724.1; NZ_CP011107.1. DR STRING; 243274.TM1448; -. DR EnsemblBacteria; AAD36516; AAD36516; TM_1448. DR EnsemblBacteria; AGL50378; AGL50378; Tmari_1454. DR GeneID; 898028; -. DR KEGG; tma:TM1448; -. DR KEGG; tmi:THEMA_07075; -. DR KEGG; tmm:Tmari_1454; -. DR KEGG; tmw:THMA_1478; -. DR PATRIC; 23937848; VBITheMar51294_1462. DR eggNOG; ENOG4105IU8; Bacteria. DR eggNOG; ENOG4111Q70; LUCA. DR OMA; IFVHIDS; -. DR OrthoDB; EOG657J73; -. DR BioCyc; TMAR243274:GC6P-1486-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR011044; Quino_amine_DH_bsu. DR InterPro; IPR011990; TPR-like_helical_dom. DR SUPFAM; SSF48452; SSF48452; 1. DR SUPFAM; SSF50969; SSF50969; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 529 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972262. SQ SEQUENCE 529 AA; 60657 MW; 3320E34A42740CE8 CRC64; MKKTILLLFL LTFSALFAQS VREMFSEAII DWAKGDISSA QQKIEEIFYK PIPAENLAEF WYLRAKLMIE TGRVREAYED LKNLLVIVPD QPEVLSLVNN LEFILQDKES DSFNMKTLKT LQGFKDGIEY FLTPTDVSIF GESIYIVDPV NNRLIESDGF NFTVRNLSFQ PEQVFTDRDG NVFLISRDGR VFKNEKEIGK FLNPIGAGVL NSGEFTLADV DKIVLISENG LKREIPIDGK PLIVDAEVYC RQVVVLDTWS NSLIVINVDT ESQKNIPLPV PTRSFEIFYD GSYLLLDQSG NLFHFDGKKL QTIGQVPQYV NIEYEYPYLF GMNWDKNSIE ISLLKSSEPI FVHIDSFELT VDKMFLYVRV ENAFGRDIDL VQLFSDLFEA RGRVPFEVSH ELREYTVYIS DEEFLSKKVY QINDRKGYCV VVPPDITFSN EQLAVLKLKN VKLYTSPEAS AALKDFCYRS GGGIGEPHFL KHNLWVFSFS YVKPITEEII PISVSFKTPD MNYSDTIYVT KKVIELGLQ // ID Q9X2C7_THEMA Unreviewed; 379 AA. AC Q9X2C7; G4FGJ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=CRISPR-associated protein, Csm5 family {ECO:0000313|EMBL:AGL50742.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36870.1}; GN OrderedLocusNames=TM_1807 {ECO:0000313|EMBL:AAD36870.1}; GN ORFNames=Tmari_1818 {ECO:0000313|EMBL:AGL50742.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36870.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36870.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36870.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50742.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50742.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36870.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50742.1; -; Genomic_DNA. DR PIR; D72208; D72208. DR RefSeq; NP_229604.1; NC_000853.1. DR RefSeq; WP_004082354.1; NZ_CP011107.1. DR STRING; 243274.TM1807; -. DR EnsemblBacteria; AAD36870; AAD36870; TM_1807. DR EnsemblBacteria; AGL50742; AGL50742; Tmari_1818. DR GeneID; 897831; -. DR KEGG; tma:TM1807; -. DR KEGG; tmi:THEMA_05155; -. DR KEGG; tmm:Tmari_1818; -. DR KEGG; tmw:THMA_1853; -. DR PATRIC; 23938603; VBITheMar51294_1828. DR eggNOG; COG1332; LUCA. DR KO; K19140; -. DR OMA; DYIEHEL; -. DR OrthoDB; EOG686NDM; -. DR BioCyc; TMAR243274:GC6P-1858-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR010173; CRISPR-assoc_prot_TM1807. DR InterPro; IPR005537; RAMP_III_fam. DR Pfam; PF03787; RAMPs; 1. DR TIGRFAMs; TIGR01899; cas_TM1807_csm5; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 379 AA; 44637 MW; 9965AE4260BA2D31 CRC64; MKVTLKTLTP LHIGSGEKYP PCNLVVLKEE ENKKTAVRLI TRKFLEVLRK HPEIKQNISE NISKPLSFKE VENVEDGVFY EVSLYSDFSS GKKNPEIPEV VHHPDGSVYV PGSSLKGAVR LALTWHVLRN NRNLLEEFRR NVQKDLQNHK RAFYQTNEFL NGLFRFAPKE INTDYFRFLR VSDSQTLRTQ LVVHDVGIFY VARPNTHPRT FPLEFVPINR DFVFDVRFVK EEYDYFLTHV RKRYGVELPG SIEEIFSIVN EFYSEVFKFE RERFKKAKEN FEKLDTSKIE ERFQKIEKVL QSKKYVLIHI GYGGGLMANS LFILLDEETR KQVRNIIKYH KDDEAPLTRR YLVQSENNSY RVISPIGWCA LWLEDSQST // ID Q9X292_THEMA Unreviewed; 109 AA. AC Q9X292; G4FGF8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36834.1}; GN OrderedLocusNames=TM_1771 {ECO:0000313|EMBL:AAD36834.1}; GN ORFNames=Tmari_1780 {ECO:0000313|EMBL:AGL50704.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36834.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36834.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36834.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50704.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50704.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36834.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50704.1; -; Genomic_DNA. DR PIR; B72213; B72213. DR RefSeq; NP_229568.1; NC_000853.1. DR RefSeq; WP_004082317.1; NZ_CP011107.1. DR STRING; 243274.TM1771; -. DR EnsemblBacteria; AAD36834; AAD36834; TM_1771. DR EnsemblBacteria; AGL50704; AGL50704; Tmari_1780. DR GeneID; 897851; -. DR KEGG; tma:TM1771; -. DR KEGG; tmi:THEMA_05370; -. DR KEGG; tmm:Tmari_1780; -. DR KEGG; tmw:THMA_1815; -. DR PATRIC; 23938522; VBITheMar51294_1790. DR eggNOG; ENOG41084Z7; Bacteria. DR eggNOG; COG1302; LUCA. DR OMA; AYVELEY; -. DR OrthoDB; EOG6GFGP8; -. DR BioCyc; TMAR243274:GC6P-1820-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR005531; Asp23. DR Pfam; PF03780; Asp23; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 109 AA; 12175 MW; FB7291FEA8D8F853 CRC64; MRIMLENGEL EITLNALKKI VYFATLESYG TVGLGDSRSF FERIFGGDRG IKIEELEDSS LNVDVYIEVE YGVNIREVAK NIADNVAHKL KTLAGCEKLN ITVHVVGIR // ID Q9X0P8_THEMA Unreviewed; 282 AA. AC Q9X0P8; G4FEI1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=2-oxoacid ferredoxin oxidoreductase, beta subunit {ECO:0000313|EMBL:AAD36241.1}; DE SubName: Full=2-oxoglutarate oxidoreductase, beta subunit {ECO:0000313|EMBL:AGL50096.1}; DE EC=1.2.7.3 {ECO:0000313|EMBL:AGL50096.1}; GN OrderedLocusNames=TM_1165 {ECO:0000313|EMBL:AAD36241.1}; GN ORFNames=Tmari_1172 {ECO:0000313|EMBL:AGL50096.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36241.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36241.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36241.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50096.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50096.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36241.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50096.1; -; Genomic_DNA. DR PIR; C72288; C72288. DR RefSeq; NP_228971.1; NC_000853.1. DR RefSeq; WP_004080204.1; NZ_CP011107.1. DR STRING; 243274.TM1165; -. DR EnsemblBacteria; AAD36241; AAD36241; TM_1165. DR EnsemblBacteria; AGL50096; AGL50096; Tmari_1172. DR GeneID; 898321; -. DR KEGG; tma:TM1165; -. DR KEGG; tmi:THEMA_08510; -. DR KEGG; tmm:Tmari_1172; -. DR KEGG; tmw:THMA_1190; -. DR PATRIC; 23937267; VBITheMar51294_1182. DR eggNOG; ENOG4105DQU; Bacteria. DR eggNOG; COG1013; LUCA. DR KO; K00175; -. DR OMA; AGKMPHY; -. DR OrthoDB; EOG647TWJ; -. DR BioCyc; TMAR243274:GC6P-1194-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR032686; PFO_beta_C. DR InterPro; IPR011896; PorB_KorB. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF12367; PFO_beta_C; 1. DR Pfam; PF02775; TPP_enzyme_C; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR TIGRFAMs; TIGR02177; PorB_KorB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50096.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 50 193 TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}. FT DOMAIN 197 256 PFO_beta_C. {ECO:0000259|Pfam:PF12367}. SQ SEQUENCE 282 AA; 31750 MW; 6670F18CAC328797 CRC64; MRLDEYISRD IAWCPGCGNF GIRTALMKAL EELNVDPRQV VIVSGIGQAA KMPQYVGVNM FNGLHGRALP VATAIKTTNP NLLVIAESGD GCMYGEGGNH FIHTIRRNPD IVNIVHDNQV YGLTKGQASP TSLKGFKTPV QVDGVILEPF NPLAVAIALD ASFVARTFIG DIEFTKDILK EAMKHKGYAL VDILQPCVTF NKLNTYEWYR ENTYYLKDHD PTDRELAFKR AIETEKLPLG IFYVNKNKET FEELARKGDR TPLYEYEVNF EKLKELIESK KS // ID Q9X2D0_THEMA Unreviewed; 140 AA. AC Q9X2D0; G4FGJ8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 77. DE SubName: Full=CRISPR-associated protein, Csm2 family {ECO:0000313|EMBL:AGL50745.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36873.1}; GN OrderedLocusNames=TM_1810 {ECO:0000313|EMBL:AAD36873.1}; GN ORFNames=Tmari_1821 {ECO:0000313|EMBL:AGL50745.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36873.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36873.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36873.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50745.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50745.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). RN [3] {ECO:0000213|PDB:5AN6} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 6-128. RX PubMed=26663887; DOI=10.1111/FEBS.13621; RA Gallo G., Augusto G., Rangel G., Zelanis A., Mori M.A., Campos C.B., RA Wurtele M.; RT "Structural basis for dimer formation of the CRISPR-associated protein RT Csm2 of Thermotoga maritima."; RL FEBS J. 283:694-703(2016). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36873.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50745.1; -; Genomic_DNA. DR PIR; G72208; G72208. DR RefSeq; NP_229607.1; NC_000853.1. DR RefSeq; WP_004082357.1; NZ_CP011107.1. DR PDB; 5AN6; X-ray; 2.40 A; A/B/C=6-128. DR PDBsum; 5AN6; -. DR STRING; 243274.TM1810; -. DR EnsemblBacteria; AAD36873; AAD36873; TM_1810. DR EnsemblBacteria; AGL50745; AGL50745; Tmari_1821. DR GeneID; 897377; -. DR KEGG; tma:TM1810; -. DR KEGG; tmi:THEMA_05140; -. DR KEGG; tmm:Tmari_1821; -. DR KEGG; tmw:THMA_1856; -. DR PATRIC; 23938609; VBITheMar51294_1831. DR eggNOG; ENOG4107FSC; Bacteria. DR eggNOG; COG1421; LUCA. DR KO; K19138; -. DR OMA; ELVEVWH; -. DR OrthoDB; EOG6NSGMD; -. DR BioCyc; TMAR243274:GC6P-1861-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR010149; CRISPR-assoc_prot_TM1810_C. DR Pfam; PF03750; DUF310; 1. DR TIGRFAMs; TIGR01870; cas_TM1810_Csm2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:5AN6}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 11 129 DUF310. {ECO:0000259|Pfam:PF03750}. SQ SEQUENCE 140 AA; 16721 MW; 83E2B874D37D845E CRC64; MAVSQGVSLK EDLKDLVRKA EEIGRELSGK LKTNQLRKFH GHLTKIWSNY IYKKKDYRDN PEKFNEEILN ELHFMKIFLA YQVGRDIEGI SELKEILEPL IDEIKTPDEF EKFKKFYDAI LAYHKFHSES EKSNRRTARR // ID Q9X0W0_THEMA Unreviewed; 265 AA. AC Q9X0W0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE SubName: Full=ABC transporter, permease protein {ECO:0000313|EMBL:AGL50164.1}; DE SubName: Full=Sugar ABC transporter, permease protein, putative {ECO:0000313|EMBL:AAD36308.1}; GN OrderedLocusNames=TM_1233 {ECO:0000313|EMBL:AAD36308.1}; GN ORFNames=Tmari_1240 {ECO:0000313|EMBL:AGL50164.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36308.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36308.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36308.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50164.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50164.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36308.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50164.1; -; Genomic_DNA. DR PIR; B72279; B72279. DR RefSeq; NP_229038.1; NC_000853.1. DR RefSeq; WP_010865285.1; NZ_CP011107.1. DR STRING; 243274.TM1233; -. DR EnsemblBacteria; AAD36308; AAD36308; TM_1233. DR EnsemblBacteria; AGL50164; AGL50164; Tmari_1240. DR GeneID; 898251; -. DR KEGG; tma:TM1233; -. DR KEGG; tmi:THEMA_08165; -. DR KEGG; tmm:Tmari_1240; -. DR KEGG; tmw:THMA_1259; -. DR PATRIC; 23937408; VBITheMar51294_1251. DR eggNOG; ENOG4108PZ5; Bacteria. DR eggNOG; COG0395; LUCA. DR KO; K02026; -. DR OMA; QFAIKLS; -. DR BioCyc; TMAR243274:GC6P-1263-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 7 30 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 67 90 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 111 127 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 133 156 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 177 199 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 232 252 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 65 252 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 265 AA; 29166 MW; 55A36C188B949B81 CRC64; MMKKFFIIFL SVIISLWFLT PVFFIVLASL TPSSDYYNPS RIFPSSLTLE HLYKLFVTLG GGKATLVSVQ VALISIGISF LLGLPAGYAL TRYVFPGKNI IRLSMLMTRS IPLIVVAVPL VVLYMRFNLA DTTLGVALAH ASMILPFVVL ITSSVFSGIS VEYEEAGMVF GLSRFQAFIR ITLPLALPGL AASAIFAFIM SWNEVFASSI LTLTNRTLPA HILNTAMASP DYFKFAAGTI MAVPAMVFIF FIRKYLVSMW GITLK // ID Q9WZH4_THEMA Unreviewed; 863 AA. AC Q9WZH4; G4FDA9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 112. DE SubName: Full=tRNA nucleotidyl transferase-related protein {ECO:0000313|EMBL:AAD35797.1}; DE SubName: Full=tRNA nucleotidyltransferase {ECO:0000313|EMBL:AGL49640.1}; DE EC=2.7.7.72 {ECO:0000313|EMBL:AGL49640.1}; GN OrderedLocusNames=TM_0715 {ECO:0000313|EMBL:AAD35797.1}; GN ORFNames=Tmari_0715 {ECO:0000313|EMBL:AGL49640.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35797.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35797.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35797.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49640.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49640.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: A tRNA precursor + 2 CTP + ATP = a tRNA with a CC 3' CCA end + 3 diphosphate. {ECO:0000256|SAAS:SAAS00415332}. CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) CC polymerase family. {ECO:0000256|RuleBase:RU003953, CC ECO:0000256|SAAS:SAAS00534214}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35797.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49640.1; -; Genomic_DNA. DR PIR; B72344; B72344. DR RefSeq; NP_228524.1; NC_000853.1. DR RefSeq; WP_004081021.1; NZ_CP011107.1. DR PDB; 3H37; X-ray; 2.85 A; A/B=437-863. DR PDB; 3H38; X-ray; 2.37 A; A=437-863. DR PDB; 3H39; X-ray; 2.85 A; A/B=437-863. DR PDB; 3H3A; X-ray; 2.80 A; A/B=437-863. DR PDBsum; 3H37; -. DR PDBsum; 3H38; -. DR PDBsum; 3H39; -. DR PDBsum; 3H3A; -. DR STRING; 243274.TM0715; -. DR EnsemblBacteria; AAD35797; AAD35797; TM_0715. DR EnsemblBacteria; AGL49640; AGL49640; Tmari_0715. DR GeneID; 898382; -. DR KEGG; tma:TM0715; -. DR KEGG; tmi:THEMA_01090; -. DR KEGG; tmm:Tmari_0715; -. DR KEGG; tmw:THMA_0730; -. DR PATRIC; 23936348; VBITheMar51294_0727. DR eggNOG; ENOG4107QU1; Bacteria. DR eggNOG; COG0517; LUCA. DR eggNOG; COG0617; LUCA. DR eggNOG; COG0618; LUCA. DR KO; K00974; -. DR OMA; VMALGIH; -. DR OrthoDB; EOG6091FN; -. DR BioCyc; TMAR243274:GC6P-741-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR003156; DHHA1_dom. DR InterPro; IPR002646; PolA_pol_head_dom. DR InterPro; IPR032828; PolyA_RNA-bd. DR Pfam; PF00571; CBS; 2. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02272; DHHA1; 1. DR Pfam; PF01743; PolyA_pol; 1. DR Pfam; PF12627; PolyA_pol_RNAbd; 1. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3H37, ECO:0000213|PDB:3H38, KW ECO:0000213|PDB:3H39, ECO:0000213|PDB:3H3A}; KW ATP-binding {ECO:0000213|PDB:3H39, ECO:0000256|SAAS:SAAS00415369}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000213|PDB:3H39, KW ECO:0000256|SAAS:SAAS00415369}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00415426, KW ECO:0000313|EMBL:AGL49640.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW RNA-binding {ECO:0000256|RuleBase:RU003953, KW ECO:0000256|SAAS:SAAS00415356}; KW Transferase {ECO:0000256|SAAS:SAAS00415426, KW ECO:0000313|EMBL:AGL49640.1}. FT DOMAIN 308 364 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 370 426 CBS. {ECO:0000259|PROSITE:PS51371}. FT NP_BIND 477 480 CTP. {ECO:0000213|PDB:3H3A}. FT NP_BIND 564 565 ATP. {ECO:0000213|PDB:3H39}. FT NP_BIND 609 618 ATP. {ECO:0000213|PDB:3H39}. FT NP_BIND 609 618 CTP. {ECO:0000213|PDB:3H3A}. FT BINDING 480 480 ATP. {ECO:0000213|PDB:3H39}. FT BINDING 565 565 CTP. {ECO:0000213|PDB:3H3A}. FT BINDING 569 569 ATP; via carbonyl oxygen. FT {ECO:0000213|PDB:3H39}. FT BINDING 569 569 CTP; via carbonyl oxygen. FT {ECO:0000213|PDB:3H3A}. FT BINDING 622 622 ATP. {ECO:0000213|PDB:3H39}. FT BINDING 622 622 CTP. {ECO:0000213|PDB:3H3A}. SQ SEQUENCE 863 AA; 98049 MW; 079E3E0A7C30C3BF CRC64; MRVITTHRSP DFDAFASCVA AKKLLDDHII VLPSNPARNL SDFLKVYSDR FEFVWDHEFE GEITELVIVD APSLDRIPES IRKKAQGAKI TVYDHHVDES PYDGIVSKVG ATITILVELI REKNIPLDPT EATLFMIALY DDTGNLLFSS TTPRDLEIAK FLLENGANLD EVALYTREEL TPRQMELLDD LIENARDYEV NGVPITISMI ECEDFVGGLG LIVSKAWEMM GKETFIAIVK MGKKIYVIGR TSSPDVDLGS LMKDLGGGGH TRAASATITG KEIDEVLKEV LNRLHDHVVP LLRARDIMSS PVKVVLSNMT IKEVDRLMKQ TGHSGFPVVE GNRLVGIVTK KAVEKAMNHG LGDRPVKSIM STNLVVASPD TPVTRLRELM VEHAIGRIPI LENGILVGIV TRSDVLRAIF GKPFKKYVMP VFQANGQIFR DVSKLLVERV DPKILNLFRL LGKFGDEVNM PVYVVGGFVR DLLLGIKNLD IDIVVEGNAL EFAEYAKRFL PGKLVKHDKF MTASLFLKGG LRIDIATARL EYYESPAKLP DVEMSTIKKD LYRRDFTINA MAIKLNPKDF GLLIDFFGGY RDLKEGVIRV LHTLSFVDDP TRILRAIRFE QRFDFRIEET TERLLKQAVE EGYLERTTGP RLRQELEKIL EEKNPLKSIR RMAQFDVIKH LFPKTYYTPS MDEKMENLFR NIPWVEENFG EVDRFYAVLH VFLEFYDDES WKEVRDRYSL RRNLINEIRH VEKSAPALLE MLSERVPASF VYPLVKGVSN ETICHFLAYL SGEKEGLFKS YLLKIKNTKL EKINGEYLIR KGITSGKIIG EVLEKILMKK LDGDTRDEEE ILEEVLASLE TEG // ID Q9WXY7_THEMA Unreviewed; 284 AA. AC Q9WXY7; G4FH48; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 99. DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:AGL49058.1}; DE EC=1.8.1.9 {ECO:0000313|EMBL:AGL49058.1}; DE SubName: Full=Thioredoxin reductase-related protein {ECO:0000313|EMBL:AAD35227.1}; GN OrderedLocusNames=TM_0134 {ECO:0000313|EMBL:AAD35227.1}; GN ORFNames=Tmari_0132 {ECO:0000313|EMBL:AGL49058.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35227.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35227.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35227.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49058.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49058.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35227.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49058.1; -; Genomic_DNA. DR PIR; D72413; D72413. DR RefSeq; NP_227949.1; NC_000853.1. DR RefSeq; WP_004082725.1; NZ_CP011107.1. DR STRING; 243274.TM0134; -. DR EnsemblBacteria; AAD35227; AAD35227; TM_0134. DR EnsemblBacteria; AGL49058; AGL49058; Tmari_0132. DR GeneID; 896961; -. DR KEGG; tma:TM0134; -. DR KEGG; tmi:THEMA_04135; -. DR KEGG; tmm:Tmari_0132; -. DR KEGG; tmw:THMA_0129; -. DR PATRIC; 23935110; VBITheMar51294_0133. DR eggNOG; ENOG4105U9C; Bacteria. DR eggNOG; COG0492; LUCA. DR OMA; FDALLIC; -. DR OrthoDB; EOG6K9QFP; -. DR BioCyc; TMAR243274:GC6P-134-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00469; PNDRDTASEII. DR SUPFAM; SSF51905; SSF51905; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49058.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 233 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. SQ SEQUENCE 284 AA; 31615 MW; 34AB75127980C7F0 CRC64; MRVGIVGAGP AGVAAAVFLR RYNVHVTVFE KNRVGGLLRN AHLVENIPVL PPASGEEICK TLEKRLFESG AELIWEEVVK VENEKILTER EIHSFDYVIV ASGTIPRRIP EFEVSEKVVY EFIDLPEFEK LAIYGAGDAA FDSALNALVR GKEVHLFNRG SRIRALPLLV ERAKKYEKFY YHERCPILKV EEESKMVKLK TEHGVFTFDA LLLSVGRLPN TSFVEPGERN FIVGDARGGF RQVSIAMGSA IETAMEILRR EGTVSATLPL KEGLLNPNGE HQAG // ID Q9WYI6_THEMA Unreviewed; 404 AA. AC Q9WYI6; G4FHR3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=Cell division protein FtsX {ECO:0000313|EMBL:AGL49274.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35438.1}; GN OrderedLocusNames=TM_0351 {ECO:0000313|EMBL:AAD35438.1}; GN ORFNames=Tmari_0349 {ECO:0000313|EMBL:AGL49274.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35438.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35438.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35438.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49274.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49274.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC {ECO:0000256|SAAS:SAAS00573676}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35438.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49274.1; -; Genomic_DNA. DR PIR; G72385; G72385. DR RefSeq; NP_228162.1; NC_000853.1. DR RefSeq; WP_004083141.1; NZ_CP011107.1. DR STRING; 243274.TM0351; -. DR EnsemblBacteria; AAD35438; AAD35438; TM_0351. DR EnsemblBacteria; AGL49274; AGL49274; Tmari_0349. DR GeneID; 897307; -. DR KEGG; tma:TM0351; -. DR KEGG; tmi:THEMA_02960; -. DR KEGG; tmm:Tmari_0349; -. DR KEGG; tmw:THMA_0359; -. DR PATRIC; 23935583; VBITheMar51294_0356. DR eggNOG; ENOG4108J5B; Bacteria. DR eggNOG; COG0577; LUCA. DR KO; K02004; -. DR OMA; VMAPKGA; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-365-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR InterPro; IPR003838; ABC_permease_dom. DR InterPro; IPR025857; MacB_PCD. DR Pfam; PF02687; FtsX; 1. DR Pfam; PF12704; MacB_PCD; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000313|EMBL:AGL49274.1}; KW Cell division {ECO:0000313|EMBL:AGL49274.1}; KW Cell membrane {ECO:0000256|SAAS:SAAS00573687}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00573687, KW ECO:0000256|SAAS:SAAS00573714, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00573714, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00573714, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 42 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 273 300 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 321 347 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 367 387 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 18 239 MacB_PCD. {ECO:0000259|Pfam:PF12704}. FT DOMAIN 281 397 FtsX. {ECO:0000259|Pfam:PF02687}. SQ SEQUENCE 404 AA; 43919 MW; 14B83A0BCDD5B934 CRC64; MEILKEVLRS LLANKMRTFL SMLGIVIGVT AVIMVMSLGA GMRESVTERL TSLGSNIIMI TPGFAGGRGG TIAQSVESLE EDDVEDILKM CPSVDKAIDL MSGSFLVQYR ETNTRSNVYS APPDIFHILN LKVSSGRTFS EEDSAANVAI IGQEVAYNLF GNENPVGKKI YLVQGNRKLV FEIIGIFERT GSILMFNPDN MILIPYETGK FRVFQTHGKV SMILATSKSA DVAQRAVMEI DHLLYTKFHE EESYYNIISQ QAILNVVSES VSIINLVLVA IAAVSLIVGG IGIMNIMLVS VVERTREIGI KMAIGASRLR ILLEFLVESV VITFVAGAIG VALGILGSNT IVNTFGSQYG LKAVVDPFSV IIAFGVSASV GLFFGFYPAY RASRLSPIEA LRYE // ID Q9WXW0_THEMA Unreviewed; 319 AA. AC Q9WXW0; G4FH20; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35199.1}; GN OrderedLocusNames=TM_0105 {ECO:0000313|EMBL:AAD35199.1}; GN ORFNames=Tmari_0102 {ECO:0000313|EMBL:AGL49028.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35199.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35199.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35199.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49028.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49028.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|SAAS:SAAS00582814}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35199.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49028.1; -; Genomic_DNA. DR PIR; A72419; A72419. DR RefSeq; NP_227921.1; NC_000853.1. DR RefSeq; WP_004082669.1; NZ_CP011107.1. DR STRING; 243274.TM0105; -. DR TCDB; 3.A.1.2.18; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35199; AAD35199; TM_0105. DR EnsemblBacteria; AGL49028; AGL49028; Tmari_0102. DR GeneID; 896932; -. DR KEGG; tma:TM0105; -. DR KEGG; tmi:THEMA_04280; -. DR KEGG; tmm:Tmari_0102; -. DR KEGG; tmw:THMA_0101; -. DR PATRIC; 23935050; VBITheMar51294_0103. DR eggNOG; ENOG4105DYV; Bacteria. DR eggNOG; COG1079; LUCA. DR KO; K02057; -. DR OMA; WVLYRTR; -. DR OrthoDB; EOG6MSS3R; -. DR BioCyc; TMAR243274:GC6P-105-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015749; P:monosaccharide transport; IBA:GOC. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00476327}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAAS:SAAS00476327, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00476193}. FT TRANSMEM 15 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 64 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 91 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 116 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 149 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 237 262 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 282 302 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 319 AA; 34272 MW; 142240DCAAE17F7B CRC64; MKILEVLWNI FSNPLFYKLT LTASTPLLFA SLGGVFSEVT GVVNIALEGI MLLGAFSSVV ITYYTGNVWL GFLLSIPIGI GFSWFHAWAS IKWRGNQIVS ATALILVAQG LTGFLMEPIF GQPGQTPYVG RIEEITLPGI SSIPFIGEAI GTISPIVLIA FAMVFFAWFL IYKTPLGLRM RSVGENPEAA DTLGVDVFKI RYFGVLMSGA LASMGGAFLS IGEVGNFREL MTGGRGFIAL AAMILGNWNP IGAMWACLMF GMSEALANQL QSSPILNVPA TAKPLFNLFP FVVTLVVVAG LIGRTRPPAA DGVPYEKEE // ID Q9X0K8_THEMA Unreviewed; 117 AA. AC Q9X0K8; G4FEM4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Flagellin protein FlaG {ECO:0000313|EMBL:AGL50054.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36200.1}; GN OrderedLocusNames=TM_1124 {ECO:0000313|EMBL:AAD36200.1}; GN ORFNames=Tmari_1130 {ECO:0000313|EMBL:AGL50054.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36200.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36200.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36200.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50054.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50054.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36200.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50054.1; -; Genomic_DNA. DR PIR; A72293; A72293. DR RefSeq; NP_228930.1; NC_000853.1. DR RefSeq; WP_004080293.1; NZ_CP011107.1. DR STRING; 243274.TM1124; -. DR DNASU; 898640; -. DR EnsemblBacteria; AAD36200; AAD36200; TM_1124. DR EnsemblBacteria; AGL50054; AGL50054; Tmari_1130. DR GeneID; 898640; -. DR KEGG; tma:TM1124; -. DR KEGG; tmi:THEMA_08725; -. DR KEGG; tmm:Tmari_1130; -. DR KEGG; tmw:THMA_1147; -. DR PATRIC; 23937183; VBITheMar51294_1140. DR eggNOG; ENOG41087GH; Bacteria. DR eggNOG; COG1334; LUCA. DR KO; K06603; -. DR OMA; STMRIDP; -. DR OrthoDB; EOG6ZPT31; -. DR BioCyc; TMAR243274:GC6P-1153-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR Gene3D; 3.30.160.170; -; 1. DR InterPro; IPR005186; FlaG. DR Pfam; PF03646; FlaG; 1. DR SUPFAM; SSF160214; SSF160214; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AGL50054.1}; KW Cilium {ECO:0000313|EMBL:AGL50054.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AGL50054.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 34 61 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 117 AA; 13692 MW; BDB44AF940E14A95 CRC64; MRIDPTDGKG NEVLRREITR RELHVKENES TPVAEMKKQQ EEDVQRAIEE FSKKLEKLRK IFRGEAEFKY DSELNMVIVK IKDTETGEII RQIPPEVMVK IAKSINELLG ILVDERV // ID Q9WYK5_THEMA Unreviewed; 1000 AA. AC Q9WYK5; G4FHT4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Cation efflux system protein, putative {ECO:0000313|EMBL:AAD35459.1}; DE SubName: Full=RND multidrug efflux transporter Acriflavin resistance protein {ECO:0000313|EMBL:AGL49295.1}; GN OrderedLocusNames=TM_0372 {ECO:0000313|EMBL:AAD35459.1}; GN ORFNames=Tmari_0370 {ECO:0000313|EMBL:AGL49295.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35459.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35459.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35459.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49295.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49295.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division CC (RND) (TC 2.A.6) family. {ECO:0000256|SAAS:SAAS00536972}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35459.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49295.1; -; Genomic_DNA. DR PIR; B72385; B72385. DR RefSeq; NP_228183.1; NC_000853.1. DR RefSeq; WP_004083186.1; NZ_CP011107.1. DR STRING; 243274.TM0372; -. DR EnsemblBacteria; AAD35459; AAD35459; TM_0372. DR EnsemblBacteria; AGL49295; AGL49295; Tmari_0370. DR GeneID; 897331; -. DR KEGG; tma:TM0372; -. DR KEGG; tmi:THEMA_02855; -. DR KEGG; tmm:Tmari_0370; -. DR KEGG; tmw:THMA_0380; -. DR PATRIC; 23935625; VBITheMar51294_0377. DR eggNOG; ENOG4105BZS; Bacteria. DR eggNOG; COG0841; LUCA. DR KO; K03296; -. DR OMA; EARIMVN; -. DR OrthoDB; EOG6SJJDZ; -. DR BioCyc; TMAR243274:GC6P-386-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 3.30.2090.10; -; 2. DR InterPro; IPR027463; AcrB_DN_DC_subdom. DR InterPro; IPR001036; Acrflvin-R. DR Pfam; PF00873; ACR_tran; 1. DR PRINTS; PR00702; ACRIFLAVINRP. DR SUPFAM; SSF82714; SSF82714; 2. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 329 348 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 355 376 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 382 406 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 426 451 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 457 480 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 512 530 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 842 859 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 866 888 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 894 916 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 937 956 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 968 994 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 1000 AA; 111705 MW; 1089AFF6F499FF51 CRC64; MKIAEISSKR PIAIFMLLMA VVFLGFISFQ HLKLDLLPQI EYPYAVVITT YMGAGTEEVE ELVTKPLEGY ISSTPGVRRF TSMSMDSVSF ILVEFDWNVK TSEAVGRLSR YVDLATRDLP EGANPVVVEF DPSLLPVYAF STEDDYEDVV SKIKRLPEVA SVEVMGKPEK IVEVILDQEK IKRFDVDPSL IETILSGNLV YPFGYVSDSE GNIYPVSVDG RFENIEDLKN TIVGFRGVKY QSLLQGKVPN ILVPVRLRNI AEVNITNESV QGEVRVNGKK ASLIAIYKRS GANTVKTVRE IKRILRDSKI NYIEAMNQAY YTERAIDNLL KNLLYGFIAA FVVVLIFLKD FTSTIVTSFS IPLSLTITFV LLYAFGLNLD TLTLGGLIMA LGMLVDNSIV VFENIYRHRS LGDPIPDAAR KGAGEVWLAI LASTLTTVSV FLPIVFFTGF VVRLFKYFAI AFVFALSSSL FVSTVVVPAG TRWIKPRRGK LTEALQKHYR KALEWCLKRK KLVLVISFAL VAISVIYLLS KPLGFLPSFQ TNLMVIDVKL PSQSSYEKTA EAVKQIEDYL NEHRNEYKIS SFYAEVGITN VYSQIMGRGQ NEARIMVNLG GSRREFAKNR EKLKNAISQL NIPEAKIEVL EQSQQIYEIL GYPVTIEVRG DDLSLIQEKA KEIFERLRKL QEVKKIQIRN SFEKEVLHVK IDRNKALMNG VVAGQVFLDL QTYLLGKKIG TLRTEEGTLP IVLKKAKFLS PEDLSKISLT GLKGDVPLGV VSNISRETLP SIVEHSDGER VVYVDLVSVE GSIGEVAKKV EKLLNEIDLS GVKVEITGQK SFMDEAFSEL QYVVYIAIAL VYMILAAQFE SFVLPFVIFF TIPFAVVGVA FAVFVNGYSL NVPVLVGLLT LSGTVVNNAI VMLTRIEQIR QEKGLLEATL EGAQSRLRPI LMTTFTTIVA LLPTALSHAE GSEIESPISW VVIFGMLISM LFTLFVIPVI YAAIRRKVRV // ID Q9X1A8_THEMA Unreviewed; 175 AA. AC Q9X1A8; G4FFC4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 101. DE SubName: Full=Ribosomal RNA small subunit methyltransferase D {ECO:0000313|EMBL:AGL50319.1}; DE EC=2.1.1.- {ECO:0000313|EMBL:AGL50319.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36458.1}; GN OrderedLocusNames=TM_1388 {ECO:0000313|EMBL:AAD36458.1}; GN ORFNames=Tmari_1395 {ECO:0000313|EMBL:AGL50319.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36458.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36458.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36458.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50319.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50319.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36458.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50319.1; -; Genomic_DNA. DR PIR; E72262; E72262. DR RefSeq; NP_229189.1; NC_000853.1. DR RefSeq; WP_004081591.1; NZ_CP011107.1. DR STRING; 243274.TM1388; -. DR EnsemblBacteria; AAD36458; AAD36458; TM_1388. DR EnsemblBacteria; AGL50319; AGL50319; Tmari_1395. DR GeneID; 898090; -. DR KEGG; tma:TM1388; -. DR KEGG; tmi:THEMA_07385; -. DR KEGG; tmm:Tmari_1395; -. DR KEGG; tmw:THMA_1415; -. DR PATRIC; 23937718; VBITheMar51294_1400. DR eggNOG; ENOG41083FP; Bacteria. DR eggNOG; COG0742; LUCA. DR OMA; IIICELH; -. DR OrthoDB; EOG64XXSX; -. DR BioCyc; TMAR243274:GC6P-1423-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0031167; P:rRNA methylation; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR004398; RNA_MeTrfase_RsmD. DR InterPro; IPR029063; SAM-dependent_MTases. DR PIRSF; PIRSF004553; CHP00095; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00095; TIGR00095; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Methyltransferase {ECO:0000313|EMBL:AGL50319.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL50319.1}. SQ SEQUENCE 175 AA; 19855 MW; 40AC2E824A1A3212 CRC64; MGETRITGGK YRGRKLKTGN FFRPTMSSVR SALFNMIDIE GKSFLELFCG SCVVSCEALS RGAERVVCVD RSKRALSICR KNLESLNETA TIIHSNVVDF LQNTGEKFDV VFLDPPYNDV EIINKTLSLL PKVMKEDSLA VLEKSKRIEL DFSNFEVVKR KDYGETELVF LKVKR // ID Q9X0F3_THEMA Unreviewed; 341 AA. AC Q9X0F3; G4FET5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 127. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36138.1}; DE SubName: Full=Putative rhamnose ABC transporter, ATP-binding component {ECO:0000313|EMBL:AGL49991.1}; GN OrderedLocusNames=TM_1063 {ECO:0000313|EMBL:AAD36138.1}; GN ORFNames=Tmari_1067 {ECO:0000313|EMBL:AGL49991.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36138.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36138.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36138.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49991.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49991.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36138.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49991.1; -; Genomic_DNA. DR PIR; B72300; B72300. DR RefSeq; NP_228869.1; NC_000853.1. DR RefSeq; WP_004080424.1; NZ_CP011107.1. DR STRING; 243274.TM1063; -. DR TCDB; 3.A.1.5.12; the atp-binding cassette (abc) superfamily. DR DNASU; 897776; -. DR EnsemblBacteria; AAD36138; AAD36138; TM_1063. DR EnsemblBacteria; AGL49991; AGL49991; Tmari_1067. DR GeneID; 897776; -. DR KEGG; tma:TM1063; -. DR KEGG; tmi:THEMA_09045; -. DR KEGG; tmm:Tmari_1067; -. DR KEGG; tmw:THMA_1085; -. DR PATRIC; 23937055; VBITheMar51294_1076. DR eggNOG; ENOG4108JQ7; Bacteria. DR eggNOG; COG4608; LUCA. DR KO; K02032; -. DR OMA; WALSRYP; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1092-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36138.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36138.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 4 262 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 341 AA; 38121 MW; 08AB5271A0941603 CRC64; MALLEVKNLK KYFPIIKRGF RRKVVGYLKA VDGISFHIEE GETLGLVGES GCGKTTTAKL IMRGIEPTEG EIVLNMDGEK VDITKLSEKE LREKGVRRFL QMIFQDPYSS LNPRMTVRDI IAEPLVVNGV IKGKEEIDAI VSDLLRAVGL RPEYMQRYPH AFSGGQRQRI AIARAIALKP KLVLCDEPTS ALDVSVQAQI INLLKDLQKE YNLTYLFISH DLGVVEHITN RVAVMYVGRI VELAETEELF SSPKHPYTEA LLSAVPKPDP KRKRKKAQLT GEVPDPSNPP SGCYFHPRCP YAKAICKEVY PDLRNVGTDQ NPHLVACHFA DSLKLEGVGT M // ID Q9WY33_THEMA Unreviewed; 344 AA. AC Q9WY33; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 89. DE SubName: Full=ABC-type Fe3+-siderophore transport system, permease component {ECO:0000313|EMBL:AGL49114.1}; DE SubName: Full=Iron(III) ABC transporter, permease protein, putative {ECO:0000313|EMBL:AAD35282.1}; GN OrderedLocusNames=TM_0190 {ECO:0000313|EMBL:AAD35282.1}; GN ORFNames=Tmari_0188 {ECO:0000313|EMBL:AGL49114.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35282.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35282.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35282.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49114.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49114.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. FecCD subfamily. CC {ECO:0000256|SAAS:SAAS00535775}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35282.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49114.1; -; Genomic_DNA. DR PIR; F72406; F72406. DR RefSeq; NP_228005.1; NC_000853.1. DR RefSeq; WP_008193921.1; NZ_CP011107.1. DR STRING; 243274.TM0190; -. DR EnsemblBacteria; AAD35282; AAD35282; TM_0190. DR EnsemblBacteria; AGL49114; AGL49114; Tmari_0188. DR GeneID; 897038; -. DR KEGG; tma:TM0190; -. DR KEGG; tmm:Tmari_0188; -. DR KEGG; tmw:THMA_0192; -. DR PATRIC; 23935240; VBITheMar51294_0192. DR eggNOG; ENOG4105EHG; Bacteria. DR eggNOG; COG0609; LUCA. DR KO; K02015; -. DR OMA; YAESSGR; -. DR OrthoDB; EOG61ZTDC; -. DR BioCyc; TMAR243274:GC6P-197-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR029022; ABC_BtuC-like. DR InterPro; IPR000522; ABC_transptr_permAse. DR PANTHER; PTHR30472; PTHR30472; 1. DR Pfam; PF01032; FecCD; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00417415}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00417415, KW ECO:0000256|SAAS:SAAS00417419, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00417419, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00417419, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00417373}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 118 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 150 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 162 183 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 203 223 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 250 277 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 289 307 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 319 339 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 344 AA; 36982 MW; B908653B6E48A41A CRC64; MVIYKNYVAR RILTILFLSF LLVLVGIYSL SHGGYSLSLK DIIGAFLGKG DRKAQLVIWS VRFPRVVTGI LVGASLAVSG AVMQGVLKNP LASPFTTGTS HGAMFGASLA IALGAGYSES TGSVTLNNPY TIALFAFLGA MSSSLVILLI GKLKEITPEA IVLMGVAMGS LFTAATTLIQ YFADDLELAT MVYWSFGDLG RTTWRENLIL LVIFLTVFAY FLWKAWDINA MVVGDEIAKS TGIEVEKVRL ILVVLSTLLT AISVAFVGII GFIGLLAPHM MRILFGEDYR FLIPLSALCG SVLLLSADTV ARVLLSPTVL PVGIVTSFLG APLFIYLLLH GEER // ID Q9WZL9_THEMA Unreviewed; 398 AA. AC Q9WZL9; G4FD63; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 89. DE SubName: Full=Lipopolysaccharide biosynthesis protein, putative {ECO:0000313|EMBL:AAD35842.1}; GN OrderedLocusNames=TM_0760 {ECO:0000313|EMBL:AAD35842.1}; GN ORFNames=Tmari_0761 {ECO:0000313|EMBL:AGL49686.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35842.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35842.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35842.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49686.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49686.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35842.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49686.1; -; Genomic_DNA. DR PIR; F72335; F72335. DR RefSeq; NP_228569.1; NC_000853.1. DR RefSeq; WP_004080941.1; NZ_CP011107.1. DR STRING; 243274.TM0760; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAD35842; AAD35842; TM_0760. DR EnsemblBacteria; AGL49686; AGL49686; Tmari_0761. DR GeneID; 898428; -. DR KEGG; tma:TM0760; -. DR KEGG; tmi:THEMA_00850; -. DR KEGG; tmm:Tmari_0761; -. DR KEGG; tmw:THMA_0779; -. DR PATRIC; 23936442; VBITheMar51294_0773. DR eggNOG; ENOG4107W3N; Bacteria. DR eggNOG; ENOG410ZWDI; LUCA. DR OMA; MINEANC; -. DR OrthoDB; EOG6Q8HZ9; -. DR BioCyc; TMAR243274:GC6P-787-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 398 AA; 46448 MW; 28C5FE4D55A25912 CRC64; MNIAILNHYA SIPEVGSAET RHFELAKRFV REGHRVDIYI GDFSHLTGKR WSETFGWSFS KDGVDFIVVE TREYTGNSLS RLLSSIDYYR NGRKKIIQKR YDVIIASSPH PFSWSLGWYY VRRKGGKFFI EIRDVWPDDL VKLGSLSYRH PVSKLFDHMC KKYYPKADGF ISLVPDLSEH FNRLKVRPEN FIYIPNGVDL KVFKDPEPCP VVDEVFSKVP DGKIKVVYAG SIVEHKGIKE FIETLSKVNK NLRDRFVFFF VGPSHADYLV SVKETAKDLQ NVFFFDPVPK RCVPYLLQKA DVLLFTLSQT VMDHPAVSSY KVVDYMASGK PVLCVDIENL PFKKTKGAVF FREDNLEEAL RRIFEEDLSE LGRRNREYVE RERDWDRLYE KLRSFVLS // ID Q9WXS9_THEMA Unreviewed; 332 AA. AC Q9WXS9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 123. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35168.1}; DE SubName: Full=Xylobiose ABC transport system, ATP-binding protein 1 {ECO:0000313|EMBL:AGL48997.1}; GN OrderedLocusNames=TM_0074 {ECO:0000313|EMBL:AAD35168.1}; GN ORFNames=Tmari_0071 {ECO:0000313|EMBL:AGL48997.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35168.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35168.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35168.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48997.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48997.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35168.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48997.1; -; Genomic_DNA. DR PIR; B72421; B72421. DR RefSeq; NP_227890.1; NC_000853.1. DR RefSeq; WP_010865043.1; NC_000853.1. DR STRING; 243274.TM0074; -. DR TCDB; 3.A.1.5.13; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35168; AAD35168; TM_0074. DR EnsemblBacteria; AGL48997; AGL48997; Tmari_0071. DR GeneID; 896899; -. DR KEGG; tma:TM0074; -. DR KEGG; tmi:THEMA_04435; -. DR KEGG; tmm:Tmari_0071; -. DR PATRIC; 23934988; VBITheMar51294_0072. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR KO; K02031; -. DR OMA; ARLAPQH; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-74-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35168.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35168.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 4 261 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 332 AA; 37209 MW; D2E5F35CF4008E5F CRC64; MEVLRTENLK SYYILDIFGK KRVVKAVDDV NISIMENEIY GIAGESGCGK STLLRALFAA IEPPQRIVGG KVLYRENGKE VDVYSLSDEE RRRLRWSFIS YVPQGSMSVL NPVVKIKETF KDFIESHTTG KTKEEAYEMA KEHIKELGLP IEILNAYPHQ LSGGMRQRVT IALATVLSPK VIIADEPTTA LDVVTQRGVV QLLKEIQSSR QNTIILVTHD MGVHANVTDR IAIMYAGKII EEGKTEEIFE NPMHPYTKYL IYSLPKFGDK GRRESAPGSP PSLADLPPGC SFHPRCPHAF DRCKKEVPPL KEYLPGHRVA CWLVEEGKNA AS // ID Q9WY81_THEMA Unreviewed; 370 AA. AC Q9WY81; G4FHF3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 96. DE SubName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000313|EMBL:AAD35330.1}; DE SubName: Full=Glycogen biosynthesis protein GlgD, glucose-1-phosphate adenylyltransferase family {ECO:0000313|EMBL:AGL49163.1}; GN OrderedLocusNames=TM_0239 {ECO:0000313|EMBL:AAD35330.1}; GN ORFNames=Tmari_0237 {ECO:0000313|EMBL:AGL49163.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35330.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35330.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35330.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49163.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49163.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate CC adenylyltransferase family. {ECO:0000256|SAAS:SAAS00569693}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35330.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49163.1; -; Genomic_DNA. DR PIR; A72403; A72403. DR RefSeq; NP_228053.1; NC_000853.1. DR RefSeq; WP_004082940.1; NZ_CP011107.1. DR STRING; 243274.TM0239; -. DR EnsemblBacteria; AAD35330; AAD35330; TM_0239. DR EnsemblBacteria; AGL49163; AGL49163; Tmari_0237. DR GeneID; 897139; -. DR KEGG; tma:TM0239; -. DR KEGG; tmi:THEMA_03530; -. DR KEGG; tmm:Tmari_0237; -. DR KEGG; tmw:THMA_0246; -. DR PATRIC; 23935353; VBITheMar51294_0242. DR eggNOG; ENOG4105EFR; Bacteria. DR eggNOG; COG0448; LUCA. DR KO; K00975; -. DR OMA; SSSKWWD; -. DR OrthoDB; EOG6W9X86; -. DR BioCyc; TMAR243274:GC6P-252-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:InterPro. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 2. DR InterPro; IPR005836; ADP_Glu_pyroP_CS. DR InterPro; IPR011832; GlgDAde_trans. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like. DR PANTHER; PTHR22572:SF9; PTHR22572:SF9; 1. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 2. DR TIGRFAMs; TIGR02092; glgD; 1. DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS00458608}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00458608}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAD35330.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35330.1}. FT DOMAIN 5 255 NTP_transferase. FT {ECO:0000259|Pfam:PF00483}. SQ SEQUENCE 370 AA; 42242 MW; 6DA96039A875EDE7 CRC64; MRVLGLILAG GKSDRLWPLT KVRASAAVPV FGKYRAIDFT LSNMVNSGIR KVGILTQYNP RSLMDHLGSG KEWDLDRKSG GLFILQPYVG PNREVWYRGT ADAIFQNMTI LRRGEEDHVL IGSGDHIYKM IYRDLFNYHL KKGADITLVV KELDETYNLS EYGIVQLDDD MRVVEIEEKP AHPKGNIAFL GVYFMNKELL KELLYATVPQ GKYDLLLDIV IPNLDRLKVY AYRFDGYWRN VKKGIKEYYR INMDILKKEV RDELFYRNGK VYTKLKDLPP PKFTTTAVVE NSLIADGSIV SGTVRNSVIF RNVRIKVGAV VENSIIMENT VVEEGAVLRN VILDKNCIVR EGRVIEGDTE LPVFEKRAVL // ID Q9X0U6_THEMA Unreviewed; 315 AA. AC Q9X0U6; G4FEC7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 126. DE SubName: Full=Mannoside ABC transport system, ATP-binding protein 2 {ECO:0000313|EMBL:AGL50150.1}; DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36294.1}; GN OrderedLocusNames=TM_1219 {ECO:0000313|EMBL:AAD36294.1}; GN ORFNames=Tmari_1226 {ECO:0000313|EMBL:AGL50150.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36294.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36294.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36294.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50150.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50150.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36294.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50150.1; -; Genomic_DNA. DR PIR; A72282; A72282. DR RefSeq; NP_229024.1; NC_000853.1. DR RefSeq; WP_004080075.1; NZ_CP011107.1. DR STRING; 243274.TM1219; -. DR TCDB; 3.A.1.5.14; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36294; AAD36294; TM_1219. DR EnsemblBacteria; AGL50150; AGL50150; Tmari_1226. DR GeneID; 898265; -. DR KEGG; tma:TM1219; -. DR KEGG; tmi:THEMA_08235; -. DR KEGG; tmm:Tmari_1226; -. DR KEGG; tmw:THMA_1245; -. DR PATRIC; 23937380; VBITheMar51294_1237. DR eggNOG; ENOG4108EBF; Bacteria. DR eggNOG; ENOG410XR2R; LUCA. DR KO; K02032; -. DR OMA; EYYRYVQ; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1249-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36294.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36294.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 4 251 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 315 AA; 36064 MW; 36A9631710E3C04D CRC64; MSLLKVQNLT KEFPLGFFGK ERLKAVDDVS FEIERSRIVS LIGESGSGKT TVGKLILKLI RPSSGQILLN GRDITQIKGR ELREYYRKVQ GVFQDPFSSF NPIYKIDRVL DMVFEEFFPD TPASERRTKM EEVIASVGMN PREILGKYPH QLSGGQLQRI LIARTLLLNV ELLIADEIIS MLDASTRVDI LNLLGDLRER GMSVIFITHD LSLGYYISDE TFIMYRGNIV EMGDTEKVFH NPIHPYTKML LESVPEIDRK WDLSKRFIPE LVSSSNAPCK YYDRCPIRDE RCLVQKPAMV EVEENHKVLC LKAGD // ID Q9WYQ2_THEMA Unreviewed; 359 AA. AC Q9WYQ2; G4FHY0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 134. DE SubName: Full=Myo-inositol ABC transporter, ATP-binding protein InoL {ECO:0000313|EMBL:AGL49343.1}; DE SubName: Full=Sugar ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35506.1}; GN OrderedLocusNames=TM_0421 {ECO:0000313|EMBL:AAD35506.1}; GN ORFNames=Tmari_0418 {ECO:0000313|EMBL:AGL49343.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35506.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35506.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35506.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49343.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49343.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00562907}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35506.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49343.1; -; Genomic_DNA. DR PIR; E72378; E72378. DR RefSeq; NP_228231.1; NC_000853.1. DR RefSeq; WP_004083278.1; NZ_CP011107.1. DR PDB; 2YYZ; X-ray; 2.11 A; A=1-359. DR PDBsum; 2YYZ; -. DR STRING; 243274.TM0421; -. DR TCDB; 3.A.1.1.38; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35506; AAD35506; TM_0421. DR EnsemblBacteria; AGL49343; AGL49343; Tmari_0418. DR GeneID; 897424; -. DR KEGG; tma:TM0421; -. DR KEGG; tmi:THEMA_02620; -. DR KEGG; tmm:Tmari_0418; -. DR KEGG; tmw:THMA_0427; -. DR PATRIC; 23935725; VBITheMar51294_0426. DR eggNOG; ENOG4108IJ9; Bacteria. DR eggNOG; COG3839; LUCA. DR KO; K17240; -. DR OMA; VAQARVC; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-436-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0016820; F:hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013611; Transp-assoc_OB_typ2. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08402; TOBE_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2YYZ}; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00452173, ECO:0000313|EMBL:AAD35506.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00452173, ECO:0000313|EMBL:AAD35506.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00452289}. FT DOMAIN 4 234 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT REGION 37 43 Sulfate 1 binding. FT {ECO:0000213|PDB:2YYZ}. FT BINDING 135 135 Sulfate 2. {ECO:0000213|PDB:2YYZ}. FT BINDING 141 141 Sulfate 2. {ECO:0000213|PDB:2YYZ}. SQ SEQUENCE 359 AA; 40387 MW; 66C17E3C5834766F CRC64; MPSIRVVNLK KYFGKVKAVD GVSFEVKDGE FVALLGPSGC GKTTTLLMLA GIYKPTSGEI YFDDVLVNDI PPKYREVGMV FQNYALYPHM TVFENIAFPL RARRISKDEV EKRVVEIARK LLIDNLLDRK PTQLSGGQQQ RVALARALVK QPKVLLFDEP LSNLDANLRM IMRAEIKHLQ QELGITSVYV THDQAEAMTM ASRIAVFNQG KLVQYGTPDE VYDSPKNMFV ASFIGNPPTN FLRDFSVSVE NKQTILKRDD VIIKLPEPVD VKLKEVVVGI RPEHCRISRE RVENSIPGVV YVVEPLGRDI IVNVKTEKGE IIKVFGDTGK APQPGENVFL VPDLRKIHLF NPETEETIL // ID Q9WZQ9_THEMA Unreviewed; 412 AA. AC Q9WZQ9; G4FD22; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 105. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2 {ECO:0000256|PIRNR:PIRNR000447}; DE EC=2.3.1.179 {ECO:0000256|PIRNR:PIRNR000447}; GN OrderedLocusNames=TM_0802 {ECO:0000313|EMBL:AAD35884.1}; GN ORFNames=Tmari_0803 {ECO:0000313|EMBL:AGL49728.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35884.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35884.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35884.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49728.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49728.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Catalyzes the condensation reaction of fatty acid CC synthesis by the addition to an acyl acceptor of two carbons from CC malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}. CC -!- CATALYTIC ACTIVITY: (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + CC malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl- CC carrier-protein] + CO(2) + [acyl-carrier-protein]. CC {ECO:0000256|PIRNR:PIRNR000447}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000256|PIRNR:PIRNR000447}. CC -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family. CC {ECO:0000256|RuleBase:RU003694}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35884.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49728.1; -; Genomic_DNA. DR PIR; C72335; C72335. DR RefSeq; NP_228611.1; NC_000853.1. DR RefSeq; WP_004080861.1; NZ_CP011107.1. DR STRING; 243274.TM0802; -. DR EnsemblBacteria; AAD35884; AAD35884; TM_0802. DR EnsemblBacteria; AGL49728; AGL49728; Tmari_0803. DR GeneID; 898470; -. DR KEGG; tma:TM0802; -. DR KEGG; tmi:THEMA_00640; -. DR KEGG; tmm:Tmari_0803; -. DR KEGG; tmw:THMA_0821; -. DR PATRIC; 23936524; VBITheMar51294_0814. DR eggNOG; ENOG4105C0Q; Bacteria. DR eggNOG; COG0304; LUCA. DR KO; K09458; -. DR OMA; FEVEQYL; -. DR OrthoDB; EOG6DG2SR; -. DR BioCyc; TMAR243274:GC6P-829-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0033817; F:beta-ketoacyl-acyl-carrier-protein synthase II activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2. DR InterPro; IPR014031; Ketoacyl_synth_C. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR016039; Thiolase-like. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR PIRSF; PIRSF000447; KAS_II; 1. DR SMART; SM00825; PKS_KS; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR TIGRFAMs; TIGR03150; fabF; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|PIRNR:PIRNR000447, KW ECO:0000313|EMBL:AGL49728.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000447}; KW Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000447}; KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000447}; KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000447}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|PIRNR:PIRNR000447, KW ECO:0000313|EMBL:AGL49728.1}. FT ACT_SITE 161 161 {ECO:0000256|PIRSR:PIRSR000447-1}. SQ SEQUENCE 412 AA; 43840 MW; B9A80242A76FA93B CRC64; MKRVVITGMG IVSPFGVGKE RNLEGLRETK VTIDRISSFD ASNLPVQIAA EVRDFKPEEY INPKLVRRTD RFVHFALVSA KEAVEDAGIN FEPYADRTAT IIGSGMGGFL TLDSENNKFL SQGPSRVSPF LIPMILIDMA SGVVAMEYGL KGPNFSSVSA CASSLHAVAL GALLIRHGYA DVAVVGGTEA TIAPLPITGF ANMRALSRRN DDPKRASRPF DKDRDGFVMG EGGAVLILEA EEVAKSRGAK ILAEIKGVGM TDDAYHFSAP DPEGRGAAEA MKLALKESSL AVEDIDYVSC HATSTPAGDE AELKAIKKVL GEHVKNVAIN SSKALIGHLL GAAGASELVL AILQMQNSFV HGMPNLDNPI DEAKGTGLVG KEPVQMEIKN FIKNSFGFGG HNVSIVVGRY ES // ID Q9WZW4_THEMA Unreviewed; 465 AA. AC Q9WZW4; G4FCW4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463}; GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463}; GN OrderedLocusNames=TM_0860 {ECO:0000313|EMBL:AAD35942.1}; GN ORFNames=Tmari_0862 {ECO:0000313|EMBL:AGL49787.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35942.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35942.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35942.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49787.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49787.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts CC with the SecYEG preprotein conducting channel. SecDF uses the CC proton motive force (PMF) to complete protein translocation after CC the ATP-dependent function of SecA. {ECO:0000256|HAMAP- CC Rule:MF_01463, ECO:0000256|SAAS:SAAS00541769}. CC -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec CC protein translocation apparatus which comprises SecA, SecYEG and CC auxiliary proteins SecDF. Other proteins may also be involved. CC {ECO:0000256|HAMAP-Rule:MF_01463}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01463}. CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01463}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35942.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49787.1; -; Genomic_DNA. DR PIR; E72325; E72325. DR RefSeq; NP_228669.1; NC_000853.1. DR RefSeq; WP_004080746.1; NZ_CP011107.1. DR STRING; 243274.TM0860; -. DR EnsemblBacteria; AAD35942; AAD35942; TM_0860. DR EnsemblBacteria; AGL49787; AGL49787; Tmari_0862. DR GeneID; 898533; -. DR KEGG; tma:TM0860; -. DR KEGG; tmi:THEMA_00335; -. DR KEGG; tmm:Tmari_0862; -. DR KEGG; tmw:THMA_0882; -. DR PATRIC; 23936648; VBITheMar51294_0873. DR eggNOG; ENOG4107QN8; Bacteria. DR eggNOG; COG0342; LUCA. DR KO; K03072; -. DR OMA; QKVIRYG; -. DR OrthoDB; EOG6N0HJT; -. DR BioCyc; TMAR243274:GC6P-890-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR GO; GO:0015031; P:protein transport; IBA:GO_Central. DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01463_B; SecD_B; 1. DR InterPro; IPR001036; Acrflvin-R. DR InterPro; IPR005791; SecD. DR InterPro; IPR022813; SecD/SecF_arch_bac. DR InterPro; IPR022645; SecD/SecF_bac. DR Pfam; PF02355; SecD_SecF; 1. DR PRINTS; PR00702; ACRIFLAVINRP. DR TIGRFAMs; TIGR00916; 2A0604s01; 1. DR TIGRFAMs; TIGR01129; secD; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01463}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425143}; KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425069}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Translocation {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425069}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425143}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425143}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01463, KW ECO:0000256|SAAS:SAAS00425069}. FT TRANSMEM 8 28 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 296 316 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 334 354 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 396 416 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 420 440 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. SQ SEQUENCE 465 AA; 50932 MW; 6CE9545B3EFD97F9 CRC64; MRGDRVRLIV VLLVLAGALL AIFWPSKGGW ISNIRLGLDI KGGARIEYMV EVQQGTENPS DVVDDVWTVL RNRLDAAGYT EAAVKKVLRD NKYYIVVEIP GATDTVQAEK LIGSTGVLYF AQVLDEYLGE DPSKVPELSL EARRENAVWL KGRDGKWYLV KKEIMGRKDL VLEAPRIVYA RPEVETRTGR YGYKVSFELA KEYVDIFKKI TQALYVPEGT YDPKKRLAIV LDDVVQFVGQ VVAIITDGKA EITGNFSLEE AKQLAAILRS GALPARLVKT SSGWVAPLLG RDVIDASLKA GIIGLILVLV YMIIYYRTMG IVADLALIYN TVLLLGVMAA GKFILTLPGI AGIILTIGTT VDGNVIIYER IKEEMRLGKP VKTSIAAGFD RSLSTILDAN ITTILTGLIL YYFGTGTIKG FAITLIIGVL GSIFVNLVFS RLLLDALARF IKPLRADEAQ GGTGQ // ID Q9WZG2_THEMA Unreviewed; 249 AA. AC Q9WZG2; G4FDC6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=Flagellar biosynthetic protein FliP {ECO:0000256|RuleBase:RU362069}; GN Name=fliP {ECO:0000256|RuleBase:RU362069}; GN OrderedLocusNames=TM_0698 {ECO:0000313|EMBL:AAD35780.1}; GN ORFNames=Tmari_0698 {ECO:0000313|EMBL:AGL49623.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35780.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35780.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35780.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49623.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49623.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Plays a role in the flagellum-specific transport system. CC {ECO:0000256|RuleBase:RU362069}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU362069}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU362069}. Bacterial flagellum basal body CC {ECO:0000256|RuleBase:RU362069}. CC -!- SIMILARITY: Belongs to the FliP/MopC/SpaP family. CC {ECO:0000256|RuleBase:RU362069}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35780.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49623.1; -; Genomic_DNA. DR PIR; H72345; H72345. DR RefSeq; NP_228507.1; NC_000853.1. DR RefSeq; WP_004081051.1; NZ_CP011107.1. DR STRING; 243274.TM0698; -. DR EnsemblBacteria; AAD35780; AAD35780; TM_0698. DR EnsemblBacteria; AGL49623; AGL49623; Tmari_0698. DR GeneID; 898365; -. DR KEGG; tma:TM0698; -. DR KEGG; tmi:THEMA_01175; -. DR KEGG; tmm:Tmari_0698; -. DR KEGG; tmw:THMA_0713; -. DR PATRIC; 23936314; VBITheMar51294_0710. DR eggNOG; ENOG4105CN7; Bacteria. DR eggNOG; COG1338; LUCA. DR KO; K02419; -. DR OMA; AIMKDFL; -. DR OrthoDB; EOG6GBMBW; -. DR BioCyc; TMAR243274:GC6P-724-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR005837; FliP. DR InterPro; IPR005838; T3SS_IM_P. DR PANTHER; PTHR30587:SF0; PTHR30587:SF0; 1. DR Pfam; PF00813; FliP; 1. DR PRINTS; PR00951; FLGBIOSNFLIP. DR PRINTS; PR01302; TYPE3IMPPROT. DR TIGRFAMs; TIGR01103; fliP; 1. DR PROSITE; PS01061; FLIP_2; 1. PE 3: Inferred from homology; KW Bacterial flagellum biogenesis {ECO:0000256|RuleBase:RU362069}; KW Bacterial flagellum protein export {ECO:0000256|RuleBase:RU362069}; KW Cell membrane {ECO:0000256|RuleBase:RU362069}; KW Cell projection {ECO:0000313|EMBL:AAD35780.1}; KW Cilium {ECO:0000313|EMBL:AAD35780.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35780.1}; KW Membrane {ECO:0000256|RuleBase:RU362069}; KW Protein transport {ECO:0000256|RuleBase:RU362069}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU362069}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362069}; KW Transport {ECO:0000256|RuleBase:RU362069}. FT TRANSMEM 45 75 Helical. {ECO:0000256|RuleBase:RU362069}. FT TRANSMEM 87 106 Helical. {ECO:0000256|RuleBase:RU362069}. FT TRANSMEM 191 215 Helical. {ECO:0000256|RuleBase:RU362069}. FT TRANSMEM 227 248 Helical. {ECO:0000256|RuleBase:RU362069}. SQ SEQUENCE 249 AA; 28168 MW; 5CD60239AAF18E55 CRC64; MRKLLLILLI FLPLLYFSQE IPFPSISIGV RPAEEPEDLV VTLEILLVLT VLALAPSILV LFTSFTRIIV VFSLFRNALG TRQTPPNQVM IGLALFLTFL IMQPVWNDIY NNAITPYLNK ETGYQEMFQR VNTRIREFMI NELKNHHNED NVFMLAKNSG IEIAKIEEAP NAVLIPAFVL GELEVAFKMG VVLYVPFIVI DMIVASILLA MGMIMIPPVF VSLPFKILIF VMANGWDLLV EGLIKSFAR // ID Q9WZ61_THEMA Unreviewed; 216 AA. AC Q9WZ61; G4FDM7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 102. DE SubName: Full=Amino acid ABC transporter, permease protein {ECO:0000313|EMBL:AAD35677.1}; GN OrderedLocusNames=TM_0592 {ECO:0000313|EMBL:AAD35677.1}; GN ORFNames=Tmari_0591 {ECO:0000313|EMBL:AGL49516.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35677.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35677.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35677.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49516.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49516.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032, CC ECO:0000256|SAAS:SAAS00561696}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35677.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49516.1; -; Genomic_DNA. DR PIR; A72357; A72357. DR RefSeq; NP_228402.1; NC_000853.1. DR RefSeq; WP_004081260.1; NZ_CP011107.1. DR STRING; 243274.TM0592; -. DR EnsemblBacteria; AAD35677; AAD35677; TM_0592. DR EnsemblBacteria; AGL49516; AGL49516; Tmari_0591. DR GeneID; 897666; -. DR KEGG; tma:TM0592; -. DR KEGG; tmi:THEMA_01700; -. DR KEGG; tmm:Tmari_0591; -. DR KEGG; tmw:THMA_0608; -. DR PATRIC; 23936099; VBITheMar51294_0603. DR eggNOG; ENOG4105E5Q; Bacteria. DR eggNOG; COG0765; LUCA. DR KO; K02029; -. DR OMA; IRILNWI; -. DR OrthoDB; EOG6MM1R5; -. DR BioCyc; TMAR243274:GC6P-617-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GOC. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00450258}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00450258, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00450217}. FT TRANSMEM 23 45 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 186 207 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 19 207 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 216 AA; 23740 MW; E227CBA943E8CD1C CRC64; MPEWLSVIVD NLPLLLKGAL RTLQLTSLAV LIGLAIGIFV GMGRLSKYRI IRYPSSVYVE FLRGTPLMVQ LFLVYFGLPE LGLEFDRFTA AVIALGINSG AYVAEIVRAG IQSVPKGQYE AARSLGMSHA QAMIYVILPQ AFRHILPALG NEFIALAKDS SLAMVIGTVE LMRSAQYIVS RTFMSFPIYG GVALIYFAIT FSVSRLVKFV EGRLKV // ID Q9WXN7_THEMA Unreviewed; 338 AA. AC Q9WXN7; G4FGU7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 95. DE SubName: Full=Beta-glucoside ABC transport system, permease protein 1 {ECO:0000313|EMBL:AGL48953.1}; DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35124.1}; GN OrderedLocusNames=TM_0030 {ECO:0000313|EMBL:AAD35124.1}; GN ORFNames=Tmari_0027 {ECO:0000313|EMBL:AGL48953.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35124.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35124.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35124.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48953.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48953.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35124.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48953.1; -; Genomic_DNA. DR PIR; H72428; H72428. DR RefSeq; NP_227846.1; NC_000853.1. DR RefSeq; WP_004082485.1; NZ_CP011107.1. DR STRING; 243274.TM0030; -. DR TCDB; 3.A.1.5.16; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35124; AAD35124; TM_0030. DR EnsemblBacteria; AGL48953; AGL48953; Tmari_0027. DR GeneID; 896850; -. DR KEGG; tma:TM0030; -. DR KEGG; tmi:THEMA_04650; -. DR KEGG; tmm:Tmari_0027; -. DR KEGG; tmw:THMA_0026; -. DR PATRIC; 23934900; VBITheMar51294_0028. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR KO; K02033; -. DR OMA; FSEYLGM; -. DR OrthoDB; EOG66F098; -. DR BioCyc; TMAR243274:GC6P-30-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 14 35 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 109 137 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 158 183 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 203 226 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 257 282 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 302 328 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 110 321 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 338 AA; 37909 MW; 05407A1C9B274912 CRC64; MGSKSMFKYL LRRFIFLLVT YIVATTIVFI LPRAIPGNPL SQILSGLSRV AQANPEAIRA AERTLMEEFG LGKPWYVQYF EFITKALRGD LGTSITFYPR KVIDLIIPVI PWTLILLLPA TIVAWILGNS LGALAAYKRN TWIDKGVLTT SLIVSQIPYY WLGMIFIFLF GVKLGWLPVQ GAYSQGTIPN LSWSFFVDVL KHYIMPFASI VVSAMGGWAI GMRLMVIYEL GSDYAMFSEY LGMKDKRIFK YVFRNSLLPQ ITGLALSLGG VLGGALITEI VFNYPGTGYL LFRALTTLDY PLIQGIFVIL IASIYLANFI VDFLYALIDP RIRLGQEA // ID Q9X2I2_THEMA Unreviewed; 794 AA. AC Q9X2I2; G4FGR1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=ATP-dependent protease LA, putative {ECO:0000313|EMBL:AAD36931.1}; DE SubName: Full=ATP-dependent protease La Type II {ECO:0000313|EMBL:AGL50808.1}; DE EC=3.4.21.53 {ECO:0000313|EMBL:AGL50808.1}; GN OrderedLocusNames=TM_1869 {ECO:0000313|EMBL:AAD36931.1}; GN ORFNames=Tmari_1884 {ECO:0000313|EMBL:AGL50808.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36931.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36931.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36931.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50808.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50808.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36931.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50808.1; -; Genomic_DNA. DR PIR; F72202; F72202. DR RefSeq; NP_229665.1; NC_000853.1. DR RefSeq; WP_004082420.1; NZ_CP011107.1. DR STRING; 243274.TM1869; -. DR EnsemblBacteria; AAD36931; AAD36931; TM_1869. DR EnsemblBacteria; AGL50808; AGL50808; Tmari_1884. DR GeneID; 897799; -. DR KEGG; tma:TM1869; -. DR KEGG; tmi:THEMA_04825; -. DR KEGG; tmm:Tmari_1884; -. DR KEGG; tmw:THMA_1919; -. DR PATRIC; 23938727; VBITheMar51294_1890. DR eggNOG; ENOG4105DAN; Bacteria. DR eggNOG; COG1067; LUCA. DR OMA; LFDWCYV; -. DR OrthoDB; EOG63RGMZ; -. DR BioCyc; TMAR243274:GC6P-1920-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central. DR GO; GO:0070361; F:mitochondrial light strand promoter anti-sense binding; IBA:GO_Central. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central. DR GO; GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IBA:GO_Central. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR027065; Lon_Prtase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008269; Pept_S16_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10046; PTHR10046; 1. DR Pfam; PF05362; Lon_C; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF54211; SSF54211; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD36931.1}; KW Protease {ECO:0000313|EMBL:AAD36931.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 639 745 Lon_C. {ECO:0000259|Pfam:PF05362}. SQ SEQUENCE 794 AA; 90264 MW; F21813702E589E05 CRC64; MIRKLRPDEI NSFDLDFLNF QTTEEVPPNE GFIGQKRAKE AIETGIRIRE KGYNIFVTGM TGTGRRTFVQ MMLQDVAKKL PVPNDWGYVY NFENPYEPKA ISFKAGQGRR FKKRLEDLIN EVVEALNKSF ESEEFARKIS EMEEKYALMR KQLWESLEAK ASELGFVVQL TPAGVVMLPV VDGKPLPPEA VNALPDQAIR EIEERQMKLK HLVDGTLYRI RKLDIEFRKS LEEFHKRTAL FAIDPLFVEV ESEFENEGVK EFLESVKKDI VENLLDFLRM DARERKEIYM RKYSLNLIVD NSDLTGAPVI YETNPTYSNL FGKIEYYVRG GFLHTDFSMI RPGSVHKANG GFLIVEAERL LSQPYAWYNL KRVLMESQIS VENLEHTLGV SSTITLKPEK IPLDLKVVII GTPYLYELLY ELDPDFRKLF RIKAEFDWEI PRNELNVQKY VSFISSVCRE KNLPHFDRGA VKRVIWYAMR NAGNSTKLSA VFGDIVNLIV ESGELARLEG SEVTTSDHVL KAYQAMENRR NLLEEKYDEM IKTFDLMIEV TGSKVGQING LTVLDLGDHS FGVPVKITAK VYLGRPGVVD IQREADLSGK IHSKAVLILE GFLGSRYAQD FPLSVSASIS FEQVYSEVEG DSASLAEALA LLSAISKVPI KQGIAVTGSI NQHGEVQPVG GIVEKVEGFY RACKTRGFDG EQGVIIPKAN AKNLVLKDEI IQAMKKGLFH IWTVETIDDA IEIVMGMKAG RVTKTGKFER NSVNYLVYRE LKKMKKLLDG VPEERKKKKR KGKK // ID Q9WZN7_THEMA Unreviewed; 157 AA. AC Q9WZN7; G4FD43; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Alkyl hydroperoxide reductase subunit C-like protein {ECO:0000313|EMBL:AGL49706.1}; DE SubName: Full=Bacterioferritin comigratory protein, ahpC/TSA family {ECO:0000313|EMBL:AAD35862.1}; GN OrderedLocusNames=TM_0780 {ECO:0000313|EMBL:AAD35862.1}; GN ORFNames=Tmari_0781 {ECO:0000313|EMBL:AGL49706.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35862.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35862.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35862.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49706.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49706.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35862.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49706.1; -; Genomic_DNA. DR PIR; E72332; E72332. DR RefSeq; NP_228589.1; NC_000853.1. DR RefSeq; WP_004080908.1; NZ_CP011107.1. DR STRING; 243274.TM0780; -. DR EnsemblBacteria; AAD35862; AAD35862; TM_0780. DR EnsemblBacteria; AGL49706; AGL49706; Tmari_0781. DR GeneID; 898448; -. DR KEGG; tma:TM0780; -. DR KEGG; tmi:THEMA_00750; -. DR KEGG; tmm:Tmari_0781; -. DR KEGG; tmw:THMA_0799; -. DR PATRIC; 23936482; VBITheMar51294_0793. DR eggNOG; ENOG4108053; Bacteria. DR eggNOG; COG1225; LUCA. DR OMA; CTKELCT; -. DR OrthoDB; EOG6ZH2P1; -. DR BioCyc; TMAR243274:GC6P-807-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 157 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 157 AA; 17272 MW; 9B85EE8AF0BF3E08 CRC64; MLKSGDKAID FELVNTDLKM VKLSDFSGKN VVLAFYPGAF TSVCEKELCT FRDSLSKFNR LNAVVLGISV DSPFANKAFA EKNHITFDLL SDFGGRVASQ YGGVHENFLN IPGYTAAKRA VYVVDGGGTI VYSWVSEDPG KEPPYEEIEE ALERLSK // ID Q9X148_THEMA Unreviewed; 454 AA. AC Q9X148; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 102. DE SubName: Full=AstB/chuR-related protein {ECO:0000313|EMBL:AAD36397.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL50255.1}; GN OrderedLocusNames=TM_1325 {ECO:0000313|EMBL:AAD36397.1}; GN ORFNames=Tmari_1331 {ECO:0000313|EMBL:AGL50255.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36397.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36397.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36397.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50255.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50255.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36397.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50255.1; -; Genomic_DNA. DR PIR; A72267; A72267. DR RefSeq; NP_229127.1; NC_000853.1. DR RefSeq; WP_010865312.1; NZ_CP011107.1. DR STRING; 243274.TM1325; -. DR EnsemblBacteria; AAD36397; AAD36397; TM_1325. DR EnsemblBacteria; AGL50255; AGL50255; Tmari_1331. DR GeneID; 898157; -. DR KEGG; tma:TM1325; -. DR KEGG; tmi:THEMA_07720; -. DR KEGG; tmm:Tmari_1331; -. DR KEGG; tmw:THMA_1349; -. DR PATRIC; 23937585; VBITheMar51294_1338. DR eggNOG; ENOG4107R8T; Bacteria. DR eggNOG; COG0641; LUCA. DR KO; K06871; -. DR OMA; YKGTMKE; -. DR OrthoDB; EOG60PH7N; -. DR BioCyc; TMAR243274:GC6P-1356-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1. DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00489002}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|SAAS:SAAS00489002}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00489002}; KW Metal-binding {ECO:0000256|SAAS:SAAS00489002}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00488995}. FT DOMAIN 88 305 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 454 AA; 52906 MW; 7A2C77B76180B7D5 CRC64; MKPSRFNLVI NESDGTLLFN TLSQALLWID RKNTNKVLKT LEDPSSTELS KTEVEKLKRG MFLLDDNFDE LEFLKFRFNT YRYSDRFLRY TIVLTHSCNF DCVYCYQKVL HISSGSYISE KVQSNFLLDV ERKLEYQKPN LLSVTFYGGE PLLLEETVVN LSSKLKRLCE KYGVKYDSFI VTNGYLLTEK MVDDLQKAGI KALDITLDGT EVYHDRYRKA RNGAPTFSSI FENIFRAVNK GLFVQIRVNV SRENIEDVKK LIDRIAEKKL RVEFNFQPIE IVEGNPTGFQ DTALNTEEFA EIETKLWWYI REKIPEYPFE YFKKPRFARC DAMCKNSFVV DVDGRVYKCW GELGMENCSG FLKETGVEFT GSYLKWLTYD PLEDEECRRC LVLPFCMGGC AFNRVVYRTL KSSKVKKPHT CIPLRYNLNE FIKIVADYKR RSAVHGISQR SSGG // ID Q9X237_THEMA Unreviewed; 88 AA. AC Q9X237; G4FG99; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36778.1}; GN OrderedLocusNames=TM_1712 {ECO:0000313|EMBL:AAD36778.1}; GN ORFNames=Tmari_1720 {ECO:0000313|EMBL:AGL50644.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36778.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36778.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36778.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50644.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50644.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36778.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50644.1; -; Genomic_DNA. DR PIR; A72222; A72222. DR RefSeq; NP_229511.1; NC_000853.1. DR RefSeq; WP_004082228.1; NZ_CP011107.1. DR STRING; 243274.TM1712; -. DR EnsemblBacteria; AAD36778; AAD36778; TM_1712. DR EnsemblBacteria; AGL50644; AGL50644; Tmari_1720. DR GeneID; 897273; -. DR KEGG; tma:TM1712; -. DR KEGG; tmi:THEMA_05680; -. DR KEGG; tmm:Tmari_1720; -. DR KEGG; tmw:THMA_1754; -. DR PATRIC; 23938400; VBITheMar51294_1730. DR OMA; WNELNQA; -. DR OrthoDB; EOG6Q8J6J; -. DR BioCyc; TMAR243274:GC6P-1760-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR007793; DivIVA_fam. DR Pfam; PF05103; DivIVA; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 4 66 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 88 AA; 10783 MW; ABAA29FC8BF142F2 CRC64; MKELEDLERI LDSMIEDYKK LKEENKELWS KVKQLNERIL HLEKEKEQLE KTIEQHKRSL NTLVEKIQRF LSLTTDQGMI QDEEENKR // ID Q9WZY6_THEMA Unreviewed; 447 AA. AC Q9WZY6; G4FCU1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 103. DE SubName: Full=Methyltransferase, putative {ECO:0000313|EMBL:AAD35965.1}; DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:AGL49811.1}; GN OrderedLocusNames=TM_0884 {ECO:0000313|EMBL:AAD35965.1}; GN ORFNames=Tmari_0886 {ECO:0000313|EMBL:AGL49811.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35965.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35965.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35965.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49811.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49811.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35965.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49811.1; -; Genomic_DNA. DR PIR; E72320; E72320. DR RefSeq; NP_228692.1; NC_000853.1. DR RefSeq; WP_004080708.1; NZ_CP011107.1. DR STRING; 243274.TM0884; -. DR EnsemblBacteria; AAD35965; AAD35965; TM_0884. DR EnsemblBacteria; AGL49811; AGL49811; Tmari_0886. DR GeneID; 898558; -. DR KEGG; tma:TM0884; -. DR KEGG; tmi:THEMA_00215; -. DR KEGG; tmm:Tmari_0886; -. DR KEGG; tmw:THMA_0906; -. DR PATRIC; 23936699; VBITheMar51294_0898. DR eggNOG; ENOG4105DCS; Bacteria. DR eggNOG; COG1032; LUCA. DR OMA; AYIMVNM; -. DR OrthoDB; EOG693GMK; -. DR BioCyc; TMAR243274:GC6P-914-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Methyltransferase {ECO:0000313|EMBL:AAD35965.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35965.1}. FT DOMAIN 201 414 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 447 AA; 52325 MW; 49102585F004BA70 CRC64; MNVLLVNPWI HDFAAYDFWL KPIGLLYVAR AMEWMGYEVH LVDLLNRHDP DLPRFTRVPK DKRYGTGKFP SQVIEKPEIL RFVPRRYKRY GAPPEFLEWK LREIGNVDLI MVTSTLSYWY PGVWETIRFL KGRYDVPIVL GGVYPRLFPK HAKKSGAIVY EKGDLVFLPR FLETLGFPSK EIPADWFEVF DPMYELYNRI GYLVFITTLG CPFRCSYCAV HRLWNGLRVR TPERVVETIE KYLNIFKVED VVFFDDAILA SGRFKDLLKL IVEKRWPVRF HLPNGIHARL LDEETAFLLK EANFRTIKLG YETSGRLQRE TGGKVYDEDL VRAARILRKA GFTEKEVSAY IMVNMPGQTK EDVLNAIKVC LSEGIGISIN EYTPIPGTKD WEKLVEEGKL DPDIDPVFLN NTVLPFWWKH GMSYEEIQEI KDFAQKLKKS EVYREFP // ID Q9X2E8_THEMA Unreviewed; 348 AA. AC Q9X2E8; G4FGL5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 109. DE RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|PIRNR:PIRNR006769}; GN OrderedLocusNames=TM_1828 {ECO:0000313|EMBL:AAD36891.1}; GN ORFNames=Tmari_1838 {ECO:0000313|EMBL:AGL50762.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36891.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36891.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36891.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50762.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50762.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone CC 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- CC pyrimidinedione 5'-phosphate. {ECO:0000256|PIRNR:PIRNR006769}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR006769, CC ECO:0000256|PIRSR:PIRSR006769-3}; CC Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR006769, CC ECO:0000256|PIRSR:PIRSR006769-3}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 2/4. CC {ECO:0000256|PIRNR:PIRNR006769}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 3/4. CC {ECO:0000256|PIRNR:PIRNR006769}. CC -!- SIMILARITY: In the C-terminal section; belongs to the HTP CC reductase family. {ECO:0000256|PIRNR:PIRNR006769}. CC -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and CC deoxycytidylate deaminase family. {ECO:0000256|PIRNR:PIRNR006769}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36891.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50762.1; -; Genomic_DNA. DR PIR; G72207; G72207. DR RefSeq; NP_229625.1; NC_000853.1. DR RefSeq; WP_004082374.1; NZ_CP011107.1. DR PDB; 2HXV; X-ray; 1.80 A; A=1-348. DR PDBsum; 2HXV; -. DR STRING; 243274.TM1828; -. DR EnsemblBacteria; AAD36891; AAD36891; TM_1828. DR EnsemblBacteria; AGL50762; AGL50762; Tmari_1838. DR GeneID; 897425; -. DR KEGG; tma:TM1828; -. DR KEGG; tmi:THEMA_05055; -. DR KEGG; tmm:Tmari_1838; -. DR KEGG; tmw:THMA_1873; -. DR PATRIC; 23938643; VBITheMar51294_1848. DR eggNOG; ENOG4105D1W; Bacteria. DR eggNOG; COG0117; LUCA. DR eggNOG; COG1985; LUCA. DR KO; K11752; -. DR OMA; HWGKQPP; -. DR OrthoDB; EOG66F07R; -. DR BioCyc; TMAR243274:GC6P-1879-MONOMER; -. DR UniPathway; UPA00275; UER00401. DR UniPathway; UPA00275; UER00402. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro. DR GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009451; P:RNA modification; IBA:GO_Central. DR Gene3D; 3.40.430.10; -; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn-bd. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR024072; DHFR-like_dom. DR InterPro; IPR004794; Eubact_RibD. DR InterPro; IPR002734; RibDG_C. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR Pfam; PF01872; RibD_C; 1. DR PIRSF; PIRSF006769; RibD; 1. DR SUPFAM; SSF53597; SSF53597; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR TIGRFAMs; TIGR00326; eubact_ribD; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2HXV}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR006769, KW ECO:0000313|EMBL:AGL50762.1}; KW Metal-binding {ECO:0000213|PDB:2HXV, ECO:0000256|PIRNR:PIRNR006769, KW ECO:0000256|PIRSR:PIRSR006769-3}; KW NADP {ECO:0000213|PDB:2HXV, ECO:0000256|PIRNR:PIRNR006769, KW ECO:0000256|PIRSR:PIRSR006769-2}; KW Nucleotide-binding {ECO:0000213|PDB:2HXV}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006769, KW ECO:0000313|EMBL:AGL50762.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Riboflavin biosynthesis {ECO:0000256|PIRNR:PIRNR006769}; KW Zinc {ECO:0000213|PDB:2HXV, ECO:0000256|PIRNR:PIRNR006769, KW ECO:0000256|PIRSR:PIRSR006769-3}. FT DOMAIN 1 124 CMP/dCMP-type deaminase. FT {ECO:0000259|PROSITE:PS51747}. FT NP_BIND 167 169 NADP. {ECO:0000213|PDB:2HXV}. FT NP_BIND 195 196 NADP. {ECO:0000213|PDB:2HXV}. FT NP_BIND 219 221 NADP. {ECO:0000213|PDB:2HXV}. FT NP_BIND 283 289 NADP. {ECO:0000213|PDB:2HXV, FT ECO:0000256|PIRSR:PIRSR006769-2}. FT ACT_SITE 51 51 Proton donor. FT {ECO:0000256|PIRSR:PIRSR006769-1}. FT METAL 49 49 Zinc; catalytic. FT {ECO:0000256|PIRSR:PIRSR006769-3}. FT METAL 49 49 Zinc; via pros nitrogen. FT {ECO:0000213|PDB:2HXV}. FT METAL 77 77 Zinc. {ECO:0000213|PDB:2HXV}. FT METAL 77 77 Zinc; catalytic. FT {ECO:0000256|PIRSR:PIRSR006769-3}. FT METAL 86 86 Zinc. {ECO:0000213|PDB:2HXV}. FT METAL 86 86 Zinc; catalytic. FT {ECO:0000256|PIRSR:PIRSR006769-3}. FT BINDING 155 155 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000213|PDB:2HXV, FT ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 162 162 NADP; via carbonyl oxygen. FT {ECO:0000213|PDB:2HXV}. FT BINDING 169 169 Substrate. FT {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 171 171 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 184 184 Substrate. FT {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 196 196 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 200 200 NADP. {ECO:0000213|PDB:2HXV, FT ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 204 204 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 207 207 Substrate. FT {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 261 261 NADP; via carbonyl oxygen. FT {ECO:0000213|PDB:2HXV}. FT BINDING 281 281 Substrate. FT {ECO:0000256|PIRSR:PIRSR006769-2}. SQ SEQUENCE 348 AA; 38866 MW; 7E2BC27F08D33FDF CRC64; MYETFMKRAI ELAKKGLGRV NPNPPVGAVV VKDGRIIAEG FHPYFGGPHA ERMAIESARK KGEDLRGATL IVTLEPCDHH GKTPPCTDLI IESGIKTVVI GTRDPNPVSG NGVEKFRNHG IEVIEGVLEE EVKKLCEFFI TYVTKKRPFV ALKYASTLDG KIADHRGDSK WITDKLRFKV HEMRNIYSAV LVGAGTVLKD NPQLTCRLKE GRNPVRVILD RKGVLSGKVF RVFEENARVI VFTESEEAEY PPHVEKALSD CSVESILRNL YERDIDSVLV EGGSKVFSEF LDHADVVFGF YSTKIFGKGL DVFSGYLSDV SVPPKFKVVN VEFSDSEFLV EMRPCSRE // ID Q9X209_THEMA Unreviewed; 71 AA. AC Q9X209; G4FG68; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36748.1}; GN OrderedLocusNames=TM_1681 {ECO:0000313|EMBL:AAD36748.1}; GN ORFNames=Tmari_1689 {ECO:0000313|EMBL:AGL50613.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36748.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36748.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36748.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50613.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50613.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36748.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50613.1; -; Genomic_DNA. DR PIR; G72226; G72226. DR RefSeq; NP_229481.1; NC_000853.1. DR RefSeq; WP_004082197.1; NZ_CP011107.1. DR STRING; 243274.TM1681; -. DR EnsemblBacteria; AAD36748; AAD36748; TM_1681. DR EnsemblBacteria; AGL50613; AGL50613; Tmari_1689. DR GeneID; 897899; -. DR KEGG; tma:TM1681; -. DR KEGG; tmi:THEMA_05835; -. DR KEGG; tmm:Tmari_1689; -. DR KEGG; tmw:THMA_1723; -. DR PATRIC; 23938336; VBITheMar51294_1698. DR OMA; EERAMLM; -. DR BioCyc; TMAR243274:GC6P-1729-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 50 71 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 71 AA; 8920 MW; 132DEFB963C36785 CRC64; MWWGRGYGWR RGWGWRGGFG FGRGPWWAYY DYPPVPPSPE EEKEMLLDYK RYLEEELRYV EERLKELENR R // ID Q9X249_THEMA Unreviewed; 373 AA. AC Q9X249; G4FGB2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Alanyl-tRNA synthetase family protein {ECO:0000313|EMBL:AGL50658.1}; DE SubName: Full=Alanyl-tRNA synthetase-related protein {ECO:0000313|EMBL:AAD36791.1}; GN OrderedLocusNames=TM_1726 {ECO:0000313|EMBL:AAD36791.1}; GN ORFNames=Tmari_1734 {ECO:0000313|EMBL:AGL50658.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36791.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36791.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36791.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50658.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50658.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36791.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50658.1; -; Genomic_DNA. DR PIR; E72216; E72216. DR RefSeq; NP_229524.1; NC_000853.1. DR RefSeq; WP_004082241.1; NZ_CP011107.1. DR STRING; 243274.TM1726; -. DR EnsemblBacteria; AAD36791; AAD36791; TM_1726. DR EnsemblBacteria; AGL50658; AGL50658; Tmari_1734. DR GeneID; 897185; -. DR KEGG; tma:TM1726; -. DR KEGG; tmi:THEMA_05605; -. DR KEGG; tmm:Tmari_1734; -. DR KEGG; tmw:THMA_1768; -. DR PATRIC; 23938428; VBITheMar51294_1744. DR eggNOG; ENOG4108HJN; Bacteria. DR eggNOG; COG2872; LUCA. DR KO; K01872; -. DR OMA; DIACQHT; -. DR OrthoDB; EOG6NWBMP; -. DR BioCyc; TMAR243274:GC6P-1774-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0002196; F:Ser-tRNA(Ala) hydrolase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central. DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro. DR GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central. DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR012947; tRNA_SAD. DR Pfam; PF07973; tRNA_SAD; 1. DR SMART; SM00863; tRNA_SAD; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF55186; SSF55186; 1. DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1. PE 4: Predicted; KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:AAD36791.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Ligase {ECO:0000313|EMBL:AAD36791.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 226 AA_TRNA_LIGASE_II_ALA. FT {ECO:0000259|PROSITE:PS50860}. FT COILED 124 148 {ECO:0000256|SAM:Coils}. FT COILED 239 276 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 373 AA; 42329 MW; EF120ECE886E013F CRC64; MTAGRIRIDE VIKDGEKIIA VSRTSPFYPD GKGGQLGDRG KIGPANVLKV KEKNGYILHY LDAHLEPGDY ECEIDPARRK DIACQHTAQH ILSAAFLKVA DLETVSFHMG ERVSTIDLNA PFVLEDVLEE AEDLANEVVR SCERVEILEI EKEEAEKMNL RKLPNVEGKV RVVKIGDFDV TACGGFHVEN TGEIGLIKIV DTEKVKKVLT RIYFTAGDRA LKDYREKDKL LKSLSRVLTT STKELLKRAE NLLEEVKEKS AKLDKLSEKY AEILSKVAEP EKVGKYYLYH FSGTPEEMKY LPKFLADRKD TIVLLEHPDR IEIVSNWIDC RKIFEKLKDQ LNVEGGSSQK RAVITANSAS RIVEKLREIL KWF // ID Q9WZK5_THEMA Unreviewed; 128 AA. AC Q9WZK5; G4FD77; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35827.1}; GN OrderedLocusNames=TM_0746 {ECO:0000313|EMBL:AAD35827.1}; GN ORFNames=Tmari_0747 {ECO:0000313|EMBL:AGL49672.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35827.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35827.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35827.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49672.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49672.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35827.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49672.1; -; Genomic_DNA. DR PIR; E72340; E72340. DR RefSeq; NP_228555.1; NC_000853.1. DR RefSeq; WP_004080971.1; NZ_CP011107.1. DR STRING; 243274.TM0746; -. DR EnsemblBacteria; AAD35827; AAD35827; TM_0746. DR EnsemblBacteria; AGL49672; AGL49672; Tmari_0747. DR GeneID; 898413; -. DR KEGG; tma:TM0746; -. DR KEGG; tmi:THEMA_00925; -. DR KEGG; tmm:Tmari_0747; -. DR KEGG; tmw:THMA_0764; -. DR PATRIC; 23936412; VBITheMar51294_0759. DR OMA; FSEEGMY; -. DR OrthoDB; EOG6Q5NW0; -. DR BioCyc; TMAR243274:GC6P-772-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 128 AA; 15088 MW; 290A1A4513749CA8 CRC64; MTRNGFLFIL FVVTLALLIV DVSFKNERKR IERLPSFDVV VETPFKETVE EMKIELNRSI LVSEVLKEVE KAEYYPEWKA FVFRSRADFE KAINVVKRET GERLSIKTTE DGVEYFFSSG MYFILKVK // ID Q9X213_THEMA Unreviewed; 394 AA. AC Q9X213; G4FG74; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=DNA/pantothenate metabolism flavoprotein {ECO:0000313|EMBL:AAD36754.1}; DE SubName: Full=Phosphopantothenoylcysteine decarboxylase / Phosphopantothenoylcysteine synthetase {ECO:0000313|EMBL:AGL50619.1}; DE EC=4.1.1.36 {ECO:0000313|EMBL:AGL50619.1}; DE EC=6.3.2.5 {ECO:0000313|EMBL:AGL50619.1}; GN OrderedLocusNames=TM_1687 {ECO:0000313|EMBL:AAD36754.1}; GN ORFNames=Tmari_1695 {ECO:0000313|EMBL:AGL50619.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36754.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36754.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36754.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50619.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50619.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36754.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50619.1; -; Genomic_DNA. DR PIR; A72223; A72223. DR RefSeq; NP_229487.1; NC_000853.1. DR RefSeq; WP_004082203.1; NZ_CP011107.1. DR STRING; 243274.TM1687; -. DR EnsemblBacteria; AAD36754; AAD36754; TM_1687. DR EnsemblBacteria; AGL50619; AGL50619; Tmari_1695. DR GeneID; 897896; -. DR KEGG; tma:TM1687; -. DR KEGG; tmi:THEMA_05805; -. DR KEGG; tmm:Tmari_1695; -. DR KEGG; tmw:THMA_1729; -. DR PATRIC; 23938348; VBITheMar51294_1704. DR eggNOG; ENOG4105CJS; Bacteria. DR eggNOG; COG0452; LUCA. DR KO; K13038; -. DR OMA; VRFIGNH; -. DR OrthoDB; EOG6FFSBB; -. DR BioCyc; TMAR243274:GC6P-1735-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IEA:UniProtKB-EC. DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:InterPro. DR GO; GO:0015941; P:pantothenate catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.10300; -; 1. DR Gene3D; 3.40.50.1950; -; 1. DR InterPro; IPR005252; CoaBC. DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C. DR InterPro; IPR003382; Flavoprotein. DR Pfam; PF04127; DFP; 1. DR Pfam; PF02441; Flavoprotein; 1. DR SUPFAM; SSF102645; SSF102645; 1. DR SUPFAM; SSF52507; SSF52507; 1. DR TIGRFAMs; TIGR00521; coaBC_dfp; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Ligase {ECO:0000313|EMBL:AGL50619.1}; KW Lyase {ECO:0000313|EMBL:AGL50619.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 127 Flavoprotein. {ECO:0000259|Pfam:PF02441}. FT DOMAIN 180 359 DFP. {ECO:0000259|Pfam:PF04127}. SQ SEQUENCE 394 AA; 43805 MW; EBCC811C151ECFCA CRC64; MRIVLGVSSG IAIYKAVDLA SKLRKEGHEL HVVMTPDATR MISPVVFSAV GNCSVYHDWM DVRNGWIPHT EISRTADVLV VAPATANTIS KIANGIADNL LTLVALAFDK DAKILVPTMN YRMYSNKLFQ ENLEKLKNNG WFVVEPEEGH LACGEVGKGR YPENEKIVEA VHLLTFPKKL AGKKVLITAG PTRERIDAVR FITNASSGKM GYALATVAKR MGARVSLVSG PTSLKPPYYV DEFVKVESAE EMYEEVMKRF EDTDIVIMNA AVGDYRPKKV FEGKLKKTEN DLVLHLERTK DILKELGQRK SNQILVGFAA EVENFEENAV KKLREKNLDL LVLNDARKAF SSDRVEVYIY GRDGFIKRID EDDKIRVACG ILDVVSNLAG GSPS // ID Q9WXM2_THEMA Unreviewed; 438 AA. AC Q9WXM2; G4FGS3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Transglutaminase-like enzyme, putative cysteine protease {ECO:0000313|EMBL:AGL48930.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35101.1}; GN OrderedLocusNames=TM_0007 {ECO:0000313|EMBL:AAD35101.1}; GN ORFNames=Tmari_0004 {ECO:0000313|EMBL:AGL48930.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35101.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35101.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35101.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48930.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48930.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35101.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48930.1; -; Genomic_DNA. DR PIR; A72430; A72430. DR RefSeq; NP_227823.1; NC_000853.1. DR RefSeq; WP_004082444.1; NZ_CP011107.1. DR STRING; 243274.TM0007; -. DR EnsemblBacteria; AAD35101; AAD35101; TM_0007. DR EnsemblBacteria; AGL48930; AGL48930; Tmari_0004. DR GeneID; 896816; -. DR KEGG; tma:TM0007; -. DR KEGG; tmi:THEMA_04765; -. DR KEGG; tmm:Tmari_0004; -. DR KEGG; tmw:THMA_0003; -. DR PATRIC; 23934854; VBITheMar51294_0005. DR eggNOG; ENOG4105QX8; Bacteria. DR eggNOG; COG1305; LUCA. DR OMA; NLKGDCG; -. DR OrthoDB; EOG6GTZFG; -. DR BioCyc; TMAR243274:GC6P-7-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR002931; Transglutaminase-like. DR Pfam; PF01841; Transglut_core; 1. DR SMART; SM00460; TGc; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL48930.1}; KW Protease {ECO:0000313|EMBL:AGL48930.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 304 365 TGc. {ECO:0000259|SMART:SM00460}. SQ SEQUENCE 438 AA; 52347 MW; A72446A49B0F9FBA CRC64; MEFLIYSLPE EVLREEMLGN FSVALKLIDD FLKKDLPLLQ RERLIYEKER IERLLEDYPF TEKEAMEKMR EMFEGFSEGE FQYLMNEGVL DYIVVEGEKR FERRFFHNLA FVRSEYRERL RKDERSEKAR RILHERLERL IKGEDPKRYR IRARITLKLK ETSSKHRVWL PFPKESLQIE SVKLLRTSHK SYYISPNDVP QRTIYFEGED STFFVEFEYI VREWVNHVDP ERVSEKVAGF EEFLKEEPPH IVFTPKLRWL TQTVVGSEVN PYLKAKRIYD WITLNVRYSY VKPYALYENI TDFVVNNLKG DCGFQALLFI TMCRIAGVPA RWQSGWYINP IFGSPHDWAL FYVEPYGWLP ADLSFGGARR DNESFRSFYF GNLDGFRMVA NDGFMKDFDP KTRFVRSDPT DNQVGEAESE EKRLPFESTI EVISFEEV // ID Q9X159_THEMA Unreviewed; 258 AA. AC Q9X159; G4FF76; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36409.1}; GN OrderedLocusNames=TM_1337 {ECO:0000313|EMBL:AAD36409.1}; GN ORFNames=Tmari_1345 {ECO:0000313|EMBL:AGL50269.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36409.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36409.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36409.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50269.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50269.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36409.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50269.1; -; Genomic_DNA. DR PIR; A72266; A72266. DR RefSeq; NP_229139.1; NC_000853.1. DR RefSeq; WP_004081536.1; NZ_CP011107.1. DR EnsemblBacteria; AAD36409; AAD36409; TM_1337. DR EnsemblBacteria; AGL50269; AGL50269; Tmari_1345. DR GeneID; 898145; -. DR KEGG; tma:TM1337; -. DR KEGG; tmi:THEMA_07660; -. DR KEGG; tmm:Tmari_1345; -. DR KEGG; tmw:THMA_1361; -. DR PATRIC; 23937607; VBITheMar51294_1349. DR eggNOG; ENOG4108T1X; Bacteria. DR eggNOG; ENOG410XRDS; LUCA. DR OrthoDB; EOG67HJR6; -. DR BioCyc; TMAR243274:GC6P-1368-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR SUPFAM; SSF50998; SSF50998; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 258 AA; 27672 MW; 26BA28534B42AD5F CRC64; MSKMFITVFF GIMLVTVSLI CIAETAPEII WQKILGGSSD DYAFSIQQTP DGGYIVAGYT ESNDGDVKGN HENGDFWIVK LDKDGNIEWQ KTLGGSNWDW AFSVQQTPDG GYIVAGFTWS NDGDVSGNHG SLDAWIVKLD KDGNIEWQKT LGGSGNDWAT SVQQTTDGGY IVAGGTYSTD GVIRGNHGSL DAWVVKLDGN GNMQWQKALG GSGSDSAWSV QQTTDGGYIV AGFTKSNDGD VTGNHGSADF WVVKLGWQ // ID Q9X063_THEMA Unreviewed; 182 AA. AC Q9X063; G4FF22; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Ribosomal-protein-S5p-alanine acetyltransferase {ECO:0000313|EMBL:AGL49895.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36047.1}; GN OrderedLocusNames=TM_0968 {ECO:0000313|EMBL:AAD36047.1}; GN ORFNames=Tmari_0970 {ECO:0000313|EMBL:AGL49895.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36047.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36047.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36047.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49895.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49895.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36047.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49895.1; -; Genomic_DNA. DR PIR; E72312; E72312. DR RefSeq; NP_228776.1; NC_000853.1. DR RefSeq; WP_004080594.1; NZ_CP011107.1. DR STRING; 243274.TM0968; -. DR EnsemblBacteria; AAD36047; AAD36047; TM_0968. DR EnsemblBacteria; AGL49895; AGL49895; Tmari_0970. DR GeneID; 898706; -. DR KEGG; tma:TM0968; -. DR KEGG; tmi:THEMA_09505; -. DR KEGG; tmm:Tmari_0970; -. DR KEGG; tmw:THMA_0991; -. DR PATRIC; 23936867; VBITheMar51294_0982. DR eggNOG; ENOG4108MK9; Bacteria. DR eggNOG; COG1670; LUCA. DR OMA; NDPEVAY; -. DR OrthoDB; EOG6BKJ7M; -. DR BioCyc; TMAR243274:GC6P-998-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IBA:GO_Central. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR Pfam; PF13302; Acetyltransf_3; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49895.1}. FT DOMAIN 7 172 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 182 AA; 21455 MW; 8F2F89F96C5A8B7B CRC64; MFEGKLVRLR AYRKEDIEKA LEFANDPEVK KCLVPGIPFP WRKEDEEKWY QSLNPFSTDS YSFAIEKLSD GEYIGGCSIN KIDWKNSVAE VGIFLGRPYW SQGYGTDAMR VLVRFIFNEM NMNKIKLHVF SFNERAKRVY EKIGFKVEGI LRQELFREGR YHDVIVMGLL KSEWEDLTET DL // ID Q9X111_THEMA Unreviewed; 41 AA. AC Q9X111; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36359.1}; GN OrderedLocusNames=TM_1285 {ECO:0000313|EMBL:AAD36359.1}; GN ORFNames=Tmari_1291 {ECO:0000313|EMBL:AGL50215.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36359.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36359.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36359.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50215.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50215.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36359.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50215.1; -; Genomic_DNA. DR PIR; D72271; D72271. DR RefSeq; NP_229089.1; NC_000853.1. DR RefSeq; WP_010865297.1; NZ_CP011107.1. DR EnsemblBacteria; AAD36359; AAD36359; TM_1285. DR EnsemblBacteria; AGL50215; AGL50215; Tmari_1291. DR GeneID; 898198; -. DR KEGG; tma:TM1285; -. DR KEGG; tmm:Tmari_1291; -. DR KEGG; tmw:THMA_1311; -. DR BioCyc; TMAR243274:GC6P-1316-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 41 AA; 5168 MW; 5A9198D4C8050ED1 CRC64; MELSSFDFTY ALPGWCIKEM RVRYFLKILW WFIYGHENFD N // ID Q9X023_THEMA Unreviewed; 154 AA. AC Q9X023; G4FF69; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Soluble lytic murein transglycosylase {ECO:0000313|EMBL:AGL49848.1}; DE EC=3.2.1.- {ECO:0000313|EMBL:AGL49848.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36002.1}; GN OrderedLocusNames=TM_0921 {ECO:0000313|EMBL:AAD36002.1}; GN ORFNames=Tmari_0923 {ECO:0000313|EMBL:AGL49848.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36002.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36002.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36002.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49848.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49848.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36002.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49848.1; -; Genomic_DNA. DR PIR; B72317; B72317. DR RefSeq; NP_228729.1; NC_000853.1. DR RefSeq; WP_004080641.1; NZ_CP011107.1. DR STRING; 243274.TM0921; -. DR CAZy; GH23; Glycoside Hydrolase Family 23. DR EnsemblBacteria; AAD36002; AAD36002; TM_0921. DR EnsemblBacteria; AGL49848; AGL49848; Tmari_0923. DR GeneID; 898595; -. DR KEGG; tma:TM0921; -. DR KEGG; tmi:THEMA_00030; -. DR KEGG; tmm:Tmari_0923; -. DR KEGG; tmw:THMA_0943; -. DR PATRIC; 23936773; VBITheMar51294_0935. DR eggNOG; ENOG4105E4C; Bacteria. DR eggNOG; COG0741; LUCA. DR OMA; MPETAEW; -. DR OrthoDB; EOG6JTCB0; -. DR BioCyc; TMAR243274:GC6P-951-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR008258; Transglycosylase_SLT_dom_1. DR Pfam; PF01464; SLT; 1. DR SUPFAM; SSF53955; SSF53955; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000313|EMBL:AGL49848.1}; KW Hydrolase {ECO:0000313|EMBL:AGL49848.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 33 131 SLT. {ECO:0000259|Pfam:PF01464}. SQ SEQUENCE 154 AA; 17964 MW; 4EEECEE0C42E598E CRC64; MRSFFLCFLL VLVFIANLYR LFPDDYYDFI SKNSDDLDPL LIQSIIWVES SFDRNAVSSL GAFGLMQIMP STAVWLKKKF SLEEDFKNPE GNIIYGIVYL KFLKDLYGDL DKAIMAYNVG PAALSEGRNL DSAKRYLKKV KRTYLIYRFL YSER // ID Q9WY25_THEMA Unreviewed; 324 AA. AC Q9WY25; G4FH95; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Putative DNA polymerase III, delta subunit {ECO:0000313|EMBL:AGL49105.1}; DE EC=2.7.7.7 {ECO:0000313|EMBL:AGL49105.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35274.1}; GN OrderedLocusNames=TM_0181 {ECO:0000313|EMBL:AAD35274.1}; GN ORFNames=Tmari_0179 {ECO:0000313|EMBL:AGL49105.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35274.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35274.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35274.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49105.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49105.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35274.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49105.1; -; Genomic_DNA. DR PIR; H72407; H72407. DR RefSeq; NP_227996.1; NC_000853.1. DR RefSeq; WP_004082816.1; NZ_CP011107.1. DR STRING; 243274.TM0181; -. DR EnsemblBacteria; AAD35274; AAD35274; TM_0181. DR EnsemblBacteria; AGL49105; AGL49105; Tmari_0179. DR GeneID; 897028; -. DR KEGG; tma:TM0181; -. DR KEGG; tmi:THEMA_03870; -. DR KEGG; tmm:Tmari_0179; -. DR KEGG; tmw:THMA_0182; -. DR PATRIC; 23935218; VBITheMar51294_0182. DR eggNOG; ENOG4105TFD; Bacteria. DR eggNOG; COG1466; LUCA. DR KO; K02340; -. DR OMA; WLEWIEK; -. DR OrthoDB; EOG6WQD7C; -. DR BioCyc; TMAR243274:GC6P-187-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR010372; DNA_pol3_delta_N. DR InterPro; IPR005790; DNA_polIII_delta. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF06144; DNA_pol3_delta; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01128; holA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AGL49105.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49105.1}. FT DOMAIN 11 155 DNA_pol3_delta. FT {ECO:0000259|Pfam:PF06144}. SQ SEQUENCE 324 AA; 38210 MW; 6A88A660F39A7211 CRC64; MPVTFLTGTA ETQKEELIKK LLKDGNVEYI RIHPEDPDKI DFIRSLLRTK TIFSNKTIID IVNFDEWKAQ EQKRLVELLK NVPEDVHIFI RSQKTGGKGV ALELPKPWET DKWLEWIEKR FRENGLLIDK DALQLFFSKV GTNDLIIERE IEKLKAYSED RKITVEDVEE VVFTYQTPGY DDFCFAVSEG KRKLAHSLLS QLWKTTESVV IATVLANHFL DLFKILVLVT KKRYYTWPDV SRVSKELGIP VPRVARFLGF SFKTWKFKVM NHLLYYDVKK VRKILRDLYD LDRAVKSEED PKPFFHEFIE EVALDVYSLQ RDEE // ID Q7DFA3_THEMA Unreviewed; 278 AA. AC Q7DFA3; G4FGT0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AGL48937.1}; DE SubName: Full=Methyl-accepting chemotaxis protein, putative {ECO:0000313|EMBL:AAD35108.1}; GN OrderedLocusNames=TM_0014 {ECO:0000313|EMBL:AAD35108.1}; GN ORFNames=Tmari_0011 {ECO:0000313|EMBL:AGL48937.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35108.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35108.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35108.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:3G67, ECO:0000213|PDB:3G6B} RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 41-253. RX PubMed=19149470; DOI=10.1021/bi801727m; RA Pollard A.M., Bilwes A.M., Crane B.R.; RT "The structure of a soluble chemoreceptor suggests a mechanism for RT propagating conformational signals."; RL Biochemistry 48:1936-1944(2009). RN [3] {ECO:0000213|PDB:3UR1} RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) OF 107-191. RA Breigel A., Li X., Bilwes A.M., Hugues K.T., Jensen G.J., Crane B.R.; RT "The structure of native bacterial chemoreceptor arrays."; RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2012). RN [4] {ECO:0000213|PDB:4JPB} RP X-RAY CRYSTALLOGRAPHY (3.19 ANGSTROMS) OF 107-192. RX PubMed=23668907; DOI=10.1021/bi400383e; RA Li X., Fleetwood A.D., Bayas C., Bilwes A.M., Ortega D.R., Falke J.J., RA Zhulin I.B., Crane B.R.; RT "The 3.2 A resolution structure of a receptor: CheA:CheW signaling RT complex defines overlapping binding sites and key residue interactions RT within bacterial chemosensory arrays."; RL Biochemistry 52:3852-3865(2013). RN [5] {ECO:0000313|EMBL:AGL48937.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48937.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35108.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48937.1; -; Genomic_DNA. DR RefSeq; NP_227830.1; NC_000853.1. DR RefSeq; WP_004082453.1; NZ_CP011107.1. DR PDB; 3G67; X-ray; 2.17 A; A/B=41-253. DR PDB; 3G6B; X-ray; 3.00 A; A/B=41-253. DR PDB; 3UR1; X-ray; 4.50 A; C/D=107-191. DR PDB; 4JPB; X-ray; 3.19 A; B/C=107-192. DR PDBsum; 3G67; -. DR PDBsum; 3G6B; -. DR PDBsum; 3UR1; -. DR PDBsum; 4JPB; -. DR DIP; DIP-60023N; -. DR STRING; 243274.TM0014; -. DR EnsemblBacteria; AAD35108; AAD35108; TM_0014. DR EnsemblBacteria; AGL48937; AGL48937; Tmari_0011. DR GeneID; 896826; -. DR KEGG; tma:TM0014; -. DR KEGG; tmi:THEMA_04730; -. DR KEGG; tmm:Tmari_0011; -. DR KEGG; tmw:THMA_0010; -. DR PATRIC; 23934868; VBITheMar51294_0012. DR eggNOG; ENOG4108KSE; Bacteria. DR eggNOG; COG0840; LUCA. DR OMA; GFTTIAR; -. DR OrthoDB; EOG6R5C3G; -. DR BioCyc; TMAR243274:GC6P-14-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro. DR InterPro; IPR004089; MCPsignal_dom. DR Pfam; PF00015; MCPsignal; 1. DR SMART; SM00283; MA; 1. DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3G67, ECO:0000213|PDB:3G6B, KW ECO:0000213|PDB:3UR1, ECO:0000213|PDB:4JPB}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 27 253 Methyl-accepting transducer. FT {ECO:0000259|PROSITE:PS50111}. FT COILED 28 55 {ECO:0000256|SAM:Coils}. FT COILED 161 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 278 AA; 31660 MW; 6D87721F29FB3492 CRC64; MREREIVDKL TSAFFAENTI ISFTSQLDEA LTRKLRRMQR RIEEVKERFV NLNRLFQELV GDFQAKSDQL VSVIQDMEKI SENIMEELKK SGTNVDQIVE RVKEASSQIG ETLENIRSIE KLIQNIMRIA RETNILALNA TIEAARAGEA GKGFMIVANE VQNLSNETNE VTKQIVEKAR EILESSQRSL ENLEFMANLF ETVGKTLQNM VRFMENNVKL LQEVRNSLDT SKESLSEKSA EIDSATKVLE ETAGGFTTIN RVINSVITAQ RKLKDLKI // ID Q9WXY6_THEMA Unreviewed; 194 AA. AC Q9WXY6; G4FH47; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Isochorismatase-related protein {ECO:0000313|EMBL:AAD35226.1}; GN OrderedLocusNames=TM_0133 {ECO:0000313|EMBL:AAD35226.1}; GN ORFNames=Tmari_0131 {ECO:0000313|EMBL:AGL49057.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35226.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35226.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35226.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49057.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49057.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35226.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49057.1; -; Genomic_DNA. DR PIR; C72413; C72413. DR RefSeq; NP_227948.1; NC_000853.1. DR RefSeq; WP_004082723.1; NZ_CP011107.1. DR STRING; 243274.TM0133; -. DR EnsemblBacteria; AAD35226; AAD35226; TM_0133. DR EnsemblBacteria; AGL49057; AGL49057; Tmari_0131. DR GeneID; 896960; -. DR KEGG; tma:TM0133; -. DR KEGG; tmi:THEMA_04140; -. DR KEGG; tmm:Tmari_0131; -. DR KEGG; tmw:THMA_0128; -. DR PATRIC; 23935108; VBITheMar51294_0132. DR eggNOG; ENOG4107ZIR; Bacteria. DR eggNOG; COG1535; LUCA. DR OMA; EWYHYAS; -. DR OrthoDB; EOG6G20K9; -. DR BioCyc; TMAR243274:GC6P-133-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.50.850; -; 1. DR InterPro; IPR000868; Isochorismatase-like. DR Pfam; PF00857; Isochorismatase; 1. DR SUPFAM; SSF52499; SSF52499; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 18 180 Isochorismatase. FT {ECO:0000259|Pfam:PF00857}. SQ SEQUENCE 194 AA; 22589 MW; D49BB58B861144C6 CRC64; MFYFPEREKK RFTLKRPALL IIDLQNYFTS PDSPAYLRGV EVAIENIRKL KISFERAKLP VIATVHVGAS PMMKKWWGNE VDKRWAVPVF SDVLLFEKNT YDAFYSTKLE EELRSKSINQ LIITGVMTHL CCETTARSAF VRNFEVIMVE DALWDKNEWY HFSSLKNLAH GVAYIAKTEE ILCALESLEQ GQRE // ID Q9X084_THEMA Unreviewed; 169 AA. AC Q9X084; G4FF06; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36068.1}; GN OrderedLocusNames=TM_0989 {ECO:0000313|EMBL:AAD36068.1}; GN ORFNames=Tmari_0992 {ECO:0000313|EMBL:AGL49917.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36068.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36068.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36068.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49917.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49917.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36068.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49917.1; -; Genomic_DNA. DR PIR; B72311; B72311. DR RefSeq; NP_228797.1; NC_000853.1. DR RefSeq; WP_004080570.1; NZ_CP011107.1. DR STRING; 243274.TM0989; -. DR EnsemblBacteria; AAD36068; AAD36068; TM_0989. DR EnsemblBacteria; AGL49917; AGL49917; Tmari_0992. DR GeneID; 897283; -. DR KEGG; tma:TM0989; -. DR KEGG; tmi:THEMA_09405; -. DR KEGG; tmm:Tmari_0992; -. DR KEGG; tmw:THMA_1011; -. DR PATRIC; 23936907; VBITheMar51294_1002. DR eggNOG; ENOG410YQM9; LUCA. DR OMA; RYWASKF; -. DR OrthoDB; EOG6SJJJW; -. DR BioCyc; TMAR243274:GC6P-1019-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 169 AA; 19719 MW; 0A0EA8A3C4B95BA4 CRC64; MNSAIEYRIS LKYVKKSTLP VKRTQKLAEF VPVFIAGKNG KEEQIPGKAE ARAKVFLPEF LNFAKKVGAI HDEQISLFQM ENDRSRKLVL KVSDDYAYLR LMIYGVLMSV LKNPVEWGYL EDLVLSMEPL TLRFWGSKIK YTFWKAKNRR VLNYLARRIL EVERLGKVT // ID Q9X014_THEMA Unreviewed; 329 AA. AC Q9X014; G4FCR4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Peptidylprolyl isomerase {ECO:0000256|RuleBase:RU363014, ECO:0000256|SAAS:SAAS00523066}; DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014, ECO:0000256|SAAS:SAAS00523066}; GN OrderedLocusNames=TM_0912 {ECO:0000313|EMBL:AAD35993.1}; GN ORFNames=Tmari_0914 {ECO:0000313|EMBL:AGL49839.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35993.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35993.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35993.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49839.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49839.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). {ECO:0000256|RuleBase:RU363014, CC ECO:0000256|SAAS:SAAS00523013}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35993.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49839.1; -; Genomic_DNA. DR PIR; G72319; G72319. DR RefSeq; NP_228720.1; NC_000853.1. DR RefSeq; WP_004080650.1; NZ_CP011107.1. DR STRING; 243274.TM0912; -. DR EnsemblBacteria; AAD35993; AAD35993; TM_0912. DR EnsemblBacteria; AGL49839; AGL49839; Tmari_0914. DR GeneID; 898586; -. DR KEGG; tma:TM0912; -. DR KEGG; tmi:THEMA_00075; -. DR KEGG; tmm:Tmari_0914; -. DR KEGG; tmw:THMA_0934; -. DR PATRIC; 23936755; VBITheMar51294_0926. DR eggNOG; ENOG410849B; Bacteria. DR eggNOG; COG0760; LUCA. DR OMA; PEGKKEM; -. DR OrthoDB; EOG6ZH2DM; -. DR BioCyc; TMAR243274:GC6P-942-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR InterPro; IPR000297; PPIase_PpiC. DR InterPro; IPR027304; Trigger_fact/SurA_dom. DR Pfam; PF13145; Rotamase_2; 1. DR SUPFAM; SSF109998; SSF109998; 1. DR PROSITE; PS50198; PPIC_PPIASE_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000256|RuleBase:RU363014, KW ECO:0000256|SAAS:SAAS00522988}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Rotamase {ECO:0000256|RuleBase:RU363014, KW ECO:0000256|SAAS:SAAS00522988}; KW Signal {ECO:0000256|RuleBase:RU363014}. FT SIGNAL 1 20 {ECO:0000256|RuleBase:RU363014}. FT CHAIN 21 329 Peptidylprolyl isomerase. FT {ECO:0000256|RuleBase:RU363014}. FT /FTId=PRO_5006776920. FT DOMAIN 191 274 PpiC. {ECO:0000259|PROSITE:PS50198}. SQ SEQUENCE 329 AA; 37374 MW; C4B0D5A2CB8B7F45 CRC64; MRKLIFVILA VLGISLFGQA TTTSSTVVAI VNGEPITSDL LELEADIDGI LRSIAQIDMR FFNVLTGTEE GLKLLLKYKQ EVLNSLIDDL LIQQLAEKEG VGVSDEEVKK EVEARLKETV ESMGITLEDL DKFLQSAGYG DLETFKKRLH WHVKTQLSLQ RLQEKITQNA TVTLEEAQNY YNQNKETYRI PAAVHLYRIT TEDKSKMDEV LSKIRKGEDF LEVATQVATG GDLGWIEEGK LEKDIESVIF DAPEGAILGP FESEGKFVLY KVVEKRSSSY KKFEEVKQEI MDKLLADKRN QLWNDWFNKV FEEFKKNSHI EIKLGGSQG // ID Q9WXS3_THEMA Unreviewed; 539 AA. AC Q9WXS3; G4FGY3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 105. DE SubName: Full=D-mannonate oxidoreductase {ECO:0000313|EMBL:AGL48991.1}; DE EC=1.1.1.57 {ECO:0000313|EMBL:AGL48991.1}; DE SubName: Full=D-mannonate oxidoreductase, putative {ECO:0000313|EMBL:AAD35162.1}; GN OrderedLocusNames=TM_0068 {ECO:0000313|EMBL:AAD35162.1}; GN ORFNames=Tmari_0065 {ECO:0000313|EMBL:AGL48991.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35162.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35162.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35162.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48991.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48991.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35162.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48991.1; -; Genomic_DNA. DR PIR; H72422; H72422. DR RefSeq; NP_227884.1; NC_000853.1. DR RefSeq; WP_004082564.1; NZ_CP011107.1. DR STRING; 243274.TM0068; -. DR EnsemblBacteria; AAD35162; AAD35162; TM_0068. DR EnsemblBacteria; AGL48991; AGL48991; Tmari_0065. DR GeneID; 896892; -. DR KEGG; tma:TM0068; -. DR KEGG; tmi:THEMA_04465; -. DR KEGG; tmm:Tmari_0065; -. DR KEGG; tmw:THMA_0064; -. DR PATRIC; 23934976; VBITheMar51294_0066. DR eggNOG; ENOG4107RXK; Bacteria. DR eggNOG; COG0246; LUCA. DR KO; K00040; -. DR OMA; DPGIINP; -. DR OrthoDB; EOG6RVFVK; -. DR BioCyc; MetaCyc:MONOMER-17954; -. DR BioCyc; TMAR243274:GC6P-68-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0008866; F:fructuronate reductase activity; IEA:UniProtKB-EC. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR013118; Mannitol_DH_C. DR InterPro; IPR013131; Mannitol_DH_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01232; Mannitol_dh; 1. DR Pfam; PF08125; Mannitol_dh_C; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL48991.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 38 197 Mannitol_dh. {ECO:0000259|Pfam:PF01232}. FT DOMAIN 236 472 Mannitol_dh_C. FT {ECO:0000259|Pfam:PF08125}. SQ SEQUENCE 539 AA; 61432 MW; 47EF19B7F733CAF0 CRC64; MRLNRETIKD RAAWEKIGVR PPYFDLDEVE KNTKEQPKWV HFGGGNIFRG FVAAVLQNLL EEGKEDTGIN VIELFDYEVI DKVYKPYDNL SIAVTIKPDG DFEKRIIASV MEALKGDPSH PDWERAKEIF RNPSLQLASL TITEKGYNIE DQAGNLFPQV MEDMKNGPVS PQTSMGKVAA LLYERFKAGR LPIALLSLDN FSRNGEKLYS SVKRISEEWV KSGLVEKDFI DYLEKDVAFP WSMIDKIVPG PSEFIKEHLE KLGIEGMEIF VTSKRTHIAP FVNMEWAQYL VIEDSFPNGR PKLEGADRNV FLTDRETVEK AERMKVTTCL NPLHTALAIF GCLLGYKKIA DEMKDPLLKK LVEGVGEEGI KVVVDPGIIN PREFLNEVIN IRLPNPYLPD TPQRIATDTS QKMPIRFGET IKAYHERPDL DPRNLKYIPL VIAGWCRYLM GIDDEGREMQ LSPDPLLENL RSYVSKIKFG DPESTDDHLK PILSSQQLFR VNLYEVGLGE KIEELFKKMI TGPRAVRKTL EEVVGREDG // ID Q9X0L0_THEMA Unreviewed; 612 AA. AC Q9X0L0; G4FEM2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36202.1}; GN OrderedLocusNames=TM_1126 {ECO:0000313|EMBL:AAD36202.1}; GN ORFNames=Tmari_1132 {ECO:0000313|EMBL:AGL50056.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36202.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36202.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36202.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50056.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50056.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36202.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50056.1; -; Genomic_DNA. DR PIR; C72293; C72293. DR RefSeq; NP_228932.1; NC_000853.1. DR RefSeq; WP_004080287.1; NZ_CP011107.1. DR STRING; 243274.TM1126; -. DR EnsemblBacteria; AAD36202; AAD36202; TM_1126. DR EnsemblBacteria; AGL50056; AGL50056; Tmari_1132. DR GeneID; 898638; -. DR KEGG; tma:TM1126; -. DR KEGG; tmi:THEMA_08715; -. DR KEGG; tmm:Tmari_1132; -. DR KEGG; tmw:THMA_1149; -. DR PATRIC; 23937187; VBITheMar51294_1142. DR eggNOG; ENOG41090FN; Bacteria. DR eggNOG; ENOG4111Q7C; LUCA. DR OMA; MEINWST; -. DR OrthoDB; EOG6NKQVW; -. DR BioCyc; TMAR243274:GC6P-1155-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 28 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 612 AA; 70814 MW; 0BB1627AB90222AF CRC64; MRNGSILVTT VIILVIVSVL GISVFFAFNQ YRENVELTAQ RLEATYRASN ILNLGVACLK KHFGFLGMEI NWSTGSVTWF DDFRKRVLLQ SDGDAWENVF SLLDTEKYYN LSSDIDFSTE ASKLGFSNFE AVAIPFKNNP FFALLVVRAQ VGKAVVYKYA VLSSDFLNKY AYFTEKETRP DGDKIYFITQ DIIDGPFRSN DVIHVKGEPL FKGSVEFKDI DLEAGEGPRY ENPPPKYLTE EDIKKYNIEK IKDYYSQQIE RIVKPASEVV LSSEPVGIEL PSINEFVESW EEKENDKTIY YKKQREIVYT LEFNTPKGSS GNDYLIKVSY KEVYRIYKSE DQEKWNFVRE EVLGEGELFH IKSKPNSDQY HLVLQGNEAR EFLGLDRNEY DIYFNGVIKT DNDVYLKNMS EGNIKPMFVD GRYTIVANNI YIEDHIIYND YREVLEEIAD KEKISGNSDQ KIAQAVIRKL GVDGNIEEDY SELLKNHESD DFLNLVAYKN VVITDKKPNM KIFASIYAFT GSFYVKGYNE KDFLKNNERE LTERELTIFG SLAQYVRGAV GTFYWSRDGK PTIKTGYRKN YIYDWRILKG FSVFGTPTVP KESNILNVRE VY // ID Q9WXR8_THEMA Unreviewed; 148 AA. AC Q9WXR8; G4FGX8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35157.1}; GN OrderedLocusNames=TM_0063 {ECO:0000313|EMBL:AAD35157.1}; GN ORFNames=Tmari_0060 {ECO:0000313|EMBL:AGL48986.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35157.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35157.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35157.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48986.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48986.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35157.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48986.1; -; Genomic_DNA. DR PIR; C72422; C72422. DR RefSeq; NP_227879.1; NC_000853.1. DR RefSeq; WP_004082554.1; NZ_CP011107.1. DR STRING; 243274.TM0063; -. DR EnsemblBacteria; AAD35157; AAD35157; TM_0063. DR EnsemblBacteria; AGL48986; AGL48986; Tmari_0060. DR GeneID; 896887; -. DR KEGG; tma:TM0063; -. DR KEGG; tmi:THEMA_04490; -. DR KEGG; tmm:Tmari_0060; -. DR KEGG; tmw:THMA_0059; -. DR PATRIC; 23934966; VBITheMar51294_0061. DR OMA; WAGFQAP; -. DR OrthoDB; EOG65QWK4; -. DR BioCyc; TMAR243274:GC6P-63-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 140 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 148 AA; 16921 MW; 3D88D45F32B795D6 CRC64; MKKIFNYVLA YLFLAVTSVL GFYVIFMEGR RFFFTLLGLT SARLQTINAV DKFVVIVLGI AFLGFFIFSE SYFRKKVESS MKDLLRAVLT VSGILMFVWA GFQAPFFFSV GYKLGLPEII IYLLKLIGGS LLIFVSSRYL KNEYLHSV // ID Q9WZZ8_THEMA Unreviewed; 336 AA. AC Q9WZZ8; G4FCS9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 108. DE SubName: Full=Galactose-1-phosphate uridylyltransferase {ECO:0000313|EMBL:AGL49823.1}; DE EC=2.7.7.10 {ECO:0000313|EMBL:AGL49823.1}; DE SubName: Full=Galactose-1-phosphate uridylyltransferase, putative {ECO:0000313|EMBL:AAD35977.1}; GN OrderedLocusNames=TM_0896 {ECO:0000313|EMBL:AAD35977.1}; GN ORFNames=Tmari_0898 {ECO:0000313|EMBL:AGL49823.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35977.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35977.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35977.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49823.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49823.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35977.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49823.1; -; Genomic_DNA. DR PIR; A72322; A72322. DR RefSeq; NP_228704.1; NC_000853.1. DR RefSeq; WP_004080684.1; NZ_CP011107.1. DR STRING; 243274.TM0896; -. DR EnsemblBacteria; AAD35977; AAD35977; TM_0896. DR EnsemblBacteria; AGL49823; AGL49823; Tmari_0898. DR GeneID; 898570; -. DR KEGG; tma:TM0896; -. DR KEGG; tmi:THEMA_00155; -. DR KEGG; tmm:Tmari_0898; -. DR KEGG; tmw:THMA_0918; -. DR PATRIC; 23936723; VBITheMar51294_0910. DR eggNOG; ENOG4105F0Z; Bacteria. DR eggNOG; COG1085; LUCA. DR KO; K00965; -. DR OMA; EIRKHYF; -. DR OrthoDB; EOG6CCH5M; -. DR BioCyc; TMAR243274:GC6P-926-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:InterPro. DR GO; GO:0017103; F:UTP:galactose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro. DR Gene3D; 3.30.428.10; -; 2. DR InterPro; IPR001937; GalP_UDPtransf1. DR InterPro; IPR005850; GalP_Utransf_C. DR InterPro; IPR005849; GalP_Utransf_N. DR InterPro; IPR011146; HIT-like. DR PANTHER; PTHR11943; PTHR11943; 1. DR Pfam; PF02744; GalP_UDP_tr_C; 1. DR Pfam; PF01087; GalP_UDP_transf; 1. DR PIRSF; PIRSF000808; GalT; 1. DR SUPFAM; SSF54197; SSF54197; 2. DR TIGRFAMs; TIGR00209; galT_1; 1. DR PROSITE; PS51084; HIT_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAD35977.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35977.1}. FT DOMAIN 197 308 HIT. {ECO:0000259|PROSITE:PS51084}. FT ACT_SITE 166 166 Tele-UMP-histidine intermediate. FT {ECO:0000256|PIRSR:PIRSR000808-1}. SQ SEQUENCE 336 AA; 39483 MW; 792CE19EED698DA8 CRC64; MPEFRKDPII KRWVIIATER AKRPHDFART KVEEVREGFC PFDYGNEHTT PPEIFAFRPA DTEPNTPGWW VRVVPNKFPA VDPNAPLRKY GRGMYDAAMG FGYHDVVVET PDHNSHLAVM DYKNVEEVIW AYKIRYEQLM KDERIKYILI FKNHGRDAGA SLSHPHSQII ALPIMPKRVQ EELDGSKEYY EYKERCPFCD IIDEEKRERE RIVEENDHFI ALEPFAARFP FETWILPKRH MNSFHLISED EVGSLAKILK NVLYRIYAAL DNPPYNLLIH TAPTSLEGKD YYHWHIEIFP RLTKVAGFEW GTGFYINTVP PEDAARYLRE VSLEQV // ID Q9WXU6_THEMA Unreviewed; 182 AA. AC Q9WXU6; G4FH06; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35185.1}; GN OrderedLocusNames=TM_0091 {ECO:0000313|EMBL:AAD35185.1}; GN ORFNames=Tmari_0088 {ECO:0000313|EMBL:AGL49014.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35185.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35185.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35185.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49014.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49014.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35185.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49014.1; -; Genomic_DNA. DR PIR; E72420; E72420. DR RefSeq; NP_227907.1; NC_000853.1. DR RefSeq; WP_004082632.1; NZ_CP011107.1. DR STRING; 243274.TM0091; -. DR EnsemblBacteria; AAD35185; AAD35185; TM_0091. DR EnsemblBacteria; AGL49014; AGL49014; Tmari_0088. DR GeneID; 896918; -. DR KEGG; tma:TM0091; -. DR KEGG; tmi:THEMA_04350; -. DR KEGG; tmm:Tmari_0088; -. DR KEGG; tmw:THMA_0087; -. DR PATRIC; 23935022; VBITheMar51294_0089. DR OMA; ENLENRY; -. DR OrthoDB; EOG6C8MXH; -. DR BioCyc; TMAR243274:GC6P-91-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 182 AA; 21624 MW; 3CE209C8DB077686 CRC64; MEKLNIYPFK KRKVKLSTFL VLLAVMLLPP VSFNIYFSYA KEQMIERLQS DYSEVLRAYS VKLSKDSSKN LEEISRVESV FMNQIKSLEV RVNQLNAFLD KRKKWEDFVK VLLNIFEDQN RTLCYLDFSQ EKAIVEFYEV SKNVVSSTFQ NSNVSTSLLF EEKLPEGFYL RKYRLEYEAV EK // ID Q9X043_THEMA Unreviewed; 316 AA. AC Q9X043; G4FF44; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36027.1}; GN OrderedLocusNames=TM_0946 {ECO:0000313|EMBL:AAD36027.1}; GN ORFNames=Tmari_0948 {ECO:0000313|EMBL:AGL49873.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36027.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36027.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36027.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49873.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49873.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36027.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49873.1; -; Genomic_DNA. DR PIR; E72313; E72313. DR RefSeq; NP_228754.1; NC_000853.1. DR RefSeq; WP_004080616.1; NZ_CP011107.1. DR STRING; 243274.TM0946; -. DR EnsemblBacteria; AAD36027; AAD36027; TM_0946. DR EnsemblBacteria; AGL49873; AGL49873; Tmari_0948. DR GeneID; 898683; -. DR KEGG; tma:TM0946; -. DR KEGG; tmi:THEMA_09615; -. DR KEGG; tmm:Tmari_0948; -. DR KEGG; tmw:THMA_0969; -. DR PATRIC; 23936823; VBITheMar51294_0960. DR eggNOG; ENOG4108KM5; Bacteria. DR eggNOG; COG5276; LUCA. DR OMA; ANFADNT; -. DR OrthoDB; EOG6X6RBS; -. DR BioCyc; TMAR243274:GC6P-976-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.130.10.10; -; 1. DR InterPro; IPR013211; LVIVD. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR Pfam; PF08309; LVIVD; 5. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 316 AA; 34249 MW; 62D122770A448F35 CRC64; MKAIFPVILA LLFLSGCFQM IPALPQEKVY ALVATGEGLE VFDVTATPVS ISFVSLANSA LDVEVSGQYA FLADGQSGIH VLDVSDPENP VQLNQLNTHY AYGVDLSGDY LYVADWTNGL LVYNVTDPSS PVLVARLEEA DWAEKVHISG NRAYVACYNE GLKVVDVSNP ANPVFLERVN FGTVRSVFVS DERIYAVVYG EGVSIIDAND LSQILGTYES QTPYDVIVSD SVLYLADYAF GVQTIDVSDP GNPFVLDHIP TSGGKAQSLW LYEGFLYIAD FNGYLTVVDV SDPSHMNEVF NVLTQGSANA VSLLVQ // ID Q9X1J6_THEMA Unreviewed; 458 AA. AC Q9X1J6; G4FFP5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=Membrane protein containing HD superfamily hydrolase domain, YQFF like protein {ECO:0000313|EMBL:AGL50440.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36575.1}; GN OrderedLocusNames=TM_1508 {ECO:0000313|EMBL:AAD36575.1}; GN ORFNames=Tmari_1516 {ECO:0000313|EMBL:AGL50440.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36575.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36575.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36575.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50440.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50440.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36575.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50440.1; -; Genomic_DNA. DR PIR; E72244; E72244. DR RefSeq; NP_229308.1; NC_000853.1. DR RefSeq; WP_004081852.1; NZ_CP011107.1. DR STRING; 243274.TM1508; -. DR EnsemblBacteria; AAD36575; AAD36575; TM_1508. DR EnsemblBacteria; AGL50440; AGL50440; Tmari_1516. DR GeneID; 897992; -. DR KEGG; tma:TM1508; -. DR KEGG; tmi:THEMA_06760; -. DR KEGG; tmm:Tmari_1516; -. DR KEGG; tmw:THMA_1540; -. DR PATRIC; 23937974; VBITheMar51294_1525. DR eggNOG; ENOG4105CTJ; Bacteria. DR eggNOG; COG1480; LUCA. DR KO; K07037; -. DR OMA; FTENIRD; -. DR OrthoDB; EOG6VXF6V; -. DR BioCyc; TMAR243274:GC6P-1548-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR006675; HDIG_dom. DR InterPro; IPR011621; Metal-dep_PHydrolase_7TM_intra. DR Pfam; PF07698; 7TM-7TMR_HD; 1. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00277; HDIG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50440.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 127 145 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 175 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 182 205 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 234 389 HDc. {ECO:0000259|SMART:SM00471}. SQ SEQUENCE 458 AA; 52167 MW; B4F2ADBF064D0247 CRC64; MNRKRFLLIT ITVILSLMLV HVRTGIRPLN FTFEALITLI VWFALVEMST RYYRKYWLSE VFTYTHLALI LLGSSFIGFS FPEIGPFVTP VYIPVALIEL VFFSPEIAIT SGFLMSLFAL YRWSYDIFLL LPFISTTFVA AVTLSKANRR LDVVKSSAFT SLALMGTSLF MKFGLKIEYT PYDLVAAILN PIFSGILVLG ILPYVEYTSR LYSNLGLVEF GNLNHPLLKM LSIKAPGTYY HSVIVANLAE TAAEKIGANP ILARIGAYYH DIGKMKRPHF FTENIRDGKN PHEDITPSLS HLVLNEHVKY GVELARKYRL PLLVEFIIPQ HHGTRSQKYF YYKAKQQFED IPEEEFRYPG PKPQFKEAAI IMLADSVEAA SRSLKSPSVS QIKECVEDVI SSIFFERQLD ESGITLSELE EISDAFLQVL VNLFSSRIEY PEEEKIQKVV KINDKNTG // ID Q9X1Z0_THEMA Unreviewed; 323 AA. AC Q9X1Z0; G4FG49; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 86. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36727.1}; GN OrderedLocusNames=TM_1660 {ECO:0000313|EMBL:AAD36727.1}; GN ORFNames=Tmari_1669 {ECO:0000313|EMBL:AGL50593.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36727.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36727.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36727.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50593.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50593.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36727.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50593.1; -; Genomic_DNA. DR PIR; B72224; B72224. DR RefSeq; NP_229460.1; NC_000853.1. DR RefSeq; WP_004082174.1; NZ_CP011107.1. DR STRING; 243274.TM1660; -. DR EnsemblBacteria; AAD36727; AAD36727; TM_1660. DR EnsemblBacteria; AGL50593; AGL50593; Tmari_1669. DR GeneID; 896851; -. DR KEGG; tma:TM1660; -. DR KEGG; tmi:THEMA_05945; -. DR KEGG; tmm:Tmari_1669; -. DR KEGG; tmw:THMA_1701; -. DR PATRIC; 23938294; VBITheMar51294_1679. DR eggNOG; ENOG4106AUG; Bacteria. DR eggNOG; COG0739; LUCA. DR OMA; EFRSTGN; -. DR OrthoDB; EOG6W71XC; -. DR BioCyc; TMAR243274:GC6P-1706-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR016047; Peptidase_M23. DR Pfam; PF01551; Peptidase_M23; 1. DR SUPFAM; SSF51261; SSF51261; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 323 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972328. FT DOMAIN 46 106 Peptidase_M23. FT {ECO:0000259|Pfam:PF01551}. SQ SEQUENCE 323 AA; 37179 MW; CEDEF9D1CCA38253 CRC64; MKRWLLLISL MVFSAVVFSF SAPVDSPRVS ATFGEYRGSG NRGPHFHMGI DFSTGLKEGV PIYASERGWL VRIEIDEDDI YGYTVVLEHE NGYRTLYAHL SRFSKKLETV ASSLKQEFGN VRIVVNFPEK EIWFEKGEVV GYSGTTGEAP IPHAHFEIRD RNEEVSYDPS TFLNLPKPVD EDIVLEKIKI GDSVYDFVEG RTYPFSGNFP DLAIKAYSKG FNNTLGLKKI SLLLEGEEIY QISFDQIPWS EFTNVWGVYD RKSVSAAYRF ELWYKLFPET FSSMIKVNKF PELGKAPDFA KYTVVIEDIW GMKKEFSFYL QRR // ID Q9WYT2_THEMA Unreviewed; 614 AA. AC Q9WYT2; G4FE10; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 88. DE SubName: Full=Dipeptide-binding ABC transporter, periplasmic substrate-binding component {ECO:0000313|EMBL:AGL49382.1}; DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligo-peptide binding protein, putative {ECO:0000313|EMBL:AAD35545.1}; GN OrderedLocusNames=TM_0460 {ECO:0000313|EMBL:AAD35545.1}; GN ORFNames=Tmari_0457 {ECO:0000313|EMBL:AGL49382.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35545.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35545.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35545.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49382.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49382.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35545.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49382.1; -; Genomic_DNA. DR PIR; D72373; D72373. DR RefSeq; NP_228270.1; NC_000853.1. DR RefSeq; WP_004081506.1; NZ_CP011107.1. DR STRING; 243274.TM0460; -. DR EnsemblBacteria; AAD35545; AAD35545; TM_0460. DR EnsemblBacteria; AGL49382; AGL49382; Tmari_0457. DR GeneID; 897491; -. DR KEGG; tma:TM0460; -. DR KEGG; tmi:THEMA_02390; -. DR KEGG; tmm:Tmari_0457; -. DR KEGG; tmw:THMA_0470; -. DR PATRIC; 23935817; VBITheMar51294_0467. DR eggNOG; ENOG4107TCA; Bacteria. DR eggNOG; COG0747; LUCA. DR KO; K02035; -. DR OMA; DKEWCIE; -. DR OrthoDB; EOG6MD90K; -. DR BioCyc; TMAR243274:GC6P-480-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GOC. DR InterPro; IPR023765; SBP_5_CS. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PROSITE; PS01040; SBP_BACTERIAL_5; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 614 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972321. FT DOMAIN 68 518 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. SQ SEQUENCE 614 AA; 70776 MW; 1023EB49E63DB27D CRC64; MKKLFVLFLA VLSVLVLAEV KNPDTIIDAT IGEPDTLDPH FAYDTASGEV IYNVYENLIA YKGESLTEFE PRLAERWEIL DDGKTYKFYI RKGVKFHEGG DLTPEDVEYS FERGLIFDPT AGPMWMLWEA LFGVDSLETF VEEKIGKPYS ELFDENGEPL PEYRDALIKI YTDYIDPAIE VEGDAVVFHL VRPFAPFMYI LAQSASWSAV LDKEWCIEIG CWDGRADTWW KYHDIRKEDS PLYARMNGTG PFKFVEWDRA QQKVILERND NYWREPAKIK RVIIWGIDEW STRRAMFLQG DADICAVPTQ YLEQVEGKPG VTVVKGLPEL AVTSLHFAWN VPEDSKYIGS GKLDGNGIPP DFFSDENVRK AFIYAFDYDT FINEVLKGLG RKIPTDLPEG LLGFNEELLN DPDAPHFDIV KATEYFKKAW NGEVWKKGFK ITLLYNTGNE VRRQAAEMLK AYIEMINPKF KVEVRGVQWP TYLDATKRGE VPAFIIGWLA DYPDPHNFIF TYYHSAGVYS GRQGENFRKF VSTPHPDLGG RSLDELIEEA IAKTDPAERQ ALYEEIQRFA MKHALGMPLY QPLGVRVQRS WVKGWYHNPM RPGDDYYVLW KAEE // ID Q9X182_THEMA Unreviewed; 360 AA. AC Q9X182; G4FF98; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 107. DE SubName: Full=Motility protein PilT {ECO:0000313|EMBL:AAD36432.1}; DE SubName: Full=Twitching motility protein PilT {ECO:0000313|EMBL:AGL50293.1}; GN OrderedLocusNames=TM_1362 {ECO:0000313|EMBL:AAD36432.1}; GN ORFNames=Tmari_1369 {ECO:0000313|EMBL:AGL50293.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36432.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36432.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36432.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50293.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50293.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36432.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50293.1; -; Genomic_DNA. DR PIR; C72263; C72263. DR RefSeq; NP_229163.1; NC_000853.1. DR RefSeq; WP_004081558.1; NZ_CP011107.1. DR STRING; 243274.TM1362; -. DR EnsemblBacteria; AAD36432; AAD36432; TM_1362. DR EnsemblBacteria; AGL50293; AGL50293; Tmari_1369. DR GeneID; 898118; -. DR KEGG; tma:TM1362; -. DR KEGG; tmm:Tmari_1369; -. DR KEGG; tmw:THMA_1387; -. DR PATRIC; 23937662; VBITheMar51294_1374. DR eggNOG; ENOG4105CZX; Bacteria. DR eggNOG; COG2805; LUCA. DR KO; K02669; -. DR OMA; PIEYVFP; -. DR OrthoDB; EOG6JMMWM; -. DR BioCyc; TMAR243274:GC6P-1395-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006321; PilT. DR InterPro; IPR001482; T2SS_protein-E. DR Pfam; PF00437; T2SSE; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01420; pilT_fam; 1. DR PROSITE; PS00662; T2SP_E; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 199 213 T2SP_E. {ECO:0000259|PROSITE:PS00662}. SQ SEQUENCE 360 AA; 40203 MW; 78DCFEEBED058377 CRC64; MEDMKVSFLK IITEAYGLRA TDVHISVGCP PYYRIDGDLV PQEKYGKLTK ESIMNALKDL FTEIGQPFPP KTKEVDFSFT VAEAIRVRGN LYYERKNPAL AFRLIPKKIR TFQELGLPEI LKTFVERKYG LILVAGPTGS GKSTTLAAMI DHINENFPHH IITIEDPIEY VFTNKKSVIH QRELGSDTDS FYNGLKYALR QDPDVILVGE MRDLETMALA LTAAETGHLV LATVHTNSAA SAPERIIDVF PAHQQRQIAL QLANTLIAVI YQRLVPKANG IGFTPILEIM VGTPAVRNLI RENKLHQLES LIQAGARHGM VLFDDALVKA ALKGEISRES ALQFARNQEE VARRLGMKPS // ID Q9WXU5_THEMA Unreviewed; 138 AA. AC Q9WXU5; G4FH05; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35184.1}; GN OrderedLocusNames=TM_0090 {ECO:0000313|EMBL:AAD35184.1}; GN ORFNames=Tmari_0087 {ECO:0000313|EMBL:AGL49013.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35184.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35184.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35184.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49013.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49013.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35184.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49013.1; -; Genomic_DNA. DR PIR; D72420; D72420. DR RefSeq; NP_227906.1; NC_000853.1. DR RefSeq; WP_004082622.1; NZ_CP011107.1. DR STRING; 243274.TM0090; -. DR EnsemblBacteria; AAD35184; AAD35184; TM_0090. DR EnsemblBacteria; AGL49013; AGL49013; Tmari_0087. DR GeneID; 896917; -. DR KEGG; tma:TM0090; -. DR KEGG; tmi:THEMA_04355; -. DR KEGG; tmm:Tmari_0087; -. DR KEGG; tmw:THMA_0086; -. DR PATRIC; 23935020; VBITheMar51294_0088. DR OMA; APAYRIF; -. DR OrthoDB; EOG6SFPCQ; -. DR BioCyc; TMAR243274:GC6P-90-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 138 AA; 16193 MW; 4497C52848ED3522 CRC64; MRGINRKFAI WFAVLTLLVL VFGFVVPDFV IFMFNTKELE QRLQNLAPAF KVFTLKQREY EEIIKTIMNT PEFQYNFTEK EISVEEVEDL LKELAETRRV TVKTLTIDAK RVIPINFFGT SISQPSVKIS LELERVKQ // ID Q9WZ94_THEMA Unreviewed; 381 AA. AC Q9WZ94; G4FDJ7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35710.1}; GN OrderedLocusNames=TM_0626 {ECO:0000313|EMBL:AAD35710.1}; GN ORFNames=Tmari_0627 {ECO:0000313|EMBL:AGL49552.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35710.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35710.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35710.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49552.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49552.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35710.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49552.1; -; Genomic_DNA. DR PIR; G72352; G72352. DR RefSeq; NP_228435.1; NC_000853.1. DR RefSeq; WP_004081181.1; NZ_CP011107.1. DR STRING; 243274.TM0626; -. DR EnsemblBacteria; AAD35710; AAD35710; TM_0626. DR EnsemblBacteria; AGL49552; AGL49552; Tmari_0627. DR GeneID; 897713; -. DR KEGG; tma:TM0626; -. DR KEGG; tmi:THEMA_01530; -. DR KEGG; tmm:Tmari_0627; -. DR KEGG; tmw:THMA_0642; -. DR PATRIC; 23936165; VBITheMar51294_0636. DR eggNOG; ENOG4108NH1; Bacteria. DR eggNOG; ENOG41105EQ; LUCA. DR OrthoDB; EOG6SFP6H; -. DR BioCyc; TMAR243274:GC6P-651-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR024873; E-NPP. DR InterPro; IPR002591; Phosphodiest/P_Trfase. DR PANTHER; PTHR10151; PTHR10151; 1. DR Pfam; PF01663; Phosphodiest; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 381 AA; 45195 MW; 67A429697E100621 CRC64; MNNKGKLAIL FIDALPYFKS RNIGQILNLY RLIPGLGYSV NQHYELLYGK TPDDVGFFGE WSLGCSTKFD TIKFRFHKTI DSILWKLKLN LIRKGYRKII LRLEDMIPLG RRKYFLRKGT YAFRELAKEG FILYNTQFRG YIEELDRTLP RNEEKRMETM FNKMFNIAKN TDHPLLFTIN IIDHIGHKYG PESPEYDYFL DLFAKKLLDL LIFLKENGFH VILFSDHGMS PYKAKVNLSD FEHYFGKFFG KYIVYFYDSL YFRAWIFDSF LYLEIEEFLN KLPGKILSSN DRKKFGVVHE EHGHVIFVLN EGFTFHPNYF GYSVMKGYHG YLPEFERQHG IAAFSRAFKI DNLFQGNPPK YLNSIDFSRI IKHILEANRN V // ID Q9WXN0_THEMA Unreviewed; 656 AA. AC Q9WXN0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AAD35117.1}; DE SubName: Full=Methyl-accepting chemotaxis sensory transducer {ECO:0000313|EMBL:AGL48946.1}; GN OrderedLocusNames=TM_0023 {ECO:0000313|EMBL:AAD35117.1}; GN ORFNames=Tmari_0020 {ECO:0000313|EMBL:AGL48946.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35117.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35117.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35117.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48946.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48946.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35117.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48946.1; -; Genomic_DNA. DR PIR; A72428; A72428. DR RefSeq; NP_227839.1; NC_000853.1. DR RefSeq; WP_010865030.1; NZ_CP011107.1. DR STRING; 243274.TM0023; -. DR EnsemblBacteria; AAD35117; AAD35117; TM_0023. DR EnsemblBacteria; AGL48946; AGL48946; Tmari_0020. DR GeneID; 896838; -. DR KEGG; tma:TM0023; -. DR KEGG; tmi:THEMA_04685; -. DR KEGG; tmm:Tmari_0020; -. DR KEGG; tmw:THMA_0019; -. DR PATRIC; 23934886; VBITheMar51294_0021. DR eggNOG; ENOG4105C8Q; Bacteria. DR eggNOG; COG0840; LUCA. DR KO; K03406; -. DR OMA; ENRTHIQ; -. DR OrthoDB; EOG6CK7NC; -. DR BioCyc; TMAR243274:GC6P-23-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR004089; MCPsignal_dom. DR Pfam; PF00015; MCPsignal; 1. DR SMART; SM00304; HAMP; 1. DR SMART; SM00283; MA; 1. DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1. DR PROSITE; PS50885; HAMP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 280 302 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 299 351 HAMP. {ECO:0000259|PROSITE:PS50885}. FT DOMAIN 370 606 Methyl-accepting transducer. FT {ECO:0000259|PROSITE:PS50111}. SQ SEQUENCE 656 AA; 72043 MW; 1334C37B2B5FCD98 CRC64; MNIRFRIIFI MVVILVSFVL SAYLVQRSTS SLLISNAKDY MEKSVSSLSK YISQKLNEVQ RNLKTLLGSS LIGGYTIASN LQSVLQGATD TVSVGIVVDE MSESAYLVLP EKIEEKNYSE YEKYLSLMKE KNKTSLVLAE SIDGKPVLLF VEGVTTFGSE PSGLIALGIS LSENTDLWKA VVEEGKASKS GYGLLVTSDG KVLIHKDMGN FMKDVKELGG FEKAFEEAKS GGEKYVEYEY NGEKKYTVWE KVPGYDFYIF STGYLDELLA EGRKATFGTI VTYVVFGGVI FAVLFVSMMP VVKRMRQQVE KVKRFGEGDL TVEFEAKGKD ELTQIEESLK EAVLSLKEMI VSIIEASKEL SGASEEIKVL SEESHKMSEN LHEEAKKILD EANNMSSALT EVTSGVEEVA ASAQNISKIT QDLTERSEAV TKAAREGTER VEAVGGVINK LKGSAERQRD YLRELVDSAK TIGEIVDTIS SIAEQTNLLA LNAAIEAARA GEAGRGFAVV ADEIRKLAEE SQRATEDIAK MLSSLRATIE HVENGSKEMF EGVDEIAVMG EEVTKRFREI LGRIEEINSM IENTAATAQE QGAAAEEMAS AMDNVTKIVE GVVESLNRME SLIEDQTESA ARVSEAAERL SELSEQLSTL VQKFKV // ID Q9X101_THEMA Unreviewed; 245 AA. AC Q9X101; G4FE74; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36349.1}; GN OrderedLocusNames=TM_1274 {ECO:0000313|EMBL:AAD36349.1}; GN ORFNames=Tmari_1279 {ECO:0000313|EMBL:AGL50203.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36349.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36349.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36349.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50203.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50203.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36349.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50203.1; -; Genomic_DNA. DR PIR; A72275; A72275. DR RefSeq; NP_229079.1; NC_000853.1. DR RefSeq; WP_004079962.1; NZ_CP011107.1. DR STRING; 243274.TM1274; -. DR EnsemblBacteria; AAD36349; AAD36349; TM_1274. DR EnsemblBacteria; AGL50203; AGL50203; Tmari_1279. DR GeneID; 898209; -. DR KEGG; tma:TM1274; -. DR KEGG; tmi:THEMA_07965; -. DR KEGG; tmm:Tmari_1279; -. DR KEGG; tmw:THMA_1299; -. DR PATRIC; 23937486; VBITheMar51294_1289. DR OMA; KSEANFQ; -. DR OrthoDB; EOG6Q2SJ4; -. DR BioCyc; TMAR243274:GC6P-1305-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 245 AA; 27083 MW; E989E0BB3089091B CRC64; MKKFLPLLFI FVVGGVVLPA SFIWTSDGYH VKFGDTLFFE AFNDGWGVGV SLSKSATNYQ KLGFLKVKTS EVTLKTGLSF GNGWNVFFCV DQRDVIPFPG SLYYEFFIGR SGGYAILKQD YIVKIGGYRL SLDNFAYMSR DTVMFHSGQF SMGGTSFAYR ALNNTVLFGI SDPDNVLFLG AGLLNWKLAG GTGFNFTLTN GVDVKLLVSA AVDEVSFGFM ARAKKGNTDL TFVLNTNEFY FSVKF // ID Q9WYF9_THEMA Unreviewed; 427 AA. AC Q9WYF9; G4FHN7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35411.1}; GN OrderedLocusNames=TM_0324 {ECO:0000313|EMBL:AAD35411.1}; GN ORFNames=Tmari_0322 {ECO:0000313|EMBL:AGL49247.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35411.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35411.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35411.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49247.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49247.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35411.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49247.1; -; Genomic_DNA. DR PIR; F72389; F72389. DR RefSeq; NP_228135.1; NC_000853.1. DR RefSeq; WP_004083077.1; NZ_CP011107.1. DR STRING; 243274.TM0324; -. DR EnsemblBacteria; AAD35411; AAD35411; TM_0324. DR EnsemblBacteria; AGL49247; AGL49247; Tmari_0322. DR GeneID; 897269; -. DR KEGG; tma:TM0324; -. DR KEGG; tmi:THEMA_03105; -. DR KEGG; tmm:Tmari_0322; -. DR KEGG; tmw:THMA_0331; -. DR PATRIC; 23935527; VBITheMar51294_0329. DR eggNOG; ENOG4105CG6; Bacteria. DR eggNOG; COG1593; LUCA. DR OMA; PSSVIMI; -. DR OrthoDB; EOG64V29B; -. DR BioCyc; TMAR243274:GC6P-337-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010656; DctM. DR InterPro; IPR004681; TRAP_transpt_permease. DR Pfam; PF06808; DctM; 1. DR PIRSF; PIRSF006066; HI0050; 1. DR TIGRFAMs; TIGR00786; dctM; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 45 67 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 133 157 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 169 191 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 212 234 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 240 256 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 276 295 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 315 344 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 400 426 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 5 417 DctM. {ECO:0000259|Pfam:PF06808}. SQ SEQUENCE 427 AA; 46409 MW; 989276D37184FCFE CRC64; MIIVLIAFAV FLMLGMPVAF AIGISGFLWF LQHPELPITI PIQRLLSQTV NFTLLAIPMF IVAGNVMNSA GVTRRLLDFA STLVGHMRGG LGQVSAVLST LMGGVSGSSI ADAAMETRML GPEMLKRGYP RGFAVAVNVW TSLITPIIPP GIAFIIYGTI GQVSIGRLFA AGIGPGLLLM IVYMITIWFV AKRLNLAPER ERRAPVNEVF RSLGKSIWAL MFPVLLIVGL RGGIFTPSEV GSFAVLYGML VGFIIHREMS LKTFYWETLE NSLGDIGSVM FILSMSTIFG YGMIWERIPE KLAEFLLGIS SNPNVLMIMI SLFLVFAGLF VDATALILML TAILLPVAEQ VGIDPVHFGL VFILSAAMGN QTPPVGASMY AGCSVLDATM EEYIQASWPF LFVTILAILI VIFFPQIVLF IPNLIFG // ID Q9WZN4_THEMA Unreviewed; 402 AA. AC Q9WZN4; G4FD47; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Transposase, putative {ECO:0000313|EMBL:AAD35858.1}; GN OrderedLocusNames=TM_0776 {ECO:0000313|EMBL:AAD35858.1}; GN ORFNames=Tmari_0777 {ECO:0000313|EMBL:AGL49702.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35858.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35858.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35858.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49702.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49702.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35858.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49702.1; -; Genomic_DNA. DR PIR; A72332; A72332. DR RefSeq; NP_228585.1; NC_000853.1. DR RefSeq; WP_004080912.1; NZ_CP011107.1. DR STRING; 243274.TM0776; -. DR EnsemblBacteria; AAD35858; AAD35858; TM_0776. DR EnsemblBacteria; AGL49702; AGL49702; Tmari_0777. DR GeneID; 898444; -. DR KEGG; tma:TM0776; -. DR KEGG; tmi:THEMA_00770; -. DR KEGG; tmm:Tmari_0777; -. DR KEGG; tmw:THMA_0795; -. DR PATRIC; 23936474; VBITheMar51294_0789. DR eggNOG; ENOG4108K3X; Bacteria. DR eggNOG; COG0675; LUCA. DR KO; K07496; -. DR OMA; HSREVWE; -. DR OrthoDB; EOG6DRPD6; -. DR BioCyc; TMAR243274:GC6P-803-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR024064; FdhE-like. DR InterPro; IPR001959; Transposase_2. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR Pfam; PF01385; OrfB_IS605; 1. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR SUPFAM; SSF144020; SSF144020; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 164 281 OrfB_IS605. {ECO:0000259|Pfam:PF01385}. FT DOMAIN 300 366 OrfB_Zn_ribbon. FT {ECO:0000259|Pfam:PF07282}. SQ SEQUENCE 402 AA; 46033 MW; 0D4696396BED1B48 CRC64; MSRRVIRTYK LAVPGHLSQT CEELNRTAAR IYNKTMSLVR KIHQKKGFWL SWPTADKYIL RWAENIKIHV HSKQAFVQLY FQALKGYFKA TKKNPDAKPP HKKKRYLPFI WKESAVKLLP DGTLRLSLGK ERESFVVQTP LKPPLRIKQT RLVFEDGYYL HLAIEVEIEE KNAGSGVMAV DLGVLRPITC FDGKEVISYH GGVLSSVLRY RNKRLASFQS AIAECKKGSR RYNKLVRAKK RVLRRLRNQI NDIMHKITSN FIGLCLRKQI GTIVIGDVTG IRERADYSDN ANQKIHQWQF RKLIEMIRYK AEQFGIEVKL ISEANTSKTC PVCGAKNNPN GRRYHCKACG FEYHRDGVGA INIWKRYPGT GQVVAGLAPV RGVRFHPHLC GHGASLAPWK VA // ID Q9X066_THEMA Unreviewed; 30 AA. AC Q9X066; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36050.1}; GN OrderedLocusNames=TM_0971 {ECO:0000313|EMBL:AAD36050.1}; GN ORFNames=Tmari_0974 {ECO:0000313|EMBL:AGL49899.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36050.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36050.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36050.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49899.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49899.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36050.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49899.1; -; Genomic_DNA. DR PIR; H72312; H72312. DR RefSeq; NP_228779.1; NC_000853.1. DR RefSeq; WP_010865228.1; NZ_CP011107.1. DR STRING; 243274.TM0971; -. DR EnsemblBacteria; AAD36050; AAD36050; TM_0971. DR EnsemblBacteria; AGL49899; AGL49899; Tmari_0974. DR GeneID; 898717; -. DR KEGG; tma:TM0971; -. DR KEGG; tmm:Tmari_0974; -. DR KEGG; tmw:THMA_0994; -. DR BioCyc; TMAR243274:GC6P-1001-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 30 AA; 3571 MW; 3BDDEFA3B86035A7 CRC64; MGMLIDRERE CEFLRRKISS NKSELLIISC // ID Q9WYI9_THEMA Unreviewed; 420 AA. AC Q9WYI9; G4FHR6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35441.1}; GN OrderedLocusNames=TM_0354 {ECO:0000313|EMBL:AAD35441.1}; GN ORFNames=Tmari_0352 {ECO:0000313|EMBL:AGL49277.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35441.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35441.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35441.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49277.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49277.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35441.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49277.1; -; Genomic_DNA. DR PIR; B72386; B72386. DR RefSeq; NP_228165.1; NC_000853.1. DR RefSeq; WP_004083147.1; NZ_CP011107.1. DR STRING; 243274.TM0354; -. DR DNASU; 897310; -. DR EnsemblBacteria; AAD35441; AAD35441; TM_0354. DR EnsemblBacteria; AGL49277; AGL49277; Tmari_0352. DR GeneID; 897310; -. DR KEGG; tma:TM0354; -. DR KEGG; tmi:THEMA_02945; -. DR KEGG; tmm:Tmari_0352; -. DR KEGG; tmw:THMA_0362; -. DR PATRIC; 23935589; VBITheMar51294_0359. DR eggNOG; ENOG410642D; Bacteria. DR eggNOG; ENOG4112CJF; LUCA. DR OMA; ACLERIT; -. DR OrthoDB; EOG6CK7J6; -. DR BioCyc; TMAR243274:GC6P-368-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR003423; OMP_efflux. DR Pfam; PF02321; OEP; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 322 363 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 49103 MW; 3C103768CE44848C CRC64; MKRFFLVFLL VPVFLAGNVF DLFKENLENS YSYWSSVEKF KEAQLNYKRY TNFWNPEISV SLGKTGITIT EDGVSDFSIS PIVNFVNIYG FELGLSFPIS VNTDDWSFNF EGTQLSVSRG LKTEYTVDRL MAESSYLSSK YSLKSTKNSV FIQTVQDIFD WYYYTKKIEI LSQRLQVLNE KLSKAKDDDE KKALEKQILS TEQTLRNAEY KLQTIQTKNI DEEVYQKTRN LLESITLPAT TLEYREDLKA LELQKKAEEI EKKTWFLPYL PDLTVSFNYD FEDSEWSIGI GFQMTLWDFG ERKLEAEKRK SQLVSLEYQE EVKNIENSLN QELVNIANLE SQLKQKEIEL EDLEESSKTS DQLFNKGFLS EEDYALSKLD YAEGTLEKEN MENSLILEKL KYISILGYDL EKFLKEGDQN // ID Q9X128_THEMA Unreviewed; 258 AA. AC Q9X128; G4FE47; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 109. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36376.1}; GN OrderedLocusNames=TM_1302 {ECO:0000313|EMBL:AAD36376.1}; GN ORFNames=Tmari_1309 {ECO:0000313|EMBL:AGL50233.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36376.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36376.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36376.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50233.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50233.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36376.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50233.1; -; Genomic_DNA. DR PIR; H72269; H72269. DR RefSeq; NP_229106.1; NC_000853.1. DR RefSeq; WP_004079917.1; NZ_CP011107.1. DR STRING; 243274.TM1302; -. DR EnsemblBacteria; AAD36376; AAD36376; TM_1302. DR EnsemblBacteria; AGL50233; AGL50233; Tmari_1309. DR GeneID; 898180; -. DR KEGG; tma:TM1302; -. DR KEGG; tmm:Tmari_1309; -. DR KEGG; tmw:THMA_1327; -. DR PATRIC; 23937544; VBITheMar51294_1318. DR eggNOG; ENOG4105CJ1; Bacteria. DR eggNOG; COG1131; LUCA. DR KO; K01990; -. DR OMA; GPEIVFA; -. DR OrthoDB; EOG65J54C; -. DR BioCyc; TMAR243274:GC6P-1333-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD36376.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD36376.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 235 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 258 AA; 29570 MW; ABDA55515DF1D407 CRC64; MRKVVEVSGV RKSFGELRVL DKVDFYAEEG DFKVIVGENG SGKSTLLKIM IGLLLPDDGE VKVLGVDVKK HWKKLSARIG VVLANERSLY WKLTAWENLD IFGGVYGVPK KVRRERMEEL LKRFGLFEYK DKPVEEFSTG MRKKLMICKA LIHDPEVLFI DEILNGLDPP SVREMVGFLD ERNRRGLTIV MISHVLHVLP ENACVVLLRN GRVQMEVRYK DIRSERSEVY EVFENLIRGR NMDEEDTPSG SEGDEDKA // ID Q9X0A7_THEMA Unreviewed; 590 AA. AC Q9X0A7; G4FEY3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36091.1}; GN OrderedLocusNames=TM_1014 {ECO:0000313|EMBL:AAD36091.1}; GN ORFNames=Tmari_1017 {ECO:0000313|EMBL:AGL49941.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36091.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36091.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36091.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49941.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49941.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36091.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49941.1; -; Genomic_DNA. DR PIR; F72305; F72305. DR RefSeq; NP_228820.1; NC_000853.1. DR RefSeq; WP_004080521.1; NZ_CP011107.1. DR STRING; 243274.TM1014; -. DR EnsemblBacteria; AAD36091; AAD36091; TM_1014. DR EnsemblBacteria; AGL49941; AGL49941; Tmari_1017. DR GeneID; 898617; -. DR KEGG; tma:TM1014; -. DR KEGG; tmi:THEMA_09285; -. DR KEGG; tmm:Tmari_1017; -. DR KEGG; tmw:THMA_1036; -. DR PATRIC; 23936957; VBITheMar51294_1027. DR eggNOG; ENOG41068NV; Bacteria. DR eggNOG; COG1542; LUCA. DR KO; K09010; -. DR OMA; WHLELAG; -. DR OrthoDB; EOG6K3ZWK; -. DR BioCyc; TMAR243274:GC6P-1043-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR007548; DUF505. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04458; DUF505; 2. DR PIRSF; PIRSF029056; DUF505; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 590 AA; 67283 MW; EE5B0814A100FFBF CRC64; MIVTKRHAIV LKKLYEKGEE FSVKEWEDFD RETLWHLELA GLVKPVGVEM YDLTFSGNIL GELLTDMIRE GVLKNPEEWD DSFRWIGSEV ISMIRYSKLA QSRVRGEVAK ALEERGFAKE GNLTPYAYTL DEIYHASHPR LVVNLKVAEY LRKMVEGPGE SSTLPVGGDE LLQLEAMRMI AFSVPRSDVY ALTGLGQQIR AALRKGLVVT DELILDELIL DTVAKAYEGN QLSDFERNAL LERGLIDWTG ELHPMAEHLY LAWKIYKKGP YLMTPAFQIS EDEARLLEVI VKLWKRHEKE DDVFPEPKQI EKAVDWEWKR KDLTVKLALY NLEGFGLLKS REHKHGARRT LVYELTSYGE EVLEDQRKSL RSVTAVGVKS ITMTKKEFAA PNMEWYEQAR KEGLVSDAAP TSSGRLYARL SVEAERRPLI TNTEMKVLRK VPYKAGVFIE DMNLSEEERI ALDSLEAKNL VEILPTDVVT LTEAGQLMKR ALSAVSDDVE APVTPLVIRL LQAIRTHGGL QMREKRIRIN PESWKVVERE LGVDPETFDD TVNLARISKF ITENALTEAG VALLQAVDEL ARKEYPWVEV // ID Q9X048_THEMA Unreviewed; 471 AA. AC Q9X048; G4FF39; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36032.1}; GN OrderedLocusNames=TM_0951 {ECO:0000313|EMBL:AAD36032.1}; GN ORFNames=Tmari_0953 {ECO:0000313|EMBL:AGL49878.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36032.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36032.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36032.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49878.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49878.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36032.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49878.1; -; Genomic_DNA. DR PIR; B72314; B72314. DR RefSeq; NP_228759.1; NC_000853.1. DR RefSeq; WP_004080611.1; NZ_CP011107.1. DR STRING; 243274.TM0951; -. DR DNASU; 898688; -. DR EnsemblBacteria; AAD36032; AAD36032; TM_0951. DR EnsemblBacteria; AGL49878; AGL49878; Tmari_0953. DR GeneID; 898688; -. DR KEGG; tma:TM0951; -. DR KEGG; tmi:THEMA_09590; -. DR KEGG; tmm:Tmari_0953; -. DR KEGG; tmw:THMA_0974; -. DR PATRIC; 23936833; VBITheMar51294_0965. DR eggNOG; ENOG4105E13; Bacteria. DR eggNOG; COG2407; LUCA. DR OMA; GFNTVRY; -. DR OrthoDB; EOG64N9SK; -. DR BioCyc; TMAR243274:GC6P-981-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0008733; F:L-arabinose isomerase activity; IEA:InterPro. DR GO; GO:0008736; F:L-fucose isomerase activity; IEA:InterPro. DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro. DR InterPro; IPR015888; Fuc_isomerase_C. DR InterPro; IPR009015; Fucose_isomerase_N/cen. DR InterPro; IPR003762; Lara_isomerase. DR Pfam; PF02952; Fucose_iso_C; 1. DR ProDom; PD018364; Lara_isomerase; 1. DR SUPFAM; SSF53743; SSF53743; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 338 465 Fucose_iso_C. {ECO:0000259|Pfam:PF02952}. SQ SEQUENCE 471 AA; 52780 MW; 1295ECCE915B6634 CRC64; MEKMTFGLIV GNREFFPDRL VEEGRERVIK VLEGMGYRVV TLSPSDTKLG AVETAKDAKK CAELFKEKAG EIDGIIVTLP NFGDEKGVAQ AIRLSGLNVP VLVHAFPDDP EKLDLQNRRD SFCGKISVSN NLKQYGIEFS LTTLHTEDPE SEVFKRDIEK FAAVCRIVKG MRNIKVGAIG ARPSAFNTVR FSEKILERMS ISVETVDLSE ILHRVSNLKD DDERVRRKLE EIKKNYRLQI VPEEKILLMA KFGSVIDEWI EENDIKALAI QCWTSLEWNL GITPCTIMSL LNEKGKPAAC EVDITGALSM YVLQLASGQP SAIVDWNNNY RDENETILFH CGNFPASIYE EKPEIKYADV IGTTVGKERA YGACAGKIKT SPFTFLRLTT DDNEGKVKAY VGEGQILDEN PKTFGSRGVA RIEKLQELMK YICENGFEHH VAINLSRVAD AVKEALEKYL GIVVHKHNAE V // ID Q9WZA0_THEMA Unreviewed; 408 AA. AC Q9WZA0; G4FDJ1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Bacterial sugar transferase {ECO:0000313|EMBL:AGL49558.1}; DE SubName: Full=Extracellular polysaccharide biosynthesis-related protein {ECO:0000313|EMBL:AAD35716.1}; GN OrderedLocusNames=TM_0632 {ECO:0000313|EMBL:AAD35716.1}; GN ORFNames=Tmari_0633 {ECO:0000313|EMBL:AGL49558.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35716.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35716.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35716.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49558.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49558.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35716.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49558.1; -; Genomic_DNA. DR PIR; E72353; E72353. DR RefSeq; NP_228441.1; NC_000853.1. DR RefSeq; WP_004081168.1; NZ_CP011107.1. DR STRING; 243274.TM0632; -. DR DNASU; 897728; -. DR EnsemblBacteria; AAD35716; AAD35716; TM_0632. DR EnsemblBacteria; AGL49558; AGL49558; Tmari_0633. DR GeneID; 897728; -. DR KEGG; tma:TM0632; -. DR KEGG; tmi:THEMA_01500; -. DR KEGG; tmm:Tmari_0633; -. DR KEGG; tmw:THMA_0648; -. DR PATRIC; 23936177; VBITheMar51294_0642. DR eggNOG; ENOG4105D3Q; Bacteria. DR eggNOG; COG2148; LUCA. DR OMA; NRNIFLD; -. DR OrthoDB; EOG6RNQJ6; -. DR BioCyc; TMAR243274:GC6P-657-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR InterPro; IPR003362; Bact_transf. DR InterPro; IPR017475; EPS_sugar_tfrase. DR Pfam; PF02397; Bac_transf; 1. DR TIGRFAMs; TIGR03025; EPS_sugtrans; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49558.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 42 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 221 402 Bac_transf. {ECO:0000259|Pfam:PF02397}. SQ SEQUENCE 408 AA; 48097 MW; 18C49E65B287FC5A CRC64; MYQLIVFDLV VLSALNLPFF NWYVGILFSL CMTLSFFAFR LYDLENVQNY NEQIIRTTVG TLFSFILILF FYPLFEKDIT RYNFFYNFLV SVVLIPPLNT LLGKLLIKNQ PTKTFLVVGR KEEIEPILKE IEEKTTGKYR FAEYINPTVE VLKRKLVHYD GVLLADPEFE DVLKKVNIER VEYLPNLVEK TLKRIPMKVL EKFREYYEVC FSAVNDDSPA KRILDIAVSL IALAVFSPIM LVVGIIIYLE DGRPVVFRQK RVGKDGKTFT MLKLRSMRKK QEKTPKFADQ EKDRILKIGR IIRPFRIDEA LQFVNVLKGE MSVVGPRPEQ EEFVKIFEKQ IPFYSLRHRV KPGITGWAQL MYKYSSNLEE VKKKLSYDLW YVKNRNIFLD LRIILQTLEA VLWRRGAK // ID Q9WXV1_THEMA Unreviewed; 306 AA. AC Q9WXV1; G4FH11; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 109. DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621}; DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621}; GN OrderedLocusNames=TM_0096 {ECO:0000313|EMBL:AAD35190.1}; GN ORFNames=Tmari_0093 {ECO:0000313|EMBL:AGL49019.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35190.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35190.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35190.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49019.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49019.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a CC modified base found in the D-loop of most tRNAs, via the reduction CC of the C5-C6 double bond in target uridines. CC {ECO:0000256|PIRNR:PIRNR006621}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|PIRNR:PIRNR006621}; CC -!- SIMILARITY: Belongs to the dus family. CC {ECO:0000256|PIRNR:PIRNR006621}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35190.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49019.1; -; Genomic_DNA. DR PIR; H72417; H72417. DR RefSeq; NP_227912.1; NC_000853.1. DR RefSeq; WP_004082642.1; NZ_CP011107.1. DR PDB; 1VHN; X-ray; 1.59 A; A=2-306. DR PDBsum; 1VHN; -. DR STRING; 243274.TM0096; -. DR EnsemblBacteria; AAD35190; AAD35190; TM_0096. DR EnsemblBacteria; AGL49019; AGL49019; Tmari_0093. DR GeneID; 896923; -. DR KEGG; tma:TM0096; -. DR KEGG; tmi:THEMA_04325; -. DR KEGG; tmm:Tmari_0093; -. DR KEGG; tmw:THMA_0092; -. DR PATRIC; 23935032; VBITheMar51294_0094. DR eggNOG; ENOG4105CEH; Bacteria. DR eggNOG; COG0042; LUCA. DR OMA; PVGIQIF; -. DR OrthoDB; EOG6VHZFQ; -. DR BioCyc; TMAR243274:GC6P-96-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central. DR GO; GO:0002943; P:tRNA dihydrouridine synthesis; IBA:GOC. DR Gene3D; 1.10.1200.80; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C. DR InterPro; IPR004652; tRNA_dU_NifR3. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PIRSF; PIRSF006621; Dus; 1. DR TIGRFAMs; TIGR00737; nifR3_yhdG; 1. DR PROSITE; PS01136; UPF0034; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VHN}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flavoprotein {ECO:0000213|PDB:1VHN, ECO:0000256|PIRNR:PIRNR006621}; KW FMN {ECO:0000213|PDB:1VHN, ECO:0000256|PIRNR:PIRNR006621}; KW Nucleotide-binding {ECO:0000213|PDB:1VHN}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621, KW ECO:0000313|EMBL:AGL49019.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}. FT NP_BIND 9 11 FMN. {ECO:0000213|PDB:1VHN}. FT NP_BIND 187 190 FMN. {ECO:0000213|PDB:1VHN}. FT ACT_SITE 91 91 Proton donor. FT {ECO:0000256|PIRSR:PIRSR006621-1}. FT BINDING 34 34 FMN; via amide nitrogen. FT {ECO:0000213|PDB:1VHN}. FT BINDING 62 62 FMN. {ECO:0000213|PDB:1VHN}. FT BINDING 88 88 FMN. {ECO:0000213|PDB:1VHN}. FT BINDING 130 130 FMN. {ECO:0000213|PDB:1VHN}. FT BINDING 158 158 FMN. {ECO:0000213|PDB:1VHN}. FT BINDING 212 212 FMN. {ECO:0000213|PDB:1VHN}. SQ SEQUENCE 306 AA; 35150 MW; 3BFB466F2E802859 CRC64; MEVKVGLAPM AGYTDSAFRT LAFEWGADFA FSEMVSAKGF LMNSQKTEEL LPQPHERNVA VQIFGSEPNE LSEAARILSE KYKWIDLNAG CPVRKVVKKG AGGALLKDLR HFRYIVRELR KSVSGKFSVK TRLGWEKNEV EEIYRILVEE GVDEVFIHTR TVVQSFTGRA EWKALSVLEK RIPTFVSGDI FTPEDAKRAL EESGCDGLLV ARGAIGRPWI FKQIKDFLRS GKYSEPSREE ILRTFERHLE LLIKTKGERK AVVEMRKFLA GYTKDLKGAR RFREKVMKIE EVQILKEMFY NFIKEV // ID Q9WZQ3_THEMA Unreviewed; 338 AA. AC Q9WZQ3; G4FD28; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35878.1}; GN OrderedLocusNames=TM_0796 {ECO:0000313|EMBL:AAD35878.1}; GN ORFNames=Tmari_0797 {ECO:0000313|EMBL:AGL49722.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35878.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35878.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35878.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49722.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49722.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35878.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49722.1; -; Genomic_DNA. DR PIR; E72334; E72334. DR RefSeq; NP_228605.1; NC_000853.1. DR RefSeq; WP_004080873.1; NZ_CP011107.1. DR PDB; 2G0T; X-ray; 2.67 A; A/B=1-338. DR PDBsum; 2G0T; -. DR STRING; 243274.TM0796; -. DR EnsemblBacteria; AAD35878; AAD35878; TM_0796. DR EnsemblBacteria; AGL49722; AGL49722; Tmari_0797. DR GeneID; 898464; -. DR KEGG; tma:TM0796; -. DR KEGG; tmi:THEMA_00670; -. DR KEGG; tmm:Tmari_0797; -. DR KEGG; tmw:THMA_0815; -. DR PATRIC; 23936512; VBITheMar51294_0808. DR eggNOG; ENOG4105ESD; Bacteria. DR eggNOG; COG3367; LUCA. DR OMA; DAGWVAT; -. DR OrthoDB; EOG6X10V0; -. DR BioCyc; TMAR243274:GC6P-823-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR011669; DUF1611. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF07755; DUF1611; 1. DR PIRSF; PIRSF026760; UCP026760; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2G0T}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT REGION 168 172 Phosphate binding. FT {ECO:0000213|PDB:2G0T}. SQ SEQUENCE 338 AA; 36982 MW; 552DF453C9CF61B9 CRC64; MDLWKLYQPG TPAAIVAWGQ LGTAHAKTTY GLLRHSRLFK PVCVVAEHEG KMASDFVKPV RYDVPVVSSV EKAKEMGAEV LIIGVSNPGG YLEEQIATLV KKALSLGMDV ISGLHFKISQ QTEFLKIAHE NGTRIIDIRI PPLELDVLRG GIYRKKIKVV GVFGTDCVVG KRTTAVQLWE RALEKGIKAG FLATGQTGIL IGADAGYVID AVPADFVSGV VEKAVLKLEK TGKEIVFVEG QGALRHPAYG QVTLGLLYGS NPDVVFLVHD PSRDHFESFP EIPKKPDFEE ERRLIETLSN AKVIGGVSLN GGFETDLPVY DPFNTDDLDE MLERAMVW // ID Q9WZA4_THEMA Unreviewed; 69 AA. AC Q9WZA4; G4FDI7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35720.1}; GN OrderedLocusNames=TM_0636 {ECO:0000313|EMBL:AAD35720.1}; GN ORFNames=Tmari_0637 {ECO:0000313|EMBL:AGL49562.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35720.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35720.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35720.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49562.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49562.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35720.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49562.1; -; Genomic_DNA. DR PIR; A72354; A72354. DR RefSeq; NP_228445.1; NC_000853.1. DR RefSeq; WP_004081161.1; NZ_CP011107.1. DR STRING; 243274.TM0636; -. DR EnsemblBacteria; AAD35720; AAD35720; TM_0636. DR EnsemblBacteria; AGL49562; AGL49562; Tmari_0637. DR GeneID; 897733; -. DR KEGG; tma:TM0636; -. DR KEGG; tmi:THEMA_01480; -. DR KEGG; tmm:Tmari_0637; -. DR KEGG; tmw:THMA_0652; -. DR PATRIC; 23936185; VBITheMar51294_0646. DR eggNOG; ENOG4106DU7; Bacteria. DR eggNOG; ENOG410Y8K8; LUCA. DR OMA; FYNETEN; -. DR OrthoDB; EOG6B62FK; -. DR BioCyc; TMAR243274:GC6P-661-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR021321; DUF2922. DR Pfam; PF11148; DUF2922; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 69 AA; 7923 MW; E595290B3B5967AC CRC64; MKRLYMDFYN EAEGKRRRII VNSPADGLTA DQVQTAMQTL LDSKVLEGYA IDRAVIVETN SNEFFDLIH // ID Q9WZB6_THEMA Unreviewed; 132 AA. AC Q9WZB6; G4FDH6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35732.1}; GN OrderedLocusNames=TM_0648 {ECO:0000313|EMBL:AAD35732.1}; GN ORFNames=Tmari_0648 {ECO:0000313|EMBL:AGL49573.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35732.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35732.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35732.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49573.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49573.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35732.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49573.1; -; Genomic_DNA. DR PIR; G72351; G72351. DR RefSeq; NP_228457.1; NC_000853.1. DR RefSeq; WP_004081150.1; NZ_CP011107.1. DR STRING; 243274.TM0648; -. DR DNASU; 897753; -. DR EnsemblBacteria; AAD35732; AAD35732; TM_0648. DR EnsemblBacteria; AGL49573; AGL49573; Tmari_0648. DR GeneID; 897753; -. DR KEGG; tma:TM0648; -. DR KEGG; tmi:THEMA_01425; -. DR KEGG; tmm:Tmari_0648; -. DR KEGG; tmw:THMA_0663; -. DR PATRIC; 23936210; VBITheMar51294_0658. DR eggNOG; COG1669; LUCA. DR KO; K07075; -. DR OMA; LEGCPAF; -. DR OrthoDB; EOG6GBMCK; -. DR BioCyc; TMAR243274:GC6P-673-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR InterPro; IPR024700; UCP020217. DR Pfam; PF01909; NTP_transf_2; 1. DR PIRSF; PIRSF020217; UCP020217; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 33 108 NTP_transf_2. {ECO:0000259|Pfam:PF01909}. SQ SEQUENCE 132 AA; 15264 MW; 4E973A6234276462 CRC64; MYEEYIRAWV ERKKKEEEKM KLLAHKALEE ARKVTGVLRE KYGAKRVVLF GSLAKYLRGA GEFTERSDID LAVEGLPKEE YFRVLSEINR LSEFEVDLID LEGCPAFLRS LIEREGMEIE EGTDSLTDSG DR // ID Q9WY50_THEMA Unreviewed; 208 AA. AC Q9WY50; G4FHC1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35299.1}; DE SubName: Full=Zn-dependent hydrolases of the metallo-beta-lactamase superfamily {ECO:0000313|EMBL:AGL49131.1}; GN OrderedLocusNames=TM_0207 {ECO:0000313|EMBL:AAD35299.1}; GN ORFNames=Tmari_0205 {ECO:0000313|EMBL:AGL49131.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35299.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35299.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35299.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49131.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49131.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35299.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49131.1; -; Genomic_DNA. DR PIR; A72406; A72406. DR RefSeq; NP_228022.1; NC_000853.1. DR RefSeq; WP_004082876.1; NZ_CP011107.1. DR PDB; 1VJN; X-ray; 2.00 A; A/B=1-208. DR PDBsum; 1VJN; -. DR STRING; 243274.TM0207; -. DR EnsemblBacteria; AAD35299; AAD35299; TM_0207. DR EnsemblBacteria; AGL49131; AGL49131; Tmari_0205. DR GeneID; 897078; -. DR KEGG; tma:TM0207; -. DR KEGG; tmi:THEMA_03690; -. DR KEGG; tmm:Tmari_0205; -. DR KEGG; tmw:THMA_0214; -. DR PATRIC; 23935286; VBITheMar51294_0209. DR eggNOG; ENOG4107WCI; Bacteria. DR eggNOG; COG2220; LUCA. DR OMA; IIPMHYK; -. DR OrthoDB; EOG6R2GZB; -. DR BioCyc; TMAR243274:GC6P-220-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR SUPFAM; SSF56281; SSF56281; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VJN}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49131.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 208 AA; 23362 MW; 496A1215990D102F CRC64; MKITWFGHAC FALEMEGKTI VTDPFDESVG YPIPNVTADV VTESHQHFDH NAHHLVKGNF RVIDRPGAYT VNGVKIKGVE TFHDPSHGRE RGKNIVFVFE GEGIKVCHLG DLGHVLTPAQ VEEIGEIDVL LVPVGGTYTI GPKEAKEVAD LLNAKVIIPM HYKTKYLKFN LLPVDDFLKL FDSYERVGNI LELFEKPKER KVVVMEVQ // ID Q9WYF3_THEMA Unreviewed; 726 AA. AC Q9WYF3; G4FHN1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 141. DE SubName: Full=Cation-transporting ATPase, P-type {ECO:0000313|EMBL:AAD35405.1}; DE SubName: Full=Lead, cadmium, zinc and mercury transporting ATPase Copper-translocating P-type ATPase {ECO:0000313|EMBL:AGL49241.1}; DE EC=3.6.3.3 {ECO:0000313|EMBL:AGL49241.1}; DE EC=3.6.3.4 {ECO:0000313|EMBL:AGL49241.1}; DE EC=3.6.3.5 {ECO:0000313|EMBL:AGL49241.1}; GN OrderedLocusNames=TM_0317 {ECO:0000313|EMBL:AAD35405.1}; GN ORFNames=Tmari_0315 {ECO:0000313|EMBL:AGL49241.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35405.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35405.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35405.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49241.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49241.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU362081}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) CC (TC 3.A.3) family. Type IB subfamily. CC {ECO:0000256|RuleBase:RU362081}. CC -!- SIMILARITY: Contains 1 HMA domain. CC {ECO:0000256|RuleBase:RU362081}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35405.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49241.1; -; Genomic_DNA. DR PIR; D72392; D72392. DR RefSeq; NP_228129.1; NC_000853.1. DR RefSeq; WP_004083057.1; NZ_CP011107.1. DR STRING; 243274.TM0317; -. DR TCDB; 3.A.3.5.33; the p-type atpase (p-atpase) superfamily. DR EnsemblBacteria; AAD35405; AAD35405; TM_0317. DR EnsemblBacteria; AGL49241; AGL49241; Tmari_0315. DR GeneID; 897259; -. DR KEGG; tma:TM0317; -. DR KEGG; tmi:THEMA_03140; -. DR KEGG; tmm:Tmari_0315; -. DR KEGG; tmw:THMA_0324; -. DR PATRIC; 23935513; VBITheMar51294_0322. DR eggNOG; ENOG4105C59; Bacteria. DR eggNOG; COG2217; LUCA. DR KO; K17686; -. DR OMA; IVEMIHN; -. DR OrthoDB; EOG6742RM; -. DR BioCyc; TMAR243274:GC6P-330-MONOMER; -. DR BRENDA; 3.6.3.54; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0008551; F:cadmium-exporting ATPase activity; IEA:UniProtKB-EC. DR GO; GO:0004008; F:copper-exporting ATPase activity; IEA:UniProtKB-EC. DR GO; GO:0043682; F:copper-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0016463; F:zinc-exporting ATPase activity; IEA:UniProtKB-EC. DR GO; GO:0035434; P:copper ion transmembrane transport; IBA:GOC. DR Gene3D; 2.70.150.10; -; 2. DR Gene3D; 3.40.1110.10; -; 1. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023299; ATPase_P-typ_cyto_domN. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR017969; Heavy-metal-associated_CS. DR InterPro; IPR006121; HMA_dom. DR InterPro; IPR027256; P-typ_ATPase_IB. DR InterPro; IPR001757; P_typ_ATPase. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00403; HMA; 1. DR PRINTS; PR00120; HATPASE. DR SUPFAM; SSF55008; SSF55008; 1. DR SUPFAM; SSF56784; SSF56784; 2. DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1. DR TIGRFAMs; TIGR01494; ATPase_P-type; 2. DR PROSITE; PS00154; ATPASE_E1_E2; 1. DR PROSITE; PS01047; HMA_1; 1. DR PROSITE; PS50846; HMA_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|RuleBase:RU362081, KW ECO:0000313|EMBL:AGL49241.1}; KW Membrane {ECO:0000256|RuleBase:RU362081}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU362081}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 101 120 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 126 143 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 164 182 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 188 205 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 339 360 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 386 413 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 681 698 Helical. {ECO:0000256|RuleBase:RU362081}. FT DOMAIN 18 83 HMA. {ECO:0000259|PROSITE:PS50846}. SQ SEQUENCE 726 AA; 79389 MW; 5DEC8DFA42F32D6D CRC64; MSDQKTMEDR AAKNEEIKKT FTVTGMTCAT CAKTVEKALK KLDGVKFAAV NLATSTGFIV AEKEISFEEI KKAVEEVGYG VTTESPEDVE RKRYEESKRN LILAWLVTAP LALLMIYHMF VSEVPYFTWI EVFAGAFVTF YVGRGTIRGA WIALTHKHTN MDTLIFFGAV TSWVTALLDS VGLPVMSFGA IGAMIVAFHI TGRFIESYLR DRASKEIKAL LKLQAKEARV ITDEGEVMMP IEAVKEGFIV LVKPGERIPV DGVIVEGQSS IDESVVTGES IPVLKKENDE VIGGSLNVSS PIKIKVTKVG EDTFLSQMVK LIQEAQGSKV PIQALADRIT MWFVPTIIVL AITSALVWYF NYERFLPFVE KAREIFPWII QTSDPLTFSI FVFVATIVIA CPCALGLATP MALVTGTGLA AKKGLLIRNA EAIQTSKDVG VVLTDKTGTL TEGSPKVVDH NLSAELIRIV ASIERNSNHP LAKAISELSQ DVVEVESVEE IPGEGVRALY GGEEYFVGKP LDYSKYESLL EEGKTIVEVR RNGEVVGFLA IEDPIREDSP EAVRRLKEMG IEPVMITGDN EKTARAVARR LGIEKFHAGV KPSEKLDLVR SYQAQGKKVA MVGDGMNDAA ALKGADVGIA IGSGTDLAID SADIIITKGG ISKVVDAIEI SRKTFKIIKQ NLFWAFFYNV IAIPMAMMGL LHPVIAELAM AFSSITVTLN SMRVRE // ID Q9X1H8_THEMA Unreviewed; 426 AA. AC Q9X1H8; G4FFK3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36535.1}; GN OrderedLocusNames=TM_1467 {ECO:0000313|EMBL:AAD36535.1}; GN ORFNames=Tmari_1474 {ECO:0000313|EMBL:AGL50398.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36535.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36535.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36535.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50398.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50398.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36535.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50398.1; -; Genomic_DNA. DR PIR; D72252; D72252. DR RefSeq; NP_229267.1; NC_000853.1. DR RefSeq; WP_004081767.1; NZ_CP011107.1. DR STRING; 243274.TM1467; -. DR EnsemblBacteria; AAD36535; AAD36535; TM_1467. DR EnsemblBacteria; AGL50398; AGL50398; Tmari_1474. DR GeneID; 898014; -. DR KEGG; tma:TM1467; -. DR KEGG; tmm:Tmari_1474; -. DR KEGG; tmw:THMA_1498; -. DR PATRIC; 23937888; VBITheMar51294_1482. DR eggNOG; ENOG4108IU7; Bacteria. DR eggNOG; COG2206; LUCA. DR OMA; KWVRHHH; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1506-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR006675; HDIG_dom. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00277; HDIG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 67 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 115 133 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 145 170 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 182 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 210 228 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 250 386 HDc. {ECO:0000259|SMART:SM00471}. SQ SEQUENCE 426 AA; 48981 MW; 9DEAFCB7BF27E280 CRC64; MIKNKNSERI FLIYSLSILA FYFFLIFMFS DYTDDWHNLG YVLLLFLTSV FFDIARTKTF EFTGGKVETS AVFIVNIFTA ALLNPLEASL AAASSAITFK IIKLFFGERY PVSRYIFNFS QFAVNTFIVS LLFHRLSGTN TFQNILAILL STVVYFLINN VFVFFGVYIL TKGDIRETAS KVLSGPVTSM ALMIPVIAVI YILYQYIGFI AIPVSLAAVL SIQVGNYYRY KYYEAKLEHL KLLAKSLEEK DEYTRGHSEK VAELAKKIAK RLGFSPKMVE RIYNAAFLHD IGKIGIPDHI LKKPTILSKE EMMIVKNHPI MGEDILREVD IFNNRESKWV RHHHERWDGK GYPDGLRGEE IPLPSRIISV ADVYEALTSD RPYRKALSHE EAKEIMMKNM KGTVLDPRLV DLLFEILEKE KEEEET // ID Q9WZT0_THEMA Unreviewed; 190 AA. AC Q9WZT0; G4FD01; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=Transcriptional regulator, TetR family {ECO:0000313|EMBL:AAD35905.1}; GN OrderedLocusNames=TM_0823 {ECO:0000313|EMBL:AAD35905.1}; GN ORFNames=Tmari_0824 {ECO:0000313|EMBL:AGL49749.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35905.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35905.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35905.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49749.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49749.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 HTH tetR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000710}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35905.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49749.1; -; Genomic_DNA. DR PIR; B72330; B72330. DR RefSeq; NP_228632.1; NC_000853.1. DR RefSeq; WP_004080830.1; NZ_CP011107.1. DR STRING; 243274.TM0823; -. DR DNASU; 898493; -. DR EnsemblBacteria; AAD35905; AAD35905; TM_0823. DR EnsemblBacteria; AGL49749; AGL49749; Tmari_0824. DR GeneID; 898493; -. DR KEGG; tma:TM0823; -. DR KEGG; tmi:THEMA_00525; -. DR KEGG; tmm:Tmari_0824; -. DR KEGG; tmw:THMA_0844; -. DR PATRIC; 23936570; VBITheMar51294_0835. DR eggNOG; ENOG4108IG5; Bacteria. DR eggNOG; COG1309; LUCA. DR KO; K09017; -. DR OMA; ELESHLF; -. DR OrthoDB; EOG654P2M; -. DR BioCyc; TMAR243274:GC6P-852-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 1. DR Gene3D; 1.10.357.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001647; HTH_TetR. DR InterPro; IPR015893; Tet_transcr_reg_TetR-like_C. DR InterPro; IPR011075; Tet_transcr_reg_TetR-rel_C. DR Pfam; PF00440; TetR_N; 1. DR PRINTS; PR00455; HTHTETR. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF48498; SSF48498; 1. DR PROSITE; PS50977; HTH_TETR_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00483316}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00482171}; KW Transcription regulation {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00482171}. FT DOMAIN 3 63 HTH tetR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50977}. SQ SEQUENCE 190 AA; 22492 MW; 7F54A3A31D07100C CRC64; MSSETRRKIL EAARKAFSKY GYDGVSMEEI AREAGVKKAL IYYYFPSKDK LFEEVWREAL EELESHLFAV TEETNSYFAK IKKFLKSYVD FVLNKTVLNE IIEKEKSTVR FEEEKWSKLR ERYESFIKRV EELIEEGKKQ NYVYKDLDSR AAAELIVNSF GDVPKDKRLL QNIQEMILRG LLNVKTEEGR // ID Q9WXR1_THEMA Unreviewed; 196 AA. AC Q9WXR1; G4FGW9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35148.1}; GN OrderedLocusNames=TM_0054 {ECO:0000313|EMBL:AAD35148.1}; GN ORFNames=Tmari_0051 {ECO:0000313|EMBL:AGL48977.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35148.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35148.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35148.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48977.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48977.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35148.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48977.1; -; Genomic_DNA. DR PIR; G72423; G72423. DR RefSeq; NP_227870.1; NC_000853.1. DR RefSeq; WP_004082541.1; NZ_CP011107.1. DR STRING; 243274.TM0054; -. DR EnsemblBacteria; AAD35148; AAD35148; TM_0054. DR EnsemblBacteria; AGL48977; AGL48977; Tmari_0051. DR GeneID; 896878; -. DR KEGG; tma:TM0054; -. DR KEGG; tmi:THEMA_04535; -. DR KEGG; tmm:Tmari_0051; -. DR KEGG; tmw:THMA_0050; -. DR PATRIC; 23934948; VBITheMar51294_0052. DR OMA; FISVWFD; -. DR OrthoDB; EOG657JB8; -. DR BioCyc; TMAR243274:GC6P-54-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.60.120.260; -; 1. DR InterPro; IPR008979; Galactose-bd-like. DR SUPFAM; SSF49785; SSF49785; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 196 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972316. SQ SEQUENCE 196 AA; 21411 MW; C294E6EFE6215514 CRC64; MKVLLISATL FSLILTGCML TTTFQTPPGT GEISEETLVS SIVEGQSPES TITTVVDNSL PESDQHGTVL YVSPSSTDVT GFISVWFDLK KLLEGKAFKG DIVKFYIDIL QTREDQATVT MNIYEETGGS TSLTKIATAL LEKNEWTTVE GTTTVPDIGN VERYLLGVCA SKPATLDFYI DNFEWEVIYQ EEGGAI // ID Q9X1N4_THEMA Unreviewed; 605 AA. AC Q9X1N4; G4FFT6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Lipopolysaccharide biosynthesis protein {ECO:0000313|EMBL:AAD36615.1}; DE SubName: Full=UDP-N-acetylglucosamine 4,6-dehydratase {ECO:0000313|EMBL:AGL50480.1}; DE EC=4.2.1.- {ECO:0000313|EMBL:AGL50480.1}; GN OrderedLocusNames=TM_1548 {ECO:0000313|EMBL:AAD36615.1}; GN ORFNames=Tmari_1556 {ECO:0000313|EMBL:AGL50480.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36615.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36615.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36615.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50480.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50480.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36615.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50480.1; -; Genomic_DNA. DR PIR; G72238; G72238. DR RefSeq; NP_229348.1; NC_000853.1. DR RefSeq; WP_004081940.1; NZ_CP011107.1. DR STRING; 243274.TM1548; -. DR EnsemblBacteria; AAD36615; AAD36615; TM_1548. DR EnsemblBacteria; AGL50480; AGL50480; Tmari_1556. DR GeneID; 897972; -. DR KEGG; tma:TM1548; -. DR KEGG; tmi:THEMA_06540; -. DR KEGG; tmm:Tmari_1556; -. DR KEGG; tmw:THMA_1583; -. DR PATRIC; 23938058; VBITheMar51294_1566. DR eggNOG; ENOG4105C5E; Bacteria. DR eggNOG; COG1086; LUCA. DR OMA; INEMMAR; -. DR OrthoDB; EOG6WQD59; -. DR BioCyc; TMAR243274:GC6P-1589-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR003869; Polysac_CapD-like. DR Pfam; PF02719; Polysacc_synt_2; 1. DR SUPFAM; SSF51735; SSF51735; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000313|EMBL:AGL50480.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 41 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 122 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 275 557 Polysacc_synt_2. FT {ECO:0000259|Pfam:PF02719}. SQ SEQUENCE 605 AA; 68389 MW; F970EC9B28C5049A CRC64; MVRKALLFVI DVALTYFAGV VALFSRFGFD FQEMSRYDES VIVYTVISAV VYILNGNYSI VWEYANARDF LILIRGSVIS YLSNLAFFYV YRGIVLPRSV GFAVFLGSMV LLVLSRITWQ WMIVNGRGKV PGEKRILIIG AGDAGVSILE EFEKHPHLGK IVAFVDDSPR KIGRKVRGVP VFGPIEKTME FVEKMNVDEI VIAIPSASRA EMERILKSID LKKVRVKTLP SVRELIEGRV RISHLKEISI EDLLGREEVK VDFHEIGKFL KGKKILVTGA GGSIGSELCK QIARMNPAEI FLLGHGETSI YLINEFLTEH FPEVKKKRII ADVADRKIME HWLTQLRPDV IFHVAAHKHV PLMEENPLEA FRVNVLGTMN LVELSERLGV KYFVFISTDK AVNPTSVMGL TKRIAELYIL SREKNSTNFS IVRFGNVLGS RGSVVEKFRR QIEKGGPVTV TDPRMKRYFM SIPEAVSLIL QSLLFSSGKD LFILDMGEQI PILKLAETMI MLSGYTPYQD IKIVFTGIRP GEKMYEELLY PYEVKELTPH SKIFRVKTSV LPGKESVEQA INRMKEAFEN SDVKGLLTEM KKLVPEAQIN VGSDN // ID Q9WYW9_THEMA Unreviewed; 162 AA. AC Q9WYW9; G4FDX1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35584.1}; GN OrderedLocusNames=TM_0499 {ECO:0000313|EMBL:AAD35584.1}; GN ORFNames=Tmari_0496 {ECO:0000313|EMBL:AGL49421.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35584.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35584.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35584.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49421.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49421.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35584.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49421.1; -; Genomic_DNA. DR PIR; B72371; B72371. DR RefSeq; NP_228309.1; NC_000853.1. DR RefSeq; WP_004081446.1; NZ_CP011107.1. DR STRING; 243274.TM0499; -. DR EnsemblBacteria; AAD35584; AAD35584; TM_0499. DR EnsemblBacteria; AGL49421; AGL49421; Tmari_0496. DR GeneID; 897540; -. DR KEGG; tma:TM0499; -. DR KEGG; tmi:THEMA_02175; -. DR KEGG; tmm:Tmari_0496; -. DR KEGG; tmw:THMA_0512; -. DR PATRIC; 23935903; VBITheMar51294_0506. DR OMA; KRIYVED; -. DR OrthoDB; EOG62VNMZ; -. DR BioCyc; TMAR243274:GC6P-523-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 162 AA; 19287 MW; 69F7F4F291FB4636 CRC64; MRRYWLVILL IAIVILFFRV KWEVKRIYVE DPEVKKMVEE ILREKRYRYK FTDTRERSLI IEKDRAIVPP NEVVLHLDWP EKVKKRVKEL VEPFFQKIGL SATESQMATA EVFLEAVIES FFEGNQSLFE NSYYCGEIYV FSNGKCVAEY DPSTGELVFL DK // ID Q9WYQ6_THEMA Unreviewed; 328 AA. AC Q9WYQ6; G4FHY4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Oxidoreductase, putative {ECO:0000313|EMBL:AAD35510.1}; GN OrderedLocusNames=TM_0425 {ECO:0000313|EMBL:AAD35510.1}; GN ORFNames=Tmari_0422 {ECO:0000313|EMBL:AGL49347.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35510.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35510.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35510.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49347.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49347.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35510.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49347.1; -; Genomic_DNA. DR PIR; A72379; A72379. DR RefSeq; NP_228235.1; NC_000853.1. DR RefSeq; WP_004083301.1; NZ_CP011107.1. DR PDB; 3IP3; X-ray; 2.14 A; A/B/C/D/E/F/G/H=2-328. DR PDBsum; 3IP3; -. DR STRING; 243274.TM0425; -. DR DNASU; 897431; -. DR EnsemblBacteria; AAD35510; AAD35510; TM_0425. DR EnsemblBacteria; AGL49347; AGL49347; Tmari_0422. DR GeneID; 897431; -. DR KEGG; tma:TM0425; -. DR KEGG; tmm:Tmari_0422; -. DR KEGG; tmw:THMA_0431; -. DR PATRIC; 23935735; VBITheMar51294_0431. DR eggNOG; ENOG4105TNP; Bacteria. DR eggNOG; COG0673; LUCA. DR OMA; AIDWIYW; -. DR OrthoDB; EOG6TXQT7; -. DR BioCyc; TMAR243274:GC6P-440-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000683; Oxidoreductase_N. DR InterPro; IPR004104; OxRdtase_C. DR Pfam; PF01408; GFO_IDH_MocA; 1. DR Pfam; PF02894; GFO_IDH_MocA_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3IP3}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 120 GFO_IDH_MocA. {ECO:0000259|Pfam:PF01408}. FT DOMAIN 138 229 GFO_IDH_MocA_C. FT {ECO:0000259|Pfam:PF02894}. FT REGION 260 263 Sulfate binding. {ECO:0000213|PDB:3IP3}. FT BINDING 249 249 Sulfate. {ECO:0000213|PDB:3IP3}. FT BINDING 267 267 Sulfate. {ECO:0000213|PDB:3IP3}. FT BINDING 274 274 Sulfate. {ECO:0000213|PDB:3IP3}. SQ SEQUENCE 328 AA; 37403 MW; 391B004D7B4DA4F6 CRC64; MLKICVIGSS GHFRYALEGL DEECSITGIA PGVPEEDLSK LEKAISEMNI KPKKYNNWWE MLEKEKPDIL VINTVFSLNG KILLEALERK IHAFVEKPIA TTFEDLEKIR SVYQKVRNEV FFTAMFGIRY RPHFLTAKKL VSEGAVGEIR LVNTQKSYKL GQRPDFYKKR ETYGGTIPWV GIHAIDWIHW ITGKKFLSVY ATHSRLHNSG HGELETTALC HFTLENEVFA SLSIDYLRPQ GAPTHDDDRM RIVGTRGIVE VINERVFLTD EKGHREVPLV EKGQIFEDFL REIRGQGKCM VTPEDSILTT EIALKARLSA DTGQIVLI // ID Q9WZU9_THEMA Unreviewed; 455 AA. AC Q9WZU9; G4FCX9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=Hemolysin-related protein {ECO:0000313|EMBL:AAD35927.1}; DE SubName: Full=Hemolysins-related protein containing CBS domains {ECO:0000313|EMBL:AGL49772.1}; GN OrderedLocusNames=TM_0845 {ECO:0000313|EMBL:AAD35927.1}; GN ORFNames=Tmari_0847 {ECO:0000313|EMBL:AGL49772.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35927.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35927.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35927.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49772.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49772.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35927.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49772.1; -; Genomic_DNA. DR PIR; F72326; F72326. DR RefSeq; NP_228654.1; NC_000853.1. DR RefSeq; WP_004080781.1; NZ_CP011107.1. DR STRING; 243274.TM0845; -. DR EnsemblBacteria; AAD35927; AAD35927; TM_0845. DR EnsemblBacteria; AGL49772; AGL49772; Tmari_0847. DR GeneID; 898516; -. DR KEGG; tma:TM0845; -. DR KEGG; tmi:THEMA_00415; -. DR KEGG; tmm:Tmari_0847; -. DR KEGG; tmw:THMA_0866; -. DR PATRIC; 23936616; VBITheMar51294_0858. DR eggNOG; ENOG4105C37; Bacteria. DR eggNOG; COG1253; LUCA. DR OMA; LSIMDLE; -. DR OrthoDB; EOG60W7V4; -. DR BioCyc; TMAR243274:GC6P-874-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR002550; DUF21. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR005170; Transptr-assoc_dom. DR Pfam; PF00571; CBS; 2. DR Pfam; PF03471; CorC_HlyC; 1. DR Pfam; PF01595; DUF21; 1. DR SMART; SM00116; CBS; 2. DR SMART; SM01091; CorC_HlyC; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51371; CBS; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00460213, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00460213, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00460213, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 93 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 100 117 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 217 277 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 286 343 CBS. {ECO:0000259|PROSITE:PS51371}. SQ SEQUENCE 455 AA; 51386 MW; D07F250607448215 CRC64; MEDPVSSVLT LGLESLLLVI LIYLSNFFSS SETALTLMSK VKIKEFLEEK EEKSAKESYI HLFNKYLTTI LISNNLVNLL ASSISTLIFL NLLRNMSEEF VAVVSTLFIT TILLIFGEIT PKVLARSDPE RVFRRSIGVI RFLTRVLDPI GRLLVKIADG IISLRHGKKV SEDLFITEED IVSIVQVGGE MGVIEEEEER IIKRAFEMKQ IAVKEIMTPR VDIVAIEENQ TVKDLIELVE DEGYSRIPVY KETIDNIVGI CYAKDVLSML AEKDCEEVKS MKVKDIMREA LYVPETMNID ELLKILKARK IHIAIVVDEY GGTAGIVTLE DIIEELFGNI MDEYDYDEIS GIRKIDERTY IVDGATPIND IEMELRVQFP ETEYETIAGY LLEHFKRIPN VGEEAVIGNL YFKVLAVGKN RIEKVMIKIL EGEEIDGEPG EAGENGSGSQ EKGVR // ID Q9X120_THEMA Unreviewed; 694 AA. AC Q9X120; G4FE55; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Membrane protein, putative {ECO:0000313|EMBL:AGL50226.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36368.1}; GN OrderedLocusNames=TM_1294 {ECO:0000313|EMBL:AAD36368.1}; GN ORFNames=Tmari_1302 {ECO:0000313|EMBL:AGL50226.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36368.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36368.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36368.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50226.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50226.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36368.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50226.1; -; Genomic_DNA. DR PIR; E72272; E72272. DR RefSeq; NP_229098.1; NC_000853.1. DR RefSeq; WP_004079930.1; NZ_CP011107.1. DR STRING; 243274.TM1294; -. DR EnsemblBacteria; AAD36368; AAD36368; TM_1294. DR EnsemblBacteria; AGL50226; AGL50226; Tmari_1302. DR GeneID; 898189; -. DR KEGG; tma:TM1294; -. DR KEGG; tmi:THEMA_07865; -. DR KEGG; tmm:Tmari_1302; -. DR KEGG; tmw:THMA_1320; -. DR PATRIC; 23937528; VBITheMar51294_1310. DR eggNOG; ENOG4107SGJ; Bacteria. DR eggNOG; COG1033; LUCA. DR KO; K07003; -. DR OMA; PDEYTEN; -. DR OrthoDB; EOG6Q2SFR; -. DR BioCyc; TMAR243274:GC6P-1325-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR004869; MMPL_dom. DR Pfam; PF03176; MMPL; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 16 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 188 208 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 220 243 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 249 274 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 294 313 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 325 346 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 372 390 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 550 567 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 579 599 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 605 625 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 637 657 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 663 686 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 203 354 MMPL. {ECO:0000259|Pfam:PF03176}. FT DOMAIN 529 623 MMPL. {ECO:0000259|Pfam:PF03176}. SQ SEQUENCE 694 AA; 78574 MW; CB4864C8CCF3B44C CRC64; MFEKYTSFVF KNRKRIFALV LVINILALFG LFRLHFTTEF SILMPQKSHQ KEIYDRMNTI FKSGEQLAVM VKMNTDPLSR EGLNKVFEIK ERLSSIEGVK TVITPVPEKF PVGFRLVETK GMAEKEYEDF LSYVQSVKDL LNVKKTDDGY YALFMILPEE SVPPEKIEKV LSDYEHYLSG TQYLEDQIFR YLLFMIFTLP PFAVVLLLNV FRVQLGRFKY AIFSLIPAGF AALWTLGIVM GWFGQDLSII TFLVPIFTIV MGSADGLHFV SHFLERKREG ETTFNAVKNT LESVGRAMIL TTLTTMAGFL SFLTLNSESM KQMGVLASIG IGLAGVSTWI VLPVILSRVE KVEPKNKESG VFRVFQKLSK RALVVTIVSV LIFLPGLFFL KADLNILKLY KSYTRVRKNV EKIEEVFGRA LPVYILFESE NLFDPSFAQK VLSMEEDLKK EGFDAFSMYD IISKLNERLF KEKGYPKILA RALILKRLLP DEYTENLVSG NTGRAFVFLN DLDREILVKV ENVVEKHGFQ VTGIPYIIKE MNDSIVPQQL LSVFLAISMV FLLLVLFQRS FLYPAKAIVP VGISLVSLFG FMGLSGIPLN LITANMAGIV IGVGIDYAIH VTELFRYYGD IEKTVRIAST PVLANAFGLS IGLSALILSP FTFHTYLVAI MWVTMTVSSF MSLVILPKLL EAKK // ID Q9WYH4_THEMA Unreviewed; 127 AA. AC Q9WYH4; G4FHQ1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35426.1}; GN OrderedLocusNames=TM_0339 {ECO:0000313|EMBL:AAD35426.1}; GN ORFNames=Tmari_0337 {ECO:0000313|EMBL:AGL49262.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35426.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35426.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35426.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49262.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49262.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35426.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49262.1; -; Genomic_DNA. DR PIR; A72388; A72388. DR RefSeq; NP_228150.1; NC_000853.1. DR RefSeq; WP_004083106.1; NZ_CP011107.1. DR STRING; 243274.TM0339; -. DR EnsemblBacteria; AAD35426; AAD35426; TM_0339. DR EnsemblBacteria; AGL49262; AGL49262; Tmari_0337. DR GeneID; 897295; -. DR KEGG; tma:TM0339; -. DR KEGG; tmi:THEMA_03020; -. DR KEGG; tmm:Tmari_0337; -. DR KEGG; tmw:THMA_0347; -. DR PATRIC; 23935557; VBITheMar51294_0343. DR eggNOG; ENOG4105N5D; Bacteria. DR eggNOG; COG3877; LUCA. DR OMA; LQFVEMF; -. DR OrthoDB; EOG6RRKPX; -. DR BioCyc; TMAR243274:GC6P-353-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR018658; DUF2089. DR Pfam; PF09862; DUF2089; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 127 AA; 14740 MW; 3444AA5F2D307B02 CRC64; MLPKCPVCGK EMIVTELHCK RDEVTVRGRF RASPFDFLDK DELEFVILFF RARGNLKEIE RYTGQGYFAL RGKLEKILEK MNLQPLGEMK EEISEEDLFK QVKEGKIGVE EALEILKKRK KGGESDV // ID Q9X0Q5_THEMA Unreviewed; 324 AA. AC Q9X0Q5; G4FEH3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Arsenical-resistance protein ACR3 {ECO:0000313|EMBL:AGL50104.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36248.1}; GN OrderedLocusNames=TM_1173 {ECO:0000313|EMBL:AAD36248.1}; GN ORFNames=Tmari_1180 {ECO:0000313|EMBL:AGL50104.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36248.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36248.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36248.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50104.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50104.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36248.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50104.1; -; Genomic_DNA. DR PIR; H72285; H72285. DR RefSeq; NP_228978.1; NC_000853.1. DR RefSeq; WP_004080192.1; NZ_CP011107.1. DR STRING; 243274.TM1173; -. DR EnsemblBacteria; AAD36248; AAD36248; TM_1173. DR EnsemblBacteria; AGL50104; AGL50104; Tmari_1180. DR GeneID; 898313; -. DR KEGG; tma:TM1173; -. DR KEGG; tmi:THEMA_08470; -. DR KEGG; tmm:Tmari_1180; -. DR KEGG; tmw:THMA_1198; -. DR PATRIC; 23937286; VBITheMar51294_1191. DR eggNOG; ENOG4107UP7; Bacteria. DR eggNOG; COG0798; LUCA. DR KO; K03325; -. DR OMA; QWRGIGV; -. DR OrthoDB; EOG6X10WB; -. DR BioCyc; TMAR243274:GC6P-1202-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015104; F:antimonite transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015105; F:arsenite transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0005342; F:organic acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015699; P:antimonite transport; IBA:GO_Central. DR GO; GO:0015700; P:arsenite transport; IBA:GO_Central. DR GO; GO:1903825; P:organic acid transmembrane transport; IBA:GOC. DR InterPro; IPR002657; BilAc:Na_symport/Acr3. DR PANTHER; PTHR10361; PTHR10361; 1. DR Pfam; PF01758; SBF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 15 35 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 41 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 127 148 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 168 186 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 198 219 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 239 257 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 266 287 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 293 313 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 324 AA; 36304 MW; 9E2C6F3AC31A4C03 CRC64; MNFIQKMASH FSKNMLFYTL GIVLVGTTVS LLGDFRGLSK LVLPVVFLMI YPMMINVSFE SLKNVKYAVN PLLVALALNF VVSPLLFYLF CLVFRVPTTI RISLILLAVA PSSSMGLGYV GLSKGNIVSA SVIVAFTFLL SMVVYPVTFH FLGVVSESYP FTEILKDLLL VLILPLTLGV LTREFLERKF KIEHRRIKPL LSLLNILALY LLISIIFLTK GKMIVQHWKN SLLVAPVSAL YYLTAISSAI LLNRYAVRLS YEDHQAVVFT TVSKNVALTI GLLATSFASG QLAMYPAIVS LFQIIFLMSY LHLSERIQKW WSKS // ID Q9WYF7_THEMA Unreviewed; 194 AA. AC Q9WYF7; G4FHN5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35409.1}; GN OrderedLocusNames=TM_0321 {ECO:0000313|EMBL:AAD35409.1}; GN ORFNames=Tmari_0319 {ECO:0000313|EMBL:AGL49245.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35409.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35409.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35409.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49245.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49245.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35409.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49245.1; -; Genomic_DNA. DR PIR; H72392; H72392. DR RefSeq; NP_228133.1; NC_000853.1. DR RefSeq; WP_004083070.1; NZ_CP011107.1. DR EnsemblBacteria; AAD35409; AAD35409; TM_0321. DR EnsemblBacteria; AGL49245; AGL49245; Tmari_0319. DR GeneID; 897263; -. DR KEGG; tma:TM0321; -. DR KEGG; tmi:THEMA_03120; -. DR KEGG; tmm:Tmari_0319; -. DR KEGG; tmw:THMA_0328; -. DR PATRIC; 23935521; VBITheMar51294_0326. DR OMA; IAGWWHN; -. DR OrthoDB; EOG6DRPGG; -. DR BioCyc; TMAR243274:GC6P-334-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR SUPFAM; SSF52317; SSF52317; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 194 AA; 22770 MW; 91BE06A0C0393B52 CRC64; MTAFSFLGDK YHDHDLFLET LKYALNCEIN DLRPEDFPEI RKLPDLVVIG RWNLLDDETP WLKEGDIKIL VDYVRSGGKL FVWHSGLARF PESYNGLVGG RFIHHPPQKK VRYYGKDIEF ELVDEHYFVD LYSDVEIFLW SESDDGTSIA GWRRRYHNGK ILALTPAHSE GLKDQVFRDF LKKVLNTFVN QTSW // ID Q9WY85_THEMA Unreviewed; 283 AA. AC Q9WY85; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Biotin synthase-related protein, radical SAM superfamily {ECO:0000313|EMBL:AGL49167.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35334.1}; GN OrderedLocusNames=TM_0243 {ECO:0000313|EMBL:AAD35334.1}; GN ORFNames=Tmari_0241 {ECO:0000313|EMBL:AGL49167.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35334.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35334.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35334.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49167.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49167.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35334.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49167.1; -; Genomic_DNA. DR PIR; D72398; D72398. DR RefSeq; NP_228057.1; NC_000853.1. DR RefSeq; WP_010865078.1; NZ_CP011107.1. DR STRING; 243274.TM0243; -. DR EnsemblBacteria; AAD35334; AAD35334; TM_0243. DR EnsemblBacteria; AGL49167; AGL49167; Tmari_0241. DR GeneID; 897144; -. DR KEGG; tma:TM0243; -. DR KEGG; tmi:THEMA_03510; -. DR KEGG; tmm:Tmari_0241; -. DR KEGG; tmw:THMA_0250; -. DR PATRIC; 23935361; VBITheMar51294_0246. DR eggNOG; ENOG4107V5F; Bacteria. DR eggNOG; COG2516; LUCA. DR KO; K01012; -. DR OMA; YYNERPG; -. DR BioCyc; TMAR243274:GC6P-256-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 22 225 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 283 AA; 32704 MW; A3FFAB0B1282DFA2 CRC64; MMLRASYGTI RKVNGNSSLE MDTAYLMLGE RCVYNCLYCA QSRSSTSPSH FLSRVTWKEV SEDLLGKLND RFKRVCIQVV SYPSYGKDLR LIIPRFRIPV SVSVRAVSIE EVVEYFELGA DRVGIAVDVP NKTLFEKIRG GKYERHLHIL EKVSEMFPGR ITTHVIVGLG ESDKDIVDFT VWARERNIVV SLFAFTPIKG TAFENRERPS LERYRKIQLV TYLLEKNLIK PENIIFDSNG KIIDVEWNGE FPEEALRTRG CPHCTRPYYN ESPRGPIYNV HWR // ID Q9WYL9_THEMA Unreviewed; 361 AA. AC Q9WYL9; G4FHU9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=ABC-type multidrug transport system, permease component {ECO:0000313|EMBL:AGL49311.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35473.1}; GN OrderedLocusNames=TM_0388 {ECO:0000313|EMBL:AAD35473.1}; GN ORFNames=Tmari_0386 {ECO:0000313|EMBL:AGL49311.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35473.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35473.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35473.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49311.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49311.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35473.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49311.1; -; Genomic_DNA. DR PIR; D72384; D72384. DR RefSeq; NP_228198.1; NC_000853.1. DR RefSeq; WP_004083211.1; NZ_CP011107.1. DR STRING; 243274.TM0388; -. DR DNASU; 897367; -. DR EnsemblBacteria; AAD35473; AAD35473; TM_0388. DR EnsemblBacteria; AGL49311; AGL49311; Tmari_0386. DR GeneID; 897367; -. DR KEGG; tma:TM0388; -. DR KEGG; tmi:THEMA_02780; -. DR KEGG; tmm:Tmari_0386; -. DR KEGG; tmw:THMA_0395; -. DR PATRIC; 23935659; VBITheMar51294_0394. DR eggNOG; ENOG4107X9Q; Bacteria. DR eggNOG; COG0842; LUCA. DR KO; K01992; -. DR OMA; KWIVVIN; -. DR OrthoDB; EOG6ZKXP7; -. DR BioCyc; TMAR243274:GC6P-402-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR InterPro; IPR000412; ABC_2_transport. DR PROSITE; PS51012; ABC_TM2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 169 192 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 213 236 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248 272 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 284 306 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 336 354 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 361 AA; 41106 MW; 72967E8C49D323DA CRC64; MRHLVVSILK NDYFRTKSVL FWNFLFPILL YLILVSIFGD MSSNMNLRIG LVGESSLVES VFSHLPSGIE IIRTQNPERD LKYGKIDVCV ILPENFDNLF TKAIIFSKTK ISVPVEITIL YAPERQESIV LANVVSNILE SLDLQLRKVK EVEVEYRKKE RQAINYSHYI LPAVLLVGVM SVGLFTVPYQ LALYREQGIL KRILASPLRG HHYFFSIVVC GLFAMSITSA SVTLFARFVY GIEFPINVSF LGGVLLSFLT FLSVSLLMVS LFKTFSALSA ASQVFNQVFM FLGGFYFDVS GIPWPIKAVV LGNPATYLVD YLRGSFGYRT IYSNHFLVPI VWIVLSFVLF FLNWRRVMMV E // ID Q9X0M9_THEMA Unreviewed; 379 AA. AC Q9X0M9; G4FEK3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=HD-GYP domain containing protein {ECO:0000313|EMBL:AGL50075.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36221.1}; GN OrderedLocusNames=TM_1145 {ECO:0000313|EMBL:AAD36221.1}; GN ORFNames=Tmari_1151 {ECO:0000313|EMBL:AGL50075.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36221.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36221.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36221.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50075.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50075.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36221.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50075.1; -; Genomic_DNA. DR PIR; E72291; E72291. DR RefSeq; NP_228951.1; NC_000853.1. DR RefSeq; WP_004080239.1; NZ_CP011107.1. DR STRING; 243274.TM1145; -. DR EnsemblBacteria; AAD36221; AAD36221; TM_1145. DR EnsemblBacteria; AGL50075; AGL50075; Tmari_1151. DR GeneID; 898619; -. DR KEGG; tma:TM1145; -. DR KEGG; tmm:Tmari_1151; -. DR KEGG; tmw:THMA_1168; -. DR PATRIC; 23937225; VBITheMar51294_1161. DR eggNOG; ENOG4108KJF; Bacteria. DR eggNOG; COG2206; LUCA. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1174-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 167 305 HDc. {ECO:0000259|SMART:SM00471}. SQ SEQUENCE 379 AA; 43727 MW; A521AA9452B40124 CRC64; MEAIQVASVK DNFVKTLEKI RKKHGVDIIA LFAIRQSLAI HVINSADNPV SFSAGTIFNL TLTPLVEEFL FNVKTFENHP QKTRFALVEN VQWELYIPVV FKEFPTGFVY VASKKKRDAE KTEGIIRDLQ DFLKAHGLEY YFLEYSVVLD QLLTTVAILI DRLFSRVSRY TLNHIYNVAF WAEEIGKIVG LDEKRLAKLY LAGLLHDIGK VYIDERILNK EGRLTLQEYQ EMKKHVDYSY NMVKDLMIWD IEDDVALWVV QHHEKFDGSG YPFGLKEEEI TPEGRILKIA DTLDAMLSPR SYRNPFPLDD VIKEIERLRG KDFDPLLADL TVDLLREKKE SLGLFEGRIL PATLIAGEGI HEGILRKNDG YHVFISDYV // ID Q9WY45_THEMA Unreviewed; 300 AA. AC Q9WY45; G4FHB6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=ABC-type nitrate/sulfonate/bicarbonate transport systems, periplasmic component {ECO:0000313|EMBL:AGL49126.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35294.1}; GN OrderedLocusNames=TM_0202 {ECO:0000313|EMBL:AAD35294.1}; GN ORFNames=Tmari_0200 {ECO:0000313|EMBL:AGL49126.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35294.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35294.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35294.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49126.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49126.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35294.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49126.1; -; Genomic_DNA. DR PIR; D72405; D72405. DR RefSeq; NP_228017.1; NC_000853.1. DR RefSeq; WP_004082867.1; NZ_CP011107.1. DR STRING; 243274.TM0202; -. DR EnsemblBacteria; AAD35294; AAD35294; TM_0202. DR EnsemblBacteria; AGL49126; AGL49126; Tmari_0200. DR GeneID; 897072; -. DR KEGG; tma:TM0202; -. DR KEGG; tmi:THEMA_03720; -. DR KEGG; tmm:Tmari_0200; -. DR KEGG; tmw:THMA_0209; -. DR PATRIC; 23935276; VBITheMar51294_0204. DR eggNOG; ENOG4105NAX; Bacteria. DR eggNOG; COG0715; LUCA. DR KO; K02051; -. DR OMA; VGVHEWK; -. DR OrthoDB; EOG6NPM9G; -. DR BioCyc; TMAR243274:GC6P-215-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR027024; UCP027386_ABC_sbc_TM0202. DR PIRSF; PIRSF027386; UCP027386_ABC_sbc_TM0202; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 300 AA; 33823 MW; 193EBDBFC28E906A CRC64; MKKVTIVVLL LTISILFGET LLNPLGPALI PVVPIMDGKI PTDVKIEIWK NPEEAVAKIV SKEVDFAVLP VTVGANLYGK GVRIKLVGVH EWKVFYLVAS DDATFDGWES LRGQEVYTPH GRGQTVDVLM RYFLSKAGLT LDRDVKILYA PPQEIVALFK SGKVKYAALP EPFVSMCLDR GKVVLDFQKE WGKELGVPGR IPIAGLFVRE GVDKETVEKV EKALIDSIRW MKENLDETVQ LSSEKLGIPA KILKSSLERI EFEYVPVEKC REEVETFLKK LNELYPEGFE KIPDEGFYWK // ID Q9WYQ8_THEMA Unreviewed; 664 AA. AC Q9WYQ8; G4FHY6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Oxidoreductase, putative {ECO:0000313|EMBL:AAD35512.1}; DE SubName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:AGL49349.1}; DE EC=1.3.99.1 {ECO:0000313|EMBL:AGL49349.1}; GN OrderedLocusNames=TM_0427 {ECO:0000313|EMBL:AAD35512.1}; GN ORFNames=Tmari_0424 {ECO:0000313|EMBL:AGL49349.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35512.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35512.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35512.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49349.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49349.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35512.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49349.1; -; Genomic_DNA. DR PIR; C72379; C72379. DR RefSeq; NP_228237.1; NC_000853.1. DR RefSeq; WP_004083312.1; NZ_CP011107.1. DR STRING; 243274.TM0427; -. DR EnsemblBacteria; AAD35512; AAD35512; TM_0427. DR EnsemblBacteria; AGL49349; AGL49349; Tmari_0424. DR GeneID; 897435; -. DR KEGG; tma:TM0427; -. DR KEGG; tmi:THEMA_02590; -. DR KEGG; tmm:Tmari_0424; -. DR KEGG; tmw:THMA_0433; -. DR PATRIC; 23935739; VBITheMar51294_0433. DR eggNOG; ENOG4105W9P; Bacteria. DR eggNOG; COG1053; LUCA. DR OMA; VNNQHMN; -. DR OrthoDB; EOG67X1NV; -. DR BioCyc; TMAR243274:GC6P-442-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:UniProtKB-EC. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR003953; FAD-binding_2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF00890; FAD_binding_2; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49349.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 20 257 FAD_binding_2. FT {ECO:0000259|Pfam:PF00890}. SQ SEQUENCE 664 AA; 75468 MW; 6CCF1757B87B5CF0 CRC64; MRESVVKLNE YTLRIFSLNT IVVGSGAAGL NAVDRVFSFG QKDVALLTDN LKWGTSRNTG SDKQTYYKLT LAGNVPDSVY ELAETLFNGG SMDGDIALVE AALSARAFFR LVELGVPFPH SRYGEYVGYK TDHDPKQRAT SAGPLTSYYM CEKLLEEIRR KGIKIFEGYQ VIGILTDRNE EKTIGLIALD LNNIDDPEKR YVLFNVKNII YATGGPAGMF YFHSVYPPVH FGATGIAFEA GVMGKNLTEW QFGIASKKFR WNLSGTYQQV IPRYVSTDEN GNDEREFLEE YFPDPSTMLN AIFLKGYQWP FDVRKIKNYG SSLIDILVFY ETVIKGRRVW LDFTRNPSWG SKNGELDFSL LGKEAYEYLK NSGALFGRPI DRLEKMNRPA IEVYLQHGID LRKEYLEIGV CAQHNNGGLH GNIWWESNLK HFFPVGEVNG SHGVYRPGGS ALNSGQVGGV RAAQYIVENY SGDPLCEEEI LEEAKDQILK KIELGESFVK KITGKSNVSS ILKEISERSM RSMGIVRSLE EAGKGKNEAL RDFNNLIEKV ELSSIRQLPF AFRLYDVLLT QYVYLSAVEN YIESGGKSRG SYIVHDPTGE LPVPNLPEMF RYSLAGESFN KKIQRVRCKE NRCEFFWDPV KEIPREDTWF ETIWNSFMRR EVFR // ID Q9X131_THEMA Unreviewed; 43 AA. AC Q9X131; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36379.1}; GN OrderedLocusNames=TM_1305 {ECO:0000313|EMBL:AAD36379.1}; GN ORFNames=Tmari_1312 {ECO:0000313|EMBL:AGL50236.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36379.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36379.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36379.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50236.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50236.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36379.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50236.1; -; Genomic_DNA. DR PIR; C72270; C72270. DR RefSeq; NP_229109.1; NC_000853.1. DR RefSeq; WP_008195306.1; NZ_CP011107.1. DR STRING; 243274.TM1305; -. DR EnsemblBacteria; AAD36379; AAD36379; TM_1305. DR EnsemblBacteria; AGL50236; AGL50236; Tmari_1312. DR GeneID; 898177; -. DR KEGG; tma:TM1305; -. DR KEGG; tmi:THEMA_07815; -. DR KEGG; tmm:Tmari_1312; -. DR KEGG; tmw:THMA_1330; -. DR BioCyc; TMAR243274:GC6P-1336-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 43 AA; 4455 MW; F47180F42B657DF5 CRC64; MKIGLVQAGG LVAVLVVAIF LEKSARGCYF AKISALSESA DID // ID Q9X077_THEMA Unreviewed; 332 AA. AC Q9X077; G4FF13; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36061.1}; GN OrderedLocusNames=TM_0982 {ECO:0000313|EMBL:AAD36061.1}; GN ORFNames=Tmari_0985 {ECO:0000313|EMBL:AGL49910.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36061.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36061.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36061.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49910.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49910.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36061.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49910.1; -; Genomic_DNA. DR PIR; C72310; C72310. DR RefSeq; NP_228790.1; NC_000853.1. DR RefSeq; WP_004080582.1; NZ_CP011107.1. DR STRING; 243274.TM0982; -. DR EnsemblBacteria; AAD36061; AAD36061; TM_0982. DR EnsemblBacteria; AGL49910; AGL49910; Tmari_0985. DR GeneID; 898728; -. DR KEGG; tma:TM0982; -. DR KEGG; tmi:THEMA_09440; -. DR KEGG; tmm:Tmari_0985; -. DR KEGG; tmw:THMA_1004; -. DR PATRIC; 23936893; VBITheMar51294_0995. DR eggNOG; ENOG4105CUC; Bacteria. DR eggNOG; COG2391; LUCA. DR KO; K07112; -. DR OMA; AQMLMIG; -. DR OrthoDB; EOG6WDSMK; -. DR BioCyc; TMAR243274:GC6P-1012-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007272; Sulf_transp. DR Pfam; PF04143; Sulf_transp; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 64 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 95 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 154 178 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 190 209 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 245 264 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 276 299 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 305 328 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 18 322 Sulf_transp. {ECO:0000259|Pfam:PF04143}. SQ SEQUENCE 332 AA; 35572 MW; 19774CE93DB4CAAD CRC64; MVWTGLLIGV LFGVILQRGR ICFNSAFRDV LIFKDNYLMR LAALTLGLES ITLLIFAQAG IITLNPKPLN WIGNIIGGFI FGMGMVLAGG CASGVTYRTG EGMTTAWFAA LAYALTAHAT KKGLFSGWIK WLSNYTVTVS NTNPVYAPKT GPTIATVLGI SPWIASIIFL ALMLWYAFGV KNKSQRPSKL NWIAASVLIA ILAPIAWWAS ASTGRNYGLG ITGGWINLVS VYANNASLNW EGAEILGIII GAAISAIAGK EFKLRMPKNP KTYAQVLLGG FLMGFGAVTA GGCNIGHFLT GVPTLAISSI VASIFFILGN WTMAWFLFGR QK // ID Q9WYD2_THEMA Unreviewed; 315 AA. AC Q9WYD2; G4FHL0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Fructokinase {ECO:0000313|EMBL:AAD35384.1}; DE EC=2.7.1.4 {ECO:0000313|EMBL:AGL49220.1}; GN OrderedLocusNames=TM_0296 {ECO:0000313|EMBL:AAD35384.1}; GN ORFNames=Tmari_0294 {ECO:0000313|EMBL:AGL49220.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35384.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35384.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35384.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49220.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49220.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35384.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49220.1; -; Genomic_DNA. DR PIR; H72394; H72394. DR RefSeq; NP_228108.1; NC_000853.1. DR RefSeq; WP_004083014.1; NZ_CP011107.1. DR STRING; 243274.TM0296; -. DR EnsemblBacteria; AAD35384; AAD35384; TM_0296. DR EnsemblBacteria; AGL49220; AGL49220; Tmari_0294. DR GeneID; 897221; -. DR KEGG; tma:TM0296; -. DR KEGG; tmi:THEMA_03245; -. DR KEGG; tmm:Tmari_0294; -. DR KEGG; tmw:THMA_0303; -. DR PATRIC; 23935471; VBITheMar51294_0301. DR eggNOG; ENOG4105D7K; Bacteria. DR eggNOG; COG0524; LUCA. DR KO; K00847; -. DR OMA; QWLHVCS; -. DR OrthoDB; EOG6716JN; -. DR BioCyc; TMAR243274:GC6P-309-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008865; F:fructokinase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF00294; PfkB; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR PROSITE; PS00583; PFKB_KINASES_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|SAAS:SAAS00446051, ECO:0000313|EMBL:AAD35384.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00446051, KW ECO:0000313|EMBL:AAD35384.1}. FT DOMAIN 2 301 PfkB. {ECO:0000259|Pfam:PF00294}. SQ SEQUENCE 315 AA; 34995 MW; 133FA536FB3ACB87 CRC64; MNVLCTGEIL IDFISEDKGK NLSQSELFRK KAGGSPLNVA VALKRLGREV SFLGKLGGDQ FSEFLLEVMK KEGIDTTHII FDSSCKTTLA FVARDAQGNP DFVFFREKPA DTNLRPEEVN IDPAQFSFLH IGSYSLAVEP SRSAYLKVME TFLEEGKPVS YDPNVRPSLI EDRNTFVKDF LEISSKVDIV KLSDKDLEYI FQEDLETAVD KIPIKENGLL FVTMGERGCL VKFKGEKRMV PSFKVKPVDA TGCGDSFTAA VIHKYLEKTP ETIEDAVEIG KFANAVAAIV ITRVGGVDAM PVLDEVEMFL SNQER // ID Q9WZ60_THEMA Unreviewed; 242 AA. AC Q9WZ60; G4FDM8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE SubName: Full=Amino acid ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35676.1}; GN OrderedLocusNames=TM_0591 {ECO:0000313|EMBL:AAD35676.1}; GN ORFNames=Tmari_0590 {ECO:0000313|EMBL:AGL49515.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35676.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35676.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35676.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49515.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49515.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35676.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49515.1; -; Genomic_DNA. DR PIR; H72356; H72356. DR RefSeq; NP_228401.1; NC_000853.1. DR RefSeq; WP_004081262.1; NZ_CP011107.1. DR SMR; Q9WZ60; 1-238. DR STRING; 243274.TM0591; -. DR EnsemblBacteria; AAD35676; AAD35676; TM_0591. DR EnsemblBacteria; AGL49515; AGL49515; Tmari_0590. DR GeneID; 897665; -. DR KEGG; tma:TM0591; -. DR KEGG; tmi:THEMA_01705; -. DR KEGG; tmm:Tmari_0590; -. DR KEGG; tmw:THMA_0607; -. DR eggNOG; ENOG4105CDA; Bacteria. DR eggNOG; COG1126; LUCA. DR KO; K02028; -. DR OMA; RIGGEMY; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-616-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0015424; F:amino acid-transporting ATPase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR030679; ABC_ATPase_HisP-typ. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR PIRSF; PIRSF039085; ABC_ATPase_HisP; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35676.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35676.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 236 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 242 AA; 27613 MW; 26F4B271C88FDE03 CRC64; MTVLKIEDLH KYFGKLYVLR GIDLEVKKGE VISIIGPSGS GKSTLLRCIN LLEEYQRGKI YFKGELITHR NINRIRSSIG MVFQQFNLFP HLSVLNNLTL APMKVKNMQK DEAVEKAKKL LERVGLIEKI NEKPGNLSGG QQQRVAIARA LMMDPELMLF DEPTSALDPE LVKEVLDVIK DLAQSGMTML IVTHEMRFAR DVSDRVVFMD EGRIVEMGPP EKIFSNPENE RTREFLEHFL SV // ID Q9WZT3_THEMA Unreviewed; 56 AA. AC Q9WZT3; G4FCZ8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35908.1}; GN OrderedLocusNames=TM_0826 {ECO:0000313|EMBL:AAD35908.1}; GN ORFNames=Tmari_0828 {ECO:0000313|EMBL:AGL49753.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35908.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35908.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35908.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49753.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49753.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35908.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49753.1; -; Genomic_DNA. DR PIR; F72327; F72327. DR RefSeq; NP_228635.1; NC_000853.1. DR RefSeq; WP_004080827.1; NZ_CP011107.1. DR STRING; 243274.TM0826; -. DR DNASU; 898496; -. DR EnsemblBacteria; AAD35908; AAD35908; TM_0826. DR EnsemblBacteria; AGL49753; AGL49753; Tmari_0828. DR GeneID; 898496; -. DR KEGG; tma:TM0826; -. DR KEGG; tmi:THEMA_00510; -. DR KEGG; tmm:Tmari_0828; -. DR KEGG; tmw:THMA_0847; -. DR PATRIC; 23936578; VBITheMar51294_0839. DR OMA; RDNDEKQ; -. DR OrthoDB; EOG6BPDNX; -. DR BioCyc; TMAR243274:GC6P-855-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 56 AA; 6597 MW; 4EC855C826871A5D CRC64; MEKKVSRNPR VLSQIDLLKL MTDGDESALR EIKRRLGLDE KKERDNDEKQ KVSDKI // ID Q9X1L3_THEMA Unreviewed; 140 AA. AC Q9X1L3; G4FFR5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 102. DE SubName: Full=Rrf2 family transcriptional regulator {ECO:0000313|EMBL:AGL50459.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36594.1}; GN OrderedLocusNames=TM_1527 {ECO:0000313|EMBL:AAD36594.1}; GN ORFNames=Tmari_1535 {ECO:0000313|EMBL:AGL50459.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36594.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36594.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36594.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50459.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50459.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36594.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50459.1; -; Genomic_DNA. DR PIR; C72241; C72241. DR RefSeq; NP_229327.1; NC_000853.1. DR RefSeq; WP_004081895.1; NZ_CP011107.1. DR STRING; 243274.TM1527; -. DR EnsemblBacteria; AAD36594; AAD36594; TM_1527. DR EnsemblBacteria; AGL50459; AGL50459; Tmari_1535. DR GeneID; 897480; -. DR KEGG; tma:TM1527; -. DR KEGG; tmi:THEMA_06655; -. DR KEGG; tmm:Tmari_1535; -. DR KEGG; tmw:THMA_1561; -. DR PATRIC; 23938014; VBITheMar51294_1545. DR eggNOG; ENOG4108AEZ; Bacteria. DR eggNOG; COG1959; LUCA. DR OMA; APAVFEC; -. DR OrthoDB; EOG6JTCBF; -. DR BioCyc; TMAR243274:GC6P-1567-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR030489; TR_Rrf2-type_CS. DR InterPro; IPR000944; Tscrpt_reg_Rrf2-type. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02082; Rrf2; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR TIGRFAMs; TIGR00738; rrf2_super; 1. DR PROSITE; PS01332; HTH_RRF2_1; 1. DR PROSITE; PS51197; HTH_RRF2_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 140 AA; 16201 MW; D9F431C47D06A3BA CRC64; MFGKCQKHVR YALRLLVRLS LENRPMSSSE LAEKELITRN FALKVLHYLK RSGLVNSIKG KNGGFVLAKS PDEISFLDVI SVFEKDLVIV DCNSRCKNYR ACRVKYFWNW LSDYLKDLFS NITIKDIASG TFTFHLEKLS // ID Q9X0P9_THEMA Unreviewed; 374 AA. AC Q9X0P9; G4FEI0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 98. DE SubName: Full=Oxygen-independent coproporphyrinogen III oxidase, putative {ECO:0000313|EMBL:AAD36242.1}; DE SubName: Full=Putative coproporphyrinogen III oxidase of BS HemN-type, oxygen-independent {ECO:0000313|EMBL:AGL50097.1}; DE EC=1.3.99.22 {ECO:0000313|EMBL:AGL50097.1}; GN OrderedLocusNames=TM_1166 {ECO:0000313|EMBL:AAD36242.1}; GN ORFNames=Tmari_1173 {ECO:0000313|EMBL:AGL50097.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36242.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36242.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36242.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50097.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50097.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36242.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50097.1; -; Genomic_DNA. DR PIR; D72288; D72288. DR RefSeq; NP_228972.1; NC_000853.1. DR RefSeq; WP_004080203.1; NZ_CP011107.1. DR STRING; 243274.TM1166; -. DR EnsemblBacteria; AAD36242; AAD36242; TM_1166. DR EnsemblBacteria; AGL50097; AGL50097; Tmari_1173. DR GeneID; 898320; -. DR KEGG; tma:TM1166; -. DR KEGG; tmi:THEMA_08505; -. DR KEGG; tmm:Tmari_1173; -. DR KEGG; tmw:THMA_1191; -. DR PATRIC; 23937269; VBITheMar51294_1183. DR eggNOG; ENOG4105CSA; Bacteria. DR eggNOG; COG0635; LUCA. DR KO; K02495; -. DR OMA; PFCVRKC; -. DR OrthoDB; EOG683S9D; -. DR BioCyc; TMAR243274:GC6P-1195-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0051989; F:coproporphyrinogen dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR004559; Coprogen_oxidase_HemN-rel. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00539; hemN_rel; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50097.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 219 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 374 AA; 43687 MW; E1D72D52EBD4D0A9 CRC64; MKLAVYVHVP FCKSKCVYCD FYSVVSEKFD EYFSHLLREI DLYEEVLSES EIKTVYFGGG TPSVVPPSFL KMVLEKLERV SRGFTPDEIT IEVNPESVET EKLKIYKQIG INRISLGVQA CDDTVLKNAG RLYKEETLKK KAKIVLEQFE NVNFDFILGL PGETDITLKK DFRFLEEFPP QHVSLYLLEV DERTRLFDLI QKGLVELPEE DDVERRHDLF VEFLKERGFL RYEISNFAKP GKKSLHNLFY WRNENYLGLG VSAGGHIGRF RYVNASDLKE YEEKITKGEL PYEYVHENTE EEEALETVFM GLRIKEGVEL NRVKILLPLL EKLQKKYPCY LKVKNGKIFL SEDGMNFSKK ILSDLIEWYR EGGR // ID Q9WZ68_THEMA Unreviewed; 546 AA. AC Q9WZ68; G4FDM0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Polymerase/histidinol phosphatase {ECO:0000313|EMBL:AGL49523.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35684.1}; GN OrderedLocusNames=TM_0599 {ECO:0000313|EMBL:AAD35684.1}; GN ORFNames=Tmari_0598 {ECO:0000313|EMBL:AGL49523.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35684.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35684.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35684.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49523.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49523.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35684.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49523.1; -; Genomic_DNA. DR PIR; H72357; H72357. DR RefSeq; NP_228409.1; NC_000853.1. DR RefSeq; WP_004081241.1; NZ_CP011107.1. DR STRING; 243274.TM0599; -. DR EnsemblBacteria; AAD35684; AAD35684; TM_0599. DR EnsemblBacteria; AGL49523; AGL49523; Tmari_0598. DR GeneID; 897675; -. DR KEGG; tma:TM0599; -. DR KEGG; tmi:THEMA_01670; -. DR KEGG; tmm:Tmari_0598; -. DR KEGG; tmw:THMA_0615; -. DR PATRIC; 23936113; VBITheMar51294_0610. DR eggNOG; ENOG4108MI5; Bacteria. DR eggNOG; ENOG410Z1K5; LUCA. DR OMA; GHINVYE; -. DR OrthoDB; EOG6038SN; -. DR BioCyc; TMAR243274:GC6P-624-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; SSF89550; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 22 98 POLIIIAc. {ECO:0000259|SMART:SM00481}. SQ SEQUENCE 546 AA; 62048 MW; 1A432BD1522E63AF CRC64; MKKLVLLILI LSCAVFGELF YGNLHSHTSY SDGSGTPDQA YEYAKRYLDV LAVTDHAYYF AQKINGKTKP YLTKLAAERH TKDGEFVALQ GFEWTAGVGH INVYESLEWI DRNQESSLEG FYRWLVEHKK LAQFNHPIST FGTFDSFRYF PEADQYVNLI EVGNGNWSSG DVINEEMFGN YILALNKGWH LGATVGQDNH KPNWGSANEG RTGIVADTLT YDDIMDALWK RHTFGSEDKN VKALLKSGSH LMGDIVSVED LSPQKISLEY EDTEKLLYLA VISQSGTVLE LRPNTERLNL TLSVTPPDGY EWYFVYMKQF DGDEIVTSPI WFQTPSPVYV NSVRVSPEEI HDGESAKVYF EIYNVTGEDQ NVKLSVLLDE NPLREVELSF SPYQVKRFVV PTGSLEKGYH RVSFVVDGKL VQSSGFSVKE KQKGVIMIDT LHENDHLEEL KALAEELEKR GYNVKYPKVM LKDLEGVDIL IISTPKEGGL SFAKKLSNKE IEAIENFKGK IYIVPGGDEE YRKLYLEKIK GEVVTLEELR KKLLEE // ID Q9WXT5_THEMA Unreviewed; 329 AA. AC Q9WXT5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Iron(III) ABC transporter, periplasmic-binding protein, putative {ECO:0000313|EMBL:AAD35174.1}; DE SubName: Full=Vitamin B12 ABC transporter, B12-binding component BtuF {ECO:0000313|EMBL:AGL49003.1}; GN OrderedLocusNames=TM_0080 {ECO:0000313|EMBL:AAD35174.1}; GN ORFNames=Tmari_0077 {ECO:0000313|EMBL:AGL49003.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35174.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35174.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35174.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49003.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49003.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains Fe/B12 periplasmic-binding domain. CC {ECO:0000256|SAAS:SAAS00514624}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35174.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49003.1; -; Genomic_DNA. DR PIR; H72421; H72421. DR RefSeq; NP_227896.1; NC_000853.1. DR RefSeq; WP_010865044.1; NZ_CP011107.1. DR STRING; 243274.TM0080; -. DR EnsemblBacteria; AAD35174; AAD35174; TM_0080. DR EnsemblBacteria; AGL49003; AGL49003; Tmari_0077. DR GeneID; 896907; -. DR KEGG; tma:TM0080; -. DR KEGG; tmm:Tmari_0077; -. DR KEGG; tmw:THMA_0076; -. DR PATRIC; 23935000; VBITheMar51294_0078. DR eggNOG; ENOG4107X30; Bacteria. DR eggNOG; COG0614; LUCA. DR KO; K02016; -. DR OMA; IAGPNGW; -. DR OrthoDB; EOG63Z761; -. DR BioCyc; TMAR243274:GC6P-80-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0036094; F:small molecule binding; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR002491; ABC_transptr_periplasmic_BD. DR Pfam; PF01497; Peripla_BP_2; 1. DR PROSITE; PS50983; FE_B12_PBP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 55 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 70 327 Fe/B12 periplasmic-binding. FT {ECO:0000259|PROSITE:PS50983}. SQ SEQUENCE 329 AA; 35989 MW; 316F5917AB452211 CRC64; MIRKPGNPPA VKGNHLPRHQ EGGNILFQGG MEVFRKLVSL ILLFVTAVAL AVTVVDNAGR VVEITSAPER VVSLSPAATR FLVFLGLEDK IVGVTDYDSY EAEKVGAMVP VNIEKVVSLN PDLVLMFGGF QLPEVPKLEK AGLKVLVVNP NSLNDIIRDV VLLGTIFDRR DLALEKSEKL REKMLEIGKK TYNVPPSKRP KVLYLISSPG PDVKEIWTCG MGSYLNEIIS LAGGVNIASG IAGPNGWPQL SIEYVVSQNP DVIIVGVYIP GTENEEIKKI LNFEPFKEIN AVKNKRVFAV DGNVASQPSP DVFELLDLFY EFFYGGKGE // ID Q9WZJ5_THEMA Unreviewed; 278 AA. AC Q9WZJ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Mannose-6-phosphate isomerase {ECO:0000313|EMBL:AAD35817.1}; DE EC=5.3.1.8 {ECO:0000313|EMBL:AGL49662.1}; GN OrderedLocusNames=TM_0736 {ECO:0000313|EMBL:AAD35817.1}; GN ORFNames=Tmari_0737 {ECO:0000313|EMBL:AGL49662.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35817.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35817.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35817.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49662.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49662.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35817.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49662.1; -; Genomic_DNA. DR PIR; C72339; C72339. DR RefSeq; NP_228545.1; NC_000853.1. DR RefSeq; WP_010865195.1; NZ_CP011107.1. DR STRING; 243274.TM0736; -. DR EnsemblBacteria; AAD35817; AAD35817; TM_0736. DR EnsemblBacteria; AGL49662; AGL49662; Tmari_0737. DR GeneID; 898403; -. DR KEGG; tma:TM0736; -. DR KEGG; tmi:THEMA_00975; -. DR KEGG; tmm:Tmari_0737; -. DR KEGG; tmw:THMA_0754; -. DR PATRIC; 23936392; VBITheMar51294_0749. DR eggNOG; ENOG4105DG6; Bacteria. DR eggNOG; COG1482; LUCA. DR KO; K01809; -. DR OMA; FECEYFR; -. DR BioCyc; TMAR243274:GC6P-762-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR001250; Man6P_Isoase-1. DR InterPro; IPR014628; Man6P_isomerase_Firm_short. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF01238; PMI_typeI; 1. DR PIRSF; PIRSF036894; PMI_Firm_short; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000313|EMBL:AAD35817.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 278 AA; 31960 MW; CEF7050D5F095902 CRC64; MMIKVFPKLR KQIWGSYRLG EMFGSNEKIG EVWLLSGHPL FITEAEGGLD LNEDMEKLIG KKLPRFPLLV KLISAEDWLS VQVHPNDDEA QELENEPWGK TEAWYFVEKG QIAIGEDPEK VKRALEDNSW DEALKKVEIE PGTFVFLPAG TVHALGPGGL LVEVQQASDL TYRVYDWGRG RELHIEKAFK VMKERKVEDL IVENFENFEC EYFRIEKLER GKLEGFCAIV ILENGVLDNR QVSPFETFIV PKGEKAELRA TALVMRIGKF FEQWGDKK // ID Q9WZA7_THEMA Unreviewed; 400 AA. AC Q9WZA7; G4FDI4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35723.1}; GN OrderedLocusNames=TM_0639 {ECO:0000313|EMBL:AAD35723.1}; GN ORFNames=Tmari_0640 {ECO:0000313|EMBL:AGL49565.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35723.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35723.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35723.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49565.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49565.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35723.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49565.1; -; Genomic_DNA. DR PIR; F72350; F72350. DR RefSeq; NP_228448.1; NC_000853.1. DR RefSeq; WP_004081158.1; NZ_CP011107.1. DR STRING; 243274.TM0639; -. DR EnsemblBacteria; AAD35723; AAD35723; TM_0639. DR EnsemblBacteria; AGL49565; AGL49565; Tmari_0640. DR GeneID; 897740; -. DR KEGG; tma:TM0639; -. DR KEGG; tmi:THEMA_01465; -. DR KEGG; tmm:Tmari_0640; -. DR KEGG; tmw:THMA_0655; -. DR PATRIC; 23936191; VBITheMar51294_0649. DR eggNOG; ENOG4108ZNC; Bacteria. DR eggNOG; ENOG4111P2X; LUCA. DR OMA; PYEYTYF; -. DR OrthoDB; EOG63NMDH; -. DR BioCyc; TMAR243274:GC6P-664-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 400 AA; 45852 MW; EC0B5831F7C2414A CRC64; MKRNLFLLIL LPALVFAGGS VSFDLSYEGS FRWTGELDWT LPLFRDWAFS FEVGVGKGYG IVHTGIIDEL KKFVEFYYFP EAFVSGKIGP FELKAGILNE ERGPGIDKLF LDDNSRFYGF PGVSLKYRQD NWHVESLWLN INEEKSFNYR TVVFDFGLLK IAYEDAVVYL NEVFNPYYFF VPLPPIAIQE IWLSQEGAPW KDESKNANAL MGGWIEFNFG AGRVYFEALI DDMSLNRLLG TGSYLNPDKV ALLLGGEYRT GAWKIYGEVS GASAYTFERT QENLPYEYTY FDTGKIEERM IGYKYGENSF SLKLGVRRFS GWCTLDLMYH YLVYGDRTPE TPWHGKEMPP DTKWLIGDLT KEHTLKVSAE SDFGEYGGKV EVWWSSLEGI GAGVFLSFKM // ID Q9WYP9_THEMA Unreviewed; 443 AA. AC Q9WYP9; G4FHX7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Myo-inositol ABC transporter, periplasmic sugar-binding protein InoE {ECO:0000313|EMBL:AGL49340.1}; DE SubName: Full=Sugar ABC transporter, periplasmic sugar-binding protein, putative {ECO:0000313|EMBL:AAD35503.1}; GN OrderedLocusNames=TM_0418 {ECO:0000313|EMBL:AAD35503.1}; GN ORFNames=Tmari_0415 {ECO:0000313|EMBL:AGL49340.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35503.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35503.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35503.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49340.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49340.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35503.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49340.1; -; Genomic_DNA. DR PIR; B72378; B72378. DR RefSeq; NP_228228.1; NC_000853.1. DR RefSeq; WP_004083271.1; NZ_CP011107.1. DR STRING; 243274.TM0418; -. DR TCDB; 3.A.1.1.38; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35503; AAD35503; TM_0418. DR EnsemblBacteria; AGL49340; AGL49340; Tmari_0415. DR GeneID; 897420; -. DR KEGG; tma:TM0418; -. DR KEGG; tmi:THEMA_02635; -. DR KEGG; tmm:Tmari_0415; -. DR KEGG; tmw:THMA_0424; -. DR PATRIC; 23935719; VBITheMar51294_0423. DR eggNOG; ENOG4105KD9; Bacteria. DR eggNOG; COG2182; LUCA. DR HOGENOM; HOG000036385; -. DR KO; K17237; -. DR OMA; GIPQDAE; -. DR OrthoDB; EOG6NSGCC; -. DR BioCyc; TMAR243274:GC6P-433-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR006059; SBP_1_dom. DR Pfam; PF01547; SBP_bac_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 443 AA; 51361 MW; 7D2C62A7EB2C564C CRC64; MRKFLMTIVL MVSLLIFAEE ITITAWTVGP DNPSYYRFDN LKTAAERLNK ILKDLGVDLT IKVDGYFDTT DWSSFKQKVV FGIKSGQTVD IICSGHDDIG AWAKAGYIIP LDEYVKKYWD EVYYDFIPSL WESTKYKGQI YGIPQDTEAR PFYINKQVLK KLGWSDEEIN SLPDRIARGE FTFEDFIEVA REAIEKGLVE WGLYHRPKAG IDYYQLMISM GIDFYDEEKA VFVYNVEEMK DYYKLLYDLA NTYKILPKNM IGTPWTSVHK DVTGGKVLAW MGGTWNWAEW KKDYGKTEEE LQEMFILAPV PKFRDRGRPN TLSHPVVYMI PSTSKYPDIA FLLITLASAP ELNMRHAVES GHLPIRWQQT VLPEYTKEFI MMEGTKLLPY SGFIPNDDMF NLYNQIIFEG MQMAESGMNP EKVAEDVAKR LKSQLKDRVV IIE // ID Q9X1R8_THEMA Unreviewed; 147 AA. AC Q9X1R8; G4FFX0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=DUF458 domain-containing protein {ECO:0000313|EMBL:AGL50514.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36649.1}; GN OrderedLocusNames=TM_1582 {ECO:0000313|EMBL:AAD36649.1}; GN ORFNames=Tmari_1590 {ECO:0000313|EMBL:AGL50514.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36649.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36649.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36649.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50514.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50514.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36649.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50514.1; -; Genomic_DNA. DR PIR; F72235; F72235. DR RefSeq; NP_229382.1; NC_000853.1. DR RefSeq; WP_004082010.1; NZ_CP011107.1. DR STRING; 243274.TM1582; -. DR DNASU; 897417; -. DR EnsemblBacteria; AAD36649; AAD36649; TM_1582. DR EnsemblBacteria; AGL50514; AGL50514; Tmari_1590. DR GeneID; 897417; -. DR KEGG; tma:TM1582; -. DR KEGG; tmi:THEMA_06370; -. DR KEGG; tmm:Tmari_1590; -. DR KEGG; tmw:THMA_1617; -. DR PATRIC; 23938128; VBITheMar51294_1601. DR eggNOG; ENOG4108XRC; Bacteria. DR eggNOG; COG1978; LUCA. DR KO; K09776; -. DR OMA; FINDVGR; -. DR OrthoDB; EOG66TG7R; -. DR BioCyc; TMAR243274:GC6P-1623-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR007405; Phage_KVP40_Orf299. DR Pfam; PF04308; RNaseH_like; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 147 AA; 16648 MW; A0978F4EE71347F8 CRC64; MKSPTWGKVD YRTVRELIKK FTEGYKYSVF VGTDSDVKDG KVIYATALVV YRFGSGATYF YTVYRDGNGK DLYSRIFKEA EMSLEMARFV EEILKLGKPV VHLDIGYEGL TKDLVSSVIG YVKGVGYPYQ IKPDSFAATK IAHKHTK // ID Q9X044_THEMA Unreviewed; 217 AA. AC Q9X044; G4FF43; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36028.1}; GN OrderedLocusNames=TM_0947 {ECO:0000313|EMBL:AAD36028.1}; GN ORFNames=Tmari_0949 {ECO:0000313|EMBL:AGL49874.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36028.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36028.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36028.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49874.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49874.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36028.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49874.1; -; Genomic_DNA. DR PIR; F72313; F72313. DR RefSeq; NP_228755.1; NC_000853.1. DR RefSeq; WP_004080615.1; NC_000853.1. DR EnsemblBacteria; AAD36028; AAD36028; TM_0947. DR EnsemblBacteria; AGL49874; AGL49874; Tmari_0949. DR GeneID; 898684; -. DR KEGG; tma:TM0947; -. DR KEGG; tmm:Tmari_0949; -. DR PATRIC; 23936825; VBITheMar51294_0961. DR eggNOG; ENOG4105E2F; Bacteria. DR eggNOG; COG4923; LUCA. DR OMA; SHPELCF; -. DR OrthoDB; EOG6PS5TQ; -. DR BioCyc; TMAR243274:GC6P-977-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR007362; DUF429. DR Pfam; PF04250; DUF429; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 217 AA; 25491 MW; D730B6780E06AB21 CRC64; MYSIVEGDRV LEIGFMEHFM FLDFPTLVDI PIGLPKKGER ECDRLTRRIL SKRAASVFTV PCRVAVYRES YEDALRVNRE CQGKGFPVQF WHIVEKVREV DVFLRSYPDL SDQIRESHPE LCFLRISSKM MKSKHTREGL NQRIEILREH LVFDVENLQR ICREYRIHIH DVLDSLVLAL AQQFPLERIP EDPPLDEHGL PMQIIAPART QRSPNPE // ID Q9WYH7_THEMA Unreviewed; 413 AA. AC Q9WYH7; G4FHQ4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Permease, putative {ECO:0000313|EMBL:AAD35428.1}; GN OrderedLocusNames=TM_0342 {ECO:0000313|EMBL:AAD35428.1}; GN ORFNames=Tmari_0340 {ECO:0000313|EMBL:AGL49265.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35428.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35428.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35428.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49265.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49265.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35428.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49265.1; -; Genomic_DNA. DR PIR; D72388; D72388. DR RefSeq; NP_228153.1; NC_000853.1. DR RefSeq; WP_004083122.1; NZ_CP011107.1. DR STRING; 243274.TM0342; -. DR EnsemblBacteria; AAD35428; AAD35428; TM_0342. DR EnsemblBacteria; AGL49265; AGL49265; Tmari_0340. DR GeneID; 897298; -. DR KEGG; tma:TM0342; -. DR KEGG; tmi:THEMA_03005; -. DR KEGG; tmm:Tmari_0340; -. DR KEGG; tmw:THMA_0350; -. DR PATRIC; 23935565; VBITheMar51294_0347. DR eggNOG; ENOG4107SFI; Bacteria. DR eggNOG; COG0477; LUCA. DR OMA; QLGWAVQ; -. DR OrthoDB; EOG6PW21X; -. DR BioCyc; TMAR243274:GC6P-356-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 45 68 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 162 190 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 224 246 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 258 280 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 292 311 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 317 336 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 357 379 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 385 406 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 10 410 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 413 AA; 46382 MW; AD39CAE75AC91FA8 CRC64; MNEILHWKRN FFLLALGRFV SILGSSVQAV AIPLFVLDLT HSGSAVALMT VAYMVPRILF TPIAGIVGDR GDRKFLMVSM DFLRGFLICF LALLAFRNSI TLPVLYVSQI AMAIMDNLFD IPTGAMFPDI VPQDFLMRAN SIMGMVRIFP QILGPALGGV IYGFYGIAIV FLVNGVSFVL SAISEIFIVY SRKVEKKPAK FSQILEDLKE GFLFIWNHEL IRTILIFALF LNLLISPLFM VVYPYTIREV MKFSAQEFGF LETSFTLGAL LGNFLIASYL SKKNMWKAMK ISIFLFELPI VFLGFLVMPD FSLNRLVLFS LFFITFLIMG FLNPIINVPL DTAFQKMTPS HIRARAFSFL ILVANGVTPL GSVLYGYLVD RVPVHFLYYV VGALSFLVAV LLLVALRGKE LPT // ID Q9WY30_THEMA Unreviewed; 368 AA. AC Q9WY30; G4FHA0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 105. DE SubName: Full=Response regulator {ECO:0000313|EMBL:AAD35279.1}; GN OrderedLocusNames=TM_0186 {ECO:0000313|EMBL:AAD35279.1}; GN ORFNames=Tmari_0184 {ECO:0000313|EMBL:AGL49110.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35279.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35279.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35279.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49110.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49110.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35279.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49110.1; -; Genomic_DNA. DR PIR; E72408; E72408. DR RefSeq; NP_228001.1; NC_000853.1. DR RefSeq; WP_004082825.1; NZ_CP011107.1. DR STRING; 243274.TM0186; -. DR EnsemblBacteria; AAD35279; AAD35279; TM_0186. DR EnsemblBacteria; AGL49110; AGL49110; Tmari_0184. DR GeneID; 897034; -. DR KEGG; tma:TM0186; -. DR KEGG; tmm:Tmari_0184; -. DR KEGG; tmw:THMA_0187; -. DR PATRIC; 23935228; VBITheMar51294_0187. DR eggNOG; ENOG4105DW3; Bacteria. DR eggNOG; COG3437; LUCA. DR KO; K07814; -. DR OMA; KICQPLR; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-192-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR Pfam; PF01966; HD; 1. DR Pfam; PF00072; Response_reg; 1. DR SMART; SM00471; HDc; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 114 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. SQ SEQUENCE 368 AA; 41788 MW; FBF5E61DB5738BCC CRC64; MTVLIVEDDD ITREAMGQYL KLSGFNVIEA ENGEKAVELS ENVDVALVDV MLPGMSGIEV VNKIKAKNPS CVVFVVTAYD DTEIVKKCVE AGADDFIKKP VNLELLRLKI THALRNRVFH MYRNSYLKSL KKKLFLLEKT AEEFFTEYED FLFEVLEILN MLSEYRDMET HRHTERVGWL SGRIAEEMGM SEVFVTEIQF AAPLHDIGKI GIPDRILLKP GILTPEEFEI MKQHTTIGFR ILSRSNSPIL QLGAEIALTH HERWDGSGYP RGLKEREIPI SGLIVAVADS FDAMVSRRPY KNPKPLEEAF REIESLSGKL YSPEVVEAFL KLEKEITDVY RREKDEDTSH NGGRSHQSSP GEGVEGIR // ID Q9X144_THEMA Unreviewed; 564 AA. AC Q9X144; G4FI07; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 120. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36392.1}; DE SubName: Full=Phospholipid-lipopolysaccharide ABC transporter {ECO:0000313|EMBL:AGL50250.1}; GN OrderedLocusNames=TM_1319 {ECO:0000313|EMBL:AAD36392.1}; GN ORFNames=Tmari_1326 {ECO:0000313|EMBL:AGL50250.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36392.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36392.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36392.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50250.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50250.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36392.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50250.1; -; Genomic_DNA. DR PIR; F72268; F72268. DR RefSeq; NP_229122.1; NC_000853.1. DR RefSeq; WP_004083354.1; NZ_CP011107.1. DR STRING; 243274.TM1319; -. DR EnsemblBacteria; AAD36392; AAD36392; TM_1319. DR EnsemblBacteria; AGL50250; AGL50250; Tmari_1326. DR GeneID; 898163; -. DR KEGG; tma:TM1319; -. DR KEGG; tmi:THEMA_07750; -. DR KEGG; tmm:Tmari_1326; -. DR KEGG; tmw:THMA_1343; -. DR PATRIC; 23937577; VBITheMar51294_1334. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K06148; -. DR OMA; VTMIVEM; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1350-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0034040; F:lipid-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0006869; P:lipid transport; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD36392.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD36392.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 58 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 244 265 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 271 292 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 18 300 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 330 560 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 564 AA; 63837 MW; 5D5894B08ABF2C72 CRC64; MKTGKFRLLR KNHIALAVLT TASLVASGFF YSRRVTLLQS AVDRAIHSKE LSSFLGDILL FLVFLLLTII FDFLASFMSA VNNVGMFKNL VRSQIRLMLD ADMLELKKQN TGEIITRMFD DGWYIISLYS STIPDLVATS FKVGLLVFVF YQLSPRILLI ALLLSPLYSF PLSSPRRRIM EHQEKERSSF EKCVKFINET LSGAAVIKAF ESKRFFYKEF GKLTNLWLNT SNTLFNVVAK TESLYPFLNG LLPILVVALS SFLIAKKEIT IGSAISFFYF ISGFYSSISN VYSSVLDIMR SRTYKERISE VMELSAEKGG GKELGDFKQM SLQNVSFGYP DGGEILTDLN IKIDAGDRVA IVASSGEGKS TLVSLFNRFL TPTKGQILIN DIPIEQYSLS SLRKKIILVR SNDILFDTTI KNNITLFEDF PEDELERILR MCECDFVEKL ENGIHTVVGE RGTKLSDGQR QRIVLARALI RKPQVLILDE ATSGVDSETE EKIFEKILKE INTVIIISHR LSTIRKAKKI IVLNNGRVEA EGTHEELMEK SPLYREIVRS QLEV // ID Q9WXY9_THEMA Unreviewed; 329 AA. AC Q9WXY9; G4FH50; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35229.1}; GN OrderedLocusNames=TM_0136 {ECO:0000313|EMBL:AAD35229.1}; GN ORFNames=Tmari_0134 {ECO:0000313|EMBL:AGL49060.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35229.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35229.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35229.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49060.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49060.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35229.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49060.1; -; Genomic_DNA. DR PIR; F72413; F72413. DR RefSeq; NP_227951.1; NC_000853.1. DR RefSeq; WP_004082729.1; NZ_CP011107.1. DR STRING; 243274.TM0136; -. DR EnsemblBacteria; AAD35229; AAD35229; TM_0136. DR EnsemblBacteria; AGL49060; AGL49060; Tmari_0134. DR GeneID; 896963; -. DR KEGG; tma:TM0136; -. DR KEGG; tmm:Tmari_0134; -. DR KEGG; tmw:THMA_0131; -. DR PATRIC; 23935114; VBITheMar51294_0135. DR eggNOG; ENOG4108MSG; Bacteria. DR eggNOG; COG0820; LUCA. DR KO; K06941; -. DR OMA; GRFQLQF; -. DR OrthoDB; EOG6JTC70; -. DR BioCyc; TMAR243274:GC6P-136-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central. DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central. DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central. DR GO; GO:0030488; P:tRNA methylation; IBA:GOC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr. DR PANTHER; PTHR30544; PTHR30544; 1. DR PIRSF; PIRSF006004; CHP00048; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 329 AA; 37490 MW; F3A8BB75956A792F CRC64; MSASSQSPKG DGLLQTISVK ILKRVGKEEV AYVYLGETSR GNLVEFVESI QPPVPREKKW VLIVSTLAGC PVGCLMCDAG GFYRGKLSAD EIFEQIDFLV KSRYPNGRIP SEKFKIQFAR MGEPALNEAV LDVLKELPAR YEAPGLMPSI STVAPCGTDS FFEDLLKIKE KHYRGKFQLQ FSIHSTDEKE RDQIIPVKKW SLEKISEFGK RFVKENDRKI TLNFAVAQEY SLDPKVIIRV FDPEKFLVKI TPVNPTYRSK ENNLNSDVDV ERKELLKHRN FIEELKKAGF EVILSIGELE ENKIGSNCGQ YVQRHLMSER KIVDGYQYV // ID Q9X0J2_THEMA Unreviewed; 78 AA. AC Q9X0J2; G4FEP0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36184.1}; GN OrderedLocusNames=TM_1108 {ECO:0000313|EMBL:AAD36184.1}; GN ORFNames=Tmari_1114 {ECO:0000313|EMBL:AGL50038.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36184.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36184.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36184.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50038.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50038.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36184.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50038.1; -; Genomic_DNA. DR PIR; F72295; F72295. DR RefSeq; NP_228914.1; NC_000853.1. DR RefSeq; WP_004080319.1; NZ_CP011107.1. DR STRING; 243274.TM1108; -. DR EnsemblBacteria; AAD36184; AAD36184; TM_1108. DR EnsemblBacteria; AGL50038; AGL50038; Tmari_1114. DR GeneID; 898657; -. DR KEGG; tma:TM1108; -. DR KEGG; tmi:THEMA_08805; -. DR KEGG; tmm:Tmari_1114; -. DR KEGG; tmw:THMA_1131; -. DR PATRIC; 23937149; VBITheMar51294_1123. DR KO; K05571; -. DR OMA; FISHVIA; -. DR OrthoDB; EOG6FNHTB; -. DR BioCyc; TMAR243274:GC6P-1137-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005451; F:monovalent cation:proton antiporter activity; IEA:InterPro. DR InterPro; IPR005133; PhaG_MnhG_YufB. DR Pfam; PF03334; PhaG_MnhG_YufB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 26 45 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 73 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 78 AA; 8771 MW; E7C63B9A0F0CAB58 CRC64; MIYVGVVLMF LGTLLSLLKK DFLLKIHLIG ISDTVGSLFI VLNFWEDVSR TILMVVLLLV WGPFVSHVIA RMYTEGSS // ID Q9WY03_THEMA Unreviewed; 434 AA. AC Q9WY03; G4FH69; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AAD35249.1}; DE EC=3.1.3.1 {ECO:0000313|EMBL:AGL49079.1}; GN OrderedLocusNames=TM_0156 {ECO:0000313|EMBL:AAD35249.1}; GN ORFNames=Tmari_0153 {ECO:0000313|EMBL:AGL49079.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35249.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35249.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35249.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49079.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49079.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. CC {ECO:0000256|RuleBase:RU003946}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35249.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49079.1; -; Genomic_DNA. DR PIR; B72410; B72410. DR RefSeq; NP_227971.1; NC_000853.1. DR RefSeq; WP_004082772.1; NZ_CP011107.1. DR STRING; 243274.TM0156; -. DR EnsemblBacteria; AAD35249; AAD35249; TM_0156. DR EnsemblBacteria; AGL49079; AGL49079; Tmari_0153. DR GeneID; 896993; -. DR KEGG; tma:TM0156; -. DR KEGG; tmi:THEMA_04025; -. DR KEGG; tmm:Tmari_0153; -. DR KEGG; tmw:THMA_0151; -. DR PATRIC; 23935154; VBITheMar51294_0154. DR eggNOG; ENOG4105G6Z; Bacteria. DR eggNOG; COG1785; LUCA. DR KO; K01077; -. DR OMA; HSAGYVP; -. DR OrthoDB; EOG661H4G; -. DR BioCyc; TMAR243274:GC6P-157-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR001952; Alkaline_phosphatase. DR InterPro; IPR018299; Alkaline_phosphatase_AS. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR Pfam; PF00245; Alk_phosphatase; 1. DR PRINTS; PR00113; ALKPHPHTASE. DR SMART; SM00098; alkPPc; 1. DR SUPFAM; SSF53649; SSF53649; 2. DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49079.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 434 AA; 48168 MW; 1815823C65A78CB0 CRC64; MKRLFTLILI SLLVALAFSQ VKNVIYLIGD GMGLSQVYLT SMLEGRPLSF MKTPYIGLVK THSANSWVTD SAAAGTALAS GFKTNNGMIN ILPDGTVVPT IFEVAKTYGV RTGIVVTCRV THATPAAFYA HVKSRDEENE IARQLVENET VDVVMGGGWA NFLPKDLGGK RDDNLNLIEL AKEKGYIYVK TREELSKISA DSDKILALFA PSHLDPASSR KEQPMLYEMV EKALEILSKD DEPFFLMVEG SQIDWEAHDN DIYGVWKEVV EFDKAVQVAL DFALKRGDTL VIVTADHETG GLGLSSGDYR VDVDKIRNFK KTTDWIMANY SPKDREKFKK AIEEYFGLTL SDEDLNRISM SKNPKIELGR ILGEKVSVGW TTTTHSGTPV PIFAFGPGAE NFTGFLDNTE IPRIIMKLTG YSLQYPLLKE PVTK // ID Q9X208_THEMA Unreviewed; 67 AA. AC Q9X208; G4FG67; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36747.1}; GN OrderedLocusNames=TM_1680 {ECO:0000313|EMBL:AAD36747.1}; GN ORFNames=Tmari_1688 {ECO:0000313|EMBL:AGL50612.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36747.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36747.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36747.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50612.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50612.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36747.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50612.1; -; Genomic_DNA. DR PIR; F72226; F72226. DR RefSeq; NP_229480.1; NC_000853.1. DR RefSeq; WP_004082196.1; NZ_CP011107.1. DR STRING; 243274.TM1680; -. DR EnsemblBacteria; AAD36747; AAD36747; TM_1680. DR EnsemblBacteria; AGL50612; AGL50612; Tmari_1688. DR GeneID; 897244; -. DR KEGG; tma:TM1680; -. DR KEGG; tmi:THEMA_05840; -. DR KEGG; tmm:Tmari_1688; -. DR KEGG; tmw:THMA_1722; -. DR PATRIC; 23938334; VBITheMar51294_1697. DR OMA; RGLGWCR; -. DR BioCyc; TMAR243274:GC6P-1728-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 67 AA; 7943 MW; 1057416EFD454AA0 CRC64; MPRLDGTGPM GLGPMTGRGL GWCRFGGSWA RPWGWWRGFG YGWRRGWPFG MGFAWRHRRG WGWRGWW // ID Q9WZC0_THEMA Unreviewed; 286 AA. AC Q9WZC0; G4FDH2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35736.1}; GN OrderedLocusNames=TM_0652 {ECO:0000313|EMBL:AAD35736.1}; GN ORFNames=Tmari_0652 {ECO:0000313|EMBL:AGL49577.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35736.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35736.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35736.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49577.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49577.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35736.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49577.1; -; Genomic_DNA. DR PIR; C72352; C72352. DR RefSeq; NP_228461.1; NC_000853.1. DR RefSeq; WP_004081143.1; NZ_CP011107.1. DR STRING; 243274.TM0652; -. DR EnsemblBacteria; AAD35736; AAD35736; TM_0652. DR EnsemblBacteria; AGL49577; AGL49577; Tmari_0652. DR GeneID; 897759; -. DR KEGG; tma:TM0652; -. DR KEGG; tmi:THEMA_01405; -. DR KEGG; tmm:Tmari_0652; -. DR KEGG; tmw:THMA_0667; -. DR PATRIC; 23936218; VBITheMar51294_0662. DR eggNOG; ENOG41083P4; Bacteria. DR eggNOG; COG1502; LUCA. DR OMA; LWKAKRY; -. DR OrthoDB; EOG65J562; -. DR BioCyc; TMAR243274:GC6P-677-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0008808; F:cardiolipin synthase activity; IBA:GO_Central. DR GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central. DR GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central. DR InterPro; IPR025202; PLD-like_dom. DR InterPro; IPR001736; PLipase_D/transphosphatidylase. DR Pfam; PF13091; PLDc_2; 2. DR SMART; SM00155; PLDc; 2. DR PROSITE; PS50035; PLD; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 74 101 PLD phosphodiesterase. FT {ECO:0000259|PROSITE:PS50035}. FT DOMAIN 221 248 PLD phosphodiesterase. FT {ECO:0000259|PROSITE:PS50035}. SQ SEQUENCE 286 AA; 33042 MW; 897E3659517A8D59 CRC64; MKRLLLPFLL LSEVLLSQVY FSTVDDLSSL VISHLESASD VTVVAYSIDP DYLGLKECSM ATEVPVEGAF VHISDGLLHS KFIVLDHKTV IFGSANFNRP SLEEHLNNLI VFHSKEIATF FERIYDWLVF GKRPQARLET EEGTFFLIPI ADGEKIVLDA LWKAKRYVLL CSYAFTDEDV FATLKFLSSR GVEIYIITDE WFESSRLREL PLETFHVLEV KEPLMHHKFL VIDGKILITG SANFTESGFH RNVEVMFETS NREYVESFEE EFNRIWRGYF VQGVRF // ID Q9X1W5_THEMA Unreviewed; 100 AA. AC Q9X1W5; G4FG19; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36697.1}; GN OrderedLocusNames=TM_1630 {ECO:0000313|EMBL:AAD36697.1}; GN ORFNames=Tmari_1639 {ECO:0000313|EMBL:AGL50563.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36697.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36697.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36697.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50563.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50563.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36697.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50563.1; -; Genomic_DNA. DR PIR; F72229; F72229. DR RefSeq; NP_229430.1; NC_000853.1. DR RefSeq; WP_004082106.1; NZ_CP011107.1. DR STRING; 243274.TM1630; -. DR EnsemblBacteria; AAD36697; AAD36697; TM_1630. DR EnsemblBacteria; AGL50563; AGL50563; Tmari_1639. DR GeneID; 897926; -. DR KEGG; tma:TM1630; -. DR KEGG; tmi:THEMA_06095; -. DR KEGG; tmm:Tmari_1639; -. DR KEGG; tmw:THMA_1671; -. DR PATRIC; 23938234; VBITheMar51294_1649. DR OMA; HEALQMI; -. DR OrthoDB; EOG6091GQ; -. DR BioCyc; TMAR243274:GC6P-1676-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 100 AA; 12116 MW; 6D6D1BD063E00974 CRC64; MSVLDEILSV LEETQEDLFD LVGKHIHQLR KKYSDAEINE ALRMILFAME ISQKPIIHRV FEDYPREKRI FVEEDLTREE MELFLKGEMN ELDLEEKNWF // ID Q9WZF4_THEMA Unreviewed; 149 AA. AC Q9WZF4; G4FDD4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Transamidase GatB domain protein {ECO:0000313|EMBL:AGL49615.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35772.1}; GN OrderedLocusNames=TM_0690 {ECO:0000313|EMBL:AAD35772.1}; GN ORFNames=Tmari_0690 {ECO:0000313|EMBL:AGL49615.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35772.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35772.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35772.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49615.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49615.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35772.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49615.1; -; Genomic_DNA. DR PIR; H72344; H72344. DR RefSeq; NP_228499.1; NC_000853.1. DR RefSeq; WP_004081070.1; NZ_CP011107.1. DR STRING; 243274.TM0690; -. DR EnsemblBacteria; AAD35772; AAD35772; TM_0690. DR EnsemblBacteria; AGL49615; AGL49615; Tmari_0690. DR GeneID; 898357; -. DR KEGG; tma:TM0690; -. DR KEGG; tmi:THEMA_01215; -. DR KEGG; tmm:Tmari_0690; -. DR KEGG; tmw:THMA_0705; -. DR PATRIC; 23936298; VBITheMar51294_0702. DR eggNOG; ENOG4105KTH; Bacteria. DR eggNOG; COG1610; LUCA. DR KO; K09117; -. DR OMA; DRLNDDM; -. DR OrthoDB; EOG69SKHS; -. DR BioCyc; TMAR243274:GC6P-716-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro. DR Gene3D; 1.10.10.410; -; 1. DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrfrase-rel. DR InterPro; IPR023168; GatB_Yqey_C. DR InterPro; IPR019004; Uncharacterised_YOR215C_mit. DR Pfam; PF09424; YqeY; 1. DR SUPFAM; SSF89095; SSF89095; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 146 YqeY. {ECO:0000259|Pfam:PF09424}. FT COILED 50 84 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 149 AA; 17323 MW; CEC2AE2CF93FAFAF CRC64; MSLKEKLMSD LKEAMKNKDM VRMNTLRMIL TTLKNLEVEK MKEATDEEVM EALMKEAKKR REAIEEYEKH GREELAEKER KELEIIESYL PKQLSEDEIR KIVMEAINEV GASSPKDLGK VMKVVMPKVK GRADGKLVNK MVREILESL // ID Q9X033_THEMA Unreviewed; 145 AA. AC Q9X033; G4FF55; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36016.1}; GN OrderedLocusNames=TM_0935 {ECO:0000313|EMBL:AAD36016.1}; GN ORFNames=Tmari_0937 {ECO:0000313|EMBL:AGL49862.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36016.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36016.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36016.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49862.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49862.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36016.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49862.1; -; Genomic_DNA. DR PIR; G72315; G72315. DR RefSeq; NP_228743.1; NC_000853.1. DR RefSeq; WP_004080627.1; NZ_CP011107.1. DR PDB; 1O50; X-ray; 1.87 A; A=1-145. DR PDBsum; 1O50; -. DR STRING; 243274.TM0935; -. DR EnsemblBacteria; AAD36016; AAD36016; TM_0935. DR EnsemblBacteria; AGL49862; AGL49862; Tmari_0937. DR GeneID; 898609; -. DR KEGG; tma:TM0935; -. DR KEGG; tmi:THEMA_09675; -. DR KEGG; tmm:Tmari_0937; -. DR KEGG; tmw:THMA_0957; -. DR PATRIC; 23936801; VBITheMar51294_0949. DR eggNOG; ENOG4106V8B; Bacteria. DR eggNOG; COG0517; LUCA. DR OMA; MMIDNNI; -. DR OrthoDB; EOG6GXTSM; -. DR BioCyc; TMAR243274:GC6P-965-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O50}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 9 71 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 89 145 CBS. {ECO:0000259|PROSITE:PS51371}. SQ SEQUENCE 145 AA; 16557 MW; F5609A5283B3C642 CRC64; MKVKDVCKLI SLKPTVVEED TPIEEIVDRI LEDPVTRTVY VARDNKLVGM IPVMHLLKVS GFHFFGFIPK EELIRSSMKR LIAKNASEIM LDPVYVHMDT PLEEALKLMI DNNIQEMPVV DEKGEIVGDL NSLEILLALW KGREK // ID Q9WYA8_THEMA Unreviewed; 410 AA. AC Q9WYA8; G4FHI5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35360.1}; GN OrderedLocusNames=TM_0271 {ECO:0000313|EMBL:AAD35360.1}; GN ORFNames=Tmari_0269 {ECO:0000313|EMBL:AGL49195.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35360.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35360.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35360.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49195.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49195.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35360.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49195.1; -; Genomic_DNA. DR PIR; E72397; E72397. DR RefSeq; NP_228084.1; NC_000853.1. DR RefSeq; WP_004082975.1; NZ_CP011107.1. DR STRING; 243274.TM0271; -. DR EnsemblBacteria; AAD35360; AAD35360; TM_0271. DR EnsemblBacteria; AGL49195; AGL49195; Tmari_0269. DR GeneID; 897186; -. DR KEGG; tma:TM0271; -. DR KEGG; tmi:THEMA_03370; -. DR KEGG; tmm:Tmari_0269; -. DR KEGG; tmw:THMA_0278; -. DR PATRIC; 23935419; VBITheMar51294_0275. DR eggNOG; ENOG4106QHT; Bacteria. DR eggNOG; ENOG410YIB1; LUCA. DR OMA; LFLDMKA; -. DR OrthoDB; EOG6XSZT2; -. DR BioCyc; TMAR243274:GC6P-284-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 410 AA; 45466 MW; 97A9267F19D4328C CRC64; MKKGIIFILL ILTALSFSQI LNYVPENFKV IRYVKDLSEF YSEIKSLPTG RFLTESLGLE MMIQGVLESQ LLSRDIEPSD FYDLLSHEFL FVQLNSEDTC FVLGPSEKAK KLKDSIKSLV VDLLGMEDVV VVEKDGYLFL GTAKAVNASL KGGGKIPDTL KTADFFGYGL LQGEKYSFTV VSTKESASDH LSIKVEIAPA DDTSRNFLEK VGQPRKVPSD YYTFGELTVI FNTENYDGLL DVLSSAGFSI ESENLPVQLP ESDIEKVVKN LFEELEPPMF LSANVSSAVM DLIAGSTPTN LEVVAKARLK TPDAVENALK AAGVQYRKEG RCFVLENGLS ICTEGDTVVL KSEQFSPRDL DITPAKNDVF FLFLDMKAVM ESLVGEGEEA YIFARGFYKD GKMVFYVNVK // ID Q9X0M5_THEMA Unreviewed; 216 AA. AC Q9X0M5; G4FEK7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Cytochrome C-type biogenesis protein (CcdA), conjectural {ECO:0000313|EMBL:AGL50071.1}; DE SubName: Full=Cytochrome C-type biogenesis protein, putative {ECO:0000313|EMBL:AAD36217.1}; GN OrderedLocusNames=TM_1141 {ECO:0000313|EMBL:AAD36217.1}; GN ORFNames=Tmari_1147 {ECO:0000313|EMBL:AGL50071.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36217.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36217.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36217.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50071.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50071.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36217.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50071.1; -; Genomic_DNA. DR PIR; A72291; A72291. DR RefSeq; NP_228947.1; NC_000853.1. DR RefSeq; WP_004080262.1; NZ_CP011107.1. DR STRING; 243274.TM1141; -. DR EnsemblBacteria; AAD36217; AAD36217; TM_1141. DR EnsemblBacteria; AGL50071; AGL50071; Tmari_1147. DR GeneID; 898623; -. DR KEGG; tma:TM1141; -. DR KEGG; tmi:THEMA_08640; -. DR KEGG; tmm:Tmari_1147; -. DR KEGG; tmw:THMA_1164; -. DR PATRIC; 23937217; VBITheMar51294_1157. DR eggNOG; ENOG4108107; Bacteria. DR eggNOG; COG0785; LUCA. DR KO; K06196; -. DR OMA; LAIPFWI; -. DR OrthoDB; EOG64BQ62; -. DR BioCyc; TMAR243274:GC6P-1170-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro. DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom. DR Pfam; PF02683; DsbD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 47 68 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 74 94 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 115 145 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 179 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 191 214 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 14 210 DsbD. {ECO:0000259|Pfam:PF02683}. SQ SEQUENCE 216 AA; 23483 MW; 630A0F84022A7A4B CRC64; MSFAVAEVSY WMALGYGLLA FFSPCVLPLI PAFLGVLFAS KGDFLKVIGF FVGISSLFSV IGVLFGLFGN FIPTYILTWI SGLALVVFGL FYLFDVELVK MKKNPNVWRY KGEGFLNGFL LGGSVGLVWI PCSSPILGSI LAIVASGREP VKGGVLLFLY SLGISIPFIL MGGFVNKLLN RVSFKKPVWM NVLKIVGSLS LILVGVLILT GRFITY // ID Q9WYU1_THEMA Unreviewed; 315 AA. AC Q9WYU1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Integral membrane protein {ECO:0000313|EMBL:AGL49392.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35554.1}; GN OrderedLocusNames=TM_0470 {ECO:0000313|EMBL:AAD35554.1}; GN ORFNames=Tmari_0467 {ECO:0000313|EMBL:AGL49392.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35554.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35554.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35554.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49392.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49392.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35554.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49392.1; -; Genomic_DNA. DR PIR; F72374; F72374. DR RefSeq; NP_228280.1; NC_000853.1. DR RefSeq; WP_010865127.1; NC_000853.1. DR STRING; 243274.TM0470; -. DR EnsemblBacteria; AAD35554; AAD35554; TM_0470. DR EnsemblBacteria; AGL49392; AGL49392; Tmari_0467. DR GeneID; 897502; -. DR KEGG; tma:TM0470; -. DR KEGG; tmi:THEMA_02340; -. DR KEGG; tmm:Tmari_0467; -. DR PATRIC; 23935837; VBITheMar51294_0477. DR eggNOG; ENOG41082KG; Bacteria. DR eggNOG; COG0392; LUCA. DR KO; K07027; -. DR OMA; RFVEYLI; -. DR OrthoDB; EOG61S2WM; -. DR BioCyc; TMAR243274:GC6P-490-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR022791; L-PG_synthase/AglD. DR Pfam; PF03706; LPG_synthase_TM; 1. DR TIGRFAMs; TIGR00374; TIGR00374; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 15 34 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 95 115 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 127 151 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 205 228 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 235 254 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 286 307 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 315 AA; 36942 MW; 880EB482C5725B85 CRC64; MDPAEFSRYF HLKSLLYMFL LCGTFVFSIV IDSLRMKWLY SFVWKEKFPL YDAFFNNYMS FVFSMLTPFY FGGQFFQTYH LSKMGFKSEH NVNVILSRFV EYLISVTVLS ILGLVRYRNF LFSNALLTSK LILLAYLISV LFIAVLMSAL INPPLIARLF NAFKRIRWID RLIKKITKAE DWDTRFLEWT EKLKESVQVL WKSGFMFFDF PLTFISLLVQ SFVLYLAIWL TSGKIGFLDV TGLFYFLSLV VFYIPTPGAS GGVEAVYQIV FSKILNSSEK TLASILIWRI STYYLPIFIG IAFLLIYRYP KEVTK // ID Q9WZV8_THEMA Unreviewed; 285 AA. AC Q9WZV8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=HD domain protein {ECO:0000313|EMBL:AGL49781.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35936.1}; GN OrderedLocusNames=TM_0854 {ECO:0000313|EMBL:AAD35936.1}; GN ORFNames=Tmari_0856 {ECO:0000313|EMBL:AGL49781.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35936.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35936.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35936.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49781.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49781.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35936.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49781.1; -; Genomic_DNA. DR PIR; G72324; G72324. DR RefSeq; NP_228663.1; NC_000853.1. DR RefSeq; WP_008193057.1; NZ_CP011107.1. DR STRING; 243274.TM0854; -. DR EnsemblBacteria; AAD35936; AAD35936; TM_0854. DR EnsemblBacteria; AGL49781; AGL49781; Tmari_0856. DR GeneID; 898526; -. DR KEGG; tma:TM0854; -. DR KEGG; tmi:THEMA_00365; -. DR KEGG; tmm:Tmari_0856; -. DR KEGG; tmw:THMA_0876; -. DR PATRIC; 23936636; VBITheMar51294_0867. DR eggNOG; ENOG4108HU6; Bacteria. DR eggNOG; COG1639; LUCA. DR OMA; VCSKPDA; -. DR OrthoDB; EOG6NGVR1; -. DR BioCyc; TMAR243274:GC6P-884-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.3150.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006675; HDIG_dom. DR InterPro; IPR013976; HDOD. DR Pfam; PF08668; HDOD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00277; HDIG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 106 244 HDc. {ECO:0000259|SMART:SM00471}. SQ SEQUENCE 285 AA; 31757 MW; 33EFC02D0B20A904 CRC64; MPAKIIDKII EEIDKLPSPN VVVQRIIAVC SKPDASSTEV ANTLMMDASL SARVLKLANS AYYGVPRKIT TLSEAVMILG FKTVRNLALS VFTYDMVFKN SSSGIDREKL WEHFIASAIA SETVAETMGY PLKEEIFIAG LLHDLGKVVY DLLFSDILET EAKIAQKTKK NLIDIEEELG IPPHSEVGAK LLRKWNFPDL LVLSAEFHHN VEGNPNELFV NQVSMVHIGD VIANLMMKGA SLSWGDPKLS PFALNVLKVK PKTFLRILDK SKEKYNKAQE FLQID // ID Q9WYF2_THEMA Unreviewed; 108 AA. AC Q9WYF2; G4FHN0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|SAAS:SAAS00088523}; DE EC=1.11.1.15 {ECO:0000256|SAAS:SAAS00088503}; GN OrderedLocusNames=TM_0316 {ECO:0000313|EMBL:AAD35404.1}; GN ORFNames=Tmari_0314 {ECO:0000313|EMBL:AGL49240.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35404.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35404.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35404.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49240.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49240.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity. CC Required for the reduction of the AhpC active site cysteine CC residues and for the regeneration of the AhpC enzyme activity. CC {ECO:0000256|SAAS:SAAS00088543}. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC {ECO:0000256|SAAS:SAAS00088505}. CC -!- SIMILARITY: Belongs to the AhpD family. CC {ECO:0000256|SAAS:SAAS00571262}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35404.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49240.1; -; Genomic_DNA. DR PIR; C72392; C72392. DR RefSeq; NP_228128.1; NC_000853.1. DR RefSeq; WP_004083056.1; NZ_CP011107.1. DR STRING; 243274.TM0316; -. DR EnsemblBacteria; AAD35404; AAD35404; TM_0316. DR EnsemblBacteria; AGL49240; AGL49240; Tmari_0314. DR GeneID; 897257; -. DR KEGG; tma:TM0316; -. DR KEGG; tmi:THEMA_03145; -. DR KEGG; tmm:Tmari_0314; -. DR KEGG; tmw:THMA_0323; -. DR PATRIC; 23935511; VBITheMar51294_0321. DR eggNOG; COG0599; LUCA. DR OMA; CVDTHSQ; -. DR OrthoDB; EOG6W45V8; -. DR BioCyc; TMAR243274:GC6P-329-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC. DR Gene3D; 1.20.1290.10; -; 1. DR InterPro; IPR029032; AhpD-like. DR InterPro; IPR004675; AhpD_core. DR InterPro; IPR003779; CMD-like. DR Pfam; PF02627; CMD; 1. DR SUPFAM; SSF69118; SSF69118; 1. DR TIGRFAMs; TIGR00778; ahpD_dom; 1. PE 3: Inferred from homology; KW Antioxidant {ECO:0000256|SAAS:SAAS00461132}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00461175}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00461184, KW ECO:0000313|EMBL:AGL49240.1}; KW Peroxidase {ECO:0000256|SAAS:SAAS00461184, KW ECO:0000313|EMBL:AGL49240.1}; KW Redox-active center {ECO:0000256|SAAS:SAAS00461089}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 12 93 CMD. {ECO:0000259|Pfam:PF02627}. SQ SEQUENCE 108 AA; 12174 MW; 0A5E33E41C3F6282 CRC64; MNEFERWRRE FPEVSGAVVR MRNKAFSDGS IPAKYKVLAA LAIAVVEKCK PCAQGYYQKA IEMGATKDEI KEILEVAVTM GACIAETWAR EVWQYERSEN DGGSCCEE // ID G4FH33_THEMA Unreviewed; 827 AA. AC G4FH33; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 11-MAY-2016, entry version 44. DE SubName: Full=Ribonucleotide reductase of class II (Coenzyme B12-dependent) {ECO:0000313|EMBL:AGL49042.1}; DE EC=1.17.4.1 {ECO:0000313|EMBL:AGL49042.1}; DE SubName: Full=Ribonucleotide reductase, B12-dependent {ECO:0000313|EMBL:AAD35212.1}; GN OrderedLocusNames=TM_0118 {ECO:0000313|EMBL:AAD35212.1}; GN ORFNames=Tmari_0116 {ECO:0000313|EMBL:AGL49042.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AGL49042.1, ECO:0000313|Proteomes:UP000013901}; RN [1] {ECO:0000313|EMBL:AAD35212.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35212.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49042.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49042.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35212.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49042.1; -; Genomic_DNA. DR PIR; F72414; F72414. DR RefSeq; NP_227934.1; NC_000853.1. DR RefSeq; WP_004082700.1; NZ_CP011107.1. DR SMR; G4FH33; 1-633. DR STRING; 243274.TM0118; -. DR EnsemblBacteria; AAD35212; AAD35212; TM_0118. DR EnsemblBacteria; AGL49042; AGL49042; Tmari_0116. DR GeneID; 896945; -. DR KEGG; tma:TM0118; -. DR KEGG; tmi:THEMA_04215; -. DR KEGG; tmm:Tmari_0116; -. DR KEGG; tmw:THMA_0114; -. DR eggNOG; ENOG4105BZH; Bacteria. DR eggNOG; COG0209; LUCA. DR KO; K00525; -. DR OMA; GANMAIL; -. DR BioCyc; TMAR243274:GC6P-118-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. DR InterPro; IPR013344; RNR_NrdJ/NrdZ. DR InterPro; IPR008926; RNR_R1-su_N. DR Pfam; PF02867; Ribonuc_red_lgC; 1. DR Pfam; PF00317; Ribonuc_red_lgN; 1. DR PRINTS; PR01183; RIBORDTASEM1. DR SUPFAM; SSF48168; SSF48168; 1. DR TIGRFAMs; TIGR02504; NrdJ_Z; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49042.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 15 99 Ribonuc_red_lgN. FT {ECO:0000259|Pfam:PF00317}. FT DOMAIN 132 628 RIBORED_LARGE. FT {ECO:0000259|Pfam:PF02867}. SQ SEQUENCE 827 AA; 94018 MW; D1B99C7F5DBB4256 CRC64; MKLSDLISRW IDVEPSKNAQ IILRDRYFMK DLDGNYLETK WEDVARRVAR VVATAELLNP SYKKNEKLDR IKEWEDIFFR VLKARLFIPN SPTLFNAGLG VKHDLLWKPI DQMTLEDYEE IYRSRNHLHM LSACFVVPVG DSIEEIFEAV KEYALITKVG GGVGSNFSEL RPKGSFVAGT HGKASGPVSF MHVFNSAISV VKQGYRRRGA LMGILNINHP DIEEFIDAKK ENTGEAVLNF FNLSVGFPMD KKEILKLYEE DGELELSHPR STIRKKVKIR ELFRKIATNA WKSGDPGLAF LGEMNKYYPL YPHRKINSTN PCGEIGLSDY EACNLGSIDV AKFYNNGFVD LEALQELVQI AVRFLDNVID VNVFPIDKIT KAVKESRRLG LGIMGFADLL YKLEIPYNSQ EARDFAANLM AFIALHAHRT SYELGKEKGN FPLLEISRYR TEDNFVPFAM GMSNYDDEIR EVMKMTKEFR RNVALLTIAP TGSISNIADT SSGLEPNFLL AYTRFVTKED GTKEPLLYVN QVLREKLNPE ILKRIEKELI EKGSLKDIPD VPEKIKKVFV VALDIDPMDH LLMQDAFQRY VDNNISKTIN MPQSATVDDV LNVYLEALRT NVRGITVYRD GSLQTQVLTK ALKTPEAPKV QFFVVDEKLK LHPRPRKDTL RSVTRKYKRP DGTTYITISF DDTGEAVEIF ISNGSEMAEA IGRLSSIALR AGVSIDEIVE QLSKVKGEYC KGLAEEIKKA LEDFAKLWLR TGEEAPESEE EPIEREKFIV AHNLRWQSGY YVDDEGNVYC PVCLSKNSLI KQEGCVSCKN CGWSKCE // ID Q9WZX9_THEMA Unreviewed; 306 AA. AC Q9WZX9; G4FCU9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Cobalt-zinc-cadmium resistance protein CzcD {ECO:0000313|EMBL:AGL49803.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35957.1}; GN OrderedLocusNames=TM_0876 {ECO:0000313|EMBL:AAD35957.1}; GN ORFNames=Tmari_0878 {ECO:0000313|EMBL:AGL49803.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35957.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35957.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35957.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49803.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49803.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF) CC transporter (TC 2.A.4) family. {ECO:0000256|SAAS:SAAS00536237}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35957.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49803.1; -; Genomic_DNA. DR PIR; F72323; F72323. DR RefSeq; NP_228684.1; NC_000853.1. DR RefSeq; WP_004080721.1; NZ_CP011107.1. DR PDB; 2ZZT; X-ray; 2.84 A; A=206-306. DR PDBsum; 2ZZT; -. DR STRING; 243274.TM0876; -. DR EnsemblBacteria; AAD35957; AAD35957; TM_0876. DR EnsemblBacteria; AGL49803; AGL49803; Tmari_0878. DR GeneID; 898549; -. DR KEGG; tma:TM0876; -. DR KEGG; tmi:THEMA_00255; -. DR KEGG; tmm:Tmari_0878; -. DR KEGG; tmw:THMA_0898; -. DR PATRIC; 23936683; VBITheMar51294_0890. DR eggNOG; ENOG41076HS; Bacteria. DR eggNOG; COG0053; LUCA. DR OMA; VMDTNSR; -. DR OrthoDB; EOG6VQPXP; -. DR BioCyc; TMAR243274:GC6P-906-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0061088; P:regulation of sequestering of zinc ion; IBA:GO_Central. DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central. DR GO; GO:0071577; P:zinc II ion transmembrane transport; IBA:GOC. DR Gene3D; 1.20.1510.10; -; 1. DR Gene3D; 3.30.70.1350; -; 1. DR InterPro; IPR002524; Cation_efflux. DR InterPro; IPR027470; Cation_efflux_CTD. DR InterPro; IPR027469; Cation_efflux_TMD. DR PANTHER; PTHR11562; PTHR11562; 1. DR Pfam; PF01545; Cation_efflux; 1. DR Pfam; PF16916; ZT_dimer; 1. DR TIGRFAMs; TIGR01297; CDF; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2ZZT}; KW Cell membrane {ECO:0000256|SAAS:SAAS00272934}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00272934, KW ECO:0000256|SAAS:SAAS00417858, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00417858, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00417858, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00417883}. FT TRANSMEM 12 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 83 100 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 112 136 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 182 202 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 215 289 ZT_dimer. {ECO:0000259|Pfam:PF16916}. SQ SEQUENCE 306 AA; 34432 MW; 85879761C27D24BE CRC64; MERHEEIKKG AWIGILGNTV LAVLKILVGL LTGSYAILAD GIDTSTDIFT SLVILLSSRI SGKPPDETHP YGHERAETIA SKIISFVMFY AGASLLVESV KRLVKQEFSL ELTLTAFIVV GISVAGKTFL FLYKLSLGKR LKSSATISDA LNMRNDIMIS GTVLAGMVAM KTFGWWWLDS LLAIFVSIMI LRTSFSVFYE AAYELMDGMK RTELDMYDDI FAVLERFPNV HNPHRVRIRR VGTKYFIEMD IEVDGKMSVK DAHELTVKIR KEMLKRRDDI EDVTIHVEPL GNVEEEGFGL KKGEKK // ID Q9X1T7_THEMA Unreviewed; 551 AA. AC Q9X1T7; G4FFY9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 103. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36668.1}; GN OrderedLocusNames=TM_1601 {ECO:0000313|EMBL:AAD36668.1}; GN ORFNames=Tmari_1609 {ECO:0000313|EMBL:AGL50533.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36668.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36668.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36668.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50533.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50533.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36668.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50533.1; -; Genomic_DNA. DR PIR; E72234; E72234. DR RefSeq; NP_229401.1; NC_000853.1. DR RefSeq; WP_004082048.1; NZ_CP011107.1. DR STRING; 243274.TM1601; -. DR EnsemblBacteria; AAD36668; AAD36668; TM_1601. DR EnsemblBacteria; AGL50533; AGL50533; Tmari_1609. DR GeneID; 897461; -. DR KEGG; tma:TM1601; -. DR KEGG; tmi:THEMA_06245; -. DR KEGG; tmm:Tmari_1609; -. DR KEGG; tmw:THMA_1641; -. DR PATRIC; 23938176; VBITheMar51294_1620. DR eggNOG; ENOG4108MNT; Bacteria. DR eggNOG; COG1031; LUCA. DR OMA; HTPGKYL; -. DR OrthoDB; EOG6M3P8Z; -. DR BioCyc; TMAR243274:GC6P-1647-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 174 414 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 551 AA; 61774 MW; C7511D9019833CFE CRC64; MRALIVDGYI DEPAAFGVPP YVSPYVRYLA GALVVHDVEV DYVTIDKMRK ESLWEIANEY DFLFVFGGIT VPGRYKGGTP LTLSELQRIL SIARRPIKIV GGPIVGGYSL RGGSVARRFD IQADYLVSGD MEAFVVSYFQ GVPDPEAKSD YELIDAVAPY GAVVLEKHPN FPHVICEIEV SRGCERRTFC SFCTEPLLHG RLKSRDVQAI LKEIESLYRA GCRAFRFGRA ANILAFGSDR NGGKPSPEIL EELYSGTREV APHLEVLHTD NANPSYLVTY EKECRKIVET IVRYNTPGDV FSFGVESFDE NVLKKNNVQG SPEEFLKAIA VVNEIGGVRV DGIPKLLPGV NLIFGLPGET EETLKKNYSY LKRILDEGYL LRRINIRKLL AYPGTPVYEY LKNKKHRIKS YLHDQWKRRI REEIDREMLK RVFPAGTVLK KVIVEYREGK TSFGRQLGSY PILVGIPGNH SGVLDVVVVS HGERSVTALP YPSFINSMSL EELTAIPGIG SALARKIILN RPFRSWEDLK KVVPAETANF LRNLGISLQQ V // ID Q9WXX6_THEMA Unreviewed; 121 AA. AC Q9WXX6; G4FH37; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 111. DE SubName: Full=Ferric uptake regulation protein {ECO:0000313|EMBL:AAD35216.1}; DE SubName: Full=Zinc uptake regulation protein ZUR {ECO:0000313|EMBL:AGL49046.1}; GN OrderedLocusNames=TM_0122 {ECO:0000313|EMBL:AAD35216.1}; GN ORFNames=Tmari_0120 {ECO:0000313|EMBL:AGL49046.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35216.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35216.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35216.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49046.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49046.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the Fur family. CC {ECO:0000256|SAAS:SAAS00578401}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35216.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49046.1; -; Genomic_DNA. DR PIR; B72415; B72415. DR RefSeq; NP_227938.1; NC_000853.1. DR RefSeq; WP_004082705.1; NZ_CP011107.1. DR STRING; 243274.TM0122; -. DR EnsemblBacteria; AAD35216; AAD35216; TM_0122. DR EnsemblBacteria; AGL49046; AGL49046; Tmari_0120. DR GeneID; 896949; -. DR KEGG; tma:TM0122; -. DR KEGG; tmi:THEMA_04195; -. DR KEGG; tmm:Tmari_0120; -. DR KEGG; tmw:THMA_0118; -. DR PATRIC; 23935084; VBITheMar51294_0120. DR eggNOG; ENOG4105NJ2; Bacteria. DR eggNOG; COG0735; LUCA. DR KO; K03711; -. DR OMA; HIICKEC; -. DR OrthoDB; EOG6J48SS; -. DR BioCyc; TMAR243274:GC6P-122-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR002481; FUR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01475; FUR; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00469751}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 121 AA; 14469 MW; E5323289C054ACA3 CRC64; MRMTKNREAV FEIIESSRVP LTAEEIHRKL DVNLSTVYRA LKFLEERNLV GSFSVGGPRY FFKKKRHYHF LICEKCGKLF PFEECVDEFL EKLQKKYDFS EESHLFLIHG ICKECKKEVE K // ID Q9X1G2_THEMA Unreviewed; 893 AA. AC Q9X1G2; G4FFI5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 123. DE RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969}; DE Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969}; DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969}; GN Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969}; GN OrderedLocusNames=TM_1450 {ECO:0000313|EMBL:AAD36518.1}; GN ORFNames=Tmari_1456 {ECO:0000313|EMBL:AGL50380.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36518.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36518.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36518.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50380.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50380.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA CC polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent CC release of RNAP and its truncated transcript from the DNA, and CC recruitment of nucleotide excision repair machinery to the damaged CC site. {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase CC family. RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family. CC {ECO:0000256|HAMAP-Rule:MF_00969}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36518.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50380.1; -; Genomic_DNA. DR PIR; F72253; F72253. DR RefSeq; NP_229249.1; NC_000853.1. DR RefSeq; WP_004081728.1; NZ_CP011107.1. DR STRING; 243274.TM1450; -. DR DNASU; 898026; -. DR EnsemblBacteria; AAD36518; AAD36518; TM_1450. DR EnsemblBacteria; AGL50380; AGL50380; Tmari_1456. DR GeneID; 898026; -. DR KEGG; tma:TM1450; -. DR KEGG; tmi:THEMA_07065; -. DR KEGG; tmm:Tmari_1456; -. DR KEGG; tmw:THMA_1480; -. DR PATRIC; 23937852; VBITheMar51294_1464. DR eggNOG; ENOG4108JA2; Bacteria. DR eggNOG; COG1197; LUCA. DR KO; K03723; -. DR OMA; FFIPEDY; -. DR OrthoDB; EOG6FNHKW; -. DR BioCyc; TMAR243274:GC6P-1488-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00969; TRCF; 1. DR InterPro; IPR003711; CarD-like/TRCF_domain. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR004576; Mfd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005118; TRCF_C. DR Pfam; PF02559; CarD_CdnL_TRCF; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF03461; TRCF; 1. DR SMART; SM01058; CarD_TRCF; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00982; TRCF; 1. DR SUPFAM; SSF141259; SSF141259; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00580; mfd; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000256|RuleBase:RU000452}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00969}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00969}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00969}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000256|RuleBase:RU000452}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000256|RuleBase:RU000452}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00969, KW ECO:0000256|RuleBase:RU000452}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 386 547 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 556 720 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT NP_BIND 399 406 ATP. {ECO:0000256|HAMAP-Rule:MF_00969}. FT COILED 322 345 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 893 AA; 103149 MW; 564E4C22787BD551 CRC64; MVEILLLPNE RFSNIEGYIF YPSRDVLPLE DVVLSPEIKG KRIEILWRLL NGENLKIATT LKALTEKVFS PDFLRENSLM IARSTKLTLS PEKLVEMGYE LVFTVQNVGE FAIRGDIIDI YSPGNDFPVR IELFGDEIEE IRFFKVDTQR SFQGVDKTLI LPFVDFYGES TLLDFLKTDA RFICEDLQKV LDEYRKFRKE MRDLLKERYN DFFDERVVEV ILKNVEKGSA PLSTRVEKKE SLPILDVDEI EEGGLVVHRE HGIAIFEGIV RLKGVLGERD YLKLKYEDAI LYVPIEKIDR VHKYIGDPSQ VKLDRMNRGK WKQTLKKVRE DIEKKIKELV ELYMKRQEAQ GLSLPGDPEL EEKFAESFPY IETPDQQQSI EEVLSDLASE KPMDRLLCGD AGVGKTEVAL RAAFRAVASG KQVAVLVPTT VLARQHYENF KERMEPFGVK VELLDSSRTA REKKEIIEKL KKGEIDIIIG THSLLNERIE FSDLGLVIID EEQKFGVEQK ERFKKLRLSV NVLTLSATPI PRTLHMALSG MKDFSVINSP PPGRKPVYVY VAEYSDDLVK GAVIREINRG GQVIYVHNRV EELPEVFEKL KRMFPELEIA VAHGKMSRKT MERIVHEFYR GNIDVLLCTT IIENGVDIPN ANTLIVDDAQ RYGLSQLYQL RGRVGRSDRR AFAYFLYPKG TPRSALERLK VLKSYTGFGS GLQIALKDME LRGVGDVLGL EQHGNVVSVG LKLYNEILKE TITRFKERRI EKKHSVNVEI ENPPGRFFIP EDYVQNPVER LRLYRRLASS LDEEDLEEIL EEMKDRFGEP PEEVKLLVDY FRLRVRASKL GIKKIRFDHS MVEIFPSRNS PFLNHPRYDR RSGSVVLYTR KDPVEFLMDM LKK // ID Q9WZM9_THEMA Unreviewed; 312 AA. AC Q9WZM9; G4FD52; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=DNA polymerase III, gamma subunit-related protein {ECO:0000313|EMBL:AAD35853.1}; GN OrderedLocusNames=TM_0771 {ECO:0000313|EMBL:AAD35853.1}; GN ORFNames=Tmari_0772 {ECO:0000313|EMBL:AGL49697.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35853.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35853.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35853.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49697.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49697.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35853.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49697.1; -; Genomic_DNA. DR PIR; A72337; A72337. DR RefSeq; NP_228580.1; NC_000853.1. DR RefSeq; WP_004080921.1; NZ_CP011107.1. DR PDB; 2GNO; X-ray; 2.00 A; A=9-312. DR PDBsum; 2GNO; -. DR STRING; 243274.TM0771; -. DR EnsemblBacteria; AAD35853; AAD35853; TM_0771. DR EnsemblBacteria; AGL49697; AGL49697; Tmari_0772. DR GeneID; 898439; -. DR KEGG; tma:TM0771; -. DR KEGG; tmi:THEMA_00795; -. DR KEGG; tmm:Tmari_0772; -. DR KEGG; tmw:THMA_0790; -. DR PATRIC; 23936464; VBITheMar51294_0784. DR eggNOG; ENOG41083B9; Bacteria. DR eggNOG; COG0470; LUCA. DR KO; K02343; -. DR OMA; HENGWEG; -. DR OrthoDB; EOG6P8TKW; -. DR BioCyc; TMAR243274:GC6P-798-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006261; P:DNA-dependent DNA replication; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF48019; SSF48019; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2GNO}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 312 AA; 36272 MW; DC44ACB82B188B12 CRC64; MNDLIRKYAK DQLETLKRII EKSEGISILI NGEDLSYPRE VSLELPEYVE KFPPKASDVL EIDPEGENIG IDDIRTIKDF LNYSPELYTR KYVIVHDCER MTQQAANAFL KALEEPPEYA VIVLNTRRWH YLLPTIKSRV FRVVVNVPKE FRDLVKEKIG DLWEELPLLE RDFKTALEAY KLGAEKLSGL MESLKVLETE KLLKKVLSKG LEGYLACREL LERFSKVESK EFFALFDQVT NTITGKDAFL LIQRLTRIIL HENTWESVED QKSVSFLDSI LRVKIANLNN KLTLMNILAI HRERKRGVNA WS // ID Q9X0J6_THEMA Unreviewed; 89 AA. AC Q9X0J6; G4FEN6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36188.1}; GN OrderedLocusNames=TM_1112 {ECO:0000313|EMBL:AAD36188.1}; GN ORFNames=Tmari_1118 {ECO:0000313|EMBL:AGL50042.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36188.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36188.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36188.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50042.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50042.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36188.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50042.1; -; Genomic_DNA. DR PIR; B72296; B72296. DR RefSeq; NP_228918.1; NC_000853.1. DR RefSeq; WP_004080314.1; NZ_CP011107.1. DR PDB; 1LKN; NMR; -; A=1-89. DR PDB; 1O5U; X-ray; 1.83 A; A/B=1-89. DR PDB; 2K9Z; NMR; -; A=1-89. DR PDBsum; 1LKN; -. DR PDBsum; 1O5U; -. DR PDBsum; 2K9Z; -. DR STRING; 243274.TM1112; -. DR EnsemblBacteria; AAD36188; AAD36188; TM_1112. DR EnsemblBacteria; AGL50042; AGL50042; Tmari_1118. DR GeneID; 898653; -. DR KEGG; tma:TM1112; -. DR KEGG; tmi:THEMA_08785; -. DR KEGG; tmm:Tmari_1118; -. DR KEGG; tmw:THMA_1135; -. DR PATRIC; 23937157; VBITheMar51294_1127. DR eggNOG; ENOG4105YGD; Bacteria. DR eggNOG; COG3450; LUCA. DR KO; K06995; -. DR OMA; IIQYGIK; -. DR OrthoDB; EOG6CK7QX; -. DR BioCyc; TMAR243274:GC6P-1141-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR008579; DUF861_Cupin_3. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF05899; Cupin_3; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1LKN, ECO:0000213|PDB:1O5U, KW ECO:0000213|PDB:2K9Z}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 14 86 Cupin_3. {ECO:0000259|Pfam:PF05899}. SQ SEQUENCE 89 AA; 10757 MW; 11E53815E3425B72 CRC64; MEVKIEKPTP EKLKELSVEK WPIWEKEVSE FDWYYDTNET CYILEGKVEV TTEDGKKYVI EKGDLVTFPK GLRCRWKVLE PVRKHYNLF // ID Q9WZ75_THEMA Unreviewed; 115 AA. AC Q9WZ75; G4FDL3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35691.1}; GN OrderedLocusNames=TM_0606 {ECO:0000313|EMBL:AAD35691.1}; GN ORFNames=Tmari_0606 {ECO:0000313|EMBL:AGL49531.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35691.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35691.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35691.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49531.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49531.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35691.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49531.1; -; Genomic_DNA. DR PIR; B72355; B72355. DR RefSeq; NP_228416.1; NC_000853.1. DR RefSeq; WP_004081223.1; NZ_CP011107.1. DR STRING; 243274.TM0606; -. DR EnsemblBacteria; AAD35691; AAD35691; TM_0606. DR EnsemblBacteria; AGL49531; AGL49531; Tmari_0606. DR GeneID; 897687; -. DR KEGG; tma:TM0606; -. DR KEGG; tmi:THEMA_01635; -. DR KEGG; tmm:Tmari_0606; -. DR KEGG; tmw:THMA_0622; -. DR PATRIC; 23936127; VBITheMar51294_0617. DR eggNOG; COG3906; LUCA. DR OMA; YATAQKV; -. DR OrthoDB; EOG6D2KZ8; -. DR BioCyc; TMAR243274:GC6P-631-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 115 AA; 13497 MW; 59AF390538DB8E1F CRC64; MSMHEHEHEH EHEHKTEVFS LIDQDGNEVF FHKLGEVEDE GNLFWVCEEV FLNDARDMIE DLGEVYIFKA DDTPEGVMLE GVEYATAQKV FEKWQNSIPD IEEIFFEADT EEDGE // ID Q9WYP6_THEMA Unreviewed; 286 AA. AC Q9WYP6; G4FHX4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35500.1}; GN OrderedLocusNames=TM_0415 {ECO:0000313|EMBL:AAD35500.1}; GN ORFNames=Tmari_0412 {ECO:0000313|EMBL:AGL49337.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35500.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35500.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35500.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49337.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49337.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35500.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49337.1; -; Genomic_DNA. DR PIR; E72381; E72381. DR RefSeq; NP_228225.1; NC_000853.1. DR RefSeq; WP_004083266.1; NZ_CP011107.1. DR PDB; 1VK4; X-ray; 1.91 A; A=1-286. DR PDBsum; 1VK4; -. DR STRING; 243274.TM0415; -. DR EnsemblBacteria; AAD35500; AAD35500; TM_0415. DR EnsemblBacteria; AGL49337; AGL49337; Tmari_0412. DR GeneID; 897416; -. DR KEGG; tma:TM0415; -. DR KEGG; tmi:THEMA_02650; -. DR KEGG; tmm:Tmari_0412; -. DR KEGG; tmw:THMA_0421; -. DR PATRIC; 23935713; VBITheMar51294_0420. DR eggNOG; ENOG4108ZTF; Bacteria. DR eggNOG; COG0524; LUCA. DR OMA; VHINPLW; -. DR OrthoDB; EOG6GBM7Z; -. DR BioCyc; TMAR243274:GC6P-430-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR016831; UCP025725_kinase-rel. DR Pfam; PF00294; PfkB; 1. DR PIRSF; PIRSF025725; UCP025725; 1. DR SUPFAM; SSF53613; SSF53613; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VK4}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|SAAS:SAAS00446051}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00446051}. FT DOMAIN 132 271 PfkB. {ECO:0000259|Pfam:PF00294}. SQ SEQUENCE 286 AA; 32062 MW; 41DFA4AF5452E5EE CRC64; MITFIGHVSK DVNVVDGKRE IAYGGGVVMG AITSSLLGVK TKVITKCTRE DVSKFSFLRD NGVEVVFLKS PRTTSIENRY GSDPDTRESF LISAADPFTE SDLAFIEGEA VHINPLWYGE FPEDLIPVLR RKVMFLSADA QGFVRVPENE KLVYRDWEMK EKYLKYLDLF KVDSREAETL TGTNDLRESC RIIRSFGAKI ILATHASGVI VFDGNFYEAS FRSWSLEGRT GRGDTCTAAF LVGFVFKKMS IEKATKFAAA VTSVKMRHPG PLRREDLEAI SGDQYF // ID Q9X197_THEMA Unreviewed; 262 AA. AC Q9X197; G4FFB3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 97. DE SubName: Full=Spermidine Putrescine ABC transporter permease component PotB {ECO:0000313|EMBL:AGL50308.1}; DE SubName: Full=Spermidine/putrescine ABC transporter, permease protein {ECO:0000313|EMBL:AAD36447.1}; GN OrderedLocusNames=TM_1377 {ECO:0000313|EMBL:AAD36447.1}; GN ORFNames=Tmari_1384 {ECO:0000313|EMBL:AGL50308.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36447.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36447.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36447.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50308.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50308.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36447.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50308.1; -; Genomic_DNA. DR PIR; B72261; B72261. DR RefSeq; NP_229178.1; NC_000853.1. DR RefSeq; WP_004081575.1; NZ_CP011107.1. DR STRING; 243274.TM1377; -. DR EnsemblBacteria; AAD36447; AAD36447; TM_1377. DR EnsemblBacteria; AGL50308; AGL50308; Tmari_1384. DR GeneID; 898101; -. DR KEGG; tma:TM1377; -. DR KEGG; tmi:THEMA_07440; -. DR KEGG; tmm:Tmari_1384; -. DR KEGG; tmw:THMA_1404; -. DR PATRIC; 23937696; VBITheMar51294_1389. DR eggNOG; ENOG4105F38; Bacteria. DR eggNOG; COG1176; LUCA. DR KO; K11071; -. DR OMA; KFFTPVY; -. DR OrthoDB; EOG6HMXBZ; -. DR BioCyc; TMAR243274:GC6P-1412-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 7 26 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 57 79 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 86 110 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 130 155 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 189 208 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 236 256 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 53 255 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 262 AA; 29660 MW; 9C44DDA5D99FE95A CRC64; MKYVYFLWLL FLFILPISIV FVYSFLEPQI YGGVKWSFSL EAYSYLPRYL ALIWRSVWIA GVATLITLVV AVPVAFYIAR SKLKNFLLLL TVVPFWTNSL IRIYAWKIVL GNNGLVNQFL GLFGIDPVQF LYNSFAVILV IVYTYLPFAI LPLYAAMEKV EDSILEASLD LGASRMYTFI RVLLPNVRAG LLTAFVFVFI PALGSYAIPD LVGGVNSKMI GNEIVRQLLT VRNWPVASAM SNILTLIALL SIIFVMKRGE KR // ID Q9X1Z8_THEMA Unreviewed; 117 AA. AC Q9X1Z8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36737.1}; GN OrderedLocusNames=TM_1670 {ECO:0000313|EMBL:AAD36737.1}; GN ORFNames=Tmari_1679 {ECO:0000313|EMBL:AGL50603.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36737.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36737.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36737.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50603.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50603.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36737.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50603.1; -; Genomic_DNA. DR PIR; D72225; D72225. DR RefSeq; NP_229470.1; NC_000853.1. DR RefSeq; WP_010865380.1; NZ_CP011107.1. DR EnsemblBacteria; AAD36737; AAD36737; TM_1670. DR EnsemblBacteria; AGL50603; AGL50603; Tmari_1679. DR GeneID; 897313; -. DR KEGG; tma:TM1670; -. DR KEGG; tmm:Tmari_1679; -. DR KEGG; tmw:THMA_1711; -. DR PATRIC; 23938312; VBITheMar51294_1688. DR OMA; EGWQYLY; -. DR OrthoDB; EOG6PW269; -. DR BioCyc; TMAR243274:GC6P-1716-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 117 AA; 13512 MW; 22B3FB0BE25C56B9 CRC64; MMSNTSSFEI PDPDSSPDEY EDWAMGFLEG ASSMIYIPSD FEQLVWAEGW QYLYYVFQVS FFMPATVTSI EIEGITEYTT KFIPFLLNNK PDFVDKTYFL SLKCTTVDGT TTAVQWR // ID Q9X179_THEMA Unreviewed; 164 AA. AC Q9X179; G4FF94; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=DUF82 domain-containing protein {ECO:0000313|EMBL:AGL50289.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36438.1}; GN OrderedLocusNames=TM_1358 {ECO:0000313|EMBL:AAD36438.1}; GN ORFNames=Tmari_1365 {ECO:0000313|EMBL:AGL50289.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36438.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36438.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36438.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50289.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50289.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36438.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50289.1; -; Genomic_DNA. DR PIR; G72262; G72262. DR RefSeq; NP_229159.1; NC_000853.1. DR RefSeq; WP_004081554.1; NZ_CP011107.1. DR STRING; 243274.TM1358; -. DR EnsemblBacteria; AAD36438; AAD36438; TM_1358. DR EnsemblBacteria; AGL50289; AGL50289; Tmari_1365. DR GeneID; 898122; -. DR KEGG; tma:TM1358; -. DR KEGG; tmi:THEMA_07550; -. DR KEGG; tmm:Tmari_1365; -. DR KEGG; tmw:THMA_1383; -. DR PATRIC; 23937654; VBITheMar51294_1370. DR eggNOG; ENOG4108KR2; Bacteria. DR eggNOG; COG1656; LUCA. DR OMA; HERKESP; -. DR OrthoDB; EOG69GZMT; -. DR BioCyc; TMAR243274:GC6P-1391-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR002782; Mut7-C_RNAse_dom. DR Pfam; PF01927; Mut7-C; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 143 Mut7-C. {ECO:0000259|Pfam:PF01927}. SQ SEQUENCE 164 AA; 18952 MW; 71B46245E886F548 CRC64; MSEVRFAVDA SLVPLAKKLR ILGVDVKVCY SEEPGKVLLI CRKEGRILLT KKCSLIKFFE KYGQKVFYIK DEKDLKRVIE HFKLKPERAR CPYCNRELLP TPREEVIEKV PLYVFLNAEK FSRCPSCGRI FWRGSHLDWV KEVIPDGSGE TETDKGNKDS GKRG // ID Q9X0N3_THEMA Unreviewed; 335 AA. AC Q9X0N3; G4FEJ8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 89. DE SubName: Full=Dipeptide transport system permease protein DppB {ECO:0000313|EMBL:AGL50080.1}; DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD36225.1}; GN OrderedLocusNames=TM_1149 {ECO:0000313|EMBL:AAD36225.1}; GN ORFNames=Tmari_1156 {ECO:0000313|EMBL:AGL50080.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36225.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36225.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36225.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50080.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50080.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36225.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50080.1; -; Genomic_DNA. DR PIR; A72289; A72289. DR RefSeq; NP_228955.1; NC_000853.1. DR RefSeq; WP_004080232.1; NZ_CP011107.1. DR STRING; 243274.TM1149; -. DR DNASU; 898337; -. DR EnsemblBacteria; AAD36225; AAD36225; TM_1149. DR EnsemblBacteria; AGL50080; AGL50080; Tmari_1156. DR GeneID; 898337; -. DR KEGG; tma:TM1149; -. DR KEGG; tmi:THEMA_08595; -. DR KEGG; tmm:Tmari_1156; -. DR KEGG; tmw:THMA_1173; -. DR PATRIC; 23937235; VBITheMar51294_1166. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR KO; K02033; -. DR OMA; KQHLARF; -. DR OrthoDB; EOG66F098; -. DR BioCyc; TMAR243274:GC6P-1178-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 32 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 103 124 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 136 164 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 203 222 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 257 278 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 308 329 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 97 326 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 335 AA; 37481 MW; 3BEAD448F69C1E1F CRC64; MSLKNYVITR ILLAAPMIFI LLALIFLVLR IIPGDPVLAI LGGKAPKEVI EQKRHELGLD KPIIVQFFDY IGDLLKGDLG KSTLTGRPVW EEIKERFPAT LELTLFAFIV AVLIGIFWGS FAAYKRDSGV DIGARMFSMV MYAVPVFWFG LMMQYIFGVI LRWLPVGGRL SPTMNLKVIT GIYSIDALFT GNWEALKDVF EHLLLPGLTL GLVISSVFVR MVRNNTVLTL AQDFVKAARA RGLKERVVLF RYALKNALVP IFTMMGLQFA LLLGGAVLTE TTFSWPGLGS YLVMKIRYRD FPAIQGTVVF FALIVVVISI LVDVINALID PRVRY // ID Q9X0U9_THEMA Unreviewed; 329 AA. AC Q9X0U9; G4FEC4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 101. DE SubName: Full=Mannoside ABC transport system, permease protein 1 {ECO:0000313|EMBL:AGL50153.1}; DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD36297.1}; GN OrderedLocusNames=TM_1222 {ECO:0000313|EMBL:AAD36297.1}; GN ORFNames=Tmari_1229 {ECO:0000313|EMBL:AGL50153.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36297.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36297.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36297.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50153.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50153.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36297.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50153.1; -; Genomic_DNA. DR PIR; D72282; D72282. DR RefSeq; NP_229027.1; NC_000853.1. DR RefSeq; WP_004080068.1; NZ_CP011107.1. DR STRING; 243274.TM1222; -. DR TCDB; 3.A.1.5.14; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36297; AAD36297; TM_1222. DR EnsemblBacteria; AGL50153; AGL50153; Tmari_1229. DR GeneID; 898262; -. DR KEGG; tma:TM1222; -. DR KEGG; tmi:THEMA_08220; -. DR KEGG; tmm:Tmari_1229; -. DR KEGG; tmw:THMA_1248; -. DR PATRIC; 23937386; VBITheMar51294_1240. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR KO; K02033; -. DR OMA; IAQAIPY; -. DR OrthoDB; EOG66F098; -. DR BioCyc; TMAR243274:GC6P-1252-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 9 26 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 103 127 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 148 169 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 189 209 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 245 271 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 291 317 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 101 310 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 329 AA; 37508 MW; 4E26B89CCC438C9B CRC64; MRKYLTKKIL IYILTFFFAV TIDWAIPRFM PGNPINFLIS RFAGLPESVK VLQSYFTQAF GLDKPLWEQY INFWKALFRG DLGISIYMYP QPVAKVIARA LPYSLIVLLP AVLLSFAIGN RFGAFVARKK RLDNFALPVF YTLTASPYFW FGILLAWIFG VVIPLFPLAG AYSFGITPSF SWDFILDFLH HWVLPFGSLF LVMLGGWAIG MRNMIIYELE ANYSRYLEAL GSSQRLIRKY AYRNAILPQI TGLAIQLGTV VAGALTTEIV FSYPGIGYIL MQGILNQDYF LIQGCFLFII LGVLLANFLV DIFYVIIDPR IRKSYSGEV // ID Q9X273_THEMA Unreviewed; 317 AA. AC Q9X273; G4FGD7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 110. DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:AAD36816.1}; GN OrderedLocusNames=TM_1751 {ECO:0000313|EMBL:AAD36816.1}; GN ORFNames=Tmari_1759 {ECO:0000313|EMBL:AGL50683.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36816.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36816.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36816.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50683.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50683.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) CC family. {ECO:0000256|RuleBase:RU361153}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36816.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50683.1; -; Genomic_DNA. DR PIR; B72216; B72216. DR RefSeq; NP_229549.1; NC_000853.1. DR RefSeq; WP_004082283.1; NZ_CP011107.1. DR PDB; 3AMC; X-ray; 1.40 A; A/B=1-317. DR PDB; 3AMD; X-ray; 2.00 A; A/B/C/D=1-317. DR PDB; 3AMG; X-ray; 2.40 A; A/B=1-317. DR PDB; 3AOF; X-ray; 1.29 A; A/B=1-317. DR PDB; 3AZR; X-ray; 1.71 A; A/B=1-317. DR PDB; 3AZS; X-ray; 1.69 A; A/B=1-317. DR PDB; 3AZT; X-ray; 1.80 A; A/B/C/D=1-317. DR PDB; 3MMU; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-317. DR PDB; 3MMW; X-ray; 1.85 A; A/B/C/D=1-317. DR PDBsum; 3AMC; -. DR PDBsum; 3AMD; -. DR PDBsum; 3AMG; -. DR PDBsum; 3AOF; -. DR PDBsum; 3AZR; -. DR PDBsum; 3AZS; -. DR PDBsum; 3AZT; -. DR PDBsum; 3MMU; -. DR PDBsum; 3MMW; -. DR STRING; 243274.TM1751; -. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR EnsemblBacteria; AAD36816; AAD36816; TM_1751. DR EnsemblBacteria; AGL50683; AGL50683; Tmari_1759. DR GeneID; 897863; -. DR KEGG; tma:TM1751; -. DR KEGG; tmm:Tmari_1759; -. DR KEGG; tmw:THMA_1793; -. DR PATRIC; 23938478; VBITheMar51294_1769. DR eggNOG; ENOG4108K2F; Bacteria. DR eggNOG; COG2730; LUCA. DR KO; K01179; -. DR OMA; WAYWEFC; -. DR OrthoDB; EOG66F040; -. DR BioCyc; MetaCyc:MONOMER-16877; -. DR BioCyc; TMAR243274:GC6P-1799-MONOMER; -. DR BRENDA; 3.2.1.4; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central. DR GO; GO:0006073; P:cellular glucan metabolic process; IBA:GO_Central. DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR018087; Glyco_hydro_5_CS. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF00150; Cellulase; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3AMC, ECO:0000213|PDB:3AMD, KW ECO:0000213|PDB:3AMG, ECO:0000213|PDB:3AOF}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361153}; KW Hydrolase {ECO:0000256|RuleBase:RU361153}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 28 288 Cellulase. {ECO:0000259|Pfam:PF00150}. FT BINDING 20 20 Beta-D-mannose. {ECO:0000213|PDB:3AZS}. FT BINDING 30 30 Beta-D-mannose. {ECO:0000213|PDB:3AZS}. FT BINDING 95 95 Glucose. {ECO:0000213|PDB:3AZT}. FT BINDING 96 96 Mannose. {ECO:0000213|PDB:3AZS}. FT BINDING 135 135 Glucose. {ECO:0000213|PDB:3AZT}. FT BINDING 136 136 Mannose. {ECO:0000213|PDB:3AZS}. FT BINDING 198 198 Glucose. {ECO:0000213|PDB:3AZT}. FT BINDING 198 198 Mannose. {ECO:0000213|PDB:3AZS}. FT BINDING 205 205 Glucose. {ECO:0000213|PDB:3AZT}. FT BINDING 205 205 Mannose. {ECO:0000213|PDB:3AZS}. FT BINDING 210 210 Beta-D-mannose. {ECO:0000213|PDB:3AZS}. FT BINDING 210 210 Glucose. {ECO:0000213|PDB:3AZT}. FT BINDING 286 286 Glucose. {ECO:0000213|PDB:3AZT}. SQ SEQUENCE 317 AA; 37384 MW; F7DF20958A9A1435 CRC64; MGVDPFERNK ILGRGINIGN ALEAPNEGDW GVVIKDEFFD IIKEAGFSHV RIPIRWSTHA YAFPPYKIMD RFFKRVDEVI NGALKRGLAV VINIHHYEEL MNDPEEHKER FLALWKQIAD RYKDYPETLF FEILNEPHGN LTPEKWNELL EEALKVIRSI DKKHTIIIGT AEWGGISALE KLSVPKWEKN SIVTIHYYNP FEFTHQGAEW VEGSEKWLGR KWGSPDDQKH LIEEFNFIEE WSKKNKRPIY IGEFGAYRKA DLESRIKWTS FVVREMEKRR WSWAYWEFCS GFGVYDTLRK TWNKDLLEAL IGGDSIE // ID Q9X0V0_THEMA Unreviewed; 557 AA. AC Q9X0V0; G4FEC3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Mannoside ABC transport system, sugar-binding protein {ECO:0000313|EMBL:AGL50154.1}; DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein {ECO:0000313|EMBL:AAD36298.1}; GN OrderedLocusNames=TM_1223 {ECO:0000313|EMBL:AAD36298.1}; GN ORFNames=Tmari_1230 {ECO:0000313|EMBL:AGL50154.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36298.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36298.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36298.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50154.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50154.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36298.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50154.1; -; Genomic_DNA. DR PIR; E72282; E72282. DR RefSeq; NP_229028.1; NC_000853.1. DR RefSeq; WP_004080066.1; NZ_CP011107.1. DR PDB; 1VR5; X-ray; 1.73 A; A/B=23-557. DR PDB; 4PFT; X-ray; 1.75 A; A/B=21-557. DR PDB; 4PFY; X-ray; 1.50 A; A/B=21-557. DR PDBsum; 1VR5; -. DR PDBsum; 4PFT; -. DR PDBsum; 4PFY; -. DR STRING; 243274.TM1223; -. DR TCDB; 3.A.1.5.14; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36298; AAD36298; TM_1223. DR EnsemblBacteria; AGL50154; AGL50154; Tmari_1230. DR GeneID; 898261; -. DR KEGG; tma:TM1223; -. DR KEGG; tmi:THEMA_08215; -. DR KEGG; tmm:Tmari_1230; -. DR KEGG; tmw:THMA_1249; -. DR PATRIC; 23937388; VBITheMar51294_1241. DR eggNOG; ENOG4107QMM; Bacteria. DR eggNOG; ENOG410XNRA; LUCA. DR HOGENOM; HOG000229872; -. DR KO; K02035; -. DR OMA; DIAGYGY; -. DR OrthoDB; EOG6SV54Z; -. DR BioCyc; TMAR243274:GC6P-1253-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0042884; P:microcin transport; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VR5, ECO:0000213|PDB:4PFT, KW ECO:0000213|PDB:4PFY}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Magnesium {ECO:0000213|PDB:4PFT, ECO:0000213|PDB:4PFY}; KW Metal-binding {ECO:0000213|PDB:4PFT, ECO:0000213|PDB:4PFY}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 70 440 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. FT REGION 247 249 Beta-D-mannose binding. FT {ECO:0000213|PDB:4PFY}. FT REGION 387 390 Beta-D-mannose binding. FT {ECO:0000213|PDB:4PFY}. FT REGION 433 434 Beta-D-mannose binding. FT {ECO:0000213|PDB:4PFY}. FT REGION 461 462 Beta-D-mannose binding. FT {ECO:0000213|PDB:4PFY}. FT REGION 512 515 Beta-D-mannose binding. FT {ECO:0000213|PDB:4PFY}. FT REGION 539 540 Beta-D-mannose binding. FT {ECO:0000213|PDB:4PFY}. FT METAL 362 362 Magnesium. {ECO:0000213|PDB:4PFT, FT ECO:0000213|PDB:4PFY}. FT METAL 364 364 Magnesium. {ECO:0000213|PDB:4PFT, FT ECO:0000213|PDB:4PFY}. FT METAL 366 366 Magnesium. {ECO:0000213|PDB:4PFT, FT ECO:0000213|PDB:4PFY}. FT METAL 368 368 Magnesium. {ECO:0000213|PDB:4PFT, FT ECO:0000213|PDB:4PFY}. FT METAL 370 370 Magnesium. {ECO:0000213|PDB:4PFT, FT ECO:0000213|PDB:4PFY}. FT BINDING 122 122 Beta-D-mannose. {ECO:0000213|PDB:4PFY}. FT BINDING 129 129 Beta-D-mannose. {ECO:0000213|PDB:4PFY}. FT BINDING 152 152 Beta-D-mannose. {ECO:0000213|PDB:4PFY}. FT BINDING 159 159 Beta-D-mannose. {ECO:0000213|PDB:4PFY}. FT BINDING 231 231 Beta-D-mannose. {ECO:0000213|PDB:4PFY}. SQ SEQUENCE 557 AA; 64078 MW; B74C0179E2FBF0F8 CRC64; MKRFLVVLVL VLALVSVFGQ TFERNKTLYW GGALWSPPSN WNPFTPWNAV AGTIGLVYEP LFLYDPLNDK FEPWLAEKGE WVSNNEYVLT LRKGLRWQDG VPLTADDVVF TFEIAKKYTG ISYSPVWNWL GRIERVDERT LKFVFSDPRY QEWKQMLINT PIVPKHIWEN KTEEEVLQAA NENPVGSGPY YVESWADDRC VFKKNGNWWG IRELGYDPKP ERIVELRVLS NNVAVGMLMK GELDWSNFFL PGVPVLKKAY GIVTWYENAP YMLPANTAGI YINVNKYPLS IPEFRRAMAY AINPEKIVTR AYENMVTAAN PAGILPLPGY MKYYPKEVVD KYGFKYDPEM AKKILDELGF KDVNKDGFRE DPNGKPFKLT IECPYGWTDW MVSIQSIAED LVKVGINVEP KYPDYSKYAD DLYGGKFDLI LNNFTTGVSA TIWSYFNGVF YPDAVESEYS YSGNFGKYAN PEVETLLDEL NRSNDDAKIK EVVAKLSEIL LKDLPFIPLW YNGAWFQASE AVWTNWPTEK NPYAVPIGWN GWWQLTGIKT LFGIEAK // ID Q9X0M4_THEMA Unreviewed; 215 AA. AC Q9X0M4; G4FEK8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Acetoin utilization acuB protein {ECO:0000313|EMBL:AGL50070.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36216.1}; GN OrderedLocusNames=TM_1140 {ECO:0000313|EMBL:AAD36216.1}; GN ORFNames=Tmari_1146 {ECO:0000313|EMBL:AGL50070.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36216.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36216.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36216.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50070.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50070.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36216.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50070.1; -; Genomic_DNA. DR PIR; H72290; H72290. DR RefSeq; NP_228946.1; NC_000853.1. DR RefSeq; WP_004080265.1; NZ_CP011107.1. DR STRING; 243274.TM1140; -. DR EnsemblBacteria; AAD36216; AAD36216; TM_1140. DR EnsemblBacteria; AGL50070; AGL50070; Tmari_1146. DR GeneID; 898624; -. DR KEGG; tma:TM1140; -. DR KEGG; tmi:THEMA_08645; -. DR KEGG; tmm:Tmari_1146; -. DR KEGG; tmw:THMA_1163; -. DR PATRIC; 23937215; VBITheMar51294_1156. DR eggNOG; ENOG4105FI1; Bacteria. DR eggNOG; COG0517; LUCA. DR KO; K04767; -. DR OMA; VWEMNYL; -. DR OrthoDB; EOG6SNDTJ; -. DR BioCyc; TMAR243274:GC6P-1169-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 63 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 81 139 CBS. {ECO:0000259|PROSITE:PS51371}. SQ SEQUENCE 215 AA; 24485 MW; F5C04BFFDC536D7F CRC64; MLVKDFMTRN PITIAPETSF SEALKLMKQN KIKRLIVMKN EKIVGIVTEK DLLYASPSKA TTLNIWELHY LLSKLKIEEI MTKDVVTVNE NTPIEDAARI MEEKDISGLP VVDDAGRLVG IITQTDIFKV FVEIFGTKRE GTIRYTMEMP DKPGELLEVA KRIYEAGGNI ISIATLFEEG KDSYLATLRV ENIDHEKFVK SLDEIDVKLL YYHSN // ID Q9X1F3_THEMA Unreviewed; 234 AA. AC Q9X1F3; G4FFH5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Translation initiation factor, eIF-2B alpha subunit-related {ECO:0000313|EMBL:AAD36509.1}; DE SubName: Full=Translation initiation factor, eIF-2B alpha subunit-related protein {ECO:0000313|EMBL:AGL50370.1}; GN OrderedLocusNames=TM_1440 {ECO:0000313|EMBL:AAD36509.1}; GN ORFNames=Tmari_1446 {ECO:0000313|EMBL:AGL50370.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36509.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36509.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36509.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50370.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50370.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits CC family. {ECO:0000256|RuleBase:RU003814}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36509.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50370.1; -; Genomic_DNA. DR PIR; E72252; E72252. DR RefSeq; NP_229239.1; NC_000853.1. DR RefSeq; WP_004081711.1; NZ_CP011107.1. DR STRING; 243274.TM1440; -. DR EnsemblBacteria; AAD36509; AAD36509; TM_1440. DR EnsemblBacteria; AGL50370; AGL50370; Tmari_1446. DR GeneID; 898035; -. DR KEGG; tma:TM1440; -. DR KEGG; tmi:THEMA_07115; -. DR KEGG; tmm:Tmari_1446; -. DR KEGG; tmw:THMA_1470; -. DR PATRIC; 23937830; VBITheMar51294_1453. DR eggNOG; ENOG4107I32; Bacteria. DR eggNOG; COG1184; LUCA. DR OMA; VADPFKF; -. DR OrthoDB; EOG6038W7; -. DR BioCyc; TMAR243274:GC6P-1478-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IBA:GO_Central. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. DR GO; GO:0019509; P:L-methionine biosynthetic process from methylthioadenosine; IBA:GO_Central. DR InterPro; IPR000649; IF-2B-related. DR Pfam; PF01008; IF-2B; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Initiation factor {ECO:0000313|EMBL:AAD36509.1}; KW Protein biosynthesis {ECO:0000313|EMBL:AAD36509.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 234 AA; 26421 MW; 9EC4EEC45EC40F9E CRC64; MEVLSFLKEL NTEGSQEVLE KLLKFLKENS EKLDSGEVSK EIGIFCEEKP MAVLEKLAFF LENHSLKELE KFERAVEKSF ARTTDYASNF FKNKKILTLS NSKTLLEVFR KARPPMVFVL ESHPGGEGKI LVESLRKIHL RAEPVEDLLA YRILRMVDVC LTGADYVDES GNVLNKVGTT TLAILSRELR KPFFVVADPF KFGSKKLKDT NLFEVVPSEL ITAIITDPEG GTLC // ID Q9WZA3_THEMA Unreviewed; 77 AA. AC Q9WZA3; G4FDI8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35719.1}; GN OrderedLocusNames=TM_0635 {ECO:0000313|EMBL:AAD35719.1}; GN ORFNames=Tmari_0636 {ECO:0000313|EMBL:AGL49561.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35719.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35719.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35719.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49561.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49561.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35719.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49561.1; -; Genomic_DNA. DR PIR; H72353; H72353. DR RefSeq; NP_228444.1; NC_000853.1. DR RefSeq; WP_004081162.1; NZ_CP011107.1. DR STRING; 243274.TM0635; -. DR EnsemblBacteria; AAD35719; AAD35719; TM_0635. DR EnsemblBacteria; AGL49561; AGL49561; Tmari_0636. DR GeneID; 897732; -. DR KEGG; tma:TM0635; -. DR KEGG; tmi:THEMA_01485; -. DR KEGG; tmm:Tmari_0636; -. DR KEGG; tmw:THMA_0651; -. DR PATRIC; 23936183; VBITheMar51294_0645. DR eggNOG; ENOG4108E6R; Bacteria. DR eggNOG; ENOG41103HC; LUCA. DR OMA; DFFNIRV; -. DR OrthoDB; EOG6NWBWV; -. DR BioCyc; TMAR243274:GC6P-660-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 77 AA; 8869 MW; 96830A414996C03B CRC64; MMTILPFLKD VLPLAVSLVE RPGDGESKKE EVKEIVFGLF DSFGIDLPFD YDILDHILDY AIDFVVDFFN DRVWNNA // ID Q9X245_THEMA Unreviewed; 392 AA. AC Q9X245; G4FGA8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36787.1}; GN OrderedLocusNames=TM_1721 {ECO:0000313|EMBL:AAD36787.1}; GN ORFNames=Tmari_1729 {ECO:0000313|EMBL:AGL50653.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36787.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36787.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36787.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50653.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50653.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36787.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50653.1; -; Genomic_DNA. DR PIR; E72219; E72219. DR RefSeq; NP_229520.1; NC_000853.1. DR RefSeq; WP_004082237.1; NZ_CP011107.1. DR STRING; 243274.TM1721; -. DR DNASU; 897878; -. DR EnsemblBacteria; AAD36787; AAD36787; TM_1721. DR EnsemblBacteria; AGL50653; AGL50653; Tmari_1729. DR GeneID; 897878; -. DR KEGG; tma:TM1721; -. DR KEGG; tmi:THEMA_05635; -. DR KEGG; tmm:Tmari_1729; -. DR KEGG; tmw:THMA_1763; -. DR PATRIC; 23938418; VBITheMar51294_1739. DR eggNOG; ENOG4106X2I; Bacteria. DR eggNOG; ENOG410YN3T; LUCA. DR OMA; SWDVRVK; -. DR OrthoDB; EOG6XQ3M6; -. DR BioCyc; TMAR243274:GC6P-1769-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 392 AA; 44690 MW; 9F686190C8ED650A CRC64; MRSLLFLLFA STTIFATPVL ILFQDSAILM ESLSVSGTET VSVPQDWNVM DVIGAKSWYV VSEKEPSWEE IIKGKTVEAV DEPPSRFEVI STSPLVLKKD TKYYIYNSTL KKWLVLEYEE PQSSRKLVMN GQGKVTLLLR SSGSWNVRYY LFEDTLTGNA FLSVSGVESA DVFLISRPAG EASIWKGMYL SASPSREMPE EHESEEVKVY HLGKVKDLDK SPVVNLIETN LFNVNEYYSY SFAVNDSIFD YQKTTFTRSF MTPVDLPGGT VSIFSNISGV DIMIGETSIP DTPKNSLLEL PVTDSWDVRV KGEILDERNY KDTYEYERTW RVTVQNLNET ESKVRINIYG NMMRLLRSSI KPLKETSDQI VFELIVPPNS EKEFEFKVRS GW // ID Q9WYN7_THEMA Unreviewed; 200 AA. AC Q9WYN7; G4FHW5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=2-oxoglutarate oxidoreductase, gamma subunit {ECO:0000313|EMBL:AGL49328.1}; DE EC=1.2.7.3 {ECO:0000313|EMBL:AGL49328.1}; DE SubName: Full=Keto/oxoacid ferredoxin oxidoreductase, gamma subunit, putative {ECO:0000313|EMBL:AAD35491.1}; GN OrderedLocusNames=TM_0406 {ECO:0000313|EMBL:AAD35491.1}; GN ORFNames=Tmari_0403 {ECO:0000313|EMBL:AGL49328.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35491.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35491.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35491.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49328.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49328.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35491.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49328.1; -; Genomic_DNA. DR PIR; D72380; D72380. DR RefSeq; NP_228216.1; NC_000853.1. DR RefSeq; WP_004083247.1; NZ_CP011107.1. DR STRING; 243274.TM0406; -. DR DNASU; 897405; -. DR EnsemblBacteria; AAD35491; AAD35491; TM_0406. DR EnsemblBacteria; AGL49328; AGL49328; Tmari_0403. DR GeneID; 897405; -. DR KEGG; tma:TM0406; -. DR KEGG; tmi:THEMA_02695; -. DR KEGG; tmm:Tmari_0403; -. DR KEGG; tmw:THMA_0412; -. DR PATRIC; 23935695; VBITheMar51294_0411. DR eggNOG; ENOG4105J7M; Bacteria. DR eggNOG; COG1014; LUCA. DR KO; K00177; -. DR OMA; IDYPKVQ; -. DR OrthoDB; EOG6HJ26D; -. DR BioCyc; TMAR243274:GC6P-421-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.920.10; -; 1. DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat. DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen. DR Pfam; PF01558; POR; 1. DR SUPFAM; SSF53323; SSF53323; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49328.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 13 177 POR. {ECO:0000259|Pfam:PF01558}. SQ SEQUENCE 200 AA; 22740 MW; D363F8DD83062DA4 CRC64; MTEPVSIRIA GISGQGNILA GLILAKALVY EGKWVVQTQS YSAQVRGDVS YCDVLYDDSP IDYPESEYFD IVCILHQKAM DELYKSVKVN GVVILDQTFV KNVPDFVKRI TRKILFVPAT ERAISEFKTA MVSNVIMVGV LAKVCNIVKL DSLKRALKDH VRRPLWDINL KALEFGYNMF EKQFKIKTER VWKRLAAGFE // ID Q9WZH1_THEMA Unreviewed; 254 AA. AC Q9WZH1; G4FDB2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=Serine protease {ECO:0000313|EMBL:AGL49637.1}; DE EC=3.4.21.- {ECO:0000313|EMBL:AGL49637.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35794.1}; GN OrderedLocusNames=TM_0712 {ECO:0000313|EMBL:AAD35794.1}; GN ORFNames=Tmari_0712 {ECO:0000313|EMBL:AGL49637.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35794.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35794.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35794.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49637.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49637.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35794.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49637.1; -; Genomic_DNA. DR PIR; G72343; G72343. DR RefSeq; NP_228521.1; NC_000853.1. DR RefSeq; WP_004081026.1; NZ_CP011107.1. DR STRING; 243274.TM0712; -. DR EnsemblBacteria; AAD35794; AAD35794; TM_0712. DR EnsemblBacteria; AGL49637; AGL49637; Tmari_0712. DR GeneID; 898379; -. DR KEGG; tma:TM0712; -. DR KEGG; tmm:Tmari_0712; -. DR KEGG; tmw:THMA_0727; -. DR PATRIC; 23936342; VBITheMar51294_0724. DR eggNOG; ENOG4105D78; Bacteria. DR eggNOG; COG1752; LUCA. DR KO; K07001; -. DR OMA; TESENTW; -. DR OrthoDB; EOG6KDKSZ; -. DR BioCyc; TMAR243274:GC6P-738-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR002641; Patatin/PLipase_A2-rel. DR Pfam; PF01734; Patatin; 1. DR SUPFAM; SSF52151; SSF52151; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49637.1}; KW Protease {ECO:0000313|EMBL:AGL49637.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 8 171 Patatin. {ECO:0000259|Pfam:PF01734}. SQ SEQUENCE 254 AA; 28280 MW; 4727C28C78EF6778 CRC64; MSVTKGIAFA AGGVKGATHI AFLERSGDVF DVVTGSSIGA VVGGLYALYG EPALVKDITF SLMKKHFEDL KKTESENTWR GLFQRSLFKA DLLFSVLKEA FGRKKFSDCK KTLGVVVFDT ENMDSLLVTE GFLIDAVVAS SSVPGYFEPI WIGGTPSLDG GVLAPTPVSQ ARELGADFVV ASAFNRERKD GFKNHFEMFF VMDRWKEILL EREELSKADF VVIHDVNEPW NAFDKYEEIY RKALKNLRGV ILPW // ID Q9X2B3_THEMA Unreviewed; 330 AA. AC Q9X2B3; G4FGI1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=CRISPR-associated RAMP Cmr3 {ECO:0000313|EMBL:AGL50727.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36856.1}; GN OrderedLocusNames=TM_1793 {ECO:0000313|EMBL:AAD36856.1}; GN ORFNames=Tmari_1803 {ECO:0000313|EMBL:AGL50727.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36856.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36856.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36856.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50727.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50727.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36856.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50727.1; -; Genomic_DNA. DR PIR; F72209; F72209. DR RefSeq; NP_229590.1; NC_000853.1. DR RefSeq; WP_004082340.1; NZ_CP011107.1. DR STRING; 243274.TM1793; -. DR EnsemblBacteria; AAD36856; AAD36856; TM_1793. DR EnsemblBacteria; AGL50727; AGL50727; Tmari_1803. DR GeneID; 897838; -. DR KEGG; tma:TM1793; -. DR KEGG; tmi:THEMA_05225; -. DR KEGG; tmm:Tmari_1803; -. DR KEGG; tmw:THMA_1839; -. DR PATRIC; 23938575; VBITheMar51294_1814. DR eggNOG; ENOG410830Y; Bacteria. DR eggNOG; COG1769; LUCA. DR KO; K09127; -. DR OMA; IYFEPED; -. DR OrthoDB; EOG67MF12; -. DR BioCyc; TMAR243274:GC6P-1844-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR010165; CRISPR-assoc_prot_TM1793. DR InterPro; IPR019117; CRISPR-assoc_protein_Cmr3. DR Pfam; PF09700; Cas_Cmr3; 1. DR TIGRFAMs; TIGR01888; cas_cmr3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 330 AA; 37914 MW; D8D24153422BA4E1 CRC64; MKLWAIYFEP EDWVGFRETR RFSFSDRVES VFPSSFPFYG AVRTALLMKN QKFDPGDVER AGDVRMFGPF VFENTPEGRK HYFPLPRNIY KTDSGYRVTP IVEIDGVYLP WKPEYKMDSK ESTSGGLIEL SDLELLRSNT QGVCKFDLVS AEKIFKKETH IGVAFEENRK KVKERMIYSI SYYRFYDGGF FMFTDDERTV ELVSKLDGVF LGMKSKWSAV EVEELNTTAF DPPDYKNVAV ALITPAVFDG GGMPKDKTIL GKRVLTTAGI RKQVVSGWDL RENKPKKIYH AVSPGAVYYL EGKVNGHVLN ESKFTDFGFG RCIFMKYEKL // ID Q9X0I9_THEMA Unreviewed; 452 AA. AC Q9X0I9; G4FEP3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 102. DE SubName: Full=NADH dehydrogenase, putative {ECO:0000313|EMBL:AAD36181.1}; DE SubName: Full=Na(+) H(+) antiporter subunit D {ECO:0000313|EMBL:AGL50035.1}; GN OrderedLocusNames=TM_1105 {ECO:0000313|EMBL:AAD36181.1}; GN ORFNames=Tmari_1111 {ECO:0000313|EMBL:AGL50035.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36181.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36181.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36181.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50035.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50035.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000320}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU000320}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36181.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50035.1; -; Genomic_DNA. DR PIR; C72295; C72295. DR RefSeq; NP_228911.1; NC_000853.1. DR RefSeq; WP_004080330.1; NZ_CP011107.1. DR STRING; 243274.TM1105; -. DR DNASU; 898660; -. DR EnsemblBacteria; AAD36181; AAD36181; TM_1105. DR EnsemblBacteria; AGL50035; AGL50035; Tmari_1111. DR GeneID; 898660; -. DR KEGG; tma:TM1105; -. DR KEGG; tmi:THEMA_08820; -. DR KEGG; tmm:Tmari_1111; -. DR KEGG; tmw:THMA_1128; -. DR PATRIC; 23937143; VBITheMar51294_1120. DR eggNOG; ENOG4106PJR; Bacteria. DR eggNOG; COG0651; LUCA. DR KO; K05568; -. DR OMA; TRSEKNT; -. DR OrthoDB; EOG6K3ZWS; -. DR BioCyc; TMAR243274:GC6P-1134-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR001750; ND/Mrp_mem. DR Pfam; PF00361; Proton_antipo_M; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 21 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 26 44 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 87 104 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 110 128 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 140 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 176 197 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 209 226 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 232 254 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 314 336 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 351 369 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 381 400 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 406 423 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 435 451 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 104 360 Proton_antipo_M. FT {ECO:0000259|Pfam:PF00361}. SQ SEQUENCE 452 AA; 50539 MW; 19BEFCD6664F4E95 CRC64; MIFLVYNFLI ISLGIVFLFL KRKAPWWTAL VNLVFTVTMV LSGYRFDLVL TGNFGVHLLL DQTSYFFLIL TAVVLLAVFT KGLNVSLSNL LLILLGALNL AFVSYDLFNI YVTVEVVSLI TFLLVVEGRK KIQYWSAFKY LILGTVGMNL YLIGIGVLYA GNGTLSISDI SKVDSFASVL VAVGLLLRAG VFLFSMWLPQ VHSEAETPIS AVLSGVVVKS AVYALVRLEH VVNWDVVKIF AIFSALSGVL FAFLSKDYKR ILAYSTLSQI GIVLASPVTA PVYALAHGVF KSWLFLLKDE LPERDVTKWK RLDFWTWLSL SLASLSIMGL PGLAGFSKNL VLEQLHGWEK IFMEVVFVGT AASFWKFLLK PFEFKKKLPG MYNPVLLIAS LTIGLYFASW ERVLESFLLM GAGLLVHFLF KNLKIEKYPL EDFESMLGVY LLGVVVCLFL SL // ID Q9WZC9_THEMA Unreviewed; 311 AA. AC Q9WZC9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35745.1}; GN OrderedLocusNames=TM_0661 {ECO:0000313|EMBL:AAD35745.1}; GN ORFNames=Tmari_0661 {ECO:0000313|EMBL:AGL49586.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35745.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35745.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35745.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49586.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49586.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35745.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49586.1; -; Genomic_DNA. DR PIR; B72349; B72349. DR RefSeq; NP_228470.1; NC_000853.1. DR RefSeq; WP_010865178.1; NZ_CP011107.1. DR STRING; 243274.TM0661; -. DR EnsemblBacteria; AAD35745; AAD35745; TM_0661. DR EnsemblBacteria; AGL49586; AGL49586; Tmari_0661. DR GeneID; 897774; -. DR KEGG; tma:TM0661; -. DR KEGG; tmi:THEMA_01360; -. DR KEGG; tmm:Tmari_0661; -. DR KEGG; tmw:THMA_0676; -. DR PATRIC; 23936236; VBITheMar51294_0671. DR eggNOG; ENOG4106CQJ; Bacteria. DR eggNOG; ENOG410Y4A3; LUCA. DR OMA; LEILFWY; -. DR OrthoDB; EOG6FBX04; -. DR BioCyc; TMAR243274:GC6P-686-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 127 154 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 311 AA; 36383 MW; CE5BDD3D1EE7D7E8 CRC64; MQMKQVLLEA RQDFLSLLKR RGWKEKDLNI LRGIFLGELS RVDVPADIFE LAIKEAVKGN LKLSSKLLGV SEIDTLEILF WYLPKKYPLP SERLKKRLKA ESVKEFIEEA NRLRVKLGKK DFMELYLHLE EAEEEEEKRE NTDLLERVRN LSIEKLSESE IEELRYFYSL LDLRGKESVR TLNVHPYILS AIIRNPSAPI VIDGSNLLWR GGLSVSYIYE VFERLAVFRE FFFPYRIVFD RNAEFVLPVH ERKGFERWKN SPNVLFESPA DGLIISLANT MDAVVLSGDR FRDHGLPRRV RVLTPEEIEK G // ID Q9WYU7_THEMA Unreviewed; 417 AA. AC Q9WYU7; G4FDZ4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35561.1}; GN OrderedLocusNames=TM_0476 {ECO:0000313|EMBL:AAD35561.1}; GN ORFNames=Tmari_0473 {ECO:0000313|EMBL:AGL49398.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35561.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35561.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35561.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49398.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49398.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35561.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49398.1; -; Genomic_DNA. DR PIR; D72372; D72372. DR RefSeq; NP_228286.1; NC_000853.1. DR RefSeq; WP_004081490.1; NZ_CP011107.1. DR STRING; 243274.TM0476; -. DR EnsemblBacteria; AAD35561; AAD35561; TM_0476. DR EnsemblBacteria; AGL49398; AGL49398; Tmari_0473. DR GeneID; 897509; -. DR KEGG; tma:TM0476; -. DR KEGG; tmi:THEMA_02305; -. DR KEGG; tmm:Tmari_0473; -. DR KEGG; tmw:THMA_0486; -. DR PATRIC; 23935851; VBITheMar51294_0483. DR eggNOG; ENOG41070J0; Bacteria. DR eggNOG; ENOG410YXCP; LUCA. DR OMA; VAGLEVY; -. DR OrthoDB; EOG6MWN7M; -. DR BioCyc; TMAR243274:GC6P-497-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 417 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972225. SQ SEQUENCE 417 AA; 44867 MW; 0DCE9B3D01EE7CBB CRC64; MKKLLALFLV LGLLVTAAFA YEDVVKVNVS GTGYFNAYLD EEGIDLEGGI SDLSVSISPS SGSVTAPATI TAEFSIDVLG TDASLSKIAV TTDLFDLTYY NSDIYGDGYV FYYVGDRALE FTPKLGLEGI SLTAYFADIV SETDLTNATN DTNNYFDDAV ALKLGVTNLD LLDATLFGAF YDTDTNNATS AYGYAAHLNL TGKDILENLV VDLAYAYEAT SMYLVEAQYS KSFEMEPVTL TVSPYFVYSE GAPTYYDDDS VDGDGWTAPW GSKLVKVGLK AEAGVTDEVT FSAELTPTYD LDANSFSLPV TLALAYDSDM AEANVSASWD DAVASATNVT IDANLTVTAV ENLTVKAAAQ YKVATNELGY NVDTSYVYGP LTTGFFFGTL FDSNSDGTAD INDYFTWYLY LKASVAF // ID Q9WYY5_THEMA Unreviewed; 303 AA. AC Q9WYY5; G4FDV6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE SubName: Full=Putative Fe-S oxidoreductase {ECO:0000313|EMBL:AGL49436.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35600.1}; GN OrderedLocusNames=TM_0515 {ECO:0000313|EMBL:AAD35600.1}; GN ORFNames=Tmari_0511 {ECO:0000313|EMBL:AGL49436.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35600.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35600.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35600.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49436.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49436.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35600.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49436.1; -; Genomic_DNA. DR PIR; A72365; A72365. DR RefSeq; NP_228325.1; NC_000853.1. DR RefSeq; WP_004081416.1; NZ_CP011107.1. DR STRING; 243274.TM0515; -. DR EnsemblBacteria; AAD35600; AAD35600; TM_0515. DR EnsemblBacteria; AGL49436; AGL49436; Tmari_0511. DR GeneID; 897560; -. DR KEGG; tma:TM0515; -. DR KEGG; tmi:THEMA_02100; -. DR KEGG; tmm:Tmari_0511; -. DR KEGG; tmw:THMA_0527; -. DR PATRIC; 23935935; VBITheMar51294_0522. DR eggNOG; ENOG4105N5T; Bacteria. DR eggNOG; COG1242; LUCA. DR KO; K07139; -. DR OMA; GGCTYCN; -. DR OrthoDB; EOG6TFCS0; -. DR BioCyc; TMAR243274:GC6P-539-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0033588; C:Elongator holoenzyme complex; IBA:GO_Central. DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016573; P:histone acetylation; IBA:GOC. DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central. DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR032432; Radical_SAM_C. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR005911; YhcC-like. DR PANTHER; PTHR11135:SF1; PTHR11135:SF1; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF16199; Radical_SAM_C; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR01212; TIGR01212; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 19 244 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 303 AA; 35078 MW; 6981ABC76028A935 CRC64; MRYRKLSDYL KERYGERVQR IVIHGGFSCP NRDGTKGKGG CIYCDATGSG FTTLMRLPIR EQVMEMKKKY EKRGIKKFIA YFQSFSNTYA PVEMLRERYE EALVDDSIVQ LSVSTRPDLV PERVLDLFEE FKKRVDVSVE LGLQTANYRT LKKINRGHTL AEFVDAAVRV KKRGIELVVH VILNLPWDDM EDVVETAKIL SALDVDGVKL HSLYVVEGTK LAEMYKKGEV KICSLEEYID RAITFLEYLS PNVVIHRLVA DPPRKGTIFG NWGKSKIEII NMIEEELERR DTYQGKKFDY LNR // ID Q9X119_THEMA Unreviewed; 207 AA. AC Q9X119; G4FE56; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 98. DE SubName: Full=Diguanylate cyclase with PAS/PAC sensor {ECO:0000313|EMBL:AGL50225.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36367.1}; GN OrderedLocusNames=TM_1293 {ECO:0000313|EMBL:AAD36367.1}; GN ORFNames=Tmari_1301 {ECO:0000313|EMBL:AGL50225.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36367.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36367.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36367.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50225.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50225.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36367.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50225.1; -; Genomic_DNA. DR PIR; D72272; D72272. DR RefSeq; NP_229097.1; NC_000853.1. DR RefSeq; WP_004079931.1; NZ_CP011107.1. DR PDB; 1VLM; X-ray; 2.20 A; A/B=1-207. DR PDBsum; 1VLM; -. DR STRING; 243274.TM1293; -. DR EnsemblBacteria; AAD36367; AAD36367; TM_1293. DR EnsemblBacteria; AGL50225; AGL50225; Tmari_1301. DR GeneID; 898190; -. DR KEGG; tma:TM1293; -. DR KEGG; tmi:THEMA_07870; -. DR KEGG; tmm:Tmari_1301; -. DR KEGG; tmw:THMA_1319; -. DR PATRIC; 23937526; VBITheMar51294_1309. DR eggNOG; ENOG4108UV3; Bacteria. DR eggNOG; COG0500; LUCA. DR OMA; KTRGEHF; -. DR OrthoDB; EOG600DMN; -. DR BioCyc; TMAR243274:GC6P-1324-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VLM}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 41 125 Methyltransf_11. FT {ECO:0000259|Pfam:PF08241}. FT METAL 43 43 Sodium; via carbonyl oxygen. FT {ECO:0000213|PDB:1VLM}. FT METAL 97 97 Sodium; via carbonyl oxygen. FT {ECO:0000213|PDB:1VLM}. FT METAL 99 99 Sodium. {ECO:0000213|PDB:1VLM}. SQ SEQUENCE 207 AA; 23919 MW; 743BD39034BC6A62 CRC64; MWHIFERFVN EYERWFLVHR FAYLSELQAV KCLLPEGRGV EIGVGTGRFA VPLKIKIGVE PSERMAEIAR KRGVFVLKGT AENLPLKDES FDFALMVTTI CFVDDPERAL KEAYRILKKG GYLIVGIVDR ESFLGREYEK NKEKSVFYKN ARFFSTEELM DLMRKAGFEE FKVVQTLFKH PSELSEIEPV KEGYGEGAFV VIRGTKK // ID Q9WXS5_THEMA Unreviewed; 347 AA. AC Q9WXS5; G4FGY5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174}; DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174}; GN OrderedLocusNames=TM_0070 {ECO:0000313|EMBL:AAD35164.1}; GN ORFNames=Tmari_0067 {ECO:0000313|EMBL:AGL48993.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35164.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35164.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35164.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48993.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48993.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic CC linkages in xylans. {ECO:0000256|RuleBase:RU361174}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) CC family. {ECO:0000256|RuleBase:RU361174}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35164.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48993.1; -; Genomic_DNA. DR PIR; B72423; B72423. DR RefSeq; NP_227886.1; NC_000853.1. DR RefSeq; WP_004082568.1; NZ_CP011107.1. DR PDB; 1VBR; X-ray; 1.80 A; A/B=20-347. DR PDB; 1VBU; X-ray; 1.80 A; A/B=20-347. DR PDBsum; 1VBR; -. DR PDBsum; 1VBU; -. DR STRING; 243274.TM0070; -. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR EnsemblBacteria; AAD35164; AAD35164; TM_0070. DR EnsemblBacteria; AGL48993; AGL48993; Tmari_0067. DR GeneID; 896895; -. DR KEGG; tma:TM0070; -. DR KEGG; tmi:THEMA_04455; -. DR KEGG; tmm:Tmari_0067; -. DR KEGG; tmw:THMA_0066; -. DR PATRIC; 23934980; VBITheMar51294_0068. DR eggNOG; ENOG4105D9F; Bacteria. DR eggNOG; COG3693; LUCA. DR KO; K01181; -. DR OMA; VKAIQFW; -. DR OrthoDB; EOG6XQ3JG; -. DR BioCyc; TMAR243274:GC6P-70-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR001000; GH10. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF00331; Glyco_hydro_10; 1. DR PRINTS; PR00134; GLHYDRLASE10. DR SMART; SM00633; Glyco_10; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR PROSITE; PS51760; GH10_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VBR, ECO:0000213|PDB:1VBU}; KW Carbohydrate metabolism {ECO:0000313|EMBL:AAD35164.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361174, KW ECO:0000313|EMBL:AAD35164.1}; KW Hydrolase {ECO:0000256|RuleBase:RU361174, KW ECO:0000313|EMBL:AAD35164.1}; KW Polysaccharide degradation {ECO:0000313|EMBL:AAD35164.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Xylan degradation {ECO:0000313|EMBL:AAD35164.1}. FT DOMAIN 19 338 GH10 (glycosyl hydrolase family 10). FT {ECO:0000259|PROSITE:PS51760}. SQ SEQUENCE 347 AA; 40675 MW; EF9F024C4DE64FD2 CRC64; MKILPSVLIL LLGCVPVFSS QNVSLRELAE KLNIYIGFAA INNFWSLSDA EKYMEVARRE FNILTPENQM KWDTIHPERD RYNFTPAEKH VEFAEENDMI VHGHTLVWHN QLPGWITGRE WTKEELLNVL EDHIKTVVSH FKGRVKIWDV VNEAVSDSGT YRESVWYKTI GPEYIEKAFR WAKEADPDAI LIYNDYSIEE INAKSNFVYN MIKELKEKGV PVDGIGFQMH IDYRGLNYDS FRRNLERFAK LGLQIYITEM DVRIPLSGSE EYYLKKQAEV CAKIFDICLD NPAVKAIQFW GFTDKYSWVP GFFKGYGKAL LFDENYNPKP CYYAIKEVLE KKIEERK // ID Q9X230_THEMA Unreviewed; 581 AA. AC Q9X230; G4FG91; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 89. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36771.1}; GN OrderedLocusNames=TM_1704 {ECO:0000313|EMBL:AAD36771.1}; GN ORFNames=Tmari_1712 {ECO:0000313|EMBL:AGL50636.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36771.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36771.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36771.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50636.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50636.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36771.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50636.1; -; Genomic_DNA. DR PIR; B72221; B72221. DR RefSeq; NP_229504.1; NC_000853.1. DR RefSeq; WP_004082220.1; NZ_CP011107.1. DR STRING; 243274.TM1704; -. DR EnsemblBacteria; AAD36771; AAD36771; TM_1704. DR EnsemblBacteria; AGL50636; AGL50636; Tmari_1712. DR GeneID; 897140; -. DR KEGG; tma:TM1704; -. DR KEGG; tmi:THEMA_05720; -. DR KEGG; tmm:Tmari_1712; -. DR KEGG; tmw:THMA_1746; -. DR PATRIC; 23938382; VBITheMar51294_1721. DR eggNOG; ENOG4107Y8P; Bacteria. DR eggNOG; COG0760; LUCA. DR OMA; LRRMKEY; -. DR OrthoDB; EOG6ZH2DM; -. DR BioCyc; TMAR243274:GC6P-1752-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016853; F:isomerase activity; IEA:InterPro. DR InterPro; IPR000297; PPIase_PpiC. DR InterPro; IPR027304; Trigger_fact/SurA_dom. DR Pfam; PF13145; Rotamase_2; 1. DR SUPFAM; SSF109998; SSF109998; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 29 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 181 284 PpiC. {ECO:0000259|Pfam:PF13145}. FT COILED 122 149 {ECO:0000256|SAM:Coils}. FT COILED 415 444 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 581 AA; 67717 MW; 014E86EB8799554F CRC64; MRKWMKKWQG VIIWTIAIAF VAGMIWWSVS INLRNTQNNV KYTLEQSLAY ITKDGTALND PIYWLMPWEV NDYYSNLLSS YQITSLDPLF EEPRLKALIA DVFLQQKVVL YYAEKNNIKP SKKEIEQEVN NVIQTIKNDQ NQLNRIERMY GSLSNYEKNY LEPQIRVQLT IKKVQEKVGV VTEDEIKKYF EENKEDLQKQ YDRVDIEAVS FDSSSTAQEF IAKASEMGFD EAASSMNVTV QPFSNATRGI FPDEIDTALF SATPGSIVGP FYFLDQWYVF RVKTSSVLTD FNAFSNSDAY SDVKTKLEQE KFQKWLEEFM KEENLSYAFN DQVLEYWWKY LKNEEDLYEK LANLLFQGEN LAAETPDELK SLFVLLSDSK IQELTKQIAE LTQYRTALEN SQEPDEDLIK KYGKLSIEEV DARKEELEKK KAELENKKRA VVDYLYENYP SSTYVLEYAY RLHPNDINIK YNYYSNLYNQ IKPYLSTGTY DPNQIFGVLL GLYTVAEATD ASTSIRLDSY YMLYDMSLAL NDPTSAKYYL DEMKKIDPNF MDYESAYNQV EAILEAMKTT EESTPSTATG E // ID Q9WZJ1_THEMA Unreviewed; 257 AA. AC Q9WZJ1; G4FD91; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35813.1}; GN OrderedLocusNames=TM_0732 {ECO:0000313|EMBL:AAD35813.1}; GN ORFNames=Tmari_0733 {ECO:0000313|EMBL:AGL49658.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35813.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35813.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35813.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49658.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49658.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35813.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49658.1; -; Genomic_DNA. DR PIR; G72338; G72338. DR RefSeq; NP_228541.1; NC_000853.1. DR RefSeq; WP_004080994.1; NZ_CP011107.1. DR STRING; 243274.TM0732; -. DR EnsemblBacteria; AAD35813; AAD35813; TM_0732. DR EnsemblBacteria; AGL49658; AGL49658; Tmari_0733. DR GeneID; 898399; -. DR KEGG; tma:TM0732; -. DR KEGG; tmi:THEMA_00995; -. DR KEGG; tmm:Tmari_0733; -. DR KEGG; tmw:THMA_0750; -. DR PATRIC; 23936384; VBITheMar51294_0745. DR eggNOG; ENOG4108E59; Bacteria. DR eggNOG; ENOG41103IP; LUCA. DR OMA; NHELLRM; -. DR OrthoDB; EOG6X9MKM; -. DR BioCyc; TMAR243274:GC6P-758-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR032548; DUF4940. DR Pfam; PF16298; DUF4940; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 257 AA; 29566 MW; 039B35FA900441CF CRC64; MLRFPENVVI CDGKRILWNG LGLPENLVFE MARTVLESNV PLKGKIFCFP AQTVLGKMAI FTDEKTQGRD VLVELLNHEL LRMRLYSEEV ENLVEVLFND WRPGKRVFIV RSKNFETRLS LREKLSSFAD VIYNAGEIDV GIAPAGTLLQ INEEKVSFSD PERDIKEAVR KALLIDRYVN EPFSFYEKLP AYNFSLNIQI PELVKIFLRT GDIQKTSELT EKNVEVVFRE ILKFEKKTLL SPRIPVEAFL ILKGGLD // ID Q9WZA2_THEMA Unreviewed; 120 AA. AC Q9WZA2; G4FDI9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35718.1}; GN OrderedLocusNames=TM_0634 {ECO:0000313|EMBL:AAD35718.1}; GN ORFNames=Tmari_0635 {ECO:0000313|EMBL:AGL49560.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35718.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35718.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35718.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49560.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49560.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35718.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49560.1; -; Genomic_DNA. DR PIR; G72353; G72353. DR RefSeq; NP_228443.1; NC_000853.1. DR RefSeq; WP_004081164.1; NZ_CP011107.1. DR STRING; 243274.TM0634; -. DR DNASU; 897731; -. DR EnsemblBacteria; AAD35718; AAD35718; TM_0634. DR EnsemblBacteria; AGL49560; AGL49560; Tmari_0635. DR GeneID; 897731; -. DR KEGG; tma:TM0634; -. DR KEGG; tmi:THEMA_01490; -. DR KEGG; tmm:Tmari_0635; -. DR KEGG; tmw:THMA_0650; -. DR PATRIC; 23936181; VBITheMar51294_0644. DR eggNOG; ENOG41073A1; Bacteria. DR eggNOG; ENOG410Z4XV; LUCA. DR OMA; QTICYLF; -. DR OrthoDB; EOG6MWNCW; -. DR BioCyc; TMAR243274:GC6P-659-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0016987; F:sigma factor activity; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR Pfam; PF04542; Sigma70_r2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 19 86 Sigma70_r2. {ECO:0000259|Pfam:PF04542}. SQ SEQUENCE 120 AA; 14263 MW; 83A26EBCF255077C CRC64; MPKRNTKKLK DEELTIDELY ERYQNEIRKK AGFFFEKFRE KISSFEDLYQ AICSIFCYAR KTWNKDKGSF SAHLKSTINR KVIDLIQGIP LPGCSDAPFD ILKTEYKSRC ELMDFEEENL // ID Q9WZX5_THEMA Unreviewed; 47 AA. AC Q9WZX5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35953.1}; GN OrderedLocusNames=TM_0871 {ECO:0000313|EMBL:AAD35953.1}; GN ORFNames=Tmari_0873 {ECO:0000313|EMBL:AGL49798.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35953.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35953.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35953.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49798.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49798.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35953.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49798.1; -; Genomic_DNA. DR PIR; B72323; B72323. DR RefSeq; NP_228680.1; NC_000853.1. DR RefSeq; WP_008193080.1; NC_000853.1. DR STRING; 243274.TM0871; -. DR EnsemblBacteria; AAD35953; AAD35953; TM_0871. DR EnsemblBacteria; AGL49798; AGL49798; Tmari_0873. DR GeneID; 898544; -. DR KEGG; tma:TM0871; -. DR KEGG; tmi:THEMA_00280; -. DR KEGG; tmm:Tmari_0873; -. DR PATRIC; 23936670; VBITheMar51294_0884. DR OrthoDB; EOG68WRCK; -. DR BioCyc; TMAR243274:GC6P-901-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 5 32 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 47 AA; 5605 MW; 880C6C041628FDB4 CRC64; MGVLAFHLTQ NNKKLEIEIK ELERTHQALK EEFYHISSYF DLLNPSE // ID Q9X028_THEMA Unreviewed; 351 AA. AC Q9X028; G4FF60; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 105. DE SubName: Full=MoxR-like ATPase {ECO:0000313|EMBL:AGL49857.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36011.1}; GN OrderedLocusNames=TM_0930 {ECO:0000313|EMBL:AAD36011.1}; GN ORFNames=Tmari_0932 {ECO:0000313|EMBL:AGL49857.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36011.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36011.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36011.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49857.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49857.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36011.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49857.1; -; Genomic_DNA. DR PIR; B72315; B72315. DR RefSeq; NP_228738.1; NC_000853.1. DR RefSeq; WP_004080632.1; NZ_CP011107.1. DR STRING; 243274.TM0930; -. DR EnsemblBacteria; AAD36011; AAD36011; TM_0930. DR EnsemblBacteria; AGL49857; AGL49857; Tmari_0932. DR GeneID; 898604; -. DR KEGG; tma:TM0930; -. DR KEGG; tmi:THEMA_09700; -. DR KEGG; tmm:Tmari_0932; -. DR KEGG; tmw:THMA_0952; -. DR PATRIC; 23936791; VBITheMar51294_0944. DR eggNOG; ENOG4105R55; Bacteria. DR eggNOG; COG0714; LUCA. DR OMA; HCDELNR; -. DR OrthoDB; EOG6C5RPP; -. DR BioCyc; TMAR243274:GC6P-960-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011704; ATPase_dyneun-rel_AAA. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF07728; AAA_5; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 16 157 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 351 AA; 40719 MW; D67306FECED61599 CRC64; MRVEEAKYLA KKIMMAGEIP LLVGHFGVGK TDIARDIARE TERKLIILVL SQMEPGDLIG LPARTEEKTV FLKPDWWPES GDTILFLDEI NRAHRSVRNA IMQLLVDRRI HNHILPEGTW IMAAMNPPEE EYDQADLITD PAFISRFFIL EVNPDVSEWL EWAEKNNVSK EVRDFIRDYP EFLFSERSLS LRTSLKPSPR SWYKLSNVLK TLTDDEKEKY GYVIAAGIVG PEAAKAFYDS FFQRVKIPSV ESVLFDGKIE NLEDIHAANT LVLRIVDFLS KVDVRTLERH LDDVSKNLVR LSEIMPKESF YGVLRFLVDE AQKEGEKSWI FDKILEKMLE REDMRKMVNE L // ID Q9X0G4_THEMA Unreviewed; 303 AA. AC Q9X0G4; G4FES3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36152.1}; GN OrderedLocusNames=TM_1075 {ECO:0000313|EMBL:AAD36152.1}; GN ORFNames=Tmari_1079 {ECO:0000313|EMBL:AGL50003.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36152.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36152.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36152.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50003.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50003.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36152.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50003.1; -; Genomic_DNA. DR PIR; C72296; C72296. DR RefSeq; NP_228881.1; NC_000853.1. DR RefSeq; WP_004080410.1; NZ_CP011107.1. DR STRING; 243274.TM1075; -. DR EnsemblBacteria; AAD36152; AAD36152; TM_1075. DR EnsemblBacteria; AGL50003; AGL50003; Tmari_1079. DR GeneID; 897083; -. DR KEGG; tma:TM1075; -. DR KEGG; tmi:THEMA_08980; -. DR KEGG; tmm:Tmari_1079; -. DR KEGG; tmw:THMA_1097; -. DR PATRIC; 23937079; VBITheMar51294_1088. DR eggNOG; ENOG4108QSM; Bacteria. DR eggNOG; COG1606; LUCA. DR KO; K06864; -. DR OMA; REGCKLK; -. DR OrthoDB; EOG6VXF76; -. DR BioCyc; TMAR243274:GC6P-1104-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF02540; NAD_synthase; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 69 NAD_synthase. {ECO:0000259|Pfam:PF02540}. SQ SEQUENCE 303 AA; 34064 MW; 2615EAD7481388C5 CRC64; MKDGKLYVAF SGGKDSSLVA ILAKMALGEE RVELVTVDWS PYTYERSREI VRNFAEKHGL KHTFIPSNRM QEKVWKHGPS CNACTRDVKT VLVKRYAQGH LVASGANASD SWGKTGLKVF DGVYSPLCRV GKEEINEMLK FLGLEVKKIG ESAGREGCKL KHLLKMLINP DYHGKAVSTA NEILLRVLEE HGFKPELANV KIIGPLSRNI ALVNVKPLPP EKVMNEIVEK LSAEETIDGV IVVDGPMKLV VLASPAIYRN EESRKWIKEG RLQPEFAFPI EIEWRESKNN KLRTFQVVDA RKE // ID Q9WYJ8_THEMA Unreviewed; 549 AA. AC Q9WYJ8; G4FHS5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Fibronectin-binding protein, putative {ECO:0000313|EMBL:AAD35450.1}; DE SubName: Full=Fibronectin/fibrinogen-binding protein {ECO:0000313|EMBL:AGL49286.1}; GN OrderedLocusNames=TM_0363 {ECO:0000313|EMBL:AAD35450.1}; GN ORFNames=Tmari_0361 {ECO:0000313|EMBL:AGL49286.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35450.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35450.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35450.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49286.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49286.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35450.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49286.1; -; Genomic_DNA. DR PIR; C72387; C72387. DR RefSeq; NP_228174.1; NC_000853.1. DR RefSeq; WP_004083167.1; NZ_CP011107.1. DR STRING; 243274.TM0363; -. DR DNASU; 897322; -. DR EnsemblBacteria; AAD35450; AAD35450; TM_0363. DR EnsemblBacteria; AGL49286; AGL49286; Tmari_0361. DR GeneID; 897322; -. DR KEGG; tma:TM0363; -. DR KEGG; tmi:THEMA_02900; -. DR KEGG; tmm:Tmari_0361; -. DR KEGG; tmw:THMA_0371; -. DR PATRIC; 23935607; VBITheMar51294_0368. DR eggNOG; ENOG4105F23; Bacteria. DR eggNOG; COG1293; LUCA. DR OMA; EMPGAHV; -. DR OrthoDB; EOG61GG68; -. DR BioCyc; TMAR243274:GC6P-377-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR008532; DUF814. DR Pfam; PF05670; DUF814; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 439 523 DUF814. {ECO:0000259|Pfam:PF05670}. FT COILED 286 316 {ECO:0000256|SAM:Coils}. FT COILED 360 394 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 549 AA; 64520 MW; 67534773551C8E44 CRC64; MPFDGLLLHK AVRELKELEG EHLRQIYQPT TVDYYFLFRS ATVRVCLRPD VSHVAIAEKE EASEKMPSSF TMLLRKELKG AKLLKVEQIG MDRTLRFSFE KFDEIEGIVQ KDLYIEIMGI HSNMILVRDR RIIDAHRRIV TKKREILPGR EFVIFPSGKV SIFELRELPP ESEKTIRNVL LSLLEGFSPV SVEELIHRTG YELDTPWKAV DQRKILEVLE EIKKELELPG VFVYYEASHP VEVSAFRFTM LSLKERYFEK PSEGINEFVR WKEEKSTFEN TKNRFIKVVV NRIEDLEDLE EKLSRELSEA EKAERYKKLG DLIVQNLWSI KGKSGEVELT DWETNEKIVV DVGKDPAQTA QKFYNTYKKL QRKKEQVEKR LEEIQREKEY LYQLWQTIED AEDLETLEEI EEEMREFGLL KERKTKKQKS KKTRFREVYY GGFKILIGRN NKQNDELVRT SSKEDLWFHA HEMPGAHVVV KTEGKKVPQE VVEYAASLAA GYSKGKNSGK VPVDYTFIKY VRKPKGFKPG MVIYKNYKTI LVEPRRIEG // ID Q9WYT3_THEMA Unreviewed; 311 AA. AC Q9WYT3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 102. DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028}; DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028}; GN OrderedLocusNames=TM_0462 {ECO:0000313|EMBL:AAD35547.1}; GN ORFNames=Tmari_0459 {ECO:0000313|EMBL:AGL49384.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35547.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35547.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35547.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49384.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49384.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil. CC {ECO:0000256|RuleBase:RU362028}. CC -!- CATALYTIC ACTIVITY: RNA uridine = RNA pseudouridine. CC {ECO:0000256|RuleBase:RU362028}. CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family. CC {ECO:0000256|RuleBase:RU362028}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35547.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49384.1; -; Genomic_DNA. DR PIR; F72373; F72373. DR RefSeq; NP_228272.1; NC_000853.1. DR RefSeq; WP_010865125.1; NZ_CP011107.1. DR STRING; 243274.TM0462; -. DR EnsemblBacteria; AAD35547; AAD35547; TM_0462. DR EnsemblBacteria; AGL49384; AGL49384; Tmari_0459. DR GeneID; 897493; -. DR KEGG; tma:TM0462; -. DR KEGG; tmi:THEMA_02380; -. DR KEGG; tmm:Tmari_0459; -. DR KEGG; tmw:THMA_0472; -. DR PATRIC; 23935821; VBITheMar51294_0469. DR eggNOG; ENOG4105C34; Bacteria. DR eggNOG; COG0564; LUCA. DR KO; K06180; -. DR OMA; HDWRFAV; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; TMAR243274:GC6P-482-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR006225; PsdUridine_synth_RluC/D. DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00005; rluA_subfam; 1. DR PROSITE; PS01129; PSI_RLU; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000256|RuleBase:RU362028}; KW Lyase {ECO:0000313|EMBL:AGL49384.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 13 83 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 311 AA; 35838 MW; 5B1E2795187FC240 CRC64; MKVWRVEKRE EGWRLDQFLK EKTPSWISRS MIQKAIKEGK VKVNGQIKKP SYKLKEGEIV EVDLPEKPQE ATVQPEEIEL KVLYEDRDII VIDKPGDMIV HPVPSKLSGT LVNALLHHCK DLQGVGGKLR PGIVHRLDKE TSGVIVVAKN DFAHQSLSKQ FKDRKVKKTY ILLVKGKMKN DEGVIDLPLA RHPVLRIKMA VVETGKEAIT EYRVLKRFDD VATLVLAFPK TGRTHQIRVH MKSLGHPIMG DKIYGKPKED EIFGIKRQML HALKLGFFHP RTGEWMEFVS PLPEDFKEAI RRIHEYVRER S // ID Q9X0F9_THEMA Unreviewed; 114 AA. AC Q9X0F9; G4FES8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Putative L-rhamnose mutarotase {ECO:0000313|EMBL:AGL49998.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36147.1}; GN OrderedLocusNames=TM_1070 {ECO:0000313|EMBL:AAD36147.1}; GN ORFNames=Tmari_1074 {ECO:0000313|EMBL:AGL49998.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36147.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36147.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36147.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49998.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49998.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36147.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49998.1; -; Genomic_DNA. DR PIR; H72298; H72298. DR RefSeq; NP_228876.1; NC_000853.1. DR RefSeq; WP_004080417.1; NZ_CP011107.1. DR PDB; 1NC7; X-ray; 1.55 A; A/B/C/D=1-114. DR PDBsum; 1NC7; -. DR STRING; 243274.TM1070; -. DR EnsemblBacteria; AAD36147; AAD36147; TM_1070. DR EnsemblBacteria; AGL49998; AGL49998; Tmari_1074. DR GeneID; 897149; -. DR KEGG; tma:TM1070; -. DR KEGG; tmi:THEMA_09010; -. DR KEGG; tmm:Tmari_1074; -. DR KEGG; tmw:THMA_1092; -. DR PATRIC; 23937069; VBITheMar51294_1083. DR eggNOG; ENOG41090KT; Bacteria. DR eggNOG; COG4288; LUCA. DR OMA; WVIPDGY; -. DR OrthoDB; EOG6XDGXR; -. DR BioCyc; TMAR243274:GC6P-1099-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.60.290.11; -; 1. DR InterPro; IPR009794; DUF1362. DR Pfam; PF07100; ASRT; 1. DR PIRSF; PIRSF008711; UCP008711; 1. DR SUPFAM; SSF89232; SSF89232; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1NC7}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT BINDING 108 108 Chloride. {ECO:0000213|PDB:1NC7}. SQ SEQUENCE 114 AA; 13061 MW; 7029A33135220C64 CRC64; MNGARKWFFP DGYIPNGKRG YLVSHESLCI MNTGDETAKI RITFLFEDSK PVVHEVEISP MKSLHLRLDK LGIPKCKPYS IMAESNVPVV MQLSRLDVGK NHYTLMTTIG YWEE // ID Q9WY69_THEMA Unreviewed; 224 AA. AC Q9WY69; G4FHE0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35318.1}; GN OrderedLocusNames=TM_0226 {ECO:0000313|EMBL:AAD35318.1}; GN ORFNames=Tmari_0224 {ECO:0000313|EMBL:AGL49150.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35318.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35318.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35318.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49150.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49150.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35318.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49150.1; -; Genomic_DNA. DR PIR; E72401; E72401. DR RefSeq; NP_228041.1; NC_000853.1. DR RefSeq; WP_004082914.1; NZ_CP011107.1. DR STRING; 243274.TM0226; -. DR EnsemblBacteria; AAD35318; AAD35318; TM_0226. DR EnsemblBacteria; AGL49150; AGL49150; Tmari_0224. DR GeneID; 897124; -. DR KEGG; tma:TM0226; -. DR KEGG; tmi:THEMA_03595; -. DR KEGG; tmm:Tmari_0224; -. DR KEGG; tmw:THMA_0233; -. DR PATRIC; 23935324; VBITheMar51294_0228. DR eggNOG; ENOG4108UQV; Bacteria. DR eggNOG; COG1811; LUCA. DR KO; K07150; -. DR OMA; IIKIKVA; -. DR OrthoDB; EOG63VC40; -. DR BioCyc; TMAR243274:GC6P-239-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007563; DUF554. DR Pfam; PF04474; DUF554; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 51 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 76 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 97 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 139 165 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 177 197 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 224 AA; 23913 MW; 95884FB5D24AFDF3 CRC64; MFHYAVLLNA LGVLIGASVG FLFKRKIPQR LHDILFTVIG LTTLGIGIRM VTQGDDFLMI LLALVAGGII GELFRIEDRI EGIGKKFSDS QGFAESFLTS SLLFLVGPMT IVGSINIGLT GNADLILVKT VLDTVSATVL TATLGTGVFL SAVSVFLVQG LLVVFAKSLT FLTGDVFISD FVGTGGVMIL GLGIRILKLR EVKVGNLLPA LVLIPIFDWL KNLF // ID Q9S5W7_THEMA Unreviewed; 253 AA. AC Q9S5W7; G4FGS9; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35107.1}; GN OrderedLocusNames=TM_0013 {ECO:0000313|EMBL:AAD35107.1}; GN ORFNames=Tmari_0010 {ECO:0000313|EMBL:AGL48936.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35107.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35107.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35107.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48936.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48936.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35107.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48936.1; -; Genomic_DNA. DR PIR; G72426; G72426. DR RefSeq; NP_227829.1; NC_000853.1. DR RefSeq; WP_004082451.1; NZ_CP011107.1. DR STRING; 243274.TM0013; -. DR EnsemblBacteria; AAD35107; AAD35107; TM_0013. DR EnsemblBacteria; AGL48936; AGL48936; Tmari_0010. DR GeneID; 896825; -. DR KEGG; tma:TM0013; -. DR KEGG; tmi:THEMA_04735; -. DR KEGG; tmm:Tmari_0010; -. DR KEGG; tmw:THMA_0009; -. DR PATRIC; 23934866; VBITheMar51294_0011. DR eggNOG; ENOG4107YJH; Bacteria. DR eggNOG; COG0426; LUCA. DR OMA; MLVPQHG; -. DR OrthoDB; EOG6RZB24; -. DR BioCyc; TMAR243274:GC6P-13-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 29 221 Lactamase_B. {ECO:0000259|SMART:SM00849}. SQ SEQUENCE 253 AA; 29162 MW; 8615CB3146773BAF CRC64; MFENEILFDN GQHKFMFLGW EEKEEEIVQT NQYLILDGNE GILLDPGGAH VFPRVMSNVA EVVDLSSIRH IFYTHQDPDV TSGILLWLSI CENAKIYISS LWVRFLPHFG IYDQKRIVPI SDKGTKIKLL SGNELEILPA HFLHSTGNFV LYDPVAKILF SGDIGAAVFE KGKRYRYVDD FERHLPLMEA FHKRYMSSNA ACKKWVDMVS KKKIDMIAPQ HGAVFRGESV KKFLEWFRNL KCGVDLIDNL YSL // ID Q9X0Q8_THEMA Unreviewed; 89 AA. AC Q9X0Q8; G4FEH0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 105. DE SubName: Full=Transcriptional regulator, metal-sensing {ECO:0000313|EMBL:AAD36251.1}; GN OrderedLocusNames=TM_1176 {ECO:0000313|EMBL:AAD36251.1}; GN ORFNames=Tmari_1183 {ECO:0000313|EMBL:AGL50107.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36251.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36251.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36251.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50107.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50107.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 HTH arsR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36251.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50107.1; -; Genomic_DNA. DR PIR; C72286; C72286. DR RefSeq; NP_228981.1; NC_000853.1. DR RefSeq; WP_004080186.1; NZ_CP011107.1. DR STRING; 243274.TM1176; -. DR EnsemblBacteria; AAD36251; AAD36251; TM_1176. DR EnsemblBacteria; AGL50107; AGL50107; Tmari_1183. DR GeneID; 898310; -. DR KEGG; tma:TM1176; -. DR KEGG; tmi:THEMA_08455; -. DR KEGG; tmm:Tmari_1183; -. DR KEGG; tmw:THMA_1201; -. DR PATRIC; 23937292; VBITheMar51294_1194. DR eggNOG; ENOG410603B; Bacteria. DR eggNOG; COG0640; LUCA. DR KO; K03892; -. DR OMA; MCELEAM; -. DR OrthoDB; EOG6B3684; -. DR BioCyc; TMAR243274:GC6P-1205-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01022; HTH_5; 1. DR PRINTS; PR00778; HTHARSR. DR SMART; SM00418; HTH_ARSR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50987; HTH_ARSR_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000711}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU000711}; KW Transcription regulation {ECO:0000256|RuleBase:RU000711}. FT DOMAIN 1 89 HTH arsR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50987}. SQ SEQUENCE 89 AA; 10307 MW; E562953C7E40E7DF CRC64; MGIEEIFKAL ACRWRVEILK EIAQKDLCMC ELEAMKHLDP STLSRHISVL KKAGLVDVIR EGKRKRLILK DPRILELIEL AERIAEGRE // ID Q9X074_THEMA Unreviewed; 87 AA. AC Q9X074; G4FF16; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Putative ACR involved in oxidation of intracellular sulfur {ECO:0000313|EMBL:AGL49907.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36058.1}; GN OrderedLocusNames=TM_0979 {ECO:0000313|EMBL:AAD36058.1}; GN ORFNames=Tmari_0982 {ECO:0000313|EMBL:AGL49907.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36058.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36058.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36058.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49907.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49907.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36058.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49907.1; -; Genomic_DNA. DR PIR; H72309; H72309. DR RefSeq; NP_228787.1; NC_000853.1. DR RefSeq; WP_004080586.1; NZ_CP011107.1. DR PDB; 1RHX; NMR; -; A=1-87. DR PDB; 1X9A; NMR; -; A/B=1-87. DR PDBsum; 1RHX; -. DR PDBsum; 1X9A; -. DR STRING; 243274.TM0979; -. DR EnsemblBacteria; AAD36058; AAD36058; TM_0979. DR EnsemblBacteria; AGL49907; AGL49907; Tmari_0982. DR GeneID; 898725; -. DR KEGG; tma:TM0979; -. DR KEGG; tmi:THEMA_09455; -. DR KEGG; tmm:Tmari_0982; -. DR KEGG; tmw:THMA_1001; -. DR PATRIC; 23936887; VBITheMar51294_0992. DR eggNOG; ENOG41064JC; Bacteria. DR eggNOG; COG2168; LUCA. DR KO; K07237; -. DR OMA; MALIIIK; -. DR OrthoDB; EOG6C2WJT; -. DR BioCyc; TMAR243274:GC6P-1009-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro. DR Gene3D; 3.40.1260.10; -; 1. DR InterPro; IPR027396; DsrEFH-like. DR InterPro; IPR007215; Sulphur_relay_TusB/DsrH. DR Pfam; PF04077; DsrH; 1. DR SUPFAM; SSF75169; SSF75169; 1. DR TIGRFAMs; TIGR03011; sulf_tusB_dsrH; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1RHX, ECO:0000213|PDB:1X9A}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 87 AA; 9876 MW; CF9B845AAF77AB9F CRC64; MALVLVKYGT DHPVEKLKIR SAKAEDKIVL IQNGVFWALE ELETPAKVYA IKDDFLARGY SEEDSKVPLI TYSEFIDLLE GEEKFIG // ID Q9X0U0_THEMA Unreviewed; 293 AA. AC Q9X0U0; G4FED3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 95. DE SubName: Full=NADH dehydrogenase, putative {ECO:0000313|EMBL:AAD36288.1}; DE SubName: Full=NADH-ubiquinone oxidoreductase chain H {ECO:0000313|EMBL:AGL50144.1}; DE EC=1.6.5.3 {ECO:0000313|EMBL:AGL50144.1}; GN OrderedLocusNames=TM_1213 {ECO:0000313|EMBL:AAD36288.1}; GN ORFNames=Tmari_1220 {ECO:0000313|EMBL:AGL50144.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36288.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36288.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36288.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50144.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50144.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU000471}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000471}. CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. CC {ECO:0000256|RuleBase:RU000471}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36288.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50144.1; -; Genomic_DNA. DR PIR; C72281; C72281. DR RefSeq; NP_229018.1; NC_000853.1. DR RefSeq; WP_004080087.1; NZ_CP011107.1. DR STRING; 243274.TM1213; -. DR DNASU; 898271; -. DR EnsemblBacteria; AAD36288; AAD36288; TM_1213. DR EnsemblBacteria; AGL50144; AGL50144; Tmari_1220. DR GeneID; 898271; -. DR KEGG; tma:TM1213; -. DR KEGG; tmi:THEMA_08265; -. DR KEGG; tmm:Tmari_1220; -. DR KEGG; tmw:THMA_1239; -. DR PATRIC; 23937368; VBITheMar51294_1231. DR eggNOG; ENOG4107UN5; Bacteria. DR eggNOG; COG0650; LUCA. DR KO; K00337; -. DR OMA; HWYELVL; -. DR OrthoDB; EOG6HB9NX; -. DR BioCyc; TMAR243274:GC6P-1243-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO. DR PANTHER; PTHR11432; PTHR11432; 1. DR Pfam; PF00146; NADHdh; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW NAD {ECO:0000256|RuleBase:RU000471}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000471, KW ECO:0000313|EMBL:AGL50144.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Ubiquinone {ECO:0000313|EMBL:AGL50144.1}. FT TRANSMEM 6 22 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 114 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 126 146 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 166 185 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 239 259 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 271 291 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 293 AA; 32284 MW; E67942A548A8D607 CRC64; MIKALFNLVL AFFLVLSLEG IARKIVARVQ RRIGPPWYQN FIDVFKALSK HPFSNGWVFD FGVLMALGGS VATAMLMPLG SLKWTPFPNT DNFFVITYLF TVGALGMAMG MVGSGNPWAS IGISRALTQM LGYELPFLVV MASVIFNYKT ASIHQLITFQ GEKWNLFSMP LGAIVAFISL IGMMGKKPFD IAIAPAEIAS GPMVELSGKY LGLLQIMHDF SLFVEISLFV NVFLGGGSLG WFLVKFVTVW VVAVLISSVL PRFRIEQMLK FYWGVPLGLA FLNALFVVLG LTL // ID Q9X0R8_THEMA Unreviewed; 68 AA. AC Q9X0R8; G4FEG0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36261.1}; GN OrderedLocusNames=TM_1186 {ECO:0000313|EMBL:AAD36261.1}; GN ORFNames=Tmari_1193 {ECO:0000313|EMBL:AGL50117.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36261.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36261.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36261.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50117.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50117.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36261.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50117.1; -; Genomic_DNA. DR PIR; H72284; H72284. DR RefSeq; NP_228991.1; NC_000853.1. DR RefSeq; WP_004080155.1; NZ_CP011107.1. DR STRING; 243274.TM1186; -. DR DNASU; 898299; -. DR EnsemblBacteria; AAD36261; AAD36261; TM_1186. DR EnsemblBacteria; AGL50117; AGL50117; Tmari_1193. DR GeneID; 898299; -. DR KEGG; tma:TM1186; -. DR KEGG; tmi:THEMA_08405; -. DR KEGG; tmm:Tmari_1193; -. DR KEGG; tmw:THMA_1211; -. DR PATRIC; 23937312; VBITheMar51294_1204. DR OMA; DEEVECP; -. DR OrthoDB; EOG6K6VB1; -. DR BioCyc; TMAR243274:GC6P-1215-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR013429; Regulatory_FmdB_Zinc_ribbon. DR Pfam; PF09723; Zn-ribbon_8; 1. DR SMART; SM00834; CxxC_CXXC_SSSS; 1. DR TIGRFAMs; TIGR02605; CxxC_CxxC_SSSS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 42 CxxC_CXXC_SSSS. FT {ECO:0000259|SMART:SM00834}. SQ SEQUENCE 68 AA; 7403 MW; C47528CDB4E20AFD CRC64; MPTYTFRCKK CGEEYTVFTS YSKIDEVRCP KCNSKEKERV YRKISFSVQG GSSSSSCGGS CGGCSGCS // ID Q9WZL0_THEMA Unreviewed; 555 AA. AC Q9WZL0; G4FD72; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE SubName: Full=Uridine kinase {ECO:0000313|EMBL:AGL49677.1}; DE EC=2.7.1.48 {ECO:0000313|EMBL:AGL49677.1}; DE SubName: Full=Uridine kinase-related protein {ECO:0000313|EMBL:AAD35832.1}; GN OrderedLocusNames=TM_0751 {ECO:0000313|EMBL:AAD35832.1}; GN ORFNames=Tmari_0752 {ECO:0000313|EMBL:AGL49677.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35832.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35832.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35832.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49677.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49677.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35832.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49677.1; -; Genomic_DNA. DR PIR; B72341; B72341. DR RefSeq; NP_228560.1; NC_000853.1. DR RefSeq; WP_004080960.1; NZ_CP011107.1. DR STRING; 243274.TM0751; -. DR DNASU; 898418; -. DR EnsemblBacteria; AAD35832; AAD35832; TM_0751. DR EnsemblBacteria; AGL49677; AGL49677; Tmari_0752. DR GeneID; 898418; -. DR KEGG; tma:TM0751; -. DR KEGG; tmi:THEMA_00900; -. DR KEGG; tmm:Tmari_0752; -. DR KEGG; tmw:THMA_0769; -. DR PATRIC; 23936422; VBITheMar51294_0764. DR eggNOG; ENOG4107RC7; Bacteria. DR eggNOG; COG0441; LUCA. DR eggNOG; COG0572; LUCA. DR KO; K00876; -. DR OMA; EKNIFPY; -. DR OrthoDB; EOG6KDKQZ; -. DR BioCyc; TMAR243274:GC6P-777-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004849; F:uridine kinase activity; IBA:GO_Central. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IBA:GO_Central. DR GO; GO:0043097; P:pyrimidine nucleoside salvage; IBA:GO_Central. DR GO; GO:0006222; P:UMP biosynthetic process; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006083; PRK/URK. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR Pfam; PF00485; PRK; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF55186; SSF55186; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU003528}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|RuleBase:RU003528, ECO:0000256|SAAS:SAAS00457248, KW ECO:0000313|EMBL:AAD35832.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU003528}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU003528, KW ECO:0000256|SAAS:SAAS00457248, ECO:0000313|EMBL:AAD35832.1}. FT DOMAIN 289 449 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 555 AA; 64987 MW; CA13264201D0BAAA CRC64; MRKITLRSKL DGREIVFEEN QNLFDIAREY QKYYRYKILA ARVNNRIIEL FRTPDRSGEL EFLDLTDPDG LRIYQRGLVF LASLAVRKLN SEWRLKVLHS LGKGIYCEIY KGNELIVPDQ NQVFAIKDKM RELVEKDLPI EKRTFYKDEA REILMKEGLV KTVNLFKYRK KRTVKLYHCD GFWAYFYGYL PPSTGRIDVF DVQPYNQGLV LVHPDPKTRE LPVIHMPKLS QVFLEYARWL NVLELEYVSD LNDIIARGER HVADLMLLSE ALHEKKISDI ADEIAKDKRK RLILIAGPSS SGKTTFAKRL SLQLRVNGLK PVAISLDDYF VDREKTPRDE NGNYDFDSIE ALDIELFNRN LQDLLAGKEV VLPKFNFKTG KRMRGPTLKL EKDNIIIVEG IHGLNERLTA SIPKEQKFKI YVSALTQLNI DDHNRVTTTD TRLIRRIVRD YKFRGHTAYD TLKMWPNVRK GEERNIFPFQ EEADVMFNSA LVYEIPVLRI FAEPLLVQVP EDVPEYSEAL RLLKLLDFFL PITNIEDIPD KSILREFIGR SIFKY // ID Q9X0A3_THEMA Unreviewed; 135 AA. AC Q9X0A3; G4FEY7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:AGL49937.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36075.1}; GN OrderedLocusNames=TM_1010 {ECO:0000313|EMBL:AAD36075.1}; GN ORFNames=Tmari_1013 {ECO:0000313|EMBL:AGL49937.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36075.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36075.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36075.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49937.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49937.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36075.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49937.1; -; Genomic_DNA. DR PIR; B72308; B72308. DR RefSeq; NP_228816.1; NC_000853.1. DR RefSeq; WP_004080530.1; NZ_CP011107.1. DR PDB; 2F4P; X-ray; 1.90 A; A/B/C/D=1-135. DR PDBsum; 2F4P; -. DR STRING; 243274.TM1010; -. DR EnsemblBacteria; AAD36075; AAD36075; TM_1010. DR EnsemblBacteria; AGL49937; AGL49937; Tmari_1013. DR GeneID; 898693; -. DR KEGG; tma:TM1010; -. DR KEGG; tmi:THEMA_09305; -. DR KEGG; tmm:Tmari_1013; -. DR KEGG; tmw:THMA_1032; -. DR PATRIC; 23936949; VBITheMar51294_1023. DR eggNOG; ENOG4108Z0A; Bacteria. DR eggNOG; COG1917; LUCA. DR OMA; VWVKMLV; -. DR OrthoDB; EOG68Q0WZ; -. DR BioCyc; TMAR243274:GC6P-1039-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR013096; Cupin_2. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF07883; Cupin_2; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2F4P}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 41 104 Cupin_2. {ECO:0000259|Pfam:PF07883}. SQ SEQUENCE 135 AA; 15052 MW; E2B0AE384EDBE8E5 CRC64; MVDDIFERGS KGSSDFFTGN VWVKMLVTDE NGVFNTQVYD VVFEPGARTH WHSHPGGQIL IVTRGKGFYQ ERGKPARILK KGDVVEIPPN VVHWHGAAPD EELVHIGIST QVHLGPAEWL GSVTEEEYRK ATEGK // ID Q9S5X5_THEMA Unreviewed; 306 AA. AC Q9S5X5; G4FEI6; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Esterase {ECO:0000313|EMBL:AAD36236.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL50091.1}; GN OrderedLocusNames=TM_1160 {ECO:0000313|EMBL:AAD36236.1}; GN ORFNames=Tmari_1167 {ECO:0000313|EMBL:AGL50091.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36236.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36236.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36236.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50091.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50091.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36236.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50091.1; -; Genomic_DNA. DR PIR; F72287; F72287. DR RefSeq; NP_228966.1; NC_000853.1. DR RefSeq; WP_004080211.1; NZ_CP011107.1. DR STRING; 243274.TM1160; -. DR ESTHER; thema-TM1160; Hormone-sensitive_lipase_like. DR EnsemblBacteria; AAD36236; AAD36236; TM_1160. DR EnsemblBacteria; AGL50091; AGL50091; Tmari_1167. DR GeneID; 898326; -. DR KEGG; tma:TM1160; -. DR KEGG; tmi:THEMA_08535; -. DR KEGG; tmm:Tmari_1167; -. DR KEGG; tmw:THMA_1185; -. DR PATRIC; 23937257; VBITheMar51294_1177. DR eggNOG; ENOG4108QZM; Bacteria. DR eggNOG; COG0657; LUCA. DR OMA; DPLVPHC; -. DR OrthoDB; EOG61P6SQ; -. DR BioCyc; TMAR243274:GC6P-1189-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR001375; Peptidase_S9. DR Pfam; PF00326; Peptidase_S9; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 285 Peptidase_S9. {ECO:0000259|Pfam:PF00326}. SQ SEQUENCE 306 AA; 35175 MW; 52EA71452E667565 CRC64; MVKLIIKFGL IIISFVVLFS NALLGLLFFF LLSLPVVRNA VLGRLPIKLK KSVTGNVYTY EYKNSLKMDV YYPSVKRESY PFVLFAHGGG WISGYRRQPN NVSWYRFLNA NGFAVATFDY RYGYFHYIED ILEDLKSAIS FLNENREHLL IKNLNLMGLS AGGHLVLYHA MRSSKEGEKD FDGNVVAWYA PCDLLDLWSM ETSSLFARFS VATTLKGFPV RKKEDYVFYS PVAWVNPKAP STMLVHGMKD DVVPYISSVK MYKKLRENGV EAKLRLHPEG KHGFEFVLKD SLTVKFLYET VSFLKR // ID Q9WZR2_THEMA Unreviewed; 307 AA. AC Q9WZR2; G4FD19; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Lipophilic protein, putative {ECO:0000313|EMBL:AAD35887.1}; DE SubName: Full=Undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:AGL49731.1}; DE EC=2.7.8.- {ECO:0000313|EMBL:AGL49731.1}; GN OrderedLocusNames=TM_0805 {ECO:0000313|EMBL:AAD35887.1}; GN ORFNames=Tmari_0806 {ECO:0000313|EMBL:AGL49731.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35887.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35887.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35887.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49731.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49731.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35887.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49731.1; -; Genomic_DNA. DR PIR; F72330; F72330. DR RefSeq; NP_228614.1; NC_000853.1. DR RefSeq; WP_004080858.1; NZ_CP011107.1. DR STRING; 243274.TM0805; -. DR EnsemblBacteria; AAD35887; AAD35887; TM_0805. DR EnsemblBacteria; AGL49731; AGL49731; Tmari_0806. DR GeneID; 898473; -. DR KEGG; tma:TM0805; -. DR KEGG; tmi:THEMA_00625; -. DR KEGG; tmm:Tmari_0806; -. DR KEGG; tmw:THMA_0824; -. DR PATRIC; 23936530; VBITheMar51294_0817. DR eggNOG; ENOG4105ESV; Bacteria. DR eggNOG; COG0472; LUCA. DR OMA; HEKATPY; -. DR OrthoDB; EOG69GZPZ; -. DR BioCyc; TMAR243274:GC6P-832-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro. DR InterPro; IPR000715; Glycosyl_transferase_4. DR PANTHER; PTHR22926; PTHR22926; 1. DR Pfam; PF00953; Glycos_transf_4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49731.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 47 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 126 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 155 172 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 184 203 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 209 228 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 258 278 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 284 304 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 307 AA; 34357 MW; 80EC7FE63302D660 CRC64; MAFLLSFLLS LFGVWFFGRV AKRLNIVDRP DGVLKPHGRE TPYLGGLGIF VGVLPFLWND TVVLLSASIA LALGLMDDLF SLSPFLRLIA EFGISLLLVW RFIGLDNLLV STFWLFFVVV LINSVNMMDG MDGLCGSLVA LSALSYFFLV RGVFFENLSL SLLGASLGYL VFNFPPARIF MGDAGSYLMA VLLSAIVLSQ NRFASFDTFL TMIFPLWIFF LDFLASVLRR YRNKKSIFRG DRNHMYDKLS RRFGVKRALF IMIATHAVFC GFSFGALGNI VMSVVTFVLA VVFSFVLIKG LGLLHYD // ID Q9X0T2_THEMA Unreviewed; 155 AA. AC Q9X0T2; G4FEE1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Na(+) H(+) antiporter subunit E {ECO:0000313|EMBL:AGL50136.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36280.1}; GN OrderedLocusNames=TM_1205 {ECO:0000313|EMBL:AAD36280.1}; GN ORFNames=Tmari_1212 {ECO:0000313|EMBL:AGL50136.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36280.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36280.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36280.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50136.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50136.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36280.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50136.1; -; Genomic_DNA. DR PIR; C72280; C72280. DR RefSeq; NP_229010.1; NC_000853.1. DR RefSeq; WP_004080108.1; NZ_CP011107.1. DR STRING; 243274.TM1205; -. DR DNASU; 898279; -. DR EnsemblBacteria; AAD36280; AAD36280; TM_1205. DR EnsemblBacteria; AGL50136; AGL50136; Tmari_1212. DR GeneID; 898279; -. DR KEGG; tma:TM1205; -. DR KEGG; tmi:THEMA_08305; -. DR KEGG; tmm:Tmari_1212; -. DR KEGG; tmw:THMA_1231; -. DR PATRIC; 23937352; VBITheMar51294_1223. DR eggNOG; ENOG4105Z3A; Bacteria. DR eggNOG; COG1863; LUCA. DR KO; K05569; -. DR OMA; ILWLVIT; -. DR OrthoDB; EOG6P5ZKJ; -. DR BioCyc; TMAR243274:GC6P-1235-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002758; Cation_antiport_E. DR Pfam; PF01899; MNHE; 1. DR PIRSF; PIRSF019239; MrpE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 76 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 155 AA; 17827 MW; 9574A73C78BDBC5F CRC64; MSVFLTSLIL WLVITRFSYS ELLAGIVVSL AVSLIFRKYH GIRFDAKLPL RIVRYAVMFL PIFIIEMVKA NIDVALRVLN PRLPLKPGFV ELKTNLKKDA SRLFLANSIT LTPGTLSVDV KDDRIFVHWI EVKSTEEKER YISGKFERLI KGVFE // ID Q9WZT9_THEMA Unreviewed; 184 AA. AC Q9WZT9; G4FCZ0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35916.1}; GN OrderedLocusNames=TM_0834 {ECO:0000313|EMBL:AAD35916.1}; GN ORFNames=Tmari_0836 {ECO:0000313|EMBL:AGL49761.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35916.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35916.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35916.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49761.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49761.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35916.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49761.1; -; Genomic_DNA. DR PIR; F72328; F72328. DR RefSeq; NP_228643.1; NC_000853.1. DR RefSeq; WP_004080804.1; NZ_CP011107.1. DR STRING; 243274.TM0834; -. DR EnsemblBacteria; AAD35916; AAD35916; TM_0834. DR EnsemblBacteria; AGL49761; AGL49761; Tmari_0836. DR GeneID; 898505; -. DR KEGG; tma:TM0834; -. DR KEGG; tmi:THEMA_00470; -. DR KEGG; tmm:Tmari_0836; -. DR KEGG; tmw:THMA_0855; -. DR PATRIC; 23936594; VBITheMar51294_0847. DR eggNOG; ENOG4108E4D; Bacteria. DR eggNOG; ENOG41103JI; LUCA. DR OMA; EPRTEYF; -. DR OrthoDB; EOG600DPG; -. DR BioCyc; TMAR243274:GC6P-863-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032607; DUF4894. DR Pfam; PF16235; DUF4894; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 184 AA; 21638 MW; 7453D8F4D59AA53F CRC64; MRSLRVLLIT MIVLYILFFV NSFFQSRREH VRVPEKVYSY LIENFNISPK SIIIDSKKAI GIVFYEGNYY LCAEDGSLVA SLSKKDLFKF YPVFLEVNLE GLRLSKSDRE ILEMLIPILK SSVVSAVFFE SKEVVLLKGS RIMFEEWKDL VENFQVIMEQ SEKMKAKERY FLTDDGRLMW IRGD // ID Q9WZS6_THEMA Unreviewed; 399 AA. AC Q9WZS6; G4FD05; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Uracil permease {ECO:0000313|EMBL:AAD35901.1}; GN OrderedLocusNames=TM_0819 {ECO:0000313|EMBL:AAD35901.1}; GN ORFNames=Tmari_0820 {ECO:0000313|EMBL:AGL49745.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35901.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35901.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35901.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49745.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49745.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35901.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49745.1; -; Genomic_DNA. DR PIR; F72329; F72329. DR RefSeq; NP_228628.1; NC_000853.1. DR RefSeq; WP_004080841.1; NZ_CP011107.1. DR STRING; 243274.TM0819; -. DR DNASU; 898488; -. DR EnsemblBacteria; AAD35901; AAD35901; TM_0819. DR EnsemblBacteria; AGL49745; AGL49745; Tmari_0820. DR GeneID; 898488; -. DR KEGG; tma:TM0819; -. DR KEGG; tmi:THEMA_00550; -. DR KEGG; tmm:Tmari_0820; -. DR KEGG; tmw:THMA_0839; -. DR PATRIC; 23936560; VBITheMar51294_0831. DR eggNOG; ENOG4105C2W; Bacteria. DR eggNOG; COG2233; LUCA. DR KO; K02824; -. DR OMA; RLTWTRT; -. DR OrthoDB; EOG6Z3KKZ; -. DR BioCyc; TMAR243274:GC6P-847-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR006042; Xan_ur_permease. DR InterPro; IPR006043; Xant/urac/vitC. DR PANTHER; PTHR11119; PTHR11119; 1. DR Pfam; PF00860; Xan_ur_permease; 1. DR TIGRFAMs; TIGR00801; ncs2; 1. DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 87 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 141 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 148 165 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 171 191 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 212 229 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 294 315 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 322 343 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 355 371 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 378 395 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 399 AA; 41845 MW; C537D2CD58354F12 CRC64; MEFEGAVTKV SGWRWFLLAL QHFVAMFGAT VLVPLITGLD PLVALLTAGI GTLIFHFVTG GIVPVFLGSS FAFIAPILAV KEIYGDLAYA TGGIFVAGLF YVLYALIVKA VGPEKVKKIL PPVVTGSMIM VIGLTLSPVA IQMASSDWPL ALIVIATVVF VSTMTRGFFS MVPVITGVVV GYVAGLFMGK IDTSVIVSTP LFSVPKVMLP KFDYGAIFMI VPVTLATFME HLGDITTNGA VVGKNFFDKP GLHRTLLGDG LATAVAGLLG GPANTTYSEN TGVLALTRVY DPSVLRGAAL VAIFAAFVSK FGAILQTIPQ AVMGGVSLIL FGMITSVGVR TMVNAEVDFS KPRNLMITAL MLTVGIGGAV LKVGRVELKG IGLAALVGIF LNLILPDRD // ID Q9WXS2_THEMA Unreviewed; 339 AA. AC Q9WXS2; G4FGY2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE SubName: Full=2-dehydro-3-deoxygluconate kinase {ECO:0000313|EMBL:AGL48990.1}; DE EC=2.7.1.45 {ECO:0000313|EMBL:AGL48990.1}; DE SubName: Full=2-keto-3-deoxygluconate kinase {ECO:0000313|EMBL:AAD35161.1}; GN OrderedLocusNames=TM_0067 {ECO:0000313|EMBL:AAD35161.1}; GN ORFNames=Tmari_0064 {ECO:0000313|EMBL:AGL48990.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35161.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35161.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35161.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48990.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48990.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35161.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48990.1; -; Genomic_DNA. DR PIR; G72422; G72422. DR RefSeq; NP_227883.1; NC_000853.1. DR RefSeq; WP_004082562.1; NZ_CP011107.1. DR PDB; 2AFB; X-ray; 2.05 A; A/B=1-339. DR PDBsum; 2AFB; -. DR STRING; 243274.TM0067; -. DR EnsemblBacteria; AAD35161; AAD35161; TM_0067. DR EnsemblBacteria; AGL48990; AGL48990; Tmari_0064. DR GeneID; 896891; -. DR KEGG; tma:TM0067; -. DR KEGG; tmi:THEMA_04470; -. DR KEGG; tmm:Tmari_0064; -. DR KEGG; tmw:THMA_0063; -. DR PATRIC; 23934974; VBITheMar51294_0065. DR eggNOG; ENOG4107QT3; Bacteria. DR eggNOG; COG0524; LUCA. DR KO; K00874; -. DR OMA; SASDNGW; -. DR OrthoDB; EOG6N682Z; -. DR BioCyc; MetaCyc:MONOMER-17956; -. DR BioCyc; TMAR243274:GC6P-67-MONOMER; -. DR BRENDA; 2.7.1.45; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008673; F:2-dehydro-3-deoxygluconokinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF00294; PfkB; 1. DR SUPFAM; SSF53613; SSF53613; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2AFB}; Calcium {ECO:0000213|PDB:2AFB}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|SAAS:SAAS00446051, ECO:0000313|EMBL:AAD35161.1}; KW Metal-binding {ECO:0000213|PDB:2AFB}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00446051, KW ECO:0000313|EMBL:AAD35161.1}. FT DOMAIN 2 310 PfkB. {ECO:0000259|Pfam:PF00294}. FT METAL 25 25 Calcium. {ECO:0000213|PDB:2AFB}. FT METAL 326 326 Calcium. {ECO:0000213|PDB:2AFB}. SQ SEQUENCE 339 AA; 37601 MW; DEE01C83C7E44D4C CRC64; MKVVTFGEIM LRLSPPDHKR IFQTDSFDVT YGGAEANVAA FLAQMGLDAY FVTKLPNNPL GDAAAGHLRK FGVKTDYIAR GGNRIGIYFL EIGASQRPSK VVYDRAHSAI SEAKREDFDW EKILDGARWF HFSGITPPLG KELPLILEDA LKVANEKGVT VSCDLNYRAR LWTKEEAQKV MIPFMEYVDV LIANEEDIEK VLGISVEGLD LKTGKLNREA YAKIAEEVTR KYNFKTVGIT LRESISATVN YWSVMVFENG QPHFSNRYEI HIVDRVGAGD SFAGALIYGS LMGFDSQKKA EFAAAASCLK HTIPGDFVVL SIEEIEKLAS GATSGRVER // ID Q9WXU9_THEMA Unreviewed; 399 AA. AC Q9WXU9; G4FH09; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=General secretion pathway protein F, putative {ECO:0000313|EMBL:AAD35188.1}; DE SubName: Full=Type II secretory pathway, component PulF / Type IV fimbrial assembly protein PilC {ECO:0000313|EMBL:AGL49017.1}; GN OrderedLocusNames=TM_0094 {ECO:0000313|EMBL:AAD35188.1}; GN ORFNames=Tmari_0091 {ECO:0000313|EMBL:AGL49017.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35188.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35188.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35188.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49017.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49017.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35188.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49017.1; -; Genomic_DNA. DR PIR; F72417; F72417. DR RefSeq; NP_227910.1; NC_000853.1. DR RefSeq; WP_004082638.1; NZ_CP011107.1. DR STRING; 243274.TM0094; -. DR EnsemblBacteria; AAD35188; AAD35188; TM_0094. DR EnsemblBacteria; AGL49017; AGL49017; Tmari_0091. DR GeneID; 896921; -. DR KEGG; tma:TM0094; -. DR KEGG; tmi:THEMA_04335; -. DR KEGG; tmm:Tmari_0091; -. DR KEGG; tmw:THMA_0090; -. DR PATRIC; 23935028; VBITheMar51294_0092. DR eggNOG; ENOG4105D7Q; Bacteria. DR eggNOG; COG1459; LUCA. DR KO; K02653; -. DR OMA; FEPLMIL; -. DR OrthoDB; EOG6Z6FTM; -. DR BioCyc; TMAR243274:GC6P-94-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003004; GspF/PilC. DR InterPro; IPR018076; T2SS_F. DR Pfam; PF00482; T2SSF; 2. DR PRINTS; PR00812; BCTERIALGSPF. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 165 187 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 218 236 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 366 387 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 65 188 T2SSF. {ECO:0000259|Pfam:PF00482}. FT DOMAIN 267 387 T2SSF. {ECO:0000259|Pfam:PF00482}. SQ SEQUENCE 399 AA; 44536 MW; 9BA9F6524DB96489 CRC64; MPFYKYVAVE GSGKKITGVI EAENKLKAIS ILSERGLMVV RVEERKKAQR SSTFFQISIS EIATFCRQLS IMISAGIRIK EALNILARQT VFSRRFRKVI LEIALNVETG DSLAEAFRKT GVFDNVLISM LEAGEEGGVL DRTLKRAADF YESIKRLQDE VKSAMAYPLF VLFFAVVIVL VISFYILPNL VRAFGTSIPL SPTIRSLLKA NEFLSENWPW FSVLVTGIIA GIFVLMKSKY GVYIKEYLSF IFPPVRKLRQ NMGLERFART LGILVGSGVR ITDAIKMAAQ ASSSPSIIRK TEEMVRKISE GKTLRDTFAE SGVFPQLIYE MIGTGEETGK VDEVMERVAD FYEDIVKNSV KQLVSLVEPL LIAGVGGFVA FLAYSIYTTV FQLQRSIGG // ID Q9X0J7_THEMA Unreviewed; 312 AA. AC Q9X0J7; G4FEN5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36189.1}; GN OrderedLocusNames=TM_1113 {ECO:0000313|EMBL:AAD36189.1}; GN ORFNames=Tmari_1119 {ECO:0000313|EMBL:AGL50043.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36189.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36189.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36189.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50043.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50043.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36189.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50043.1; -; Genomic_DNA. DR PIR; F72291; F72291. DR RefSeq; NP_228919.1; NC_000853.1. DR RefSeq; WP_004080312.1; NZ_CP011107.1. DR STRING; 243274.TM1113; -. DR EnsemblBacteria; AAD36189; AAD36189; TM_1113. DR EnsemblBacteria; AGL50043; AGL50043; Tmari_1119. DR GeneID; 898652; -. DR KEGG; tma:TM1113; -. DR KEGG; tmi:THEMA_08780; -. DR KEGG; tmm:Tmari_1119; -. DR KEGG; tmw:THMA_1136; -. DR PATRIC; 23937159; VBITheMar51294_1128. DR eggNOG; ENOG4108E5A; Bacteria. DR eggNOG; ENOG410XTNT; LUCA. DR OMA; EVEANTH; -. DR OrthoDB; EOG6CS01M; -. DR BioCyc; TMAR243274:GC6P-1142-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 312 AA; 36083 MW; 7133143D4CF79975 CRC64; MRKWGLGILI VFLFAFSFST TIYKYNKELG RWEKEVKKDV FVLPPAQRQT TGSVVEMNSY RGKGQWYYYM EYDLGDGEEL FSFWAGQNTV VGTVTVWNDS EYLYVRVDID DEWYLEETHL NVLSEEPEGN QAPGQFPFKE EFDSPVSTYT FEVPLSFLFQ NSFTRLNRLN NKYYILLHGV VNSSGREETA WGGRLSQCVK IHLSGTRVTW FVKKPGVYVA KVLEVEANTH LSIYVNFPDP SNEKDSVDLK VAYGDEIPTE WFDDLSFLED SFSLWQKINV PRSLSADTYT STGVITFTIN NSKLYIDVSP ER // ID Q9WXT3_THEMA Unreviewed; 256 AA. AC Q9WXT3; G4FGZ3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE SubName: Full=Iron(III) ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35172.1}; DE SubName: Full=Vitamin B12 ABC transporter, ATPase component BtuD {ECO:0000313|EMBL:AGL49001.1}; GN OrderedLocusNames=TM_0078 {ECO:0000313|EMBL:AAD35172.1}; GN ORFNames=Tmari_0075 {ECO:0000313|EMBL:AGL49001.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35172.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35172.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35172.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49001.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49001.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35172.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49001.1; -; Genomic_DNA. DR PIR; F72421; F72421. DR RefSeq; NP_227894.1; NC_000853.1. DR RefSeq; WP_004082601.1; NZ_CP011107.1. DR STRING; 243274.TM0078; -. DR EnsemblBacteria; AAD35172; AAD35172; TM_0078. DR EnsemblBacteria; AGL49001; AGL49001; Tmari_0075. DR GeneID; 896904; -. DR KEGG; tma:TM0078; -. DR KEGG; tmi:THEMA_04415; -. DR KEGG; tmm:Tmari_0075; -. DR KEGG; tmw:THMA_0074; -. DR PATRIC; 23934996; VBITheMar51294_0076. DR eggNOG; ENOG4105E0A; Bacteria. DR eggNOG; COG1120; LUCA. DR KO; K02013; -. DR OMA; TIYRICK; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; TMAR243274:GC6P-78-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35172.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35172.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 239 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 256 AA; 28724 MW; 725DA5365C84E156 CRC64; MEIVRIENLF FQYRGGFSLK NINLSVKKGE FFGIIGPNGS GKTTLLKILV GIFRPQKGTV QLLGRIPWET SRKEMAKIVT LVSQDFFPSY DFSVKEIVEM GRLPHLSLLS GTSRKDEEIV LKSLELTGTL KFVDRNFWTL SSGERRKVVL SKAIVQDTEI LLIDELTAHL DYNNVSLVGN VLKRLKESGK TIISVFHDIN VASALCDRIG VMKNGEMIKT GAPPEVVTEE VLRNTFETEF VVLEHPVTGR PLAFLK // ID Q9X275_THEMA Unreviewed; 99 AA. AC Q9X275; G4FGD9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 77. DE SubName: Full=Excinuclease ABC subunit B {ECO:0000313|EMBL:AGL50685.1}; DE SubName: Full=Excinuclease ABC, subunit B-related protein {ECO:0000313|EMBL:AAD36818.1}; GN OrderedLocusNames=TM_1753 {ECO:0000313|EMBL:AAD36818.1}; GN ORFNames=Tmari_1761 {ECO:0000313|EMBL:AGL50685.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36818.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36818.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36818.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50685.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50685.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36818.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50685.1; -; Genomic_DNA. DR PIR; D72216; D72216. DR RefSeq; NP_229551.1; NC_000853.1. DR RefSeq; WP_004082286.1; NZ_CP011107.1. DR SMR; Q9X275; 12-94. DR STRING; 243274.TM1753; -. DR EnsemblBacteria; AAD36818; AAD36818; TM_1753. DR EnsemblBacteria; AGL50685; AGL50685; Tmari_1761. DR GeneID; 897862; -. DR KEGG; tma:TM1753; -. DR KEGG; tmi:THEMA_05470; -. DR KEGG; tmm:Tmari_1761; -. DR KEGG; tmw:THMA_1795; -. DR PATRIC; 23938482; VBITheMar51294_1771. DR eggNOG; COG0556; LUCA. DR KO; K03702; -. DR BioCyc; TMAR243274:GC6P-1801-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009381; F:excinuclease ABC activity; IEA:InterPro. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro. DR GO; GO:0009432; P:SOS response; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004807; UvrB. DR InterPro; IPR024759; UvrB_YAD/RRR_dom. DR PANTHER; PTHR24029; PTHR24029; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF12344; UvrB; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 99 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. SQ SEQUENCE 99 AA; 11484 MW; BEF790D11D53682F CRC64; MREEEKQVNY RGVNLLREGL DLLEVSPVAI MDADVEGFLR SETTLIQIIG RTARNVNGKV IMYADRITNA MKRAIEETNR RRRIQLEYNR KHGITLQIA // ID Q9X1E9_THEMA Unreviewed; 131 AA. AC Q9X1E9; G4FFH0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 87. DE SubName: Full=Succinyl-CoA synthetase, alpha subunit-related enzyme {ECO:0000313|EMBL:AGL50365.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36505.1}; GN OrderedLocusNames=TM_1435 {ECO:0000313|EMBL:AAD36505.1}; GN ORFNames=Tmari_1441 {ECO:0000313|EMBL:AGL50365.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36505.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36505.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36505.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50365.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50365.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36505.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50365.1; -; Genomic_DNA. DR PIR; H72254; H72254. DR RefSeq; NP_229235.1; NC_000853.1. DR RefSeq; WP_004081702.1; NZ_CP011107.1. DR SMR; Q9X1E9; 6-122. DR STRING; 243274.TM1435; -. DR DNASU; 898040; -. DR EnsemblBacteria; AAD36505; AAD36505; TM_1435. DR EnsemblBacteria; AGL50365; AGL50365; Tmari_1441. DR GeneID; 898040; -. DR KEGG; tma:TM1435; -. DR KEGG; tmi:THEMA_07140; -. DR KEGG; tmm:Tmari_1441; -. DR KEGG; tmw:THMA_1465; -. DR PATRIC; 23937818; VBITheMar51294_1447. DR eggNOG; ENOG410838Z; Bacteria. DR eggNOG; COG1832; LUCA. DR KO; K06929; -. DR OMA; SAEKCIM; -. DR OrthoDB; EOG6RG006; -. DR BioCyc; TMAR243274:GC6P-1473-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0048037; F:cofactor binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR003781; CoA-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF13380; CoA_binding_2; 1. DR SMART; SM00881; CoA_binding; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 95 CoA_binding. {ECO:0000259|SMART:SM00881}. SQ SEQUENCE 131 AA; 15001 MW; 74B3D38218021DE9 CRC64; MDPKKFKKIA LVGATVNPRK YGNVILKDLV SKGFEVLPVN PKYDEIEGFR VYKSVEELPE NIDVIVFVVP PEVALEETKK AYDAGFRRFW YQPGAFSEEI KRFLDSLKDV EYSAEKCIMV ETSSSRGFLN L // ID Q9X0R3_THEMA Unreviewed; 179 AA. AC Q9X0R3; G4FEG5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 107. DE SubName: Full=ADP-ribose pyrophosphatase {ECO:0000313|EMBL:AGL50112.1}; DE EC=3.6.1.13 {ECO:0000313|EMBL:AGL50112.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36256.1}; GN OrderedLocusNames=TM_1181 {ECO:0000313|EMBL:AAD36256.1}; GN ORFNames=Tmari_1188 {ECO:0000313|EMBL:AGL50112.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36256.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36256.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36256.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50112.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50112.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CC {ECO:0000256|RuleBase:RU003476}. CC -!- SIMILARITY: Contains nudix hydrolase domain. CC {ECO:0000256|SAAS:SAAS00499431}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36256.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50112.1; -; Genomic_DNA. DR PIR; H72286; H72286. DR RefSeq; NP_228986.1; NC_000853.1. DR RefSeq; WP_004080176.1; NZ_CP011107.1. DR STRING; 243274.TM1181; -. DR EnsemblBacteria; AAD36256; AAD36256; TM_1181. DR EnsemblBacteria; AGL50112; AGL50112; Tmari_1188. DR GeneID; 898304; -. DR KEGG; tma:TM1181; -. DR KEGG; tmi:THEMA_08430; -. DR KEGG; tmm:Tmari_1188; -. DR KEGG; tmw:THMA_1206; -. DR PATRIC; 23937302; VBITheMar51294_1199. DR eggNOG; ENOG4108YZ4; Bacteria. DR eggNOG; COG0494; LUCA. DR KO; K01515; -. DR OMA; ENPLECA; -. DR OrthoDB; EOG6VMTQG; -. DR BioCyc; TMAR243274:GC6P-1210-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|RuleBase:RU003476, KW ECO:0000256|SAAS:SAAS00499465, ECO:0000313|EMBL:AGL50112.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 39 167 Nudix hydrolase. FT {ECO:0000259|PROSITE:PS51462}. SQ SEQUENCE 179 AA; 20337 MW; 5CB4FA7D3E0B3BA1 CRC64; MKFYEEKIDS KRVFEGKMIS VRVDRVRLPD GRESTREVVD HPGAVVIVPV LGGKILFVEQ YRYPIEQVLL ELPAGKLDPG ESPEECAKRE LEEETGYRAK KLSYLGKIFT TPGFTTEVIH IFAAEDLEKT SQNTDPDEFI EVKEVPIEEA LSLLKNAEIE DSKTICALTR FFFAKGVIR // ID Q9X110_THEMA Unreviewed; 331 AA. AC Q9X110; G4FE64; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Oxidase-related protein {ECO:0000313|EMBL:AAD36358.1}; DE SubName: Full=Rieske (2Fe-2S) domain protein {ECO:0000313|EMBL:AGL50214.1}; GN OrderedLocusNames=TM_1284 {ECO:0000313|EMBL:AAD36358.1}; GN ORFNames=Tmari_1290 {ECO:0000313|EMBL:AGL50214.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36358.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36358.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36358.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50214.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50214.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 Rieske domain. CC {ECO:0000256|RuleBase:RU004493}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36358.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50214.1; -; Genomic_DNA. DR PIR; G72273; G72273. DR RefSeq; NP_229088.1; NC_000853.1. DR RefSeq; WP_004079950.1; NZ_CP011107.1. DR STRING; 243274.TM1284; -. DR EnsemblBacteria; AAD36358; AAD36358; TM_1284. DR EnsemblBacteria; AGL50214; AGL50214; Tmari_1290. DR GeneID; 898199; -. DR KEGG; tma:TM1284; -. DR KEGG; tmi:THEMA_07915; -. DR KEGG; tmm:Tmari_1290; -. DR KEGG; tmw:THMA_1310; -. DR PATRIC; 23937508; VBITheMar51294_1300. DR eggNOG; ENOG4108KUH; Bacteria. DR eggNOG; COG4638; LUCA. DR OMA; MIKNQWY; -. DR OrthoDB; EOG6DNT94; -. DR BioCyc; TMAR243274:GC6P-1315-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 2.102.10.10; -; 1. DR InterPro; IPR017941; Rieske_2Fe-2S. DR Pfam; PF00355; Rieske; 1. DR SUPFAM; SSF50022; SSF50022; 1. DR PROSITE; PS51296; RIESKE; 1. PE 4: Predicted; KW 2Fe-2S {ECO:0000256|RuleBase:RU004492}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|RuleBase:RU004492}; KW Iron-sulfur {ECO:0000256|RuleBase:RU004492}; KW Metal-binding {ECO:0000256|RuleBase:RU004492}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 6 113 Rieske. {ECO:0000259|PROSITE:PS51296}. SQ SEQUENCE 331 AA; 38880 MW; 6A5E686D41B1BF99 CRC64; MIKNQWYVVL SSRELKKGQL IGVTRFGEKL AFWRDSNGKV HCISDICCHR GASISHGKVL SNGERVMCPF HGFEYDSQGR VRTIPANGRN TPVPENFRVK SYPTYELADF IWIWYGDREP EKPPKYFDDI TDELVYTEFK EVWNVHYSRA IENQLDPIHL PFVHYNTIGR GNRTVVDGPI VEWKDDEMFY FYVFNRIDDG TPARKPEEMD PKRKSKVYLE FKFPNIWQNH ISEKIRVTAA FTPIDDDHTM IYLRFYVGLT GIKFLDKLIA VLGKPFNKIV LHQDKRVVET QIPKRSELRM GENLIPGDAP ILEYRKKREA LKSMQQNNRV K // ID Q9X2A7_THEMA Unreviewed; 273 AA. AC Q9X2A7; G4FGH4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36850.1}; GN OrderedLocusNames=TM_1787 {ECO:0000313|EMBL:AAD36850.1}; GN ORFNames=Tmari_1796 {ECO:0000313|EMBL:AGL50720.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36850.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36850.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36850.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50720.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50720.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36850.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50720.1; -; Genomic_DNA. DR PIR; F72211; F72211. DR RefSeq; NP_229584.1; NC_000853.1. DR RefSeq; WP_004082333.1; NZ_CP011107.1. DR EnsemblBacteria; AAD36850; AAD36850; TM_1787. DR EnsemblBacteria; AGL50720; AGL50720; Tmari_1796. DR GeneID; 897841; -. DR KEGG; tma:TM1787; -. DR KEGG; tmi:THEMA_05265; -. DR KEGG; tmm:Tmari_1796; -. DR KEGG; tmw:THMA_1831; -. DR PATRIC; 23938559; VBITheMar51294_1807. DR eggNOG; ENOG4108PAA; Bacteria. DR eggNOG; ENOG410XPK1; LUCA. DR OMA; TSFNWAV; -. DR OrthoDB; EOG6CS08B; -. DR BioCyc; TMAR243274:GC6P-1837-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 29 47 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 78 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 106 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 113 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 163 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 175 192 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 198 216 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 223 245 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 251 271 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 2 129 EamA. {ECO:0000259|Pfam:PF00892}. FT DOMAIN 140 270 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 273 AA; 29827 MW; 15A6C863A41E43D5 CRC64; MKPVFYPLLS VLVASFSGIL IKLSSLPPAT IAFYRVFIAS LFFFLVKRRV ELFSLKKEVL SLATGFFLAM HFFFWVSAFN HTTVAGAVIP LTLQPVLTGL LSWLVYGERL SPFRIVTGSM VVAGVVLALA GKEGFSGISR GDLLAVIGVV FFCGYLVLGR YLNRAMGSMN FSLKTHALAS TVLAFLVPSF RVVEAREWFI LIGLGVGCSF LGYLLINLSL KYLPSSVVGV VLVGEPVLSI LWSFLLLGET VTFFEIIGFI VAMIGLVLFI LKT // ID Q9X0R4_THEMA Unreviewed; 1170 AA. AC Q9X0R4; G4FEG4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 117. DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894}; GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894}; GN OrderedLocusNames=TM_1182 {ECO:0000313|EMBL:AAD36257.1}; GN ORFNames=Tmari_1189 {ECO:0000313|EMBL:AGL50113.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36257.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36257.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36257.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50113.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50113.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Required for chromosome condensation and partitioning. CC {ECO:0000256|HAMAP-Rule:MF_01894}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}. CC -!- DOMAIN: Contains large globular domains required for ATP CC hydrolysis at each terminus and a third globular domain forming a CC flexible hinge near the middle of the molecule. These domains are CC separated by coiled-coil structures. {ECO:0000256|HAMAP- CC Rule:MF_01894}. CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000256|HAMAP- CC Rule:MF_01894}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36257.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50113.1; -; Genomic_DNA. DR PIR; A72287; A72287. DR RefSeq; NP_228987.1; NC_000853.1. DR RefSeq; WP_004080167.1; NZ_CP011107.1. DR PDB; 1E69; X-ray; 3.10 A; A/B/C/D/E/F=1-152, A/B/C/D/E/F=1023-1170. DR PDB; 1GXJ; X-ray; 2.00 A; A/B=485-670. DR PDB; 1GXK; X-ray; 3.00 A; A/B/C/D=485-670. DR PDB; 1GXL; X-ray; 3.00 A; A/B/C/D=473-685. DR PDBsum; 1E69; -. DR PDBsum; 1GXJ; -. DR PDBsum; 1GXK; -. DR PDBsum; 1GXL; -. DR STRING; 243274.TM1182; -. DR EnsemblBacteria; AAD36257; AAD36257; TM_1182. DR EnsemblBacteria; AGL50113; AGL50113; Tmari_1189. DR GeneID; 898303; -. DR KEGG; tma:TM1182; -. DR KEGG; tmi:THEMA_08425; -. DR KEGG; tmm:Tmari_1189; -. DR KEGG; tmw:THMA_1207; -. DR PATRIC; 23937304; VBITheMar51294_1200. DR eggNOG; ENOG4105CDB; Bacteria. DR eggNOG; COG1196; LUCA. DR KO; K03529; -. DR OMA; AFQTASN; -. DR OrthoDB; EOG6WQD34; -. DR BioCyc; TMAR243274:GC6P-1211-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 3. DR HAMAP; MF_01894; Smc_prok; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003395; RecF/RecN/SMC_N. DR InterPro; IPR024704; SMC. DR InterPro; IPR010935; SMC_hinge. DR InterPro; IPR011890; SMC_prok. DR Pfam; PF06470; SMC_hinge; 1. DR Pfam; PF02463; SMC_N; 1. DR PIRSF; PIRSF005719; SMC; 1. DR SMART; SM00968; SMC_hinge; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF75553; SSF75553; 1. DR TIGRFAMs; TIGR02168; SMC_prok_B; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1E69, ECO:0000213|PDB:1GXJ, KW ECO:0000213|PDB:1GXK, ECO:0000213|PDB:1GXL}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894}; KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_01894}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 514 630 SMC_hinge. {ECO:0000259|SMART:SM00968}. FT NP_BIND 32 39 ATP. {ECO:0000256|HAMAP-Rule:MF_01894}. FT COILED 227 492 {ECO:0000256|HAMAP-Rule:MF_01894}. FT COILED 664 1017 {ECO:0000256|HAMAP-Rule:MF_01894}. SQ SEQUENCE 1170 AA; 137589 MW; 81B203B54B336DE4 CRC64; MRLKKLYLKG FKSFGRPSLI GFSDRVTAIV GPNGSGKSNI IDAIKWVFGE QSKKELRASE KFDMIFAGSE NLPPAGSAYV ELVFEENGEE ITVARELKRT GENTYYLNGS PVRLKDIRDR FAGTGLGVDF YSIVGQGQID RIVNASPEEL RLLLEEAAGV SIYREKKKET ELNLERTKAN LDRVKDVLFE RERQMKSLYL KAKRAERFKE YTAQLEELQK IYYGNVLKRE RKKLEFYQEE EKKTNEKIKN IQKELVELET KWSTLRSEFG EMDQEIERYT KLLEDYKKRQ NDLVEMKGFY SSKLADSENK YVELSTRLDE LEKRREEYKK RLEEMEYIFK GVMGDYERKA KELEKFEKEK ENLLSRFNDK EKEFLRVRDE ISKLEKQILK LENELLRIGE TLEDLEKRRK ITENQILTRR RELEDKKNEF KEISRRVEEL DEEEKKLTEE LNAVRERLEE IEGEIRRVNL EIDAKEKRLR EIQFEKEMIE RDMREYRGFS RAVRAVFEEK ERFPGLVDVV SNLIEVDEKY SLAVSVLLGG TAQNIVVRNV DTAKAIVEFL KQNEAGRVTI LPLDLIDGSF NRISGLENER GFVGYAVDLV KFPSDLEVLG GFLFGNSVVV ETLDDAIRMK KKYRLNTRIA TLDGELISGR GAITGGREER SSNVFERRIK LKHLEQEMEE TERQIAEKRD ELASLKTEQE NLKNQEALVQ RELFELSRKS SSTKTVLSEI LRSINQLQEE VENLEKLLVE YRAKEEGLNA RREKIFEEID ELKQNRENLQ RSLTEYSEEL EKEKKILDEL NEKIFTLRAE VGNLLETKDR YEKEMRDTGK MIERIARETE DIKLQMTSLE EEMENYRKFI REHEREIEHL KKEMDSVFEA MKLHRSGKEE KMRELQEVEN RMDELKEEKE RLRNHLHQID LALQETRLKI ANLLEEFSGN EEDVEELDEE KLEEIYRQIK DLENKIKYLG PVDLTAIDEY EKLREEYEEI LKQKEDLEEA KRKLEEIIEK TDREAESLLF DVYQRVNESF NRFISLLFFG GEGRLNIVSE AKSILDAGFE ISIRKPGRRD QKLSLLSGGE KALVGLALLF ALMEIKPSPF YVLDEVDSPL DDYNAERFKR LLKENSKHTQ FIVITHNKIV MEAADLLHGV TMVNGVSAIV PVEVEKILEV // ID Q9WYE4_THEMA Unreviewed; 764 AA. AC Q9WYE4; G4FHM2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Alpha-xylosidase {ECO:0000313|EMBL:AAD35396.1}; DE EC=3.2.1.- {ECO:0000313|EMBL:AGL49232.1}; GN OrderedLocusNames=TM_0308 {ECO:0000313|EMBL:AAD35396.1}; GN ORFNames=Tmari_0306 {ECO:0000313|EMBL:AGL49232.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35396.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35396.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35396.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49232.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49232.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. CC {ECO:0000256|RuleBase:RU361185}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35396.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49232.1; -; Genomic_DNA. DR PIR; A72394; A72394. DR RefSeq; NP_228120.1; NC_000853.1. DR RefSeq; WP_004083036.1; NZ_CP011107.1. DR STRING; 243274.TM0308; -. DR CAZy; GH31; Glycoside Hydrolase Family 31. DR EnsemblBacteria; AAD35396; AAD35396; TM_0308. DR EnsemblBacteria; AGL49232; AGL49232; Tmari_0306. DR GeneID; 897243; -. DR KEGG; tma:TM0308; -. DR KEGG; tmi:THEMA_03185; -. DR KEGG; tmm:Tmari_0306; -. DR KEGG; tmw:THMA_0315; -. DR PATRIC; 23935495; VBITheMar51294_0313. DR eggNOG; ENOG4105CJQ; Bacteria. DR eggNOG; COG1501; LUCA. DR KO; K01811; -. DR OMA; TPDLYKR; -. DR OrthoDB; EOG6Z99WN; -. DR BioCyc; TMAR243274:GC6P-321-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011013; Gal_mutarotase_SF_dom. DR InterPro; IPR000322; Glyco_hydro_31. DR InterPro; IPR025887; Glyco_hydro_31_N_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF13802; Gal_mutarotas_2; 1. DR Pfam; PF01055; Glyco_hydro_31; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR SUPFAM; SSF74650; SSF74650; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361185, KW ECO:0000313|EMBL:AGL49232.1}; KW Hydrolase {ECO:0000256|RuleBase:RU361185, KW ECO:0000313|EMBL:AGL49232.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 153 212 Gal_mutarotas_2. FT {ECO:0000259|Pfam:PF13802}. SQ SEQUENCE 764 AA; 88984 MW; F412501933E2512B CRC64; MRFTEGLWRL REGVQLFRPE QVYEYSCDGK KLILRSPFRR VEHRGQTLQG PVFEIEISSP FENVIRIRFR HFKGVLEKPP YYEIYQDESF TPDIKETEGS FIFTSGKAKA IIRKNPFGVE FFYEDRFLTK SDLGYAVAPE GRFCLERLHL SVGEMIYGLG ERFSAFVKNA QRVVMWNEDA GTISDMTYKN IPFYVSIRKY GVFVNDPGKV DFEIATEHVE KVQFSVKGET LDYFIIAGKD LKEVLERYTL LTGRPELPPA WSFGLWLTTS FTTQYDERTV MEFVDGMRER DIPLHVFHFD CFWMKEFHWV DLEWNRENFP DPEGLLKRLK EKGLKVCVWI NPYVSQFSSL FDEGKEKGYF LKKPDGDVWQ TDDWQPGMAI IDFTNPEVRK WFASKLERLI DMGVDCFKTD FGEKIPTDVV YYDGSDPEKM HNYYTYLYNK VVFETIERKL GKRNAVVFAR SATAGSQKFP VHWGGDCLAS YESMAETLRG GLSLALCGFG FWSHDIGGFE DITTPDLYKR WVAFGLLSSH SRLHGNSMYK VPWNFDEEAV EVLRFFTKLK CKLMPYIFAS AVEVHERGIP VMRPMILEFP DDPTCLYLDR QYMLGESLLV APIFSETGEV TYYLPEGVWT HFLTGERVEG GRWRTEKYDY FGLPLFTRPN SIIPTGSVDD RPDYDYADGV TLNVFEISNK TAHVYNTRGE VELSVKVERK GNEIHVEVLK DSRKPWKLLF WNERLEAVEG AETRELEKGT EVVLSFQRAI LKTK // ID Q9WYC1_THEMA Unreviewed; 403 AA. AC Q9WYC1; G4FHJ9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=AraM protein, putative {ECO:0000313|EMBL:AAD35373.1}; DE SubName: Full=Arabinose operon protein AraM {ECO:0000313|EMBL:AGL49209.1}; GN OrderedLocusNames=TM_0285 {ECO:0000313|EMBL:AAD35373.1}; GN ORFNames=Tmari_0283 {ECO:0000313|EMBL:AGL49209.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35373.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35373.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35373.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49209.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49209.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35373.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49209.1; -; Genomic_DNA. DR PIR; C72396; C72396. DR RefSeq; NP_228097.1; NC_000853.1. DR RefSeq; WP_004082995.1; NZ_CP011107.1. DR STRING; 243274.TM0285; -. DR EnsemblBacteria; AAD35373; AAD35373; TM_0285. DR EnsemblBacteria; AGL49209; AGL49209; Tmari_0283. DR GeneID; 897203; -. DR KEGG; tma:TM0285; -. DR KEGG; tmi:THEMA_03300; -. DR KEGG; tmm:Tmari_0283; -. DR KEGG; tmw:THMA_0292; -. DR PATRIC; 23935449; VBITheMar51294_0290. DR eggNOG; ENOG4108MDK; Bacteria. DR eggNOG; COG0371; LUCA. DR KO; K00096; -. DR OMA; IEMFHEE; -. DR OrthoDB; EOG683S69; -. DR BioCyc; TMAR243274:GC6P-298-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR032837; G1PDH. DR Pfam; PF13685; Fe-ADH_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 403 AA; 45764 MW; 3888C90DEC0D3880 CRC64; MKDILGKTFE CSCGKTHEVP DIEILETSIR EAPDVFSDAF FIADLNTASL VDLPGKRSFV FNERRPLATM ENVEKIVKAS GDFPEIVSIG SGSLTDIARY AAYLSGKRFS CVPTAPSVDA YTSTVAPILV NGVKKTFMAI PPRRILLDIE VLRNAPMDLL RAGVGDIVAK IPARMDWILS HIVTGEYICD FVWDDMKDLL KEILLKSKDI LNRERSAIKT LIEAHLVSGI NMVIMGNSRP ASGAEHMVSH LIEMFHEEKE EMPPFHGLTV MIGVFVSMKA YEALVEKKEI PLEEYSIEER RKELLELFEE RKVEEFLKTY AGKKLPKIEA DIVREPMESI YKEFFPHLKR TLETIDVNSM INSYSKDFLS KVVRLANTIR DRFTVLDVFD EMKILKNFSK IVF // ID Q9WZ97_THEMA Unreviewed; 418 AA. AC Q9WZ97; G4FDJ4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35713.1}; GN OrderedLocusNames=TM_0629 {ECO:0000313|EMBL:AAD35713.1}; GN ORFNames=Tmari_0630 {ECO:0000313|EMBL:AGL49555.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35713.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35713.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35713.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49555.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49555.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35713.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49555.1; -; Genomic_DNA. DR PIR; B72353; B72353. DR RefSeq; NP_228438.1; NC_000853.1. DR RefSeq; WP_004081174.1; NZ_CP011107.1. DR STRING; 243274.TM0629; -. DR EnsemblBacteria; AAD35713; AAD35713; TM_0629. DR EnsemblBacteria; AGL49555; AGL49555; Tmari_0630. DR GeneID; 897717; -. DR KEGG; tma:TM0629; -. DR KEGG; tmi:THEMA_01515; -. DR KEGG; tmm:Tmari_0630; -. DR KEGG; tmw:THMA_0645; -. DR PATRIC; 23936171; VBITheMar51294_0639. DR BioCyc; TMAR243274:GC6P-654-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 45 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 68 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 80 99 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 128 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 198 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 210 235 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 276 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 316 336 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 348 370 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 382 411 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 418 AA; 48062 MW; 23CA01A2AB25C252 CRC64; MNEMSSHMLS MEKQLYKTKR KISLENFLVN LFFVTVLFPY VTFGLPASSD SQPWAVLVGS LLLIFNLVKN RNIHFHKITL MIIFLSLICI LNVTVFFIFQ GGELTFYLRT IFKYINFMII IPIVIIYFER FSPNILSFSI LLWFMIVIAQ VITKKVLIDF VLPRNTIVYG RNFAIGFAPE PAYMAKVCIF FLLMIDYYKN LRSIKPVKAM ILTLFALVMI LASASLTGFV LVIIYFLIKL FLSARKSNFG KVQKIILICV LIVTLILFLP LLMNFVTKHD FSNFGKVGYY ISKMLENRSL FIFIVDQSFK SRLSGFIRNF SSFVSGNVFG SGVPIYPTGS IFSPVYDSGI FGLLFSASIL SIFILSVFRI KKKKLRNYLI ELFVMFIFLT FSESLATSYI AFIAGISLYL YNKVVNEF // ID Q9WZR7_THEMA Unreviewed; 420 AA. AC Q9WZR7; G4FD14; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Chitobiose ABC transport system, sugar-binding protein {ECO:0000313|EMBL:AGL49736.1}; DE SubName: Full=Sugar ABC transporter, periplasmic sugar-binding protein {ECO:0000313|EMBL:AAD35892.1}; GN OrderedLocusNames=TM_0810 {ECO:0000313|EMBL:AAD35892.1}; GN ORFNames=Tmari_0811 {ECO:0000313|EMBL:AGL49736.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35892.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35892.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35892.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49736.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49736.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35892.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49736.1; -; Genomic_DNA. DR PIR; C72331; C72331. DR RefSeq; NP_228619.1; NC_000853.1. DR RefSeq; WP_004080852.1; NZ_CP011107.1. DR STRING; 243274.TM0810; -. DR TCDB; 3.A.1.1.40; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35892; AAD35892; TM_0810. DR EnsemblBacteria; AGL49736; AGL49736; Tmari_0811. DR GeneID; 898478; -. DR KEGG; tma:TM0810; -. DR KEGG; tmi:THEMA_00600; -. DR KEGG; tmm:Tmari_0811; -. DR KEGG; tmw:THMA_0829; -. DR PATRIC; 23936540; VBITheMar51294_0822. DR eggNOG; ENOG4107RKH; Bacteria. DR eggNOG; COG1653; LUCA. DR KO; K17244; -. DR OMA; MLITGPQ; -. DR OrthoDB; EOG69KTVN; -. DR BioCyc; TMAR243274:GC6P-837-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR006059; SBP_1_dom. DR Pfam; PF01547; SBP_bac_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 420 AA; 48305 MW; 2043A4D98AB7D467 CRC64; MRKFLVILMV VLLAVLALSK TKIVFWTMSL KPTFTDFIQG IIDRYEELNP DVEIVWEDVP WDVLQQKLLA AFSSGNPPDV VNLNAQWTIE FAQKKVLFPL NDLLPEEVIN QYFDNMIKGL TWKDGIYGIP WYTAVDVIFY NKEIFEKAGL DPKYPPRTWD EILLYSVLIK EKTGKYGALP TIFQDPSAIF NWDGLNLYTV DENNRIKEVL FDRPEYAHTL NKWATLYKQK YIPSEIVQGG EWTRATELYQ AGELAMLITG VQFADRVKWN APEIYEKSDV APIPAPKPGV RMSGWYSTLN VVRGSKNPKE AAKFAAFVAN LENQIAFCKL VTIFPTLKAA VNDPWFSKDD GTLAAKARIM GAKYLENITF YNDDIPFRKE AFDRLKDAII QVFLGQKDPE TALKETAKYW RYLIQTQQSK // ID Q9X1W6_THEMA Unreviewed; 261 AA. AC Q9X1W6; G4FG20; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36698.1}; GN OrderedLocusNames=TM_1631 {ECO:0000313|EMBL:AAD36698.1}; GN ORFNames=Tmari_1640 {ECO:0000313|EMBL:AGL50564.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36698.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36698.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36698.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50564.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50564.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36698.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50564.1; -; Genomic_DNA. DR PIR; G72229; G72229. DR RefSeq; NP_229431.1; NC_000853.1. DR RefSeq; WP_004082107.1; NZ_CP011107.1. DR PDB; 1VPQ; X-ray; 2.20 A; A=1-261. DR PDBsum; 1VPQ; -. DR STRING; 243274.TM1631; -. DR EnsemblBacteria; AAD36698; AAD36698; TM_1631. DR EnsemblBacteria; AGL50564; AGL50564; Tmari_1640. DR GeneID; 897591; -. DR KEGG; tma:TM1631; -. DR KEGG; tmi:THEMA_06090; -. DR KEGG; tmm:Tmari_1640; -. DR KEGG; tmw:THMA_1672; -. DR PATRIC; 23938236; VBITheMar51294_1650. DR eggNOG; ENOG4105I3N; Bacteria. DR eggNOG; COG1801; LUCA. DR OMA; WSYDHWE; -. DR OrthoDB; EOG6C8MZR; -. DR BioCyc; TMAR243274:GC6P-1677-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.20.20.410; -; 1. DR InterPro; IPR002763; DUF72. DR Pfam; PF01904; DUF72; 1. DR SUPFAM; SSF117396; SSF117396; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VPQ}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT BINDING 72 72 Sulfate 1. {ECO:0000213|PDB:1VPQ}. FT BINDING 114 114 Sulfate 1. {ECO:0000213|PDB:1VPQ}. FT BINDING 117 117 Sulfate 2; via amide nitrogen. FT {ECO:0000213|PDB:1VPQ}. FT BINDING 145 145 Sulfate 1. {ECO:0000213|PDB:1VPQ}. FT BINDING 145 145 Sulfate 2. {ECO:0000213|PDB:1VPQ}. FT BINDING 180 180 Sulfate 3. {ECO:0000213|PDB:1VPQ}. FT BINDING 191 191 Sulfate 1. {ECO:0000213|PDB:1VPQ}. FT BINDING 207 207 Sulfate 2. {ECO:0000213|PDB:1VPQ}. FT BINDING 208 208 Sulfate 1. {ECO:0000213|PDB:1VPQ}. FT BINDING 239 239 Sulfate 1. {ECO:0000213|PDB:1VPQ}. SQ SEQUENCE 261 AA; 31727 MW; 2309227536AE9C86 CRC64; MVYVGTSGFS FEDWKGVVYP EHLKPSQFLK YYWAVLGFRI VELNFTYYTQ PSWRSFVQML RKTPPDFYFT VKTPGSVTHV LWKEGKDPKE DMENFTRQIE PLIEEQRLKM TLAQFPFSFK FSRKNVEYLE KLRESYPYEL AVEFRHYSWD REETYEFLRN HGITFVVVDE PKLPGLFPYR PITTTDYAYF RFHGRNERWF EAEGEERYDY LYSEEELKTL FEDVVELSRR VKETYVFFNN CYKGQAAINA LQFKKMLEER V // ID Q9X1N2_THEMA Unreviewed; 955 AA. AC Q9X1N2; G4FFT4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Single stranded DNA-specific exonuclease, putative {ECO:0000313|EMBL:AAD36613.1}; DE SubName: Full=Single-stranded-DNA-specific exonuclease RecJ {ECO:0000313|EMBL:AGL50478.1}; DE EC=3.1.-.- {ECO:0000313|EMBL:AGL50478.1}; GN OrderedLocusNames=TM_1546 {ECO:0000313|EMBL:AAD36613.1}; GN ORFNames=Tmari_1554 {ECO:0000313|EMBL:AGL50478.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36613.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36613.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36613.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50478.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50478.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36613.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50478.1; -; Genomic_DNA. DR PIR; F72243; F72243. DR RefSeq; NP_229346.1; NC_000853.1. DR RefSeq; WP_004081936.1; NZ_CP011107.1. DR STRING; 243274.TM1546; -. DR EnsemblBacteria; AAD36613; AAD36613; TM_1546. DR EnsemblBacteria; AGL50478; AGL50478; Tmari_1554. DR GeneID; 897973; -. DR KEGG; tma:TM1546; -. DR KEGG; tmi:THEMA_06550; -. DR KEGG; tmm:Tmari_1554; -. DR KEGG; tmw:THMA_1581; -. DR PATRIC; 23938054; VBITheMar51294_1564. DR eggNOG; ENOG4105C2R; Bacteria. DR eggNOG; COG0608; LUCA. DR KO; K07462; -. DR OMA; DISYKIA; -. DR OrthoDB; EOG63C0P5; -. DR BioCyc; TMAR243274:GC6P-1587-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR003156; DHHA1_dom. DR InterPro; IPR004610; RecJ. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02272; DHHA1; 1. DR TIGRFAMs; TIGR00644; recJ; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Exonuclease {ECO:0000313|EMBL:AAD36613.1}; KW Hydrolase {ECO:0000313|EMBL:AAD36613.1}; KW Nuclease {ECO:0000313|EMBL:AAD36613.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 79 225 DHH. {ECO:0000259|Pfam:PF01368}. FT DOMAIN 370 433 DHHA1. {ECO:0000259|Pfam:PF02272}. SQ SEQUENCE 955 AA; 109079 MW; 8E33C2CD85CA1802 CRC64; MKKWELSQPD EKAVSEISQY FGLNEIASRI LVNRGFTTRE AVEAFLFVNE SHQHDPFLFN DMEKAVETLL EARSKNELVL IHGDYDVDGI TSTVMLKEFL EENGWRVDVY IPHRIEEGYG IQPENISTFK ENNVSCLVTV DCGITALDSV ALAKKFGMKV IVTDHHEVNG DLPPADAIVN PKVPGENYPF RDLAGVGVTY KLVQALSEAT NYPHPERFLE LVALGTVADM VTLLDENRYF VKKGIELLAN TKRVGLKRLL ERLGLRNLTS HDISYKIAPR LNAAGRMGSA NDAFNLLIMN DPAKADSVVD RLMELNSIRR KTEWAIYKEA IEIIETNDLW KDPVIVVAKE NWHVGVIGIV AAKLANRYEK PVAVVSLDEK IAKGSIRSYN GYDIMNIFNE DILKIFEEIG GHSSAVGFSL KRDQLEPFRD YIRNISLEER EEKVIVDAEV RMEDIDDRFI EDIKKLMPFG QGNPEPVLLF KDVLVEKIHF FGEDGSNVFL HLKNGEKNLE VVGYNFKNLS SSLSTLPVTP TRGDVVVNLR PMGNGVSYYL ISLDVKPVFS VKNREVSHIL SRSKEERTLI KVPYPSKTKL LLSIKEELRG KLAIVSLTNA TTQNILGCLS RYYTSRNLGF VNSTFSKEEE SDIVLFTLAG FLKKHRLDEF DVFVVNEFQD FLAHRDSELV KSFLDIVDKH PGKFIFVASM EHPGLEEFLK KEKYDVVELR TGEPEEFLFS DQRNSFDLGS LVDAHSFAVV VSEKKLIPDL YRKIGKDAIV YYTSMDMEKK IKAIGLMESG SARKAIITSN TDGLPTHIKG DIFFYDFPLS IYEIVDLLRR KSVVNLCYSS SDIEKRRYEL NKLFPDREKL KEIAITAMNL KDKEKLEKIL ESEYDLSSAT LRKIYLDLLE ESGFNFDRWS FSEDERIPWR LLERELEIAQ FERTVSVLSK DLKWIFNFFK DTVVK // ID Q9WXP5_THEMA Unreviewed; 120 AA. AC Q9WXP5; G4FGV5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE RecName: Full=6-carboxy-5,6,7,8-tetrahydropterin synthase {ECO:0000256|PIRNR:PIRNR006113}; DE EC=4.-.-.- {ECO:0000256|PIRNR:PIRNR006113}; GN OrderedLocusNames=TM_0038 {ECO:0000313|EMBL:AAD35132.1}; GN ORFNames=Tmari_0035 {ECO:0000313|EMBL:AGL48961.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35132.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35132.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35132.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48961.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48961.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin 3'-triphosphate + H(2)O = CC 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate. CC {ECO:0000256|PIRNR:PIRNR006113}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRNR:PIRNR006113, CC ECO:0000256|PIRSR:PIRSR006113-2}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR006113, CC ECO:0000256|PIRSR:PIRSR006113-2}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC {ECO:0000256|PIRNR:PIRNR006113}. CC -!- SIMILARITY: Belongs to the PTPS family. QueD subfamily. CC {ECO:0000256|PIRNR:PIRNR006113}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35132.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48961.1; -; Genomic_DNA. DR PIR; C72425; C72425. DR RefSeq; NP_227854.1; NC_000853.1. DR RefSeq; WP_004082502.1; NZ_CP011107.1. DR STRING; 243274.TM0038; -. DR EnsemblBacteria; AAD35132; AAD35132; TM_0038. DR EnsemblBacteria; AGL48961; AGL48961; Tmari_0035. DR GeneID; 896861; -. DR KEGG; tma:TM0038; -. DR KEGG; tmi:THEMA_04610; -. DR KEGG; tmm:Tmari_0035; -. DR KEGG; tmw:THMA_0034; -. DR PATRIC; 23934916; VBITheMar51294_0036. DR eggNOG; ENOG4105MJ5; Bacteria. DR eggNOG; COG0720; LUCA. DR KO; K01737; -. DR OMA; MVVWIFE; -. DR OrthoDB; EOG6FFSCJ; -. DR BioCyc; TMAR243274:GC6P-38-MONOMER; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR007115; 6-PTP_synth/QueD. DR PANTHER; PTHR12589; PTHR12589; 1. DR Pfam; PF01242; PTPS; 1. DR PIRSF; PIRSF006113; PTP_synth; 1. DR TIGRFAMs; TIGR03367; queuosine_QueD; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000256|PIRNR:PIRNR006113}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR006113, KW ECO:0000256|PIRSR:PIRSR006113-2}; KW Queuosine biosynthesis {ECO:0000256|PIRNR:PIRNR006113}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000256|PIRNR:PIRNR006113, ECO:0000256|PIRSR:PIRSR006113-2}. FT ACT_SITE 22 22 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR006113-1}. FT ACT_SITE 66 66 Charge relay system. FT {ECO:0000256|PIRSR:PIRSR006113-1}. FT ACT_SITE 107 107 Charge relay system. FT {ECO:0000256|PIRSR:PIRSR006113-1}. FT METAL 13 13 Zinc. {ECO:0000256|PIRSR:PIRSR006113-2}. FT METAL 26 26 Zinc. {ECO:0000256|PIRSR:PIRSR006113-2}. FT METAL 28 28 Zinc. {ECO:0000256|PIRSR:PIRSR006113-2}. SQ SEQUENCE 120 AA; 14223 MW; 540360E1F7DD41B2 CRC64; MILVKKFSFE AAHNLTRYLG KCERLHGHTY RLVVKIEGPL NEEEMVMDFA ELKKIVEELV ISKLDHSYLN DMFDQPTTER VAIWIWDQLS KEMEKRGVRL HEIELWETET SGVVYRGEKV // ID Q9X0S5_THEMA Unreviewed; 334 AA. AC Q9X0S5; G4FEE8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE SubName: Full=Dipeptide transport system permease protein DppB {ECO:0000313|EMBL:AGL50129.1}; DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD36273.1}; GN OrderedLocusNames=TM_1198 {ECO:0000313|EMBL:AAD36273.1}; GN ORFNames=Tmari_1205 {ECO:0000313|EMBL:AGL50129.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36273.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36273.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36273.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50129.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50129.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36273.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50129.1; -; Genomic_DNA. DR PIR; C72284; C72284. DR RefSeq; NP_229003.1; NC_000853.1. DR RefSeq; WP_004080128.1; NZ_CP011107.1. DR STRING; 243274.TM1198; -. DR TCDB; 3.A.1.5.31; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36273; AAD36273; TM_1198. DR EnsemblBacteria; AGL50129; AGL50129; Tmari_1205. DR GeneID; 898286; -. DR KEGG; tma:TM1198; -. DR KEGG; tmi:THEMA_08340; -. DR KEGG; tmm:Tmari_1205; -. DR KEGG; tmw:THMA_1224; -. DR PATRIC; 23937338; VBITheMar51294_1216. DR eggNOG; ENOG4106K96; Bacteria. DR eggNOG; ENOG410YAXK; LUCA. DR KO; K02033; -. DR OMA; QEEMMRT; -. DR OrthoDB; EOG66F098; -. DR BioCyc; TMAR243274:GC6P-1228-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 33 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 111 137 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 157 177 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 197 215 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 263 289 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 301 324 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 109 324 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 334 AA; 38061 MW; 723CE300AD8951F1 CRC64; MNFIKGYLIP RLLQYFIVTF LGLSAIFFLP RLLPTDPVKQ QLQQYQTFGV YIPPEQQEEM MRTLRQLYGL EGTLWEQYLD FWKRLLTGDF GPSFSRFPVS VSKVISQALP WTVGLLSLTT ILSWIIAVIV GGIVGYYRKR WMEALDVVVM IIRPIPYYVM ALICLILFAY VFPIFPLSGG IGIGQKLSFD LETILSIVKH GTLPALTLMI VGIAWQFQSM KLIVQIVKSE DHVWYAKTAG VTEKMIVRNH VIRNAMLPMI TQLGLQFGGI FSGALITEMV FAYPGIGWIL YDAIMKADYN LIMGVMCIST IAITTSILLL DLIYPLFDPR VRYR // ID Q9WYF4_THEMA Unreviewed; 207 AA. AC Q9WYF4; G4FHN2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000313|EMBL:AGL49242.1}; DE EC=2.1.1.17 {ECO:0000313|EMBL:AGL49242.1}; DE SubName: Full=Ubiquinone/menaquinone biosynthesis-related protein {ECO:0000313|EMBL:AAD35406.1}; GN OrderedLocusNames=TM_0318 {ECO:0000313|EMBL:AAD35406.1}; GN ORFNames=Tmari_0316 {ECO:0000313|EMBL:AGL49242.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35406.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35406.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35406.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49242.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49242.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35406.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49242.1; -; Genomic_DNA. DR PIR; E72392; E72392. DR RefSeq; NP_228130.1; NC_000853.1. DR RefSeq; WP_004083064.1; NZ_CP011107.1. DR STRING; 243274.TM0318; -. DR EnsemblBacteria; AAD35406; AAD35406; TM_0318. DR EnsemblBacteria; AGL49242; AGL49242; Tmari_0316. DR GeneID; 897260; -. DR KEGG; tma:TM0318; -. DR KEGG; tmi:THEMA_03135; -. DR KEGG; tmm:Tmari_0316; -. DR KEGG; tmw:THMA_0325; -. DR PATRIC; 23935515; VBITheMar51294_0323. DR eggNOG; ENOG4107XIH; Bacteria. DR eggNOG; ENOG4111H81; LUCA. DR OMA; CSIPDPV; -. DR OrthoDB; EOG6X3W5K; -. DR BioCyc; TMAR243274:GC6P-331-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methyltransferase {ECO:0000313|EMBL:AGL49242.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49242.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Ubiquinone {ECO:0000313|EMBL:AAD35406.1}. FT TRANSMEM 147 169 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 43 138 Methyltransf_11. FT {ECO:0000259|Pfam:PF08241}. SQ SEQUENCE 207 AA; 24092 MW; 9BE827FCBBE9FADE CRC64; MSVERKYDRF AALYDKFESF IEKKFFSRFR EELFKRVEGK KILEVGIGTG KNVPYYSDDM DVVGVDISEG MLRVCQERLK KFPEKKVKLL RADVQNLPFS DGEYDCVVST FVFCTVPDPV KGLKEVHRVL RPSGKAVFLE HMRSRKWYVN VILFLMHIFT KLLLGTSMLR KTVDNIKKAG FVIEEEKYLL SDVVRLIIAR KGSEESD // ID Q9X0S9_THEMA Unreviewed; 823 AA. AC Q9X0S9; G4FEE4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 102. DE SubName: Full=Maltose ABC transporter, permease protein {ECO:0000313|EMBL:AAD36277.1}; DE SubName: Full=Maltose/maltodextrin ABC transporter, permease protein MalG {ECO:0000313|EMBL:AGL50133.1}; GN OrderedLocusNames=TM_1202 {ECO:0000313|EMBL:AAD36277.1}; GN ORFNames=Tmari_1209 {ECO:0000313|EMBL:AGL50133.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36277.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36277.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36277.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50133.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50133.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36277.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50133.1; -; Genomic_DNA. DR PIR; H72282; H72282. DR RefSeq; NP_229007.1; NC_000853.1. DR RefSeq; WP_004080111.1; NZ_CP011107.1. DR STRING; 243274.TM1202; -. DR TCDB; 3.A.1.1.22; the atp-binding cassette (abc) superfamily. DR DNASU; 898282; -. DR EnsemblBacteria; AAD36277; AAD36277; TM_1202. DR EnsemblBacteria; AGL50133; AGL50133; Tmari_1209. DR GeneID; 898282; -. DR KEGG; tma:TM1202; -. DR KEGG; tmi:THEMA_08320; -. DR KEGG; tmm:Tmari_1209; -. DR KEGG; tmw:THMA_1228; -. DR PATRIC; 23937346; VBITheMar51294_1220. DR eggNOG; ENOG4105EG2; Bacteria. DR eggNOG; COG3833; LUCA. DR KO; K10110; -. DR OMA; FAYLTNI; -. DR OrthoDB; EOG60PHFH; -. DR BioCyc; TMAR243274:GC6P-1232-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0015609; F:maltooligosaccharide-importing ATPase activity; IBA:GO_Central. DR GO; GO:0015423; F:maltose-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0042956; P:maltodextrin transport; IBA:GO_Central. DR GO; GO:0015768; P:maltose transport; IBA:GOC. DR GO; GO:0015772; P:oligosaccharide transport; IBA:GOC. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 33 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 607 634 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 646 670 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 676 698 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 740 763 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 787 808 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 611 808 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. FT COILED 201 253 {ECO:0000256|SAM:Coils}. FT COILED 319 346 {ECO:0000256|SAM:Coils}. FT COILED 384 418 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 823 AA; 95232 MW; 6DAC1AC3A97946DF CRC64; MVQRRGNIFT HIFLIFIIAV ILFPVVWVVT TSLRRDEAAF SSKLFTSRLT LQHYRDLVAP EKNLPFLVQD LQAMISKVKP YDTWSEEELK DAVESSIEKV KAYLSETETR LNDAVNSFEK VDAFLNDHSE EIKNRTIEEM RELLSSIQIP DLSDSVENRA ALYLVLSKER YNSTAHKALK ELLERFTGVD TGTRDGYEKA IESLKESYEK LADGYDGLIK ETQRELNAVK EEMSSLRQQY SALQDNVMEA NLVIEKDIIP ELERIKISLS ELNNLREQIR QTALRSPFPV NDEEFSRNVS EAVQMLNKFL NEMGSFAEYD SLKNSLVELK KELTKLSEGS EDLRNRLLFS DLVKIYEELH PRLIRILKET AETIASIKDR IAVLNVLNER LKDLEIQEKD LTAKISEYQQ KISEVQQKLL EPQRTLNLIV FRYELEKTIS SLERVKAFKK TDLLRYSSAL KTLRNFMNSY WKKDELYSRI SRAVKEMRWI EEYRDFASKF DVFPENLKAI LEEMHTSLSD LERSYGDFIS LSSQGVYVSS SVLSRMYDIV KMDFVNKVRA NMSVASRRAG NLIDLVPFSE VKKDLRNIDR ELFRIDQIWK QKTKHYFWLW VLNSVIVSLI VAFITTTVCA IAAYPFSRMR FFGRRYGIMA LLLIQMFPGV IFMIAIYDLL NFMGKYIPFI GIDTLGGLIF AYLTNIAYNM YLIKGFYDTI PTSLEEAAIV DGATRFQSFY KIIIPLARPI LTVVFLLVFI GTFNEYVVAR IILQNVRHYT YALGLQAFAT GPYETEWGLF TAAALLGMTP MVILFLSLQR YLVSGLTRGA VKE // ID Q9WZS4_THEMA Unreviewed; 674 AA. AC Q9WZS4; G4FD07; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AGL49743.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35899.1}; GN OrderedLocusNames=TM_0817 {ECO:0000313|EMBL:AAD35899.1}; GN ORFNames=Tmari_0818 {ECO:0000313|EMBL:AGL49743.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35899.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35899.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35899.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49743.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49743.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35899.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49743.1; -; Genomic_DNA. DR PIR; D72329; D72329. DR RefSeq; NP_228626.1; NC_000853.1. DR RefSeq; WP_004080845.1; NZ_CP011107.1. DR STRING; 243274.TM0817; -. DR DNASU; 898485; -. DR EnsemblBacteria; AAD35899; AAD35899; TM_0817. DR EnsemblBacteria; AGL49743; AGL49743; Tmari_0818. DR GeneID; 898485; -. DR KEGG; tma:TM0817; -. DR KEGG; tmi:THEMA_00565; -. DR KEGG; tmm:Tmari_0818; -. DR KEGG; tmw:THMA_0836; -. DR PATRIC; 23936554; VBITheMar51294_0829. DR eggNOG; ENOG4107XXG; Bacteria. DR eggNOG; COG1033; LUCA. DR KO; K07003; -. DR OMA; VFIDIRA; -. DR OrthoDB; EOG64N9SC; -. DR BioCyc; TMAR243274:GC6P-844-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR004869; MMPL_dom. DR Pfam; PF03176; MMPL; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 212 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 246 266 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 286 305 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 311 334 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 355 374 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 528 546 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 553 575 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 581 600 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 620 641 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 647 668 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 48 328 MMPL. {ECO:0000259|Pfam:PF03176}. FT DOMAIN 388 666 MMPL. {ECO:0000259|Pfam:PF03176}. SQ SEQUENCE 674 AA; 76651 MW; B21D18BCAAEDC506 CRC64; MRRYLFTTTY VVLVFLSFFV VFSLGKIETG PEVFLPGYNG DPEKTTNENV KNLFRVNKEF GGSSSIVIVV ESDKNFFEDA RTLYELHRAL EEREDISSVM SPVNLPKLSG FRMDYYFKDE KISKDVLNDP NAKSFITEDG KYALLNVIFK EGVNARDKIP EIKRLVSSYF EKNYLFGEPV IDSTLFKELV KQTFVYPVFM FLVIFLLFYY QLRSFRAAIF SLIVPVLATF FVFAVFFAMG KSLNTMTVMT ITFLLIIGSA YGLHFYNALF RFSDKREAVK HIFKPILFSM LTTAAGFMSF VFIDIRAFRE LGILVSSGLA VVVLVIFTSG VEIFRNYTPK RTPRSFGMKY VGRKIALIVL VVFLVMAALS PFLLKRVQVG SDMVSYFERD SELRKAYDLI VKKFNTREPI YLVLEKNVPF VGTDSKILKE LIEKIEKSEY VSSVVFPVDI PVPIMYTLSR TNPFLKTFVG DRNRIRLIVN LTPEGYEHVK KVVDLINEVV SETGWSHYVA GSVLIWNDIN ESIMRSQIQS IVLASILIFA MVFIIFRRPL TTLSVMIPIA FTTVFNFLFM ALFGISLDVS TSITSGILMG LVIDYSIHIA SEERRLRDPY LVVKNVGPSV LTNALGLISG FAVLLFSELA LFKNISLLMM LGIGVGAIFT LIVQPMILEK RENS // ID Q9X1Y1_THEMA Unreviewed; 198 AA. AC Q9X1Y1; G4FG37; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Hydrolase (HAD superfamily), YqeK {ECO:0000313|EMBL:AGL50581.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36715.1}; GN OrderedLocusNames=TM_1648 {ECO:0000313|EMBL:AAD36715.1}; GN ORFNames=Tmari_1657 {ECO:0000313|EMBL:AGL50581.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36715.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36715.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36715.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50581.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50581.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36715.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50581.1; -; Genomic_DNA. DR PIR; E72227; E72227. DR RefSeq; NP_229448.1; NC_000853.1. DR RefSeq; WP_004082149.1; NZ_CP011107.1. DR STRING; 243274.TM1648; -. DR EnsemblBacteria; AAD36715; AAD36715; TM_1648. DR EnsemblBacteria; AGL50581; AGL50581; Tmari_1657. DR GeneID; 897917; -. DR KEGG; tma:TM1648; -. DR KEGG; tmi:THEMA_06005; -. DR KEGG; tmm:Tmari_1657; -. DR KEGG; tmw:THMA_1689; -. DR PATRIC; 23938270; VBITheMar51294_1667. DR eggNOG; ENOG41083T0; Bacteria. DR eggNOG; COG1713; LUCA. DR OMA; HTTGREN; -. DR OrthoDB; EOG6B8XJX; -. DR BioCyc; TMAR243274:GC6P-1694-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR005249; CHP00488. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00488; TIGR00488; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50581.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 16 144 HDc. {ECO:0000259|SMART:SM00471}. SQ SEQUENCE 198 AA; 22734 MW; 965008324ADCC91C CRC64; MVVITNELES IMERLLSRKR INHVRSVVEF SRKLGEMYGA DSNKLELAAI SHDLFRDVPP RKLLKMAQAY GLKISELERT HPVLLHGKVA AEFLKRRFNV EDEEVLNAVA YHTSGHVSFK TVGKILFIAD SLEFTRDFPG VDELRRIAFR NLEEGFFQVL KNKIFYAVGK NYLLIPETVE LWNSILMGRG GLVDEEVE // ID Q9X1X3_THEMA Unreviewed; 207 AA. AC Q9X1X3; G4FG27; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 106. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36705.1}; GN OrderedLocusNames=TM_1638 {ECO:0000313|EMBL:AAD36705.1}; GN ORFNames=Tmari_1647 {ECO:0000313|EMBL:AGL50571.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36705.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36705.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36705.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50571.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50571.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36705.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50571.1; -; Genomic_DNA. DR PIR; F72230; F72230. DR RefSeq; NP_229438.1; NC_000853.1. DR RefSeq; WP_004082120.1; NZ_CP011107.1. DR STRING; 243274.TM1638; -. DR EnsemblBacteria; AAD36705; AAD36705; TM_1638. DR EnsemblBacteria; AGL50571; AGL50571; Tmari_1647. DR GeneID; 897922; -. DR KEGG; tma:TM1638; -. DR KEGG; tmi:THEMA_06055; -. DR KEGG; tmm:Tmari_1647; -. DR KEGG; tmw:THMA_1679; -. DR PATRIC; 23938250; VBITheMar51294_1657. DR eggNOG; ENOG4105FEX; Bacteria. DR eggNOG; ENOG410XQRE; LUCA. DR KO; K01990; -. DR OMA; QARISYC; -. DR OrthoDB; EOG65J54C; -. DR BioCyc; TMAR243274:GC6P-1684-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD36705.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD36705.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 207 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 207 AA; 23097 MW; C0DFA4C0384F0038 CRC64; MKKSYGKKKK VLDGVSFSLE KGKSLGIVGQ NSAGKTTLLK ILATILKPDE GRLFLFEKNA LKDLSYIRKR IAFVPEFPAL LEELTVRENL LFFSRLRGVK MENFIVSELM LEPFMGTLVR NASKGVKQRT ALAVALFGNP ELLILDEPTS GLDVESASIV RSKLKRLKEE GITVIISSHI REDIEELCDE ILVINGENGG DGFERDR // ID Q9WYP1_THEMA Unreviewed; 149 AA. AC Q9WYP1; G4FHW9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35495.1}; GN OrderedLocusNames=TM_0410 {ECO:0000313|EMBL:AAD35495.1}; GN ORFNames=Tmari_0407 {ECO:0000313|EMBL:AGL49332.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35495.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35495.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35495.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49332.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49332.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35495.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49332.1; -; Genomic_DNA. DR PIR; H72380; H72380. DR RefSeq; NP_228220.1; NC_000853.1. DR RefSeq; WP_004083256.1; NZ_CP011107.1. DR STRING; 243274.TM0410; -. DR EnsemblBacteria; AAD35495; AAD35495; TM_0410. DR EnsemblBacteria; AGL49332; AGL49332; Tmari_0407. DR GeneID; 897409; -. DR KEGG; tma:TM0410; -. DR KEGG; tmi:THEMA_02675; -. DR KEGG; tmm:Tmari_0407; -. DR KEGG; tmw:THMA_0416; -. DR PATRIC; 23935703; VBITheMar51294_0415. DR eggNOG; ENOG41080U3; Bacteria. DR eggNOG; COG1683; LUCA. DR OMA; YDGGHNL; -. DR OrthoDB; EOG6QZMWM; -. DR BioCyc; TMAR243274:GC6P-425-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR007553; DUF523. DR Pfam; PF04463; DUF523; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 143 DUF523. {ECO:0000259|Pfam:PF04463}. SQ SEQUENCE 149 AA; 16304 MW; 26E89F146BE6AE70 CRC64; MKILVSACLL GLPTRYDGRS VADERVLSLL KRHDLIPVCP EQLGGLPTPR PRCEIYGGCG WTGKERVLDE FGSDRTENFL RGAETTLKVA RLLKVDLAIL KSKSPSCGKR FVYDGSFSGR LVPGKGVTAF VLERNGVEVL DETEIPGDL // ID Q9WXQ3_THEMA Unreviewed; 39 AA. AC Q9WXQ3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35140.1}; GN OrderedLocusNames=TM_0046 {ECO:0000313|EMBL:AAD35140.1}; GN ORFNames=Tmari_0043 {ECO:0000313|EMBL:AGL48969.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35140.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35140.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35140.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48969.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48969.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35140.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48969.1; -; Genomic_DNA. DR PIR; C72426; C72426. DR RefSeq; NP_227862.1; NC_000853.1. DR RefSeq; WP_010865037.1; NZ_CP011107.1. DR STRING; 243274.TM0046; -. DR EnsemblBacteria; AAD35140; AAD35140; TM_0046. DR EnsemblBacteria; AGL48969; AGL48969; Tmari_0043. DR GeneID; 896870; -. DR KEGG; tma:TM0046; -. DR KEGG; tmm:Tmari_0043; -. DR KEGG; tmw:THMA_0042; -. DR PATRIC; 23934932; VBITheMar51294_0044. DR BioCyc; TMAR243274:GC6P-46-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 39 AA; 4237 MW; 579E062544272B24 CRC64; MEGSLRAAKN PIPFRGLGVS KEPYRMVKTG EKSTCQGVL // ID Q9X0K9_THEMA Unreviewed; 134 AA. AC Q9X0K9; G4FEM3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36201.1}; GN OrderedLocusNames=TM_1125 {ECO:0000313|EMBL:AAD36201.1}; GN ORFNames=Tmari_1131 {ECO:0000313|EMBL:AGL50055.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36201.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36201.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36201.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50055.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50055.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36201.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50055.1; -; Genomic_DNA. DR PIR; B72293; B72293. DR RefSeq; NP_228931.1; NC_000853.1. DR RefSeq; WP_004080292.1; NZ_CP011107.1. DR STRING; 243274.TM1125; -. DR EnsemblBacteria; AAD36201; AAD36201; TM_1125. DR EnsemblBacteria; AGL50055; AGL50055; Tmari_1131. DR GeneID; 898639; -. DR KEGG; tma:TM1125; -. DR KEGG; tmi:THEMA_08720; -. DR KEGG; tmm:Tmari_1131; -. DR KEGG; tmw:THMA_1148; -. DR PATRIC; 23937185; VBITheMar51294_1141. DR OMA; SKYGVGH; -. DR OrthoDB; EOG6NSGJV; -. DR BioCyc; TMAR243274:GC6P-1154-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 134 AA; 15273 MW; 7EECA313F0810C13 CRC64; MRNGSLIVET LISLFLILLT VVIFTTIIVG VAKNVTFTEE SIETFLFTNF AYDFLSKYEV GHEIEQGVYE EINREFWKDK WNDQNPPFPH IDPSVSTVED VALPSSSDVK YKKITLKIKI NEGASIERIV IIGD // ID Q9WYS6_THEMA Unreviewed; 404 AA. AC Q9WYS6; G4FE25; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 108. DE SubName: Full=Putative GTP-binding protein {ECO:0000313|EMBL:AGL49367.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35530.1}; GN OrderedLocusNames=TM_0445 {ECO:0000313|EMBL:AAD35530.1}; GN ORFNames=Tmari_0442 {ECO:0000313|EMBL:AGL49367.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35530.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35530.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35530.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49367.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49367.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35530.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49367.1; -; Genomic_DNA. DR PIR; H72377; H72377. DR RefSeq; NP_228255.1; NC_000853.1. DR RefSeq; WP_004081521.1; NZ_CP011107.1. DR STRING; 243274.TM0445; -. DR EnsemblBacteria; AAD35530; AAD35530; TM_0445. DR EnsemblBacteria; AGL49367; AGL49367; Tmari_0442. DR GeneID; 897463; -. DR KEGG; tma:TM0445; -. DR KEGG; tmi:THEMA_02500; -. DR KEGG; tmm:Tmari_0442; -. DR KEGG; tmw:THMA_0451; -. DR PATRIC; 23935775; VBITheMar51294_0451. DR eggNOG; ENOG4105F4F; Bacteria. DR eggNOG; COG1160; LUCA. DR OMA; PQDIQAP; -. DR OrthoDB; EOG6X9MJ2; -. DR BioCyc; TMAR243274:GC6P-460-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR023873; FeFe-hyd_GTPase_HydF. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03918; GTP_HydF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 12 124 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. SQ SEQUENCE 404 AA; 45091 MW; CF4C255CB053978A CRC64; MRLPDAGFRR YIVVAGRRNV GKSSFMNALV GQNVSIVSEY AGTTTDPVYK SMELYPVGPV TLVDTPGLDD VGELGRLRVE KARRVFYRAD CGILVTDSEP TPYEDDVVNL FKEMEIPFVV VVNKIDVLGE KAEELKGLYE SRYEAKVLLV SALQKKGFDD IGKTISEILP GDEEIPYLGD LIDGGDLVIL VVPIDLGAPK GRLIMPQVHA IREALDREAI ALVVKERELR YVMENIGMKP KLVITDSQVV MKVASDVPED VELTTFSIVE SRYRGDLAYF VESVRKIEEL EDGDTVVIME GCTHRPLTED IGRVKIPRWL VNHTGAQLNF KVIAGKDFPD LEEIEGAKLI IHCGGCVLNR AAMMRRVRMA KRLGIPMTNY GVTISYLHGV LDRAIRPFRE EVKV // ID Q9WXU4_THEMA Unreviewed; 153 AA. AC Q9WXU4; G4FH04; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35183.1}; GN OrderedLocusNames=TM_0089 {ECO:0000313|EMBL:AAD35183.1}; GN ORFNames=Tmari_0086 {ECO:0000313|EMBL:AGL49012.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35183.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35183.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35183.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49012.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49012.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35183.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49012.1; -; Genomic_DNA. DR PIR; C72420; C72420. DR RefSeq; NP_227905.1; NC_000853.1. DR RefSeq; WP_004082621.1; NZ_CP011107.1. DR STRING; 243274.TM0089; -. DR EnsemblBacteria; AAD35183; AAD35183; TM_0089. DR EnsemblBacteria; AGL49012; AGL49012; Tmari_0086. DR GeneID; 896916; -. DR KEGG; tma:TM0089; -. DR KEGG; tmi:THEMA_04360; -. DR KEGG; tmm:Tmari_0086; -. DR KEGG; tmw:THMA_0085; -. DR PATRIC; 23935018; VBITheMar51294_0087. DR OMA; FEISGEN; -. DR OrthoDB; EOG6K9QHR; -. DR BioCyc; TMAR243274:GC6P-89-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 153 AA; 17143 MW; 3059E8A5E96C12A1 CRC64; MNRRTVILLV IMGVVWSFVL FYLFAGNRES GTLQVERPTD FTALVNKIQI NPLLKKTAQE NPPEFSYRVF NSVTLSFGKE AADTLIVTLP TLKYRFLGFI RTGDGLKIFL SDGGKLFEVS GESPTFGNYV VTYVSSLGVL VLDVENGRFF SIR // ID Q9WZ57_THEMA Unreviewed; 336 AA. AC Q9WZ57; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=Rod shape-determining protein MreB {ECO:0000313|EMBL:AAD35673.1}; GN OrderedLocusNames=TM_0588 {ECO:0000313|EMBL:AAD35673.1}; GN ORFNames=Tmari_0586 {ECO:0000313|EMBL:AGL49511.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35673.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35673.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35673.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49511.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49511.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- INTERACTION: CC Q9X2H8:TM_1864; NbExp=11; IntAct=EBI-7816271, EBI-7816285; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35673.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49511.1; -; Genomic_DNA. DR PIR; E72359; E72359. DR RefSeq; NP_228398.1; NC_000853.1. DR RefSeq; WP_010865154.1; NZ_CP011107.1. DR PDB; 1JCE; X-ray; 2.10 A; A=1-336. DR PDB; 1JCF; X-ray; 2.10 A; A=1-336. DR PDB; 1JCG; X-ray; 3.10 A; A=1-336. DR PDB; 2WUS; X-ray; 2.90 A; A/B=1-336. DR PDBsum; 1JCE; -. DR PDBsum; 1JCF; -. DR PDBsum; 1JCG; -. DR PDBsum; 2WUS; -. DR MINT; MINT-7893468; -. DR STRING; 243274.TM0588; -. DR EnsemblBacteria; AAD35673; AAD35673; TM_0588. DR EnsemblBacteria; AGL49511; AGL49511; Tmari_0586. DR GeneID; 897660; -. DR KEGG; tma:TM0588; -. DR KEGG; tmi:THEMA_01725; -. DR KEGG; tmm:Tmari_0586; -. DR KEGG; tmw:THMA_0603; -. DR PATRIC; 23936087; VBITheMar51294_0597. DR eggNOG; ENOG4105DFF; Bacteria. DR eggNOG; COG1077; LUCA. DR KO; K03569; -. DR OMA; HETGIVT; -. DR OrthoDB; EOG66QM00; -. DR BioCyc; TMAR243274:GC6P-613-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro. DR InterPro; IPR004753; MreB_Mrl. DR Pfam; PF06723; MreB_Mbl; 1. DR PRINTS; PR01652; SHAPEPROTEIN. DR TIGRFAMs; TIGR00904; mreB; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1JCE, ECO:0000213|PDB:1JCF, KW ECO:0000213|PDB:1JCG, ECO:0000213|PDB:2WUS}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000213|PDB:1JCG}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT NP_BIND 13 14 ATP analog. {ECO:0000213|PDB:1JCG}. FT NP_BIND 156 158 ATP analog. {ECO:0000213|PDB:1JCG}. FT NP_BIND 204 207 ATP analog. {ECO:0000213|PDB:1JCG}. FT NP_BIND 286 287 ATP analog. {ECO:0000213|PDB:1JCG}. FT BINDING 131 131 ATP analog. {ECO:0000213|PDB:1JCG}. SQ SEQUENCE 336 AA; 35787 MW; B9A5FB8C9FE59A6E CRC64; MLRKDIGIDL GTANTLVFLR GKGIVVNEPS VIAIDSTTGE ILKVGLEAKN MIGKTPATIK AIRPMRDGVI ADYTVALVML RYFINKAKGG MNLFKPRVVI GVPIGITDVE RRAILDAGLE AGASKVFLIE EPMAAAIGSN LNVEEPSGNM VVDIGGGTTE VAVISLGSIV TWESIRIAGD EMDEAIVQYV RETYRVAIGE RTAERVKIEI GNVFPSKEND ELETTVSGID LSTGLPRKLT LKGGEVREAL RSVVVAIVES VRTTLEKTPP ELVSDIIERG IFLTGGGSLL RGLDTLLQKE TGISVIRSEE PLTAVAKGAG MVLDKVNILK KLQGAG // ID Q9X018_THEMA Unreviewed; 284 AA. AC Q9X018; G4FCR0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=DUF114 domain-containing protein {ECO:0000313|EMBL:AGL49843.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35997.1}; GN OrderedLocusNames=TM_0916 {ECO:0000313|EMBL:AAD35997.1}; GN ORFNames=Tmari_0918 {ECO:0000313|EMBL:AGL49843.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35997.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35997.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35997.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49843.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49843.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35997.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49843.1; -; Genomic_DNA. DR PIR; C72320; C72320. DR RefSeq; NP_228724.1; NC_000853.1. DR RefSeq; WP_004080646.1; NZ_CP011107.1. DR STRING; 243274.TM0916; -. DR EnsemblBacteria; AAD35997; AAD35997; TM_0916. DR EnsemblBacteria; AGL49843; AGL49843; Tmari_0918. DR GeneID; 898590; -. DR KEGG; tma:TM0916; -. DR KEGG; tmi:THEMA_00055; -. DR KEGG; tmm:Tmari_0918; -. DR KEGG; tmw:THMA_0938; -. DR PATRIC; 23936763; VBITheMar51294_0930. DR eggNOG; ENOG4105ERM; Bacteria. DR eggNOG; COG0616; LUCA. DR OMA; LMDLYPQ; -. DR OrthoDB; EOG68WR7V; -. DR BioCyc; TMAR243274:GC6P-946-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.90.226.10; -; 1. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR002825; Pept_S49_ser-pept_pro. DR Pfam; PF01972; SDH_sah; 1. DR SUPFAM; SSF52096; SSF52096; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 284 AA; 32143 MW; 2D0B0D47CDF66121 CRC64; MVDIGTLIFQ IFWMIFIFSL ITPFLKNSAL KSAREALIRE IEKKRNSRVI TLIHRTESIS FLGFPVRRYI DIEDSEEILR AIKLTPSDMP IDLILHTPGG LVLAAEQIAR ALKMHKGKVT VFVPHYAMSG GTLIALAADE IIMDENAVLG PLDPQIGNMP APSILAAVKK KDVNEVDDQT LILADIAEKA IRQVKEFVVE ILSDKVSKEK AEKIADKLCS GYWTHDYPLN YEKLREMGIQ VKTDMPQEIY DLMDLYKQAE PKRPSVNYIP APYYNRKETG NGNR // ID Q9WZW9_THEMA Unreviewed; 140 AA. AC Q9WZW9; G4FCV9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Putative activity regulator of membrane protease YbbK {ECO:0000313|EMBL:AGL49792.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35947.1}; GN OrderedLocusNames=TM_0865 {ECO:0000313|EMBL:AAD35947.1}; GN ORFNames=Tmari_0867 {ECO:0000313|EMBL:AGL49792.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35947.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35947.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35947.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49792.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49792.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35947.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49792.1; -; Genomic_DNA. DR PIR; D72322; D72322. DR RefSeq; NP_228674.1; NC_000853.1. DR RefSeq; WP_004080739.1; NZ_CP011107.1. DR STRING; 243274.TM0865; -. DR EnsemblBacteria; AAD35947; AAD35947; TM_0865. DR EnsemblBacteria; AGL49792; AGL49792; Tmari_0867. DR GeneID; 898538; -. DR KEGG; tma:TM0865; -. DR KEGG; tmi:THEMA_00310; -. DR KEGG; tmm:Tmari_0867; -. DR KEGG; tmw:THMA_0887; -. DR PATRIC; 23936658; VBITheMar51294_0878. DR eggNOG; ENOG4105VHJ; Bacteria. DR eggNOG; COG1585; LUCA. DR OMA; VEHETWT; -. DR OrthoDB; EOG62G5TH; -. DR BioCyc; TMAR243274:GC6P-895-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR002810; NfeD-like_C. DR Pfam; PF01957; NfeD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49792.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000313|EMBL:AGL49792.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 41 62 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 6 139 NfeD. {ECO:0000259|Pfam:PF01957}. SQ SEQUENCE 140 AA; 15724 MW; 665E0944775E1DF0 CRC64; MEAWVFWLVL GVILMVAEIL TPTFFIFWFG VGALAASLVS LYLGVYVQII VFAAVSIVLV FLTRRLVQNW ESPRKIHVEE IAGKVALVIE TIDNRKGTGL VKIDGDVWRA YAEDDDEVIE KGEHVKIMKV EGAHVVVKRV // ID Q9X039_THEMA Unreviewed; 410 AA. AC Q9X039; G4FF49; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36022.1}; GN OrderedLocusNames=TM_0941 {ECO:0000313|EMBL:AAD36022.1}; GN ORFNames=Tmari_0943 {ECO:0000313|EMBL:AGL49868.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36022.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36022.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36022.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49868.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49868.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36022.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49868.1; -; Genomic_DNA. DR PIR; E72316; E72316. DR RefSeq; NP_228749.1; NC_000853.1. DR RefSeq; WP_004080621.1; NZ_CP011107.1. DR STRING; 243274.TM0941; -. DR EnsemblBacteria; AAD36022; AAD36022; TM_0941. DR EnsemblBacteria; AGL49868; AGL49868; Tmari_0943. DR GeneID; 898678; -. DR KEGG; tma:TM0941; -. DR KEGG; tmi:THEMA_09645; -. DR KEGG; tmm:Tmari_0943; -. DR KEGG; tmw:THMA_0963; -. DR PATRIC; 23936813; VBITheMar51294_0955. DR eggNOG; ENOG4107E0H; Bacteria. DR eggNOG; ENOG410Z6MJ; LUCA. DR OMA; CDGREVQ; -. DR OrthoDB; EOG6T4RWC; -. DR BioCyc; TMAR243274:GC6P-971-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 410 AA; 46345 MW; 1A1ED672DC81AE0D CRC64; MVRRISFLIL ILSSLLLFSK EVLFNTYNNT GIVSLTNRTF PFETSRDLEP FKASLETIYT PPKVRGITID LPDSTTLVLS NGVTIGVDVG DIRIPEDVFA ELLESTDLTF VYDAFPVEVF SRDRVVVKGS ITKEKLEYYL SFFFKKIEVP RRIEGTIDVT PKPPEVRYSK VWHPLIGTVV FLNVTDDSTF VTLWNGREGK LWYQTTEATK LEVEVVDSLG QSTSLSFEAL PVSFAERSYQ SSVEFGQSLI LPPLVNWFLP STGEKITVFS PEFPGVYHLI GCDESGNFLR MEIDVRDTTP PLVLSPEKIE DASSFRVEYI CDGREAQKIP DGHHVVFVKA TDTFGNTSTA FFVVNRPHRV IVRERPVPVY LGPKRKIQIG GLSLKGSLIY GWTREEVEVM VGEEVYKLEK // ID Q9X003_THEMA Unreviewed; 101 AA. AC Q9X003; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35982.1}; GN OrderedLocusNames=TM_0901 {ECO:0000313|EMBL:AAD35982.1}; GN ORFNames=Tmari_0903 {ECO:0000313|EMBL:AGL49828.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35982.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35982.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35982.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49828.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49828.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35982.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49828.1; -; Genomic_DNA. DR PIR; D72318; D72318. DR RefSeq; NP_228709.1; NC_000853.1. DR RefSeq; WP_008193125.1; NZ_CP011107.1. DR STRING; 243274.TM0901; -. DR EnsemblBacteria; AAD35982; AAD35982; TM_0901. DR EnsemblBacteria; AGL49828; AGL49828; Tmari_0903. DR GeneID; 898575; -. DR KEGG; tma:TM0901; -. DR KEGG; tmi:THEMA_00130; -. DR KEGG; tmm:Tmari_0903; -. DR KEGG; tmw:THMA_0923; -. DR PATRIC; 23936733; VBITheMar51294_0915. DR OMA; KESNTAE; -. DR OrthoDB; EOG6VQPZV; -. DR BioCyc; TMAR243274:GC6P-931-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 101 AA; 11636 MW; 93EE0D73E2E38C1B CRC64; MIRPVDFQGF VVKGVESVQN VSQTLNQQTL VQQALSQHLL HQIQREQSSV KESNTAERAE VRTSTERRQR GFPQTRTHSS LKKKKTSIKE ENKGLFMDVR T // ID Q9WY92_THEMA Unreviewed; 337 AA. AC Q9WY92; G4FHG4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=DNA processing chain A {ECO:0000313|EMBL:AAD35341.1}; DE SubName: Full=Rossmann fold nucleotide-binding protein Smf possibly involved in DNA uptake {ECO:0000313|EMBL:AGL49174.1}; GN OrderedLocusNames=TM_0250 {ECO:0000313|EMBL:AAD35341.1}; GN ORFNames=Tmari_0248 {ECO:0000313|EMBL:AGL49174.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35341.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35341.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35341.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49174.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49174.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35341.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49174.1; -; Genomic_DNA. DR PIR; C72399; C72399. DR RefSeq; NP_228064.1; NC_000853.1. DR RefSeq; WP_004082954.1; NZ_CP011107.1. DR STRING; 243274.TM0250; -. DR EnsemblBacteria; AAD35341; AAD35341; TM_0250. DR EnsemblBacteria; AGL49174; AGL49174; Tmari_0248. DR GeneID; 897158; -. DR KEGG; tma:TM0250; -. DR KEGG; tmi:THEMA_03475; -. DR KEGG; tmm:Tmari_0248; -. DR KEGG; tmw:THMA_0257; -. DR PATRIC; 23935375; VBITheMar51294_0253. DR eggNOG; ENOG4105C79; Bacteria. DR eggNOG; COG0758; LUCA. DR KO; K04096; -. DR OMA; GEYWAKH; -. DR OrthoDB; EOG6DG2TK; -. DR BioCyc; TMAR243274:GC6P-263-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009294; P:DNA mediated transformation; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR003488; DprA. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02481; DNA_processg_A; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR TIGRFAMs; TIGR00732; dprA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 337 AA; 37973 MW; 59BFD4CDAED1F4A0 CRC64; MSPLEMALLV HRGEFHLREL EPELPLEKFL KNADPKKTRK FLEKCGKEEL ERQKELIRKH NVKLVSFWED DYPQHLREIR YPPAVLFVRG DAELLKEKCV GVVGTRRPTS YGVNVTKRFV KLLSEYFVIV SGMAFGIDSV AHKEALSSGG KTVAVLGTGV DVVYPRSNER LFHEIVKNGC VVSEYPMGTR ARKHHFPARN RIIAGLSDAI IVTEAPIKSG ALITVKFALE SGRDVFAVPG DIDRKTSEGT NYLIKSGAYP LTDEEDLETH FGIRRIASPS LDDDKKKIYD LLRSSPKTVD ELVEELGWSV SEVLRVISEM ELMGMIWFDG GAYRLLG // ID Q9WYS9_THEMA Unreviewed; 711 AA. AC Q9WYS9; G4FE22; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35531.1}; GN OrderedLocusNames=TM_0448 {ECO:0000313|EMBL:AAD35531.1}; GN ORFNames=Tmari_0445 {ECO:0000313|EMBL:AGL49370.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35531.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35531.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35531.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49370.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49370.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell outer membrane CC {ECO:0000256|SAAS:SAAS00560981}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35531.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49370.1; -; Genomic_DNA. DR PIR; A72375; A72375. DR RefSeq; NP_228258.1; NC_000853.1. DR RefSeq; WP_004081518.1; NZ_CP011107.1. DR STRING; 243274.TM0448; -. DR EnsemblBacteria; AAD35531; AAD35531; TM_0448. DR EnsemblBacteria; AGL49370; AGL49370; Tmari_0445. DR GeneID; 897467; -. DR KEGG; tma:TM0448; -. DR KEGG; tmi:THEMA_02485; -. DR KEGG; tmm:Tmari_0445; -. DR KEGG; tmw:THMA_0454; -. DR PATRIC; 23935781; VBITheMar51294_0454. DR eggNOG; ENOG41081M6; Bacteria. DR eggNOG; COG4775; LUCA. DR OMA; GNTIFTD; -. DR OrthoDB; EOG67DPGW; -. DR BioCyc; TMAR243274:GC6P-463-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR InterPro; IPR000184; Bac_surfAg_D15. DR InterPro; IPR010827; Surface_Ag_variable_number. DR Pfam; PF01103; Bac_surface_Ag; 1. DR Pfam; PF07244; POTRA; 3. PE 4: Predicted; KW Cell outer membrane {ECO:0000256|SAAS:SAAS00560982}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00560982, KW ECO:0000256|SAAS:SAAS00560990}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00560990}; KW Transmembrane beta strand {ECO:0000256|SAAS:SAAS00560990}. FT DOMAIN 419 709 Bac_surface_Ag. FT {ECO:0000259|Pfam:PF01103}. SQ SEQUENCE 711 AA; 80939 MW; 434C3954E809FFB4 CRC64; MKKELVLLMV LLAVSAMAIY ISEVDFKGLN TLNSEFIVQK VGKLFGEVSS DEIQEYLKKV FNLGYFSSLT PSLEPADVGY RLVVSLEENP VVKDWKLEIE GPGLVDKKEL EELVKIEKGM PLNVNLLKET FEAIRNRYQE AGYFLVEING SFENGTYRIV VKEYALWDIV FNGETDGLDI VSILSKAKIK TLRDYYASSP LVRFFTMSKK DFYPTLSEVN KLISVLNSYP FFSRETSVDF KKTTVKDIEE KNVVIMVINV VQRRIFEGEK KFKEILFHGN TIFTDQELLR ASGLSTDETY TNSQILLAMN RLVDFYERNN YPYVWVEARV EDDRLVFNVY EKYVRSVKIE GLKRTRPYVV ENLITIKEGE PLNKEEIMLT YSYLQNSRYF DSVNIYPQLS QNATQVDVVV DLKEAEKTRN FIGGLGWTMP KEGEWWQGFS GTVQLSAVNS FGYGESFSID LNLGFIERSV EGTVKLPIKL DVPMNLELGA GYTNYATSSG TDTVSLKGIV STLPYKGHSF GVGALYEKEL VEDSKGTLAA LFKYRYNTKN SAILPTEGYY LSFDLTRAGL FGLNDQKYWK GILTSEAYYP IFESLFWSFK GTGGMVRNEI GTELLEVSGP YAVRGYNYFE TEKMFKLSAD LNWILQKENV PVVTGLFVDY GGIEENGNMN TLSSAGVKLD LVVPLLGSVE VGGAYRFNEK DWQFYFFMGS W // ID Q9WY26_THEMA Unreviewed; 397 AA. AC Q9WY26; G4FH96; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 110. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35275.1}; GN OrderedLocusNames=TM_0182 {ECO:0000313|EMBL:AAD35275.1}; GN ORFNames=Tmari_0180 {ECO:0000313|EMBL:AGL49106.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35275.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35275.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35275.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49106.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49106.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35275.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49106.1; -; Genomic_DNA. DR PIR; A72408; A72408. DR RefSeq; NP_227997.1; NC_000853.1. DR RefSeq; WP_004082817.1; NZ_CP011107.1. DR PDB; 4Q37; X-ray; 3.19 A; A/B/C/D/E/F=1-120. DR PDBsum; 4Q37; -. DR DIP; DIP-61050N; -. DR STRING; 243274.TM0182; -. DR EnsemblBacteria; AAD35275; AAD35275; TM_0182. DR EnsemblBacteria; AGL49106; AGL49106; Tmari_0180. DR GeneID; 897030; -. DR KEGG; tma:TM0182; -. DR KEGG; tmi:THEMA_03865; -. DR KEGG; tmm:Tmari_0180; -. DR KEGG; tmw:THMA_0183; -. DR PATRIC; 23935220; VBITheMar51294_0183. DR eggNOG; ENOG4107RNT; Bacteria. DR eggNOG; COG1032; LUCA. DR OMA; DFIFGFP; -. DR OrthoDB; EOG683S9D; -. DR BioCyc; TMAR243274:GC6P-188-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR023980; CHP04013_B12-bd/rSAM. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR020612; Methylthiotransferase_CS. DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR04013; B12_SAM_MJ_1487; 1. DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4Q37}; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00489002}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|SAAS:SAAS00489002}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00489002}; KW Metal-binding {ECO:0000256|SAAS:SAAS00489002}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00488995}. FT DOMAIN 139 362 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 397 AA; 45100 MW; AFD7BC72E460FDF8 CRC64; MYILFREMKN NWYSLAALLS TIYSRHLDVE ARPVKFEEIK KFPPEKTIVA YSFMSFDLDT VREEVKTLKE RGYTLIAGGP HVTADPEGCL RMGFDHVFTG DGEENILKFL MGERKKIFDG ISKRVNLNHY PPFLPSKGIY MPIEITRGCP FSCAYCQTPI IAGRRVRHRD VDVVVHYAKL GVKHGRKLAR FIAPNSFGYG SKNGVTPNVE KIEELLYGLK KVGIEEIYFG TFPSEVRPES VTDEVLKVVK KYVNNRSIVI GAQSGSDRIL KIIKRGHTVE QVEEAIEKIS LHGFIPHVDF IFGFPFETEE DVEKTFSFIV KIVERYGAKI HAHTFMPLPG TELFNAGPGR LTEVHYKFLG RLASKGILDG YWMKQEMLAR KVYEIASGGS TDVTSDR // ID Q9WY98_THEMA Unreviewed; 222 AA. AC Q9WY98; G4FHH4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Phosphate transport regulator {ECO:0000313|EMBL:AGL49184.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35348.1}; GN OrderedLocusNames=TM_0260 {ECO:0000313|EMBL:AAD35348.1}; GN ORFNames=Tmari_0258 {ECO:0000313|EMBL:AGL49184.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35348.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35348.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35348.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49184.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49184.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35348.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49184.1; -; Genomic_DNA. DR PIR; C72400; C72400. DR RefSeq; NP_228073.1; NC_000853.1. DR RefSeq; WP_004082964.1; NZ_CP011107.1. DR STRING; 243274.TM0260; -. DR EnsemblBacteria; AAD35348; AAD35348; TM_0260. DR EnsemblBacteria; AGL49184; AGL49184; Tmari_0258. DR GeneID; 897170; -. DR KEGG; tma:TM0260; -. DR KEGG; tmi:THEMA_03425; -. DR KEGG; tmm:Tmari_0258; -. DR KEGG; tmw:THMA_0267; -. DR PATRIC; 23935397; VBITheMar51294_0264. DR eggNOG; ENOG41081U3; Bacteria. DR eggNOG; COG1392; LUCA. DR KO; K07220; -. DR OMA; NSMNPVD; -. DR OrthoDB; EOG6WMHZ7; -. DR BioCyc; TMAR243274:GC6P-273-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR018445; Put_Phosphate_transp_reg. DR Pfam; PF01865; PhoU_div; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 222 AA; 25926 MW; 22E680FFB3CB3B52 CRC64; MKFIEKMLPE ESPIDLLINL SRRGEAAVVL LKDAIEDYFT GKFGEGHLNR VISLERESDE IKSKLKKMYL KMKYTYFEKD DFLYIVHKAD EILDVVRDIV IMLDMNRVED VPENIKELFA ELVENVLDTI RETTEAIEQL RTLAESGFSP FEKEKEEREI FDVSMEEREV DTISRNLGKK LYSLKNSMNP VDLIFLNKVA RLISKIADQG KDITKRINSI LR // ID Q9WXS0_THEMA Unreviewed; 246 AA. AC Q9WXS0; G4FGY0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 107. DE SubName: Full=Transcriptional regulator, IclR family {ECO:0000313|EMBL:AAD35159.1}; GN OrderedLocusNames=TM_0065 {ECO:0000313|EMBL:AAD35159.1}; GN ORFNames=Tmari_0062 {ECO:0000313|EMBL:AGL48988.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35159.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35159.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35159.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48988.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48988.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 HTH iclR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000705}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35159.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48988.1; -; Genomic_DNA. DR PIR; E72422; E72422. DR RefSeq; NP_227881.1; NC_000853.1. DR RefSeq; WP_004082558.1; NZ_CP011107.1. DR PDB; 1MKM; X-ray; 2.20 A; A/B=1-246. DR PDBsum; 1MKM; -. DR STRING; 243274.TM0065; -. DR EnsemblBacteria; AAD35159; AAD35159; TM_0065. DR EnsemblBacteria; AGL48988; AGL48988; Tmari_0062. DR GeneID; 896889; -. DR KEGG; tma:TM0065; -. DR KEGG; tmi:THEMA_04480; -. DR KEGG; tmm:Tmari_0062; -. DR KEGG; tmw:THMA_0061; -. DR PATRIC; 23934970; VBITheMar51294_0063. DR eggNOG; ENOG4105J4Q; Bacteria. DR eggNOG; COG1414; LUCA. DR OMA; WRDREEV; -. DR OrthoDB; EOG6MWN8D; -. DR BioCyc; TMAR243274:GC6P-65-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.450.40; -; 1. DR InterPro; IPR029016; GAF_dom-like. DR InterPro; IPR014757; Tscrpt_reg_IclR_C. DR InterPro; IPR005471; Tscrpt_reg_IclR_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF09339; HTH_IclR; 1. DR Pfam; PF01614; IclR; 1. DR SMART; SM00346; HTH_ICLR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF55781; SSF55781; 1. DR PROSITE; PS51077; HTH_ICLR; 1. DR PROSITE; PS51078; ICLR_ED; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1MKM}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000705}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU000705, KW ECO:0000256|SAAS:SAAS00422568}; KW Transcription regulation {ECO:0000256|RuleBase:RU000705, KW ECO:0000256|SAAS:SAAS00422568}. FT DOMAIN 1 62 HTH iclR-type DNA-binding. FT {ECO:0000259|PROSITE:PS51077}. FT DOMAIN 63 246 IclR-ED (iclR effector binding). FT {ECO:0000259|PROSITE:PS51078}. SQ SEQUENCE 246 AA; 28119 MW; AD68B31A05A27D91 CRC64; MNTLKKAFEI LDFIVKNPGD VSVSEIAEKF NMSVSNAYKY MVVLEEKGFV LRKKDKRYVP GYKLIEYGSF VLRRFNIRDI AHDHLVDIMK RTGETVHLIL KDGFEGVYID KVEGEQSIPM VSRLGMKVDL YSTASGKSIL AFVPEKELKE YLKIVELKPK TPNTITNPRV LKRELEKIRK RGYAVDNEEN EIGIMCVGVP IFDHNGYPVA GVSISGVARK FTEEKIEEYS DVLKEKAEEI SRKLGY // ID Q9WYA5_THEMA Unreviewed; 768 AA. AC Q9WYA5; G4FHI2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE SubName: Full=5-methyltetrahydrofolate S-homocysteine methyltransferase {ECO:0000313|EMBL:AAD35357.1}; DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:AGL49192.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AGL49192.1}; GN OrderedLocusNames=TM_0268 {ECO:0000313|EMBL:AAD35357.1}; GN ORFNames=Tmari_0266 {ECO:0000313|EMBL:AGL49192.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35357.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35357.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35357.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49192.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49192.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35357.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49192.1; -; Genomic_DNA. DR PIR; B72397; B72397. DR RefSeq; NP_228081.1; NC_000853.1. DR RefSeq; WP_004082972.1; NZ_CP011107.1. DR PDB; 1Q7M; X-ray; 2.10 A; A/B=1-566. DR PDB; 1Q7Q; X-ray; 3.10 A; A/B=1-566. DR PDB; 1Q7Z; X-ray; 1.70 A; A/B=1-566. DR PDB; 1Q85; X-ray; 2.00 A; A/B=1-566. DR PDB; 1Q8A; X-ray; 1.70 A; A/B=1-566. DR PDB; 1Q8J; X-ray; 1.90 A; A/B=1-566. DR PDB; 3BOF; X-ray; 1.70 A; A/B=1-566. DR PDB; 3BOL; X-ray; 1.85 A; A/B=1-566. DR PDBsum; 1Q7M; -. DR PDBsum; 1Q7Q; -. DR PDBsum; 1Q7Z; -. DR PDBsum; 1Q85; -. DR PDBsum; 1Q8A; -. DR PDBsum; 1Q8J; -. DR PDBsum; 3BOF; -. DR PDBsum; 3BOL; -. DR STRING; 243274.TM0268; -. DR EnsemblBacteria; AAD35357; AAD35357; TM_0268. DR EnsemblBacteria; AGL49192; AGL49192; Tmari_0266. DR GeneID; 897179; -. DR KEGG; tma:TM0268; -. DR KEGG; tmi:THEMA_03385; -. DR KEGG; tmm:Tmari_0266; -. DR KEGG; tmw:THMA_0275; -. DR PATRIC; 23935413; VBITheMar51294_0272. DR eggNOG; ENOG4105C3R; Bacteria. DR eggNOG; COG0646; LUCA. DR eggNOG; COG1410; LUCA. DR KO; K00548; -. DR OMA; IGKNIVC; -. DR OrthoDB; EOG6091CH; -. DR BioCyc; TMAR243274:GC6P-281-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.20.20.20; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR003726; HCY_dom. DR InterPro; IPR017215; MetH_bac. DR InterPro; IPR000489; Pterin-binding_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF00809; Pterin_bind; 1. DR Pfam; PF02574; S-methyl_trans; 1. DR PIRSF; PIRSF037472; DHPS_mtfrase; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. DR PROSITE; PS50970; HCY; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1Q7M, ECO:0000213|PDB:1Q7Q, KW ECO:0000213|PDB:1Q7Z, ECO:0000213|PDB:1Q85}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000213|PDB:3BOF, ECO:0000213|PDB:3BOL}; KW Methyltransferase {ECO:0000313|EMBL:AAD35357.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35357.1}; KW Zinc {ECO:0000213|PDB:3BOF, ECO:0000213|PDB:3BOL}. FT DOMAIN 4 287 Hcy-binding. FT {ECO:0000259|PROSITE:PS50970}. FT DOMAIN 315 556 Pterin-binding. FT {ECO:0000259|PROSITE:PS50972}. FT DOMAIN 557 650 B12-binding N-terminal. FT {ECO:0000259|PROSITE:PS51337}. FT DOMAIN 648 768 B12-binding. FT {ECO:0000259|PROSITE:PS51332}. FT METAL 207 207 Zinc. {ECO:0000213|PDB:3BOF, FT ECO:0000213|PDB:3BOL}. FT METAL 234 234 Zinc. {ECO:0000213|PDB:3BOL}. FT METAL 272 272 Zinc. {ECO:0000213|PDB:3BOF, FT ECO:0000213|PDB:3BOL}. FT METAL 273 273 Zinc. {ECO:0000213|PDB:3BOF, FT ECO:0000213|PDB:3BOL}. FT DISULFID 207 272 {ECO:0000213|PDB:1Q7M, FT ECO:0000213|PDB:1Q7Q}. SQ SEQUENCE 768 AA; 85704 MW; 39E1A42EDE37A26C CRC64; MRNRREVSKL LSERVLLLDG AYGTEFMKYG YDDLPEELNI KAPDVVLKVH RSYIESGSDV ILTNTFGATR MKLRKHGLED KLDPIVRNAV RIARRAAGEK LVFGDIGPTG ELPYPLGSTL FEEFYENFRE TVEIMVEEGV DGIIFETFSD ILELKAAVLA AREVSRDVFL IAHMTFDEKG RSLTGTDPAN FAITFDELDI DALGINCSLG PEEILPIFQE LSQYTDKFLV VEPNAGKPIV ENGKTVYPLK PHDFAVHIDS YYELGVNIFG GCCGTTPEHV KLFRKVLGNR KPLQRKKKRI FAVSSPSKLV TFDHFVVIGE RINPAGRKKL WAEMQKGNEE IVIKEAKTQV EKGAEVLDVN FGIESQIDVR YVEKIVQTLP YVSNVPLSLD IQNVDLTERA LRAYPGRSLF NSAKVDEEEL EMKINLLKKY GGTLIVLLMG KDVPKSFEER KEYFEKALKI LERHDFSDRV IFDPGVLPLG AEGKPVEVLK TIEFISSKGF NTTVGLSNLS FGLPDRSYYN TAFLVLGISK GLSSAIMNPL DETLMKTLNA TLVILEKKEL PRAEVKEEKL VEIILSGNRS ELEKLVEDFL KEKDPLSVIE EHLRPAMERI GELYDKGKIF LPQLILAAQT VKPVFDKLTS MLPSDSQGET FVIATVKGDV HDIGKNIVAS VIRSSGYRVV DLGKDVDTSE IVEAVEKERP VALGLSAMMT TTVGRIKEVV EKLKEKNLKI PVIVGGASLN EKLAKELGAD YYAKNASEAV KILKSLGR // ID Q9WYG2_THEMA Unreviewed; 327 AA. AC Q9WYG2; G4FHP0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 108. DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AGL49250.1}; DE EC=1.1.1.95 {ECO:0000313|EMBL:AGL49250.1}; DE SubName: Full=Phosphoglycerate dehydrogenase, putative {ECO:0000313|EMBL:AAD35414.1}; GN OrderedLocusNames=TM_0327 {ECO:0000313|EMBL:AAD35414.1}; GN ORFNames=Tmari_0325 {ECO:0000313|EMBL:AGL49250.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35414.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35414.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35414.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49250.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49250.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35414.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49250.1; -; Genomic_DNA. DR PIR; A72390; A72390. DR RefSeq; NP_228138.1; NC_000853.1. DR RefSeq; WP_004083086.1; NZ_CP011107.1. DR STRING; 243274.TM0327; -. DR EnsemblBacteria; AAD35414; AAD35414; TM_0327. DR EnsemblBacteria; AGL49250; AGL49250; Tmari_0325. DR GeneID; 897272; -. DR KEGG; tma:TM0327; -. DR KEGG; tmi:THEMA_03090; -. DR KEGG; tmm:Tmari_0325; -. DR KEGG; tmw:THMA_0334; -. DR PATRIC; 23935533; VBITheMar51294_0332. DR eggNOG; ENOG4108JQ1; Bacteria. DR eggNOG; COG0111; LUCA. DR KO; K00058; -. DR OMA; EPMEANH; -. DR OrthoDB; EOG6VXFC3; -. DR BioCyc; TMAR243274:GC6P-340-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0009070; P:serine family amino acid biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR029753; D-isomer_DH_CS. DR InterPro; IPR029752; D-isomer_DH_CS1. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003720, KW ECO:0000313|EMBL:AGL49250.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 13 311 2-Hacid_dh. {ECO:0000259|Pfam:PF00389}. FT DOMAIN 104 279 2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}. SQ SEQUENCE 327 AA; 36040 MW; 40683898A5732539 CRC64; MKKILIVTRT FGKYSQEPVE FLRKEGFEII RSDTIDPDIL KEVDALIVGT HPVTAEMVEN SSLKIIAKHG VGVDNIDLEA ATKKGIPVTI TAGANSLSVA ELTIAFIFAL SRGLVWAHNK LFLERRWEGT VGQEVSGKTL GVVGFGSIGR EVVKKAVCLG MNVLVYDPYV SKDSVRLLEA TPVDDLEQLL KESDFVSLHV PLNESTKNMI GERELSLMKK SAFLINTSRG ELVDEEALVK ALKEGRIAGA ALDVFSEEPP DANSPLFECP NLITTAHIGA HTKEAIFRMN MMAAQSIVDF FKGRIPRYVV NKEVIRILKE KGYQEIS // ID Q9X0I7_THEMA Unreviewed; 317 AA. AC Q9X0I7; G4FEP5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 103. DE SubName: Full=Oxygen-independent coproporphyrinogen III oxidase {ECO:0000313|EMBL:AGL50033.1}; DE EC=1.-.-.- {ECO:0000313|EMBL:AGL50033.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36179.1}; GN OrderedLocusNames=TM_1103 {ECO:0000313|EMBL:AAD36179.1}; GN ORFNames=Tmari_1109 {ECO:0000313|EMBL:AGL50033.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36179.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36179.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36179.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50033.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50033.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36179.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50033.1; -; Genomic_DNA. DR PIR; A72295; A72295. DR RefSeq; NP_228909.1; NC_000853.1. DR RefSeq; WP_004080334.1; NZ_CP011107.1. DR STRING; 243274.TM1103; -. DR DNASU; 898662; -. DR EnsemblBacteria; AAD36179; AAD36179; TM_1103. DR EnsemblBacteria; AGL50033; AGL50033; Tmari_1109. DR GeneID; 898662; -. DR KEGG; tma:TM1103; -. DR KEGG; tmi:THEMA_08830; -. DR KEGG; tmm:Tmari_1109; -. DR KEGG; tmw:THMA_1126; -. DR PATRIC; 23937139; VBITheMar51294_1118. DR eggNOG; ENOG4107S0U; Bacteria. DR eggNOG; COG1243; LUCA. DR OMA; LAGPFHP; -. DR OrthoDB; EOG6KWXVC; -. DR BioCyc; TMAR243274:GC6P-1132-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0033588; C:Elongator holoenzyme complex; IBA:GO_Central. DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0016573; P:histone acetylation; IBA:GOC. DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central. DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central. DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR032432; Radical_SAM_C. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF16199; Radical_SAM_C; 1. DR SMART; SM00729; Elp3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50033.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 214 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 317 AA; 36069 MW; 054B39C33D074B55 CRC64; MKIIPVFLPY AGCKKRCVFC DQIKATGQAK VPSLDDIARI IEEYSRTSNE YELGFYGGTF TGLSEEKMEE YLRFVKRFPV VKSVRVSTRP DEINERKLKI LKKYGVNVIE IGVQSFLDEV LERSKRGYTS EEAEGACKLI KKNGFVLSVH LMVGLPGSDR RGEILSALRT VECGADMVRI HPTLVFEGTE LHRMMEEGEY TPLNVEEAVD VCSDLVCIFE GWGTKVIRIG YHVPVELRKY VVAGPIDPSL GDRVRRTTMK KVIESLKPSR IVVPKNYLVW FEEAKVEVGD EFRFDDLSYA DALFFTGKEV VERWLNG // ID Q9WZ50_THEMA Unreviewed; 141 AA. AC Q9WZ50; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35666.1}; GN OrderedLocusNames=TM_0581 {ECO:0000313|EMBL:AAD35666.1}; GN ORFNames=Tmari_0579 {ECO:0000313|EMBL:AGL49504.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35666.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35666.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35666.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49504.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49504.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35666.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49504.1; -; Genomic_DNA. DR PIR; F72358; F72358. DR RefSeq; NP_228391.1; NC_000853.1. DR RefSeq; WP_010865152.1; NZ_CP011107.1. DR PDB; 2Q78; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-141. DR PDBsum; 2Q78; -. DR STRING; 243274.TM0581; -. DR EnsemblBacteria; AAD35666; AAD35666; TM_0581. DR EnsemblBacteria; AGL49504; AGL49504; Tmari_0579. DR GeneID; 897651; -. DR KEGG; tma:TM0581; -. DR KEGG; tmi:THEMA_01760; -. DR KEGG; tmm:Tmari_0579; -. DR KEGG; tmw:THMA_0596; -. DR PATRIC; 23936073; VBITheMar51294_0590. DR eggNOG; ENOG410663D; Bacteria. DR eggNOG; COG5496; LUCA. DR OMA; IVMSGDE; -. DR BioCyc; TMAR243274:GC6P-606-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.10.129.10; -; 1. DR InterPro; IPR029069; HotDog_dom. DR SUPFAM; SSF54637; SSF54637; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2Q78}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 141 AA; 15868 MW; 7782CA9AC9F408F8 CRC64; MMDFDFLEGK RLTEDVALDE TMVWNEDIEM LDLHLVATSA LIGVVHRVSY ELLSRYLPND YTAVVVETLA RHVKAVPTGT RVAVGVRVVG VVGNRVKFRG IVMSGDEKIL EAEFVRAIVP REKLRRLALE KAEKTSRLFG I // ID Q9WZB9_THEMA Unreviewed; 268 AA. AC Q9WZB9; G4FDH3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 97. DE SubName: Full=Hydrolase (HAD superfamily) {ECO:0000313|EMBL:AGL49576.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35735.1}; GN OrderedLocusNames=TM_0651 {ECO:0000313|EMBL:AAD35735.1}; GN ORFNames=Tmari_0651 {ECO:0000313|EMBL:AGL49576.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35735.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35735.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35735.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49576.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49576.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35735.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49576.1; -; Genomic_DNA. DR PIR; B72352; B72352. DR RefSeq; NP_228460.1; NC_000853.1. DR RefSeq; WP_004081144.1; NZ_CP011107.1. DR PDB; 1NF2; X-ray; 2.20 A; A/B/C=1-268. DR PDBsum; 1NF2; -. DR STRING; 243274.TM0651; -. DR EnsemblBacteria; AAD35735; AAD35735; TM_0651. DR EnsemblBacteria; AGL49576; AGL49576; Tmari_0651. DR GeneID; 897756; -. DR KEGG; tma:TM0651; -. DR KEGG; tmi:THEMA_01410; -. DR KEGG; tmm:Tmari_0651; -. DR KEGG; tmw:THMA_0666; -. DR PATRIC; 23936216; VBITheMar51294_0661. DR eggNOG; ENOG41081ZY; Bacteria. DR eggNOG; COG0561; LUCA. DR KO; K07024; -. DR OMA; GDPAYMQ; -. DR OrthoDB; EOG6RZB77; -. DR BioCyc; TMAR243274:GC6P-676-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IBA:GOC. DR GO; GO:0044283; P:small molecule biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR000150; Hypothet_cof. DR Pfam; PF08282; Hydrolase_3; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00099; Cof-subfamily; 1. DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1. DR PROSITE; PS01228; COF_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1NF2}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49576.1}; KW Magnesium {ECO:0000213|PDB:1NF2}; KW Metal-binding {ECO:0000213|PDB:1NF2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 258 HAD-like_dom. {ECO:0000259|Pfam:PF08282}. FT METAL 8 8 Magnesium. {ECO:0000213|PDB:1NF2}. FT METAL 10 10 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:1NF2}. FT METAL 214 214 Magnesium. {ECO:0000213|PDB:1NF2}. FT METAL 215 215 Magnesium. {ECO:0000213|PDB:1NF2}. FT DISULFID 35 265 {ECO:0000213|PDB:1NF2}. SQ SEQUENCE 268 AA; 31187 MW; 02BB5753D5D46EED CRC64; MYRVFVFDLD GTLLNDNLEI SEKDRRNIEK LSRKCYVVFA SGRMLVSTLN VEKKYFKRTF PTIAYNGAIV YLPEEGVILN EKIPPEVAKD IIEYIKPLNV HWQAYIDDVL YSEKDNEEIK SYARHSNVDY RVEPNLSELV SKMGTTKLLL IDTPERLDEL KEILSERFKD VVKVFKSFPT YLEIVPKNVD KGKALRFLRE RMNWKKEEIV VFGDNENDLF MFEEAGLRVA MENAIEKVKE ASDIVTLTNN DSGVSYVLER ISTDCLDE // ID Q9X1T1_THEMA Unreviewed; 333 AA. AC Q9X1T1; G4FFY3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=3-to-5 oligoribonuclease A {ECO:0000313|EMBL:AGL50527.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36662.1}; GN OrderedLocusNames=TM_1595 {ECO:0000313|EMBL:AAD36662.1}; GN ORFNames=Tmari_1603 {ECO:0000313|EMBL:AGL50527.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36662.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36662.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36662.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50527.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50527.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36662.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50527.1; -; Genomic_DNA. DR PIR; G72233; G72233. DR RefSeq; NP_229395.1; NC_000853.1. DR RefSeq; WP_004082036.1; NZ_CP011107.1. DR STRING; 243274.TM1595; -. DR EnsemblBacteria; AAD36662; AAD36662; TM_1595. DR EnsemblBacteria; AGL50527; AGL50527; Tmari_1603. DR GeneID; 897398; -. DR KEGG; tma:TM1595; -. DR KEGG; tmi:THEMA_06275; -. DR KEGG; tmm:Tmari_1603; -. DR KEGG; tmw:THMA_1635; -. DR PATRIC; 23938164; VBITheMar51294_1614. DR eggNOG; ENOG4105SFS; Bacteria. DR eggNOG; COG0618; LUCA. DR KO; K06881; -. DR OMA; DTHPFGW; -. DR OrthoDB; EOG6FBX0G; -. DR BioCyc; TMAR243274:GC6P-1641-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR003156; DHHA1_dom. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02272; DHHA1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 13 151 DHH. {ECO:0000259|Pfam:PF01368}. FT DOMAIN 250 306 DHHA1. {ECO:0000259|Pfam:PF02272}. SQ SEQUENCE 333 AA; 37478 MW; DEADBB206DD57809 CRC64; MDEIVKVLSQ HDRILVVGHI MPDGDCVSSV LSLTLGLEKL GKEVKAAVDY KIPYVFEKFP YIDKIEENPN FDPELLVVVD ASSPDRIGKF QDLLDKVPSV VIDHHSTNTN FGNWNWVDPS FAATAQMIFR INKALGVEYD SNLATLNYLG IATDTGFFRH SNADVRVFED AYKLVKMGAD AHFVAKEILE NKRFEQFKLF AEVLERLQLL ENGKIAYSYI DYDTYLRHNC TDEDSAGFVG ELRSIRGVEV AVLFMEFPRG KIHVSMRSKD WFNVNEVAFE LGGGGHPRAA GVTFEGKKIE EVIPRVINHL LKKFKEGVES ESEKIPEGDV LGG // ID Q9WZ86_THEMA Unreviewed; 30 AA. AC Q9WZ86; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35702.1}; GN OrderedLocusNames=TM_0617 {ECO:0000313|EMBL:AAD35702.1}; GN ORFNames=Tmari_0617 {ECO:0000313|EMBL:AGL49542.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35702.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35702.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35702.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49542.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49542.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35702.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49542.1; -; Genomic_DNA. DR PIR; E72356; E72356. DR RefSeq; NP_228427.1; NC_000853.1. DR RefSeq; WP_010865166.1; NZ_CP011107.1. DR EnsemblBacteria; AAD35702; AAD35702; TM_0617. DR EnsemblBacteria; AGL49542; AGL49542; Tmari_0617. DR GeneID; 897703; -. DR KEGG; tma:TM0617; -. DR KEGG; tmi:THEMA_01580; -. DR KEGG; tmm:Tmari_0617; -. DR KEGG; tmw:THMA_0633; -. DR KO; K07076; -. DR OrthoDB; EOG62ZJ58; -. DR BioCyc; TMAR243274:GC6P-642-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 30 AA; 3451 MW; 1B35D98427C4B639 CRC64; MVLFASHAKR KITAFSDIDL LVVYDDPTQR // ID Q9X0S1_THEMA Unreviewed; 718 AA. AC Q9X0S1; G4FEF7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Phage T7 exclusion protein {ECO:0000313|EMBL:AGL50120.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36264.1}; GN OrderedLocusNames=TM_1189 {ECO:0000313|EMBL:AAD36264.1}; GN ORFNames=Tmari_1196 {ECO:0000313|EMBL:AGL50120.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36264.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36264.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36264.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50120.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50120.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36264.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50120.1; -; Genomic_DNA. DR PIR; C72285; C72285. DR RefSeq; NP_228994.1; NC_000853.1. DR RefSeq; WP_004080141.1; NZ_CP011107.1. DR EnsemblBacteria; AAD36264; AAD36264; TM_1189. DR EnsemblBacteria; AGL50120; AGL50120; Tmari_1196. DR GeneID; 898295; -. DR KEGG; tma:TM1189; -. DR KEGG; tmi:THEMA_08385; -. DR KEGG; tmm:Tmari_1196; -. DR KEGG; tmw:THMA_1215; -. DR PATRIC; 23937320; VBITheMar51294_1207. DR eggNOG; ENOG4107UM5; Bacteria. DR eggNOG; COG4928; LUCA. DR OMA; NPWWFSG; -. DR OrthoDB; EOG6HXJ1B; -. DR BioCyc; TMAR243274:GC6P-1219-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011646; KAP_P-loop. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF07693; KAP_NTPase; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 23 293 KAP NTPase. {ECO:0000259|Pfam:PF07693}. SQ SEQUENCE 718 AA; 84737 MW; 7DC6636EBC3CBC9E CRC64; MTEKKIILAD EPLKSPDQDK LGFAPFAKRI ATVIQSVQLR ESIVFAVYGK WGSGKTTFIN FLTSYLNHDS SITIVKFDPW WFSEKEDLIR QFLSNLQFTL NKSTKFKDIA KMLKPYIETL GEIPKFGWIF KIASRFKKNL QKSVIETKEE IINRLKEKDG KIVVIIDDID RLTAKEIREL FTIVKAIADF PNTVYILAFD KDIVIRALEK VQEGKGEDYL EKIIQIPIEL PLADKTSIRK MLFEELDAVL SGTSNELFDS TYWRNVYWDG IDPFINTVRN VKRLINTIRV TYPSVKNEVN AVDFIAIETL RVFCPEVYSI VKDYPDMFCG YSGEIYDVSR RHIEFLKQFH QNWLSRLNFP DDLKENIKNL LKRLFPKFES VFENIYYGPD WEREWRKKYR ICCKEIFPRF FIFSVPSDDL SKHEMDFILS SLHNKEALIE HLKRLATQIR SDGSTRLSIF LERMEDYASE ISQDYIPVVI EVFFTIGDKL IIPEDENKSF LIPWGNDIRM ERIIWRLLRR YDNNSKRFEV LKNAFKNGQA LFMMVNVLIL FWQQHRKYRD AKESDAILLD ENHLKTLQEI VLDKIRKAVE EGSLLNTPSL PVILHQWREW ANEDEVKEWV KEIVFSDEKL PIFLTKFLQK TVSWTETSRA TNIYWQIDLN WLKDFINLDF LEKRCNEILS NDSIIGTLED KQKLAIRLFL NEKTKSLDSS TEEQGKDG // ID Q9WYX9_THEMA Unreviewed; 309 AA. AC Q9WYX9; G4FDW2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 107. DE SubName: Full=UDP-glucose 4-epimerase {ECO:0000313|EMBL:AGL49430.1}; DE EC=5.1.3.2 {ECO:0000313|EMBL:AGL49430.1}; DE SubName: Full=UDP-glucose 4-epimerase, putative {ECO:0000313|EMBL:AAD35594.1}; GN OrderedLocusNames=TM_0509 {ECO:0000313|EMBL:AAD35594.1}; GN ORFNames=Tmari_0505 {ECO:0000313|EMBL:AGL49430.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35594.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35594.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35594.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49430.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49430.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35594.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49430.1; -; Genomic_DNA. DR PIR; C72368; C72368. DR RefSeq; NP_228319.1; NC_000853.1. DR RefSeq; WP_004081431.1; NZ_CP011107.1. DR PDB; 4ZRM; X-ray; 1.90 A; A/B=1-309. DR PDB; 4ZRN; X-ray; 2.00 A; A/B=1-309. DR PDBsum; 4ZRM; -. DR PDBsum; 4ZRN; -. DR STRING; 243274.TM0509; -. DR EnsemblBacteria; AAD35594; AAD35594; TM_0509. DR EnsemblBacteria; AGL49430; AGL49430; Tmari_0505. DR GeneID; 897553; -. DR KEGG; tma:TM0509; -. DR KEGG; tmi:THEMA_02130; -. DR KEGG; tmm:Tmari_0505; -. DR KEGG; tmw:THMA_0521; -. DR PATRIC; 23935923; VBITheMar51294_0516. DR eggNOG; ENOG4108IAJ; Bacteria. DR eggNOG; COG0451; LUCA. DR KO; K01784; -. DR OMA; ECSHIAP; -. DR OrthoDB; EOG69GZPD; -. DR BioCyc; TMAR243274:GC6P-533-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR008089; Nuc_sugar_epim. DR Pfam; PF01370; Epimerase; 1. DR PRINTS; PR01713; NUCEPIMERASE. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4ZRM, ECO:0000213|PDB:4ZRN}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000313|EMBL:AGL49430.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 237 Epimerase. {ECO:0000259|Pfam:PF01370}. SQ SEQUENCE 309 AA; 34900 MW; 0200114370F1D001 CRC64; MNILVTGGAG FIGSHVVDKL IENGYGVIVV DNLSSGKVEN LNRNALFYEQ SIEDEEMMER IFSLHRPEYV FHLAAQASVA ISVREPARDA KTNIIGSLVL LEKSIKYGVK KFIFSSTGGA IYGENVKVFP TPETEIPHPI SPYGIAKYST EMYLEFFARE YGLKYTVLRY ANVYGPRQDP YGEAGVVAIF TERMLRGEEV HIFGDGEYVR DYVYVDDVVR ANLLAMEKGD NEVFNIGTGR GTTVNQLFKL LKEITGYDKE PVYKPPRKGD VRKSILDYTK AKEKLGWEPK VSLEEGLKLT VEYFRKTLE // ID Q9X0G9_THEMA Unreviewed; 143 AA. AC Q9X0G9; G4FER8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Ribose 5-phosphate isomerase B {ECO:0000313|EMBL:AGL50008.1}; DE EC=5.3.1.6 {ECO:0000313|EMBL:AGL50008.1}; DE SubName: Full=Sugar-phosphate isomerase {ECO:0000313|EMBL:AAD36157.1}; GN OrderedLocusNames=TM_1080 {ECO:0000313|EMBL:AAD36157.1}; GN ORFNames=Tmari_1084 {ECO:0000313|EMBL:AGL50008.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36157.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36157.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36157.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50008.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50008.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36157.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50008.1; -; Genomic_DNA. DR PIR; H72296; H72296. DR RefSeq; NP_228886.1; NC_000853.1. DR RefSeq; WP_004080405.1; NZ_CP011107.1. DR PDB; 1O1X; X-ray; 1.90 A; A=2-143. DR PDBsum; 1O1X; -. DR STRING; 243274.TM1080; -. DR EnsemblBacteria; AAD36157; AAD36157; TM_1080. DR EnsemblBacteria; AGL50008; AGL50008; Tmari_1084. DR GeneID; 897426; -. DR KEGG; tma:TM1080; -. DR KEGG; tmi:THEMA_08955; -. DR KEGG; tmm:Tmari_1084; -. DR KEGG; tmw:THMA_1102; -. DR PATRIC; 23937089; VBITheMar51294_1093. DR eggNOG; ENOG4108YZG; Bacteria. DR eggNOG; COG0698; LUCA. DR KO; K01808; -. DR OMA; DYPDFVH; -. DR OrthoDB; EOG679TJ4; -. DR BioCyc; TMAR243274:GC6P-1109-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro. DR Gene3D; 3.40.1400.10; -; 1. DR InterPro; IPR004785; RpiB. DR InterPro; IPR003500; RpiB_LacA_LacB. DR PANTHER; PTHR30345; PTHR30345; 1. DR Pfam; PF02502; LacAB_rpiB; 1. DR PIRSF; PIRSF005384; RpiB_LacA_B; 1. DR SUPFAM; SSF89623; SSF89623; 1. DR TIGRFAMs; TIGR01120; rpiB; 1. DR TIGRFAMs; TIGR00689; rpiB_lacA_lacB; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O1X}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000313|EMBL:AAD36157.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT ACT_SITE 65 65 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR005384-1}. FT ACT_SITE 98 98 Proton donor. FT {ECO:0000256|PIRSR:PIRSR005384-1}. SQ SEQUENCE 143 AA; 15867 MW; 3E17D72A10FFCCBD CRC64; MKIAIASDHA AFELKEKVKN YLLGKGIEVE DHGTYSEESV DYPDYAKKVV QSILSNEADF GILLCGTGLG MSIAANRYRG IRAALCLFPD MARLARSHNN ANILVLPGRL IGAELAFWIV DTFLSTPFDG GRHERRIRKI DEV // ID Q9X236_THEMA Unreviewed; 88 AA. AC Q9X236; G4FG98; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36777.1}; GN OrderedLocusNames=TM_1711 {ECO:0000313|EMBL:AAD36777.1}; GN ORFNames=Tmari_1719 {ECO:0000313|EMBL:AGL50643.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36777.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36777.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36777.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50643.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50643.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36777.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50643.1; -; Genomic_DNA. DR PIR; H72221; H72221. DR RefSeq; NP_229510.1; NC_000853.1. DR RefSeq; WP_004082227.1; NZ_CP011107.1. DR STRING; 243274.TM1711; -. DR EnsemblBacteria; AAD36777; AAD36777; TM_1711. DR EnsemblBacteria; AGL50643; AGL50643; Tmari_1719. DR GeneID; 897883; -. DR KEGG; tma:TM1711; -. DR KEGG; tmi:THEMA_05685; -. DR KEGG; tmm:Tmari_1719; -. DR KEGG; tmw:THMA_1753; -. DR PATRIC; 23938398; VBITheMar51294_1729. DR OMA; REGDQEP; -. DR OrthoDB; EOG6GJBXH; -. DR BioCyc; TMAR243274:GC6P-1759-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 56 83 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 88 AA; 10370 MW; 266C73A075E617B8 CRC64; MKKKISVRLG KKVYNLVTDE DLEIVNQTIE KIEKDFKRYE EFIDEVGIDN ILFVMLANTV LENVKMSERI RNLKKKLSQA LREGDQEP // ID Q9WYQ3_THEMA Unreviewed; 304 AA. AC Q9WYQ3; G4FHY1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35507.1}; GN OrderedLocusNames=TM_0422 {ECO:0000313|EMBL:AAD35507.1}; GN ORFNames=Tmari_0419 {ECO:0000313|EMBL:AGL49344.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35507.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35507.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35507.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49344.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49344.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35507.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49344.1; -; Genomic_DNA. DR PIR; F72378; F72378. DR RefSeq; NP_228232.1; NC_000853.1. DR RefSeq; WP_004083281.1; NZ_CP011107.1. DR STRING; 243274.TM0422; -. DR EnsemblBacteria; AAD35507; AAD35507; TM_0422. DR EnsemblBacteria; AGL49344; AGL49344; Tmari_0419. DR GeneID; 897427; -. DR KEGG; tma:TM0422; -. DR KEGG; tmi:THEMA_02615; -. DR KEGG; tmm:Tmari_0419; -. DR KEGG; tmw:THMA_0428; -. DR PATRIC; 23935727; VBITheMar51294_0427. DR eggNOG; ENOG4108WD7; Bacteria. DR eggNOG; COG1082; LUCA. DR OMA; VAHAFLS; -. DR OrthoDB; EOG61KBFT; -. DR BioCyc; TMAR243274:GC6P-437-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF01261; AP_endonuc_2; 1. DR SUPFAM; SSF51658; SSF51658; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 26 245 AP_endonuc_2. {ECO:0000259|Pfam:PF01261}. SQ SEQUENCE 304 AA; 34613 MW; 29AF39EEF1347446 CRC64; MIKGIGTNVD TRRVNGSIKR LVSELEFFKS IGFDYVEIPA AGLDVIARGR IIRKRLERVK ELLSNYNFRY TVHAPDVINL KIKTNPWHYR VMEATIEFAG EINAEVVVYH YGEVDHSIDV PERVQRKAEI VALRELADLA KEKGVVIGVE NVGHPVSEVL KLVRAVNHPN VKLVIDVGHL FIVSNYTGID FYDELKKGLP YAVELHLSDN FGESPQTYQK IPDVEAFRFV YGIGDLHLPI GEGDIPYNKV FRIIRESGFD GIVILEINSM DRFADEYADS LNLLRKRLIL AADNNKTKKR RKVK // ID Q9X0Y9_THEMA Unreviewed; 276 AA. AC Q9X0Y9; G4FE86; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=Phosphate transport system permease protein PstA {ECO:0000256|RuleBase:RU363043}; GN OrderedLocusNames=TM_1262 {ECO:0000313|EMBL:AAD36336.1}; GN ORFNames=Tmari_1267 {ECO:0000313|EMBL:AGL50191.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36336.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36336.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36336.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50191.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50191.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363043}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363043}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. CysTW subfamily. CC {ECO:0000256|RuleBase:RU363043}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363043}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36336.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50191.1; -; Genomic_DNA. DR PIR; A72276; A72276. DR RefSeq; NP_229067.1; NC_000853.1. DR RefSeq; WP_004079997.1; NZ_CP011107.1. DR STRING; 243274.TM1262; -. DR DNASU; 898221; -. DR EnsemblBacteria; AAD36336; AAD36336; TM_1262. DR EnsemblBacteria; AGL50191; AGL50191; Tmari_1267. DR GeneID; 898221; -. DR KEGG; tma:TM1262; -. DR KEGG; tmi:THEMA_08025; -. DR KEGG; tmm:Tmari_1267; -. DR KEGG; tmw:THMA_1287; -. DR PATRIC; 23937464; VBITheMar51294_1278. DR eggNOG; ENOG4105E2Z; Bacteria. DR eggNOG; COG0581; LUCA. DR KO; K02038; -. DR OMA; YHVYVLA; -. DR OrthoDB; EOG6TJ81W; -. DR BioCyc; TMAR243274:GC6P-1293-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR005672; Phosphate_PstA. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR00974; 3a0107s02c; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU363043}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363043, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363043, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363043, KW ECO:0000256|SAAS:SAAS00524216}. FT TRANSMEM 9 34 Helical. {ECO:0000256|RuleBase:RU363043}. FT TRANSMEM 54 84 Helical. {ECO:0000256|RuleBase:RU363043}. FT TRANSMEM 96 119 Helical. {ECO:0000256|RuleBase:RU363043}. FT TRANSMEM 125 145 Helical. {ECO:0000256|RuleBase:RU363043}. FT TRANSMEM 220 238 Helical. {ECO:0000256|RuleBase:RU363043}. FT TRANSMEM 244 267 Helical. {ECO:0000256|RuleBase:RU363043}. FT DOMAIN 59 265 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 276 AA; 29618 MW; A6D8568F17A0D788 CRC64; MRKDLIASYV FRAVSYVAFA VVVIMFVLVL AGGVKYFSPS FFLDYPKNGM TEGGIFPAIL GSFYLMVLTF LISIPLGIFT GVFLSEYGNN VIAKWIDISL TALSGIPSVV YGLFGLAFFC VALQFGTSML AAALTLSLMT LPVIASSTRE TLKAIPVEIR EAALALGATK EEVIFKVLLP AARKGIITAV LVGGGRALGE TAPVLLTGAV FYSTQLPKSL LSPVMTLPTH IYYITAAYGE SAQWMAKGTA AFLMIVVALI YGTAFFLRRR KNGAHH // ID Q9X0G7_THEMA Unreviewed; 170 AA. AC Q9X0G7; G4FES0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36155.1}; GN OrderedLocusNames=TM_1078 {ECO:0000313|EMBL:AAD36155.1}; GN ORFNames=Tmari_1082 {ECO:0000313|EMBL:AGL50006.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36155.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36155.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36155.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50006.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50006.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36155.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50006.1; -; Genomic_DNA. DR PIR; F72296; F72296. DR RefSeq; NP_228884.1; NC_000853.1. DR RefSeq; WP_004080407.1; NZ_CP011107.1. DR STRING; 243274.TM1078; -. DR EnsemblBacteria; AAD36155; AAD36155; TM_1078. DR EnsemblBacteria; AGL50006; AGL50006; Tmari_1082. DR GeneID; 897060; -. DR KEGG; tma:TM1078; -. DR KEGG; tmi:THEMA_08965; -. DR KEGG; tmm:Tmari_1082; -. DR KEGG; tmw:THMA_1100; -. DR PATRIC; 23937085; VBITheMar51294_1091. DR eggNOG; ENOG4108UP4; Bacteria. DR eggNOG; COG1507; LUCA. DR KO; K09009; -. DR OMA; VAFREKM; -. DR OrthoDB; EOG6R87MJ; -. DR BioCyc; TMAR243274:GC6P-1107-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR007511; DUF501. DR Pfam; PF04417; DUF501; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 170 AA; 19882 MW; DC7487719DB03D41 CRC64; MGDPRDEKIV GWQLGRKITN MRRVVFRCPY GYPVVIESFP IKDGKPFPTL YWLTCPHLRK EVSKLESQGY VKEFEEKLER EGKLREKMKK AHVEIIKKRA ELLPEDHPFR EILSKVGTGG IRDFTKLKCL HLHLADYLAG VKNPVGEMVW DLVERKFCEE KLCRAGEARE // ID Q9X1C3_THEMA Unreviewed; 327 AA. AC Q9X1C3; G4FFD9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 125. DE SubName: Full=ABC-type multidrug transport system, ATPase component {ECO:0000313|EMBL:AGL50334.1}; DE SubName: Full=Antibiotic ABC transporter, ATP-binding protein, putative {ECO:0000313|EMBL:AAD36474.1}; GN OrderedLocusNames=TM_1403 {ECO:0000313|EMBL:AAD36474.1}; GN ORFNames=Tmari_1410 {ECO:0000313|EMBL:AGL50334.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36474.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36474.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36474.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50334.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50334.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36474.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50334.1; -; Genomic_DNA. DR PIR; D72257; D72257. DR RefSeq; NP_229204.1; NC_000853.1. DR RefSeq; WP_004081632.1; NZ_CP011107.1. DR PDB; 4YER; X-ray; 2.35 A; A/B=1-327. DR PDBsum; 4YER; -. DR STRING; 243274.TM1403; -. DR EnsemblBacteria; AAD36474; AAD36474; TM_1403. DR EnsemblBacteria; AGL50334; AGL50334; Tmari_1410. DR GeneID; 898073; -. DR KEGG; tma:TM1403; -. DR KEGG; tmi:THEMA_07300; -. DR KEGG; tmm:Tmari_1410; -. DR KEGG; tmw:THMA_1432; -. DR PATRIC; 23937752; VBITheMar51294_1415. DR eggNOG; ENOG4105CJ1; Bacteria. DR eggNOG; COG1131; LUCA. DR KO; K01990; -. DR OMA; REEGPEN; -. DR OrthoDB; EOG65J54C; -. DR BioCyc; TMAR243274:GC6P-1440-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0043215; P:daunorubicin transport; IEA:InterPro. DR GO; GO:1900753; P:doxorubicin transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR005894; DrrA. DR InterPro; IPR025302; DUF4162. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF13732; DUF4162; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01188; drrA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4YER}; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD36474.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD36474.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 236 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT NP_BIND 40 45 ADP. {ECO:0000213|PDB:4YER}. FT NP_BIND 134 137 ADP. {ECO:0000213|PDB:4YER}. FT BINDING 14 14 ADP. {ECO:0000213|PDB:4YER}. SQ SEQUENCE 327 AA; 37564 MW; 5C933F7D019FBA86 CRC64; MEDIIVVENL VKKFGDFEAV KGVSFSVKKG EIFAFLGPNG AGKTTTIHML TTLLKPTSGK AWVAGHDVLK EPREVRRKIG IVFQDQSLDR ELTAYENMYI HGKIYGYGGE KLKKRILELL EFVELLEFKD KPVKTFSGGM ARRLEIARSL IHEPEVLFLD EPTIGLDPHT RAHMWEYISK MKKEHNMTIF LTTHYMDEAE QLADRVAIID HGKIIALGTP TELKRMVGKE IIYVRFSEAV ECLEGDFIES CRKLPDGRLE LNVEDSGRAI PKIFELAQQK GLKIEEITYH KPTLNDVFLH LTGRELREEG PENSFKTMAR MRMRMRR // ID Q9WZC7_THEMA Unreviewed; 53 AA. AC Q9WZC7; G4FDG5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 104. DE RecName: Full=Rubredoxin {ECO:0000256|PIRNR:PIRNR000071}; GN OrderedLocusNames=TM_0659 {ECO:0000313|EMBL:AAD35743.1}; GN ORFNames=Tmari_0659 {ECO:0000313|EMBL:AGL49584.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35743.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35743.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35743.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49584.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49584.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; CC Evidence={ECO:0000256|PIRNR:PIRNR000071, CC ECO:0000256|PIRSR:PIRSR000071-1}; CC Note=Binds 1 Fe(3+) ion per subunit. CC {ECO:0000256|PIRNR:PIRNR000071, ECO:0000256|PIRSR:PIRSR000071-1}; CC -!- SIMILARITY: Belongs to the rubredoxin family. CC {ECO:0000256|PIRNR:PIRNR000071}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35743.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49584.1; -; Genomic_DNA. DR PIR; H72348; H72348. DR RefSeq; NP_228468.1; NC_000853.1. DR RefSeq; WP_004081114.1; NZ_CP011107.1. DR SMR; Q9WZC7; 1-53. DR STRING; 243274.TM0659; -. DR EnsemblBacteria; AAD35743; AAD35743; TM_0659. DR EnsemblBacteria; AGL49584; AGL49584; Tmari_0659. DR GeneID; 897770; -. DR KEGG; tma:TM0659; -. DR KEGG; tmi:THEMA_01370; -. DR KEGG; tmm:Tmari_0659; -. DR KEGG; tmw:THMA_0674; -. DR PATRIC; 23936232; VBITheMar51294_0669. DR eggNOG; ENOG4105VCQ; Bacteria. DR eggNOG; COG1773; LUCA. DR OMA; SKDMFEP; -. DR OrthoDB; EOG69SKK0; -. DR BioCyc; TMAR243274:GC6P-684-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR Gene3D; 2.20.28.10; -; 1. DR InterPro; IPR024922; Rubredoxin. DR InterPro; IPR024934; Rubredoxin-like_dom. DR InterPro; IPR004039; Rubredoxin-type_fold. DR InterPro; IPR024935; Rubredoxin_dom. DR InterPro; IPR018527; Rubredoxin_Fe_BS. DR Pfam; PF00301; Rubredoxin; 1. DR PIRSF; PIRSF000071; Rubredoxin; 1. DR PRINTS; PR00163; RUBREDOXIN. DR PROSITE; PS00202; RUBREDOXIN; 1. DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Electron transport {ECO:0000256|PIRNR:PIRNR000071, KW ECO:0000256|SAAS:SAAS00496620}; KW Iron {ECO:0000256|PIRNR:PIRNR000071, ECO:0000256|PIRSR:PIRSR000071-1, KW ECO:0000256|SAAS:SAAS00496614}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000071, KW ECO:0000256|PIRSR:PIRSR000071-1, ECO:0000256|SAAS:SAAS00496609}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|PIRNR:PIRNR000071, KW ECO:0000256|SAAS:SAAS00496620}. FT DOMAIN 1 52 Rubredoxin-like. FT {ECO:0000259|PROSITE:PS50903}. FT METAL 6 6 Iron. {ECO:0000256|PIRSR:PIRSR000071-1}. FT METAL 9 9 Iron. {ECO:0000256|PIRSR:PIRSR000071-1}. FT METAL 39 39 Iron. {ECO:0000256|PIRSR:PIRSR000071-1}. FT METAL 42 42 Iron. {ECO:0000256|PIRSR:PIRSR000071-1}. SQ SEQUENCE 53 AA; 5985 MW; C96ED64F90F81941 CRC64; MKKYRCKLCG YIYDPEQGDP DSGIEPGTPF EDLPDDWVCP LCGASKEDFE PVE // ID Q9X1P4_THEMA Unreviewed; 182 AA. AC Q9X1P4; G4FFU6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=HDIG domain protein {ECO:0000313|EMBL:AGL50490.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36624.1}; GN OrderedLocusNames=TM_1558 {ECO:0000313|EMBL:AAD36624.1}; GN ORFNames=Tmari_1566 {ECO:0000313|EMBL:AGL50490.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36624.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36624.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36624.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50490.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50490.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36624.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50490.1; -; Genomic_DNA. DR PIR; A72240; A72240. DR RefSeq; NP_229358.1; NC_000853.1. DR RefSeq; WP_004081962.1; NZ_CP011107.1. DR STRING; 243274.TM1558; -. DR EnsemblBacteria; AAD36624; AAD36624; TM_1558. DR EnsemblBacteria; AGL50490; AGL50490; Tmari_1566. DR GeneID; 897967; -. DR KEGG; tma:TM1558; -. DR KEGG; tmi:THEMA_06490; -. DR KEGG; tmm:Tmari_1566; -. DR KEGG; tmw:THMA_1593; -. DR PATRIC; 23938078; VBITheMar51294_1576. DR eggNOG; ENOG4108UNR; Bacteria. DR eggNOG; COG2316; LUCA. DR KO; K06951; -. DR OMA; FKEKSFA; -. DR OrthoDB; EOG6038WN; -. DR BioCyc; TMAR243274:GC6P-1599-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR006675; HDIG_dom. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00277; HDIG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 16 122 HDc. {ECO:0000259|SMART:SM00471}. SQ SEQUENCE 182 AA; 20704 MW; D12C4E5DFDF81300 CRC64; MISRERAMEL LKTHVKTKNL VKHCLAAEAV MRALAREFNE DEEKWGLAGL LHDLDYDYTK DKPEEHGLKT LEILKDEDVP EDVLNAILAH CEKKTPETLM EKALYAVDPT TGFIVAAALI RPEKKLDVID VDFLLRRFKE KAFAKGASRE QMRTCENFGL SLEKFLEISL EAMKTIASEL GL // ID Q9WYL7_THEMA Unreviewed; 321 AA. AC Q9WYL7; G4FHU7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=Bacterioferritin comigratory protein/NADH dehydrogenase {ECO:0000313|EMBL:AAD35471.1}; DE SubName: Full=Nitroreductase {ECO:0000313|EMBL:AGL49309.1}; GN OrderedLocusNames=TM_0386 {ECO:0000313|EMBL:AAD35471.1}; GN ORFNames=Tmari_0384 {ECO:0000313|EMBL:AGL49309.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35471.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35471.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35471.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49309.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49309.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35471.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49309.1; -; Genomic_DNA. DR PIR; B72384; B72384. DR RefSeq; NP_228196.1; NC_000853.1. DR RefSeq; WP_004083209.1; NZ_CP011107.1. DR PDB; 4EO3; X-ray; 1.65 A; A/B=2-321. DR PDBsum; 4EO3; -. DR STRING; 243274.TM0386; -. DR EnsemblBacteria; AAD35471; AAD35471; TM_0386. DR EnsemblBacteria; AGL49309; AGL49309; Tmari_0384. DR GeneID; 897363; -. DR KEGG; tma:TM0386; -. DR KEGG; tmi:THEMA_02790; -. DR KEGG; tmm:Tmari_0384; -. DR KEGG; tmw:THMA_0393; -. DR PATRIC; 23935655; VBITheMar51294_0392. DR eggNOG; ENOG4108E2E; Bacteria. DR eggNOG; COG0778; LUCA. DR eggNOG; COG1225; LUCA. DR OMA; RIRREWI; -. DR OrthoDB; EOG6ZH2P1; -. DR BioCyc; TMAR243274:GC6P-400-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.109.10; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR029479; Nitroreductase. DR InterPro; IPR000415; Nitroreductase-like. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00578; AhpC-TSA; 1. DR Pfam; PF00881; Nitroreductase; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF55469; SSF55469; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4EO3}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flavoprotein {ECO:0000213|PDB:4EO3}; FMN {ECO:0000213|PDB:4EO3}; KW Nucleotide-binding {ECO:0000213|PDB:4EO3}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 138 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. FT NP_BIND 150 154 FMN. {ECO:0000213|PDB:4EO3}. FT NP_BIND 259 263 FMN. {ECO:0000213|PDB:4EO3}. FT NP_BIND 308 310 FMN. {ECO:0000213|PDB:4EO3}. FT BINDING 178 178 FMN. {ECO:0000213|PDB:4EO3}. FT BINDING 207 207 FMN. {ECO:0000213|PDB:4EO3}. FT DISULFID 179 227 {ECO:0000213|PDB:4EO3}. SQ SEQUENCE 321 AA; 37186 MW; FC8DB0ACED0387A0 CRC64; MRVKHFELLT DEGKTFTHVD LYGKYTILFF FPKAGTSGCT REAVEFSREN FEKAQVVGIS RDSVEALKRF KEKNDLKVTL LSDPEGILHE FFNVLENGKT VRSTFLIDRW GFVRKEWRRV KVEGHVQEVK EALDRLIEED LSLNKHIEWR RARRALKKDR VPREELELLI KAAHLAPSCM NNQPWRFVVV DEEELLKKIH EALPGGNYWM KNAPALIAVH SKKDFDCALP DNRDYFLFDT GLAVGNLLVQ ATQMGLVAHP VAGYDPVKVK EILKIPEDHV LITLIAVGYL GDESELSEKH RELERSERVR KELSEIVRWN L // ID Q9WZH5_THEMA Unreviewed; 515 AA. AC Q9WZH5; G4FDA8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Acetyl-coenzyme A carboxyl transferase alpha chain / Acetyl-coenzyme A carboxyl transferase beta chain Propionyl-CoA carboxylase beta chain {ECO:0000313|EMBL:AGL49641.1}; DE EC=6.4.1.2 {ECO:0000313|EMBL:AGL49641.1}; DE EC=6.4.1.3 {ECO:0000313|EMBL:AGL49641.1}; DE SubName: Full=Propionyl-CoA carboxylase, beta subunit {ECO:0000313|EMBL:AAD35798.1}; GN OrderedLocusNames=TM_0716 {ECO:0000313|EMBL:AAD35798.1}; GN ORFNames=Tmari_0716 {ECO:0000313|EMBL:AGL49641.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35798.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35798.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35798.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49641.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49641.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35798.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49641.1; -; Genomic_DNA. DR PIR; C72344; C72344. DR RefSeq; NP_228525.1; NC_000853.1. DR RefSeq; WP_004081020.1; NZ_CP011107.1. DR PDB; 1VRG; X-ray; 2.30 A; A/B/C/D/E/F=1-515. DR PDBsum; 1VRG; -. DR STRING; 243274.TM0716; -. DR EnsemblBacteria; AAD35798; AAD35798; TM_0716. DR EnsemblBacteria; AGL49641; AGL49641; Tmari_0716. DR GeneID; 898383; -. DR KEGG; tma:TM0716; -. DR KEGG; tmm:Tmari_0716; -. DR KEGG; tmw:THMA_0731; -. DR PATRIC; 23936350; VBITheMar51294_0728. DR eggNOG; ENOG4105D8K; Bacteria. DR eggNOG; COG4799; LUCA. DR OMA; YLAMGSK; -. DR OrthoDB; EOG696BWK; -. DR BioCyc; TMAR243274:GC6P-742-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.226.10; -; 2. DR InterPro; IPR000022; Carboxyl_trans. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR011763; COA_CT_C. DR InterPro; IPR011762; COA_CT_N. DR Pfam; PF01039; Carboxyl_trans; 1. DR SUPFAM; SSF52096; SSF52096; 2. DR PROSITE; PS50989; COA_CT_CTER; 1. DR PROSITE; PS50980; COA_CT_NTER; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VRG}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Ligase {ECO:0000313|EMBL:AGL49641.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49641.1}. FT DOMAIN 9 223 Carboxyltransferase. FT {ECO:0000259|PROSITE:PS50980}. FT DOMAIN 224 507 COA_CT_CTER. FT {ECO:0000259|PROSITE:PS50989}. SQ SEQUENCE 515 AA; 56415 MW; 1A3FF6445F16BA7D CRC64; MSLRDKIEEL KKIEKEIEQG GGPEKVEKQH RAGKLTAWER LELLLDPGTF VEIDKFVEHR NTYFGLDKVK LPRDGVITGV GEINGRKVAV FSQDFTVMGG SLGEMHAKKI VKLLDLALKM GIPVIGINDS GGARIQEGVD ALAGYGEIFL RNTLASGVVP QITVIAGPCA GGAVYSPALT DFIVMVDQTA RMFITGPNVI KAVTGEEISQ EDLGGAMVHN QKSGNAHFLA DNDEKAMSLV RTLLSYLPSN NAEEPPVEDP DTSLETPEDI LDILPDNPNK GYDVRDVIKR VVDHGEFFEV QPYFAKNIVI GFARIQGKTV GIVANQPSVL AGVLDIDSSD KAARFIRFLD AFNIPILTFV DTPGYLPGVA QEHGGIIRHG AKLLYAYSEA TVPKITVILR KAYGGAYIAM GSKHLGADMV LAWPSAEIAV MGPEGAANII FKREIEASSN PEETRRKLIE EYKQQFANPY IAASRGYVDM VIDPRETRKY IMRALEVCET KVEYRPKKKH GNIPL // ID Q9X142_THEMA Unreviewed; 31 AA. AC Q9X142; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36390.1}; GN OrderedLocusNames=TM_1316 {ECO:0000313|EMBL:AAD36390.1}; GN ORFNames=Tmari_1323 {ECO:0000313|EMBL:AGL50247.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36390.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36390.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36390.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50247.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50247.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36390.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50247.1; -; Genomic_DNA. DR PIR; D72268; D72268. DR RefSeq; NP_229120.1; NC_000853.1. DR RefSeq; WP_010865309.1; NZ_CP011107.1. DR STRING; 243274.TM1316; -. DR EnsemblBacteria; AAD36390; AAD36390; TM_1316. DR EnsemblBacteria; AGL50247; AGL50247; Tmari_1323. DR GeneID; 898166; -. DR KEGG; tma:TM1316; -. DR KEGG; tmi:THEMA_07765; -. DR KEGG; tmm:Tmari_1323; -. DR KEGG; tmw:THMA_1340; -. DR BioCyc; TMAR243274:GC6P-1347-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 31 AA; 3178 MW; 1B03705C506B34BC CRC64; MQKMPKPVVP NDYLNPGKGC GGAGLVCGWC G // ID Q9X243_THEMA Unreviewed; 220 AA. AC Q9X243; G4FGA5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|PIRNR:PIRNR001461}; DE EC=5.1.3.1 {ECO:0000256|PIRNR:PIRNR001461}; GN OrderedLocusNames=TM_1718 {ECO:0000313|EMBL:AAD36784.1}; GN ORFNames=Tmari_1726 {ECO:0000313|EMBL:AGL50650.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36784.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36784.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36784.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50650.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50650.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = D-xylulose 5- CC phosphate. {ECO:0000256|PIRNR:PIRNR001461}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|PIRSR:PIRSR001461-2}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000256|PIRSR:PIRSR001461-2}; CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family. CC {ECO:0000256|PIRNR:PIRNR001461}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36784.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50650.1; -; Genomic_DNA. DR PIR; B72219; B72219. DR RefSeq; NP_229517.1; NC_000853.1. DR RefSeq; WP_004082234.1; NZ_CP011107.1. DR STRING; 243274.TM1718; -. DR EnsemblBacteria; AAD36784; AAD36784; TM_1718. DR EnsemblBacteria; AGL50650; AGL50650; Tmari_1726. DR GeneID; 897233; -. DR KEGG; tma:TM1718; -. DR KEGG; tmi:THEMA_05650; -. DR KEGG; tmm:Tmari_1726; -. DR KEGG; tmw:THMA_1760; -. DR PATRIC; 23938412; VBITheMar51294_1736. DR eggNOG; ENOG4105DJV; Bacteria. DR eggNOG; COG0036; LUCA. DR KO; K01783; -. DR OMA; GANYITF; -. DR OrthoDB; EOG67HK17; -. DR BioCyc; TMAR243274:GC6P-1766-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central. DR GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; IBA:GO_Central. DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central. DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR026019; Ribul_P_3_epim. DR InterPro; IPR000056; Ribul_P_3_epim-like. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR PANTHER; PTHR11749; PTHR11749; 1. DR Pfam; PF00834; Ribul_P_3_epim; 1. DR PIRSF; PIRSF001461; RPE; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR01163; rpe; 1. DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1. DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001461}; KW Cobalt {ECO:0000256|PIRSR:PIRSR001461-2}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000256|PIRNR:PIRNR001461, KW ECO:0000313|EMBL:AGL50650.1}; KW Manganese {ECO:0000256|PIRSR:PIRSR001461-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000256|PIRSR:PIRSR001461-2}. FT REGION 140 143 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR001461-3}. FT ACT_SITE 33 33 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR001461-1}. FT ACT_SITE 173 173 Proton donor. FT {ECO:0000256|PIRSR:PIRSR001461-1}. FT METAL 31 31 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT METAL 33 33 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT METAL 64 64 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT METAL 173 173 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT BINDING 7 7 Substrate. FT {ECO:0000256|PIRSR:PIRSR001461-3}. FT BINDING 64 64 Substrate. FT {ECO:0000256|PIRSR:PIRSR001461-3}. FT BINDING 175 175 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR001461-3}. SQ SEQUENCE 220 AA; 24805 MW; 7F90FFD9796CDBCD CRC64; MVKIAASILA CDLARLADEV KRVEEHVDMI HFDVMDGHFV PNISFGLPVL KALRKETKLP ISVHLMITNP EDYIDRFIEE GADMVAIHYE STFHLHRLVH RVKDLGARAF VAINPHTPIN LLSEIITDVD GVLVMSVNPG FSGQRFIARS LEKIRNLRKM VKELGLETEI MVDGGVNEEN ASILVKNGAT ILVMGYGIFR NDNYVELIKS IKQEREEFAD // ID Q9WZ89_THEMA Unreviewed; 479 AA. AC Q9WZ89; G4FDK2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Lipopolysaccharide biosynthesis protein {ECO:0000313|EMBL:AAD35705.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL49545.1}; GN OrderedLocusNames=TM_0620 {ECO:0000313|EMBL:AAD35705.1}; GN ORFNames=Tmari_0620 {ECO:0000313|EMBL:AGL49545.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35705.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35705.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35705.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49545.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49545.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35705.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49545.1; -; Genomic_DNA. DR PIR; D72354; D72354. DR RefSeq; NP_228430.1; NC_000853.1. DR RefSeq; WP_004081192.1; NZ_CP011107.1. DR STRING; 243274.TM0620; -. DR EnsemblBacteria; AAD35705; AAD35705; TM_0620. DR EnsemblBacteria; AGL49545; AGL49545; Tmari_0620. DR GeneID; 897706; -. DR KEGG; tma:TM0620; -. DR KEGG; tmi:THEMA_01565; -. DR KEGG; tmm:Tmari_0620; -. DR KEGG; tmw:THMA_0636; -. DR PATRIC; 23936151; VBITheMar51294_0629. DR eggNOG; ENOG4107W87; Bacteria. DR eggNOG; COG2244; LUCA. DR OMA; YIAPFLI; -. DR OrthoDB; EOG6R87BG; -. DR BioCyc; TMAR243274:GC6P-645-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR029303; Polysacc_synt_C. DR InterPro; IPR002797; Polysacc_synth. DR Pfam; PF01943; Polysacc_synt; 1. DR Pfam; PF14667; Polysacc_synt_C; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 49 70 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 82 108 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 120 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 170 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 176 197 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 218 235 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 276 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 297 321 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 327 346 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 358 378 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 384 405 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 417 433 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 439 457 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 339 457 Polysacc_synt_C. FT {ECO:0000259|Pfam:PF14667}. SQ SEQUENCE 479 AA; 54124 MW; 4AAF3E4371D3DCAC CRC64; MTPNERDLLK KYISFSLGTW FRALISFFTT PITTWMINPE EFGKATMFST VYSILLLVAL LGTPNSFLRF FPQKSEEEKP VLLWSSVMPP VLLSILLSLV VFIFRSSINT FLVGTPDSKA HVILIATLIT GIFQTFNLNL VRSKGRAILF SAIQVIQSLS QMGFIVLYAL LVSRDFYTLL YAQLFSNVVA LAVGMLFERS YWFPVKIDKK LVFEVIKYGY PFVFSGLLLW LLNWIDRFVL RLYTSFSDIG LYSAAFKIVS AMSLLTTGFS TLWYPFAYEQ YEKNPEDKMI FKRALDYMAF LVFSAGFLLL SFKDVIFLLL ARSYRPAAAI SPFLILNPVM ITMAIVVARG IDFSKKTYWF IVSDGAAALF NLAGNFLLVP TLGAKGAAVS TGLSFIIVFA IESSVSKKLY PVPYDLKKVY CLVSLFVFSA VLHTFSQNLL LPVLSSVFGV FVTIFAYKSE FLKVVSIGVE FLKTTFHRK // ID Q9X087_THEMA Unreviewed; 1289 AA. AC Q9X087; G4FF03; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36071.1}; GN OrderedLocusNames=TM_0992 {ECO:0000313|EMBL:AAD36071.1}; GN ORFNames=Tmari_0995 {ECO:0000313|EMBL:AGL49920.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36071.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36071.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36071.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49920.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49920.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36071.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49920.1; -; Genomic_DNA. DR PIR; F72308; F72308. DR RefSeq; NP_228800.1; NC_000853.1. DR RefSeq; WP_004080565.1; NZ_CP011107.1. DR STRING; 243274.TM0992; -. DR EnsemblBacteria; AAD36071; AAD36071; TM_0992. DR EnsemblBacteria; AGL49920; AGL49920; Tmari_0995. DR GeneID; 897277; -. DR KEGG; tma:TM0992; -. DR KEGG; tmi:THEMA_09390; -. DR KEGG; tmm:Tmari_0995; -. DR KEGG; tmw:THMA_1014; -. DR PATRIC; 23936913; VBITheMar51294_1005. DR eggNOG; ENOG4106NAX; Bacteria. DR eggNOG; ENOG410YDSE; LUCA. DR OMA; GGWILEN; -. DR OrthoDB; EOG664CC0; -. DR BioCyc; TMAR243274:GC6P-1022-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.120.10.30; -; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 611 638 {ECO:0000256|SAM:Coils}. FT COILED 817 841 {ECO:0000256|SAM:Coils}. FT COILED 896 923 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1289 AA; 148493 MW; 82E5081AD98ADCAA CRC64; MKKLAVVVAI LLTFYLCVFS NDSDALRYRL NTISELNKSY LKAIQNIVGY NGLFKSGSDF FLETLYSNDP LLARYQKESQ EAIRKVQEAR REGASNEEIL KLQLAYQEAR LRENKQFIAL IESNLYNSID YLASETLKNS LKTANKIIDD VLKNWKEILK PLLEGDFGGV IKNAILQLID STYKITFIDY CKANYGATEK IAQYWWKTYF VEPFESSEEK KVLDEVLTKA SDELKDRLKD RLTERLKLEI VSKGNALAEK VIEETAKKSA ESILKNIIET PSLIVELFTK YYNVVDFQIT FNDIASNEVV FIKQIRELVG NDENEINRCY FDRAYFLSKK KAAKKAAIND VGEKTQQGST KGQRKSEEDV IPQEVIAKAE EIVLAKDPFL KVSAVQNIET RIEEMNDLSL RDALPDLNSA KRLIEYTFGQ LENNEITLGE YNYEINRIVS VYTGQLNTAK KTIANNLESE YHKGSISQSE YSEKLKQLDK DVEGNIRQLN DFVYLKHQEI EKQRQLFKEK LSQLVKTLDQ GSEMKLLQDS LLAKFNQFLK LYKQKIGQAV WSFAFSSFSE MMEGFTNGIG KAFMKELNSK SPSFFLLQNG GWILENLLAI CQEDERLTRA LIEKVDKLSE EIKALYESFP RYCYTDEDGL VSYSKNAMLI EEFKSSLLQR LEKTLEWKTT ISQWVYMTEL KNEMTKRYLE VYLAFLREKV KIFQETFQVV VDSFDSLKSS YLEKWEDRIE QMAFTIKDMW KQKITPDEAR NELKRISQTT EAVDSMYEHW IEMRDMLEVM SSDLYRISSA GVEMLNLEPS KEYSSYINSM IEENKSLKKS ASQVIEEYEK ASLHDYSHDL KALILDYYRS DDNSYLWKGI STQIGGISFL LILDDPDIMG VIGGDLEKAL NLCQRFEKFI KDAEERVKAT NEADRVLNTY LDKVEIEVES IEKAGGFTTL TKKEALTELL TEAEKKAIEA FQSYGFECTS WRSSRWWDLK RRIESISVPE EKVGQAVEGN ASSFPSIEKP ERIIFGDLVW LNVMQDGYPT HRFSLSPDGK KLLIERQTGF SLYNIETKTL EEFSLPEPVK ATLSRDYNFE WISEDEVYFY AYNGEGFEID ESGSYKEKPV TTIQGMGFIL HSFSPSGEYI LASRLTSNGD AIHVLRVSDA KIEQIGTTYD KSILQWVPGT DSVFFKDQNS KMNIYDVESK TLKTYDVTLE NYVCALLPGG KWIVYGNSLE VIAQNLSTSE KITLWKGNES EQGANVLSGI YPLRGNIVLL LWMHHTEPFD YGVQICEIE // ID Q9WZH6_THEMA Unreviewed; 134 AA. AC Q9WZH6; G4FDA6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase Biotin carboxyl carrier protein {ECO:0000313|EMBL:AGL49643.1}; DE SubName: Full=Propionyl-CoA carboxylase, gamma subunit {ECO:0000313|EMBL:AAD35799.1}; GN OrderedLocusNames=TM_0717 {ECO:0000313|EMBL:AAD35799.1}; GN ORFNames=Tmari_0718 {ECO:0000313|EMBL:AGL49643.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35799.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35799.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35799.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49643.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49643.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35799.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49643.1; -; Genomic_DNA. DR PIR; C72341; C72341. DR RefSeq; NP_228526.1; NC_000853.1. DR RefSeq; WP_004081018.1; NZ_CP011107.1. DR STRING; 243274.TM0717; -. DR EnsemblBacteria; AAD35799; AAD35799; TM_0717. DR EnsemblBacteria; AGL49643; AGL49643; Tmari_0718. DR GeneID; 898384; -. DR KEGG; tma:TM0717; -. DR KEGG; tmi:THEMA_01075; -. DR KEGG; tmm:Tmari_0718; -. DR KEGG; tmw:THMA_0733; -. DR PATRIC; 23936354; VBITheMar51294_0730. DR eggNOG; ENOG4105PV1; Bacteria. DR eggNOG; COG0511; LUCA. DR OMA; NEIMAPD; -. DR OrthoDB; EOG6CVV6Z; -. DR BioCyc; TMAR243274:GC6P-743-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR011053; Single_hybrid_motif. DR Pfam; PF00364; Biotin_lipoyl; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 55 134 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. SQ SEQUENCE 134 AA; 15131 MW; A3BFBAACE8574EC1 CRC64; MVRKFRVVVN GKEYIVEVEE IGNVRKKEPA EKPAKEVSQK TVQEIPKEEP KPVVLEREKS SDQEEKLVKA PMAGIVLKVL VKEGQKVNVG DKLLVFEAMK MENELQSEFS GTVKEILVKE GDNIETGQIL MKIV // ID Q9X264_THEMA Unreviewed; 259 AA. AC Q9X264; G4FGC8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Acid sugar phosphatase {ECO:0000256|PIRNR:PIRNR000915}; DE EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR000915}; GN OrderedLocusNames=TM_1742 {ECO:0000313|EMBL:AAD36807.1}; GN ORFNames=Tmari_1750 {ECO:0000313|EMBL:AGL50674.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36807.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36807.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36807.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50674.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50674.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Catalyzes the dephosphorylation of 2-6 carbon acid CC sugars in vitro. {ECO:0000256|PIRNR:PIRNR000915}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRNR:PIRNR000915}; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD CC family. {ECO:0000256|PIRNR:PIRNR000915}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36807.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50674.1; -; Genomic_DNA. DR PIR; E72218; E72218. DR RefSeq; NP_229540.1; NC_000853.1. DR RefSeq; WP_004082267.1; NZ_CP011107.1. DR PDB; 1PW5; X-ray; 2.80 A; A=1-253. DR PDB; 1VJR; X-ray; 2.40 A; A=1-259. DR PDBsum; 1PW5; -. DR PDBsum; 1VJR; -. DR STRING; 243274.TM1742; -. DR EnsemblBacteria; AAD36807; AAD36807; TM_1742. DR EnsemblBacteria; AGL50674; AGL50674; Tmari_1750. DR GeneID; 897111; -. DR KEGG; tma:TM1742; -. DR KEGG; tmi:THEMA_05525; -. DR KEGG; tmm:Tmari_1750; -. DR KEGG; tmw:THMA_1784; -. DR PATRIC; 23938460; VBITheMar51294_1760. DR eggNOG; ENOG4105D4U; Bacteria. DR eggNOG; COG0647; LUCA. DR KO; K02566; -. DR OMA; FGMKAIM; -. DR OrthoDB; EOG615VGZ; -. DR BioCyc; TMAR243274:GC6P-1790-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 2. DR Gene3D; 3.40.50.10410; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006357; HAD-SF_hydro_IIA. DR InterPro; IPR023215; NPhePase-like_dom. DR Pfam; PF13344; Hydrolase_6; 1. DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01460; HAD-SF-IIA; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1PW5, ECO:0000213|PDB:1VJR}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Magnesium {ECO:0000256|PIRNR:PIRNR000915}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000915}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT REGION 44 45 Sulfate 1 binding. FT {ECO:0000213|PDB:1PW5}. FT REGION 209 212 Sulfate 2 binding. FT {ECO:0000213|PDB:1PW5}. FT BINDING 183 183 Sulfate 1. {ECO:0000213|PDB:1PW5}. FT BINDING 209 209 Sulfate 1. {ECO:0000213|PDB:1PW5}. SQ SEQUENCE 259 AA; 28805 MW; 7705F951764B8D7B CRC64; MLDKIELFIL DMDGTFYLDD SLLPGSLEFL ETLKEKNKRF VFFTNNSSLG AQDYVRKLRN MGVDVPDDAV VTSGEITAEH MLKRFGRCRI FLLGTPQLKK VFEAYGHVID EENPDFVVLG FDKTLTYERL KKACILLRKG KFYIATHPDI NCPSKEGPVP DAGSIMAAIE ASTGRKPDLI AGKPNPLVVD VISEKFGVPK ERMAMVGDRL YTDVKLGKNA GIVSILVLTG ETTPEDLERA ETKPDFVFKN LGELAKAVQ // ID Q9WXP8_THEMA Unreviewed; 129 AA. AC Q9WXP8; G4FGV8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000313|EMBL:AAD35135.1}; DE EC=2.7.6.3 {ECO:0000313|EMBL:AGL48964.1}; GN OrderedLocusNames=TM_0041 {ECO:0000313|EMBL:AAD35135.1}; GN ORFNames=Tmari_0038 {ECO:0000313|EMBL:AGL48964.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35135.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35135.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35135.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48964.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48964.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35135.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48964.1; -; Genomic_DNA. DR PIR; F72425; F72425. DR RefSeq; NP_227857.1; NC_000853.1. DR RefSeq; WP_004082507.1; NC_000853.1. DR STRING; 243274.TM0041; -. DR EnsemblBacteria; AAD35135; AAD35135; TM_0041. DR EnsemblBacteria; AGL48964; AGL48964; Tmari_0038. DR GeneID; 896865; -. DR KEGG; tma:TM0041; -. DR KEGG; tmm:Tmari_0038; -. DR PATRIC; 23934922; VBITheMar51294_0039. DR eggNOG; ENOG4105K8U; Bacteria. DR eggNOG; COG0801; LUCA. DR KO; K00950; -. DR OMA; QGDNFYN; -. DR OrthoDB; EOG6XHC8G; -. DR BioCyc; TMAR243274:GC6P-41-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.70.560; -; 1. DR InterPro; IPR000550; Hppk. DR Pfam; PF01288; HPPK; 1. DR SUPFAM; SSF55083; SSF55083; 1. DR TIGRFAMs; TIGR01498; folK; 1. DR PROSITE; PS00794; HPPK; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000313|EMBL:AAD35135.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35135.1}. FT DOMAIN 62 73 HPPK. {ECO:0000259|PROSITE:PS00794}. SQ SEQUENCE 129 AA; 15093 MW; BCEF86AA9A6D9ED0 CRC64; MNKRNIKVEK VSSVIETEPY GYEDQPRFLN AVCIAQTPLS PHELLNTLLQ IERNMGRVRT IRWGPRIIDL DIVFYEDLVL SEEDLIIPHP DAHNRTFVLE PLCEIAPDLI HPVMGKTVRE LLEDLRRRR // ID Q9WY58_THEMA Unreviewed; 128 AA. AC Q9WY58; G4FHC9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Endoribonuclease L-PSP {ECO:0000313|EMBL:AGL49139.1}; DE SubName: Full=Protein synthesis inhibitor, putative {ECO:0000313|EMBL:AAD35307.1}; GN OrderedLocusNames=TM_0215 {ECO:0000313|EMBL:AAD35307.1}; GN ORFNames=Tmari_0213 {ECO:0000313|EMBL:AGL49139.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35307.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35307.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35307.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49139.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49139.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35307.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49139.1; -; Genomic_DNA. DR PIR; A72404; A72404. DR RefSeq; NP_228030.1; NC_000853.1. DR RefSeq; WP_004082892.1; NZ_CP011107.1. DR PDB; 2B33; X-ray; 2.30 A; A/B=1-128. DR PDBsum; 2B33; -. DR STRING; 243274.TM0215; -. DR EnsemblBacteria; AAD35307; AAD35307; TM_0215. DR EnsemblBacteria; AGL49139; AGL49139; Tmari_0213. DR GeneID; 897099; -. DR KEGG; tma:TM0215; -. DR KEGG; tmi:THEMA_03650; -. DR KEGG; tmm:Tmari_0213; -. DR KEGG; tmw:THMA_0222; -. DR PATRIC; 23935302; VBITheMar51294_0217. DR eggNOG; ENOG4105KME; Bacteria. DR eggNOG; COG0251; LUCA. DR KO; K09022; -. DR OMA; GSYFKEP; -. DR OrthoDB; EOG6QVRPF; -. DR BioCyc; TMAR243274:GC6P-228-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.30.1330.40; -; 1. DR InterPro; IPR013813; Endoribo_LPSP/chorism_mut-like. DR InterPro; IPR006056; RidA. DR InterPro; IPR019897; RidA_CS. DR InterPro; IPR006175; YjgF/YER057c/UK114. DR PANTHER; PTHR11803; PTHR11803; 1. DR Pfam; PF01042; Ribonuc_L-PSP; 1. DR SUPFAM; SSF55298; SSF55298; 1. DR TIGRFAMs; TIGR00004; TIGR00004; 1. DR PROSITE; PS01094; UPF0076; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2B33}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 128 AA; 14268 MW; 31DF688739F9857B CRC64; MKRFVETDKA PKAIGPYSQA VVVGNMMFVS GQIPIDPETG ELVQGTIEEK TERVLENLKA ILEAGGFSLK DVVKVTVFTT SMDYFQRVNE VYSRYFGDHR PARSFVAVAQ LPRNVEIEIE AIAVKEGE // ID Q9WZU2_THEMA Unreviewed; 401 AA. AC Q9WZU2; G4FCY6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35920.1}; GN OrderedLocusNames=TM_0838 {ECO:0000313|EMBL:AAD35920.1}; GN ORFNames=Tmari_0840 {ECO:0000313|EMBL:AGL49765.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35920.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35920.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35920.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49765.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49765.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35920.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49765.1; -; Genomic_DNA. DR PIR; B72329; B72329. DR RefSeq; NP_228647.1; NC_000853.1. DR RefSeq; WP_004080795.1; NZ_CP011107.1. DR STRING; 243274.TM0838; -. DR EnsemblBacteria; AAD35920; AAD35920; TM_0838. DR EnsemblBacteria; AGL49765; AGL49765; Tmari_0840. DR GeneID; 898509; -. DR KEGG; tma:TM0838; -. DR KEGG; tmi:THEMA_00450; -. DR KEGG; tmm:Tmari_0840; -. DR KEGG; tmw:THMA_0859; -. DR PATRIC; 23936602; VBITheMar51294_0851. DR eggNOG; ENOG4105XCY; Bacteria. DR eggNOG; COG1361; LUCA. DR OMA; IRRRANF; -. DR OrthoDB; EOG6WDSD4; -. DR BioCyc; TMAR243274:GC6P-867-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 55 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 401 AA; 47365 MW; 86BC0860AA8C0AC0 CRC64; MKYFSKSPEE WQKRDEEKEK EFRNRKNRIR RRANFILVVN LVIVVFLVFF TKAFFSNKPE GVIGPFQLVI ETKESYLPND PLDVRVKVFN REKKKENLVL EDFVFSIKRE NDTVYEFHFP QRVEKEMEAF ESVLVFDLLR EEELSNLPGG NYTITVSVKL NGQRVVISKV VSVIEKWQIE VEDLKDFYFP YENVHFFVYL ENISSKSRKI RVESIGLIIL KGNEAVFERD IPIEKDFVIN PMMVEQIHEV SFSAPKESGD YIIKLKLKTE SSLIEKSIPL FVTREYQKDL KGLSLVIEGK KFVASGERYD FSVKLLNEEK KRKYIVLKNI MIVLTHKEPV FSYAYSEEYR MTIEGYSSRE IFKTTSYDII KLEDPGTYKL IVVIESEEDR LMKEMEIVVS E // ID Q9WY32_THEMA Unreviewed; 358 AA. AC Q9WY32; G4FHA3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Iron(III) ABC transporter, periplasmic iron-binding protein, putative {ECO:0000313|EMBL:AAD35281.1}; DE SubName: Full=Iron(III) dicitrate-binding protein {ECO:0000313|EMBL:AGL49113.1}; GN OrderedLocusNames=TM_0189 {ECO:0000313|EMBL:AAD35281.1}; GN ORFNames=Tmari_0187 {ECO:0000313|EMBL:AGL49113.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35281.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35281.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35281.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49113.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49113.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains Fe/B12 periplasmic-binding domain. CC {ECO:0000256|SAAS:SAAS00514624}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35281.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49113.1; -; Genomic_DNA. DR PIR; E72406; E72406. DR RefSeq; NP_228004.1; NC_000853.1. DR RefSeq; WP_004082831.1; NZ_CP011107.1. DR PDB; 2ETV; X-ray; 1.70 A; A/B=25-358. DR PDBsum; 2ETV; -. DR STRING; 243274.TM0189; -. DR DNASU; 897037; -. DR EnsemblBacteria; AAD35281; AAD35281; TM_0189. DR EnsemblBacteria; AGL49113; AGL49113; Tmari_0187. DR GeneID; 897037; -. DR KEGG; tma:TM0189; -. DR KEGG; tmi:THEMA_03820; -. DR KEGG; tmm:Tmari_0187; -. DR KEGG; tmw:THMA_0191; -. DR PATRIC; 23935238; VBITheMar51294_0191. DR eggNOG; ENOG4105S10; Bacteria. DR eggNOG; COG0614; LUCA. DR KO; K02016; -. DR OMA; CLRLLTY; -. DR OrthoDB; EOG6GR37R; -. DR BioCyc; TMAR243274:GC6P-196-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0036094; F:small molecule binding; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR002491; ABC_transptr_periplasmic_BD. DR Pfam; PF01497; Peripla_BP_2; 1. DR PROSITE; PS50983; FE_B12_PBP; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2ETV}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 40 310 Fe/B12 periplasmic-binding. FT {ECO:0000259|PROSITE:PS50983}. FT MOD_RES 25 25 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 56 56 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 69 69 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 85 85 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 86 86 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 97 97 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 120 120 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 123 123 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 128 128 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 158 158 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 175 175 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 200 200 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 211 211 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 232 232 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 238 238 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 263 263 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 275 275 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 278 278 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 319 319 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 330 330 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. FT MOD_RES 345 345 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETV}. SQ SEQUENCE 358 AA; 40070 MW; 5E0B990B9D4DA205 CRC64; MKFKVFISVF LILSVALFSE GIVIKDLLGR EVEIPSNVNR IVAVGPGALR LIAYLKATDM VVGVEDFEKL RPYGRPYILA YPELKKLPSV GPGGPGKLPD LESLITLQPD VVFITYVDRK TAKDIQEKTG IPVVVLSYGN LGTFEDEDLF RSIELAGKIL GREERAHEVV DFIRKAQEDL VTRSEGVESP TVYVGGIGYK GAHGIDSTEA KYPPFVVLHA RNVVDELGEG HKFIDPEKLL VWNPEYIFID ENGLSLVLDD YSKHREFYES LSAVKRGKVY GILPYNYYTT NIGTALADAY FIGKVLYPER FTDIDPEEKA DEIYEFLLGK RVYGEMAEQF GGFGKIDLPS GRILRGTW // ID Q9WYP5_THEMA Unreviewed; 334 AA. AC Q9WYP5; G4FHX3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:AAD35499.1}; DE SubName: Full=Myo-inositol 2-dehydrogenase 1 {ECO:0000313|EMBL:AGL49336.1}; DE EC=1.1.1.18 {ECO:0000313|EMBL:AGL49336.1}; GN OrderedLocusNames=TM_0414 {ECO:0000313|EMBL:AAD35499.1}; GN ORFNames=Tmari_0411 {ECO:0000313|EMBL:AGL49336.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35499.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35499.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35499.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49336.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49336.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35499.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49336.1; -; Genomic_DNA. DR PIR; D72381; D72381. DR RefSeq; NP_228224.1; NC_000853.1. DR RefSeq; WP_004083264.1; NZ_CP011107.1. DR PDB; 3EZY; X-ray; 2.04 A; A/B/C/D=2-334. DR PDBsum; 3EZY; -. DR STRING; 243274.TM0414; -. DR DNASU; 897415; -. DR EnsemblBacteria; AAD35499; AAD35499; TM_0414. DR EnsemblBacteria; AGL49336; AGL49336; Tmari_0411. DR GeneID; 897415; -. DR KEGG; tma:TM0414; -. DR KEGG; tmi:THEMA_02655; -. DR KEGG; tmm:Tmari_0411; -. DR KEGG; tmw:THMA_0420; -. DR PATRIC; 23935711; VBITheMar51294_0419. DR eggNOG; ENOG4105DRI; Bacteria. DR eggNOG; COG0673; LUCA. DR KO; K00010; -. DR OMA; YDQRVEI; -. DR OrthoDB; EOG6M9DZF; -. DR BioCyc; MetaCyc:MONOMER-17948; -. DR BioCyc; TMAR243274:GC6P-429-MONOMER; -. DR BRENDA; 1.1.1.369; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR030827; Myo_inos_iolG. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000683; Oxidoreductase_N. DR InterPro; IPR004104; OxRdtase_C. DR Pfam; PF01408; GFO_IDH_MocA; 1. DR Pfam; PF02894; GFO_IDH_MocA_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR04380; myo_inos_iolG; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3EZY}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49336.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 120 GFO_IDH_MocA. {ECO:0000259|Pfam:PF01408}. FT DOMAIN 132 236 GFO_IDH_MocA_C. FT {ECO:0000259|Pfam:PF02894}. SQ SEQUENCE 334 AA; 37485 MW; 97A3569F165A64A7 CRC64; MRIGVIGLGR IGTIHAENLK MIDDAILYAI SDVREDRLRE MKEKLGVEKA YKDPHELIED PNVDAVLVCS STNTHSELVI ACAKAKKHVF CEKPLSLNLA DVDRMIEETK KADVILFTGF NRRFDRNFKK LKEAVENGTI GKPHVLRITS RDPAPPPLDY IRVSGGIFLD MTIHDFDMAR YIMGEEVEEV FADGSVLVDE EIGKAGDVDT AVVVLRFKSG ALGVIDNSRR AVYGYDQRIE VFGSKGRIFA DNVRETTVVL TDEQGDRGSR YLYFFLERYR DSYLEELKTF IKNVKSGEPP AVSGEDGKMA LLLGYAAKKS LEEKRSVKLE EVIG // ID Q9X0L6_THEMA Unreviewed; 305 AA. AC Q9X0L6; G4FEL6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=MoxR protein, putative {ECO:0000313|EMBL:AAD36208.1}; DE SubName: Full=MoxR-like ATPase {ECO:0000313|EMBL:AGL50062.1}; GN OrderedLocusNames=TM_1132 {ECO:0000313|EMBL:AAD36208.1}; GN ORFNames=Tmari_1138 {ECO:0000313|EMBL:AGL50062.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36208.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36208.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36208.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50062.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50062.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36208.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50062.1; -; Genomic_DNA. DR PIR; H72289; H72289. DR RefSeq; NP_228938.1; NC_000853.1. DR RefSeq; WP_004080275.1; NZ_CP011107.1. DR STRING; 243274.TM1132; -. DR EnsemblBacteria; AAD36208; AAD36208; TM_1132. DR EnsemblBacteria; AGL50062; AGL50062; Tmari_1138. DR GeneID; 898632; -. DR KEGG; tma:TM1132; -. DR KEGG; tmi:THEMA_08685; -. DR KEGG; tmm:Tmari_1138; -. DR KEGG; tmw:THMA_1155; -. DR PATRIC; 23937199; VBITheMar51294_1148. DR eggNOG; ENOG4105C7R; Bacteria. DR eggNOG; COG0714; LUCA. DR KO; K03924; -. DR OMA; ARISMGY; -. DR OrthoDB; EOG6J74XF; -. DR BioCyc; TMAR243274:GC6P-1161-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011703; ATPase_AAA-3. DR InterPro; IPR016366; ATPase_chaperone_AAA_MoxR_prd. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF07726; AAA_3; 1. DR PIRSF; PIRSF002849; AAA_ATPase_chaperone_MoxR_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 32 162 AAA_3. {ECO:0000259|Pfam:PF07726}. SQ SEQUENCE 305 AA; 34432 MW; FB734C22B3DDCFE7 CRC64; MIERVINNIE KVIKGKREAI EVVVAALLAK GHVLMEDVPG VGKTMLARAL ALSLGVDFRR VQFTPDLLPT DLTGLYIYDR KKEDFVFKKG PVFTDVLLAD EINRATPRTQ SALLEAMAEG QVTVDGVTHR LSERFFVIAT QNPIEYEGTF PLPEAQLDRF MICVKMGYPD EEAEIQMLTS QEKEHPISQL EPVMNPDELS ELQKKVRNVF VSDEVKKYIV DIASATRNHP SLLLGMSPRG SIALMHFSMA LAFMDGRDFT LPDDVKRAAV YVIPHRVIQS AESKLKREKK EDIVREILDR VKVVK // ID Q9X0E0_THEMA Unreviewed; 331 AA. AC Q9X0E0; G4FEU8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:AAD36127.1}; DE SubName: Full=Endoglucanase M {ECO:0000313|EMBL:AGL49978.1}; DE EC=3.2.1.4 {ECO:0000313|EMBL:AGL49978.1}; GN OrderedLocusNames=TM_1050 {ECO:0000313|EMBL:AAD36127.1}; GN ORFNames=Tmari_1054 {ECO:0000313|EMBL:AGL49978.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36127.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36127.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36127.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49978.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49978.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36127.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49978.1; -; Genomic_DNA. DR PIR; D72301; D72301. DR RefSeq; NP_228856.1; NC_000853.1. DR RefSeq; WP_004080460.1; NZ_CP011107.1. DR PDB; 3ISX; X-ray; 1.40 A; A=1-331. DR PDB; 4P6Y; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-331. DR PDBsum; 3ISX; -. DR PDBsum; 4P6Y; -. DR STRING; 243274.TM1050; -. DR MEROPS; M42.010; -. DR EnsemblBacteria; AAD36127; AAD36127; TM_1050. DR EnsemblBacteria; AGL49978; AGL49978; Tmari_1054. DR GeneID; 897098; -. DR KEGG; tma:TM1050; -. DR KEGG; tmi:THEMA_09110; -. DR KEGG; tmm:Tmari_1054; -. DR KEGG; tmw:THMA_1072; -. DR PATRIC; 23937029; VBITheMar51294_1063. DR eggNOG; ENOG4105CN9; Bacteria. DR eggNOG; COG1363; LUCA. DR KO; K01179; -. DR OMA; TIHFCAT; -. DR OrthoDB; EOG6V4GDH; -. DR BioCyc; TMAR243274:GC6P-1079-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR Gene3D; 2.40.30.40; -; 1. DR InterPro; IPR008007; Peptidase_M42. DR InterPro; IPR023367; Peptidase_M42_dom2. DR Pfam; PF05343; Peptidase_M42; 1. DR PIRSF; PIRSF001123; PepA_GA; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3ISX, ECO:0000213|PDB:4P6Y}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000313|EMBL:AGL49978.1}; KW Hydrolase {ECO:0000313|EMBL:AGL49978.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT ACT_SITE 197 197 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR001123-1}. SQ SEQUENCE 331 AA; 36065 MW; BE8DDEB0CEED5595 CRC64; MKELIRKLTE AFGPSGREEE VRSIILEELE GHIDGHRIDG LGNLIVWKGS GEKKVILDAH IDEIGVVVTN VDDKGFLTIE PVGGVSPYML LGKRIRFENG TIGVVGMEGE TTEERQENVR KLSFDKLFID IGANSREEAQ KMCPIGSFGV YDSGFVEVSG KYVSKAMDDR IGCAVIVEVF KRIKPAVTLY GVFSVQEEVG LVGASVAGYG VPADEAIAID VTDSADTPKA IKRHAMRLSG GPALKVKDRA SISSKRILEN LIEIAEKFDI KYQMEVLTFG GTNAMGYQRT REGIPSATVS IPTRYVHSPS EMIAPDDVEA TVDLLIRYLG A // ID Q9X1T2_THEMA Unreviewed; 265 AA. AC Q9X1T2; G4FFY4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|PIRNR:PIRNR000477}; DE EC=2.4.2.1 {ECO:0000256|PIRNR:PIRNR000477}; DE AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|PIRNR:PIRNR000477}; GN OrderedLocusNames=TM_1596 {ECO:0000313|EMBL:AAD36663.1}; GN ORFNames=Tmari_1604 {ECO:0000313|EMBL:AGL50528.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36663.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36663.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36663.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50528.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50528.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: The purine nucleoside phosphorylases catalyze the CC phosphorolytic breakdown of the N-glycosidic bond in the beta- CC (deoxy)ribonucleoside molecules, with the formation of the CC corresponding free purine bases and pentose-1-phosphate. CC {ECO:0000256|PIRNR:PIRNR000477}. CC -!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine + CC alpha-D-ribose 1-phosphate. {ECO:0000256|PIRNR:PIRNR000477}. CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage. CC {ECO:0000256|PIRNR:PIRNR000477}. CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. CC {ECO:0000256|PIRNR:PIRNR000477}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36663.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50528.1; -; Genomic_DNA. DR PIR; H72233; H72233. DR RefSeq; NP_229396.1; NC_000853.1. DR RefSeq; WP_004082038.1; NZ_CP011107.1. DR PDB; 1VMK; X-ray; 2.01 A; A/B/C=1-265. DR PDBsum; 1VMK; -. DR STRING; 243274.TM1596; -. DR EnsemblBacteria; AAD36663; AAD36663; TM_1596. DR EnsemblBacteria; AGL50528; AGL50528; Tmari_1604. DR GeneID; 897943; -. DR KEGG; tma:TM1596; -. DR KEGG; tmi:THEMA_06270; -. DR KEGG; tmm:Tmari_1604; -. DR KEGG; tmw:THMA_1636; -. DR PATRIC; 23938166; VBITheMar51294_1615. DR eggNOG; ENOG4105CB1; Bacteria. DR eggNOG; COG0005; LUCA. DR KO; K03783; -. DR OMA; IPNFPYS; -. DR OrthoDB; EOG6423M2; -. DR BioCyc; TMAR243274:GC6P-1642-MONOMER; -. DR UniPathway; UPA00606; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IBA:GO_Central. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0043101; P:purine-containing compound salvage; IBA:GO_Central. DR Gene3D; 3.40.50.1580; -; 1. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR001369; PNP/MTAP. DR InterPro; IPR011270; Pur_Nuc_Pase_Ino/Guo-sp. DR InterPro; IPR011268; Purine_phosphorylase. DR PANTHER; PTHR11904; PTHR11904; 1. DR PANTHER; PTHR11904:SF9; PTHR11904:SF9; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR PIRSF; PIRSF000477; PurNPase; 1. DR SUPFAM; SSF53167; SSF53167; 1. DR TIGRFAMs; TIGR01700; PNPH; 1. DR TIGRFAMs; TIGR01697; PNPH-PUNA-XAPA; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VMK}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000477, KW ECO:0000313|EMBL:AGL50528.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|PIRNR:PIRNR000477, KW ECO:0000313|EMBL:AGL50528.1}. FT DOMAIN 21 262 PNP_UDP_1. {ECO:0000259|Pfam:PF01048}. SQ SEQUENCE 265 AA; 29173 MW; 273B1A69DD8A5422 CRC64; MMKKIEEART FISERTNLSP DILIILGSGF GPFIEKVEDP VIIDYKDIPH FPQPTVEGHS GKLVFGRISD KPVMIMAGRF HLYEGHDPAT VAFPVYLAKY VGVKGVVVTN AAGAINPEFK PGEIILVRDI INFMFRNPLR GPNDEKIGPR FPDMSSVVDP EWARKIQERL SLKEGVYIGV LGPSYETPAE IRVFEKLGAD LVGMSTVPEV IAAKHCGLKV VVFSCVTNMA AGITHGRLSH EEVVRTTKMA QGKIEKALTT AVEVF // ID Q9X2C0_THEMA Unreviewed; 220 AA. AC Q9X2C0; G4FGI8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=CRISPR-associated protein, family {ECO:0000313|EMBL:AGL50734.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36863.1}; GN OrderedLocusNames=TM_1800 {ECO:0000313|EMBL:AAD36863.1}; GN ORFNames=Tmari_1810 {ECO:0000313|EMBL:AGL50734.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36863.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36863.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36863.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50734.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50734.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36863.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50734.1; -; Genomic_DNA. DR PIR; E72210; E72210. DR RefSeq; NP_229597.1; NC_000853.1. DR RefSeq; WP_004082347.1; NZ_CP011107.1. DR STRING; 243274.TM1800; -. DR EnsemblBacteria; AAD36863; AAD36863; TM_1800. DR EnsemblBacteria; AGL50734; AGL50734; Tmari_1810. DR GeneID; 897778; -. DR KEGG; tma:TM1800; -. DR KEGG; tmi:THEMA_05190; -. DR KEGG; tmm:Tmari_1810; -. DR KEGG; tmw:THMA_1846; -. DR PATRIC; 23938589; VBITheMar51294_1821. DR eggNOG; ENOG4108YX3; Bacteria. DR eggNOG; COG1688; LUCA. DR KO; K19116; -. DR OMA; ESAVYIF; -. DR OrthoDB; EOG6RRKM2; -. DR BioCyc; TMAR243274:GC6P-1851-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR021124; CRISPR-assoc_prot_Cas5. DR InterPro; IPR013421; CRISPR-assoc_prot_Cas5_HALMA. DR InterPro; IPR013422; CRISPR-assoc_prot_Cas5_N. DR Pfam; PF09704; Cas_Cas5d; 1. DR TIGRFAMs; TIGR02592; cas_Cas5h; 1. DR TIGRFAMs; TIGR02593; CRISPR_cas5; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 220 AA; 25407 MW; FAB48B4AC3E6EF7F CRC64; MKVLVFDVSA PYALFRRPYT TTSSYTLPFP PRTTLLGLVG CVLGYSTPER LDSAKVAVQI KNPLKFLRTG TNFVETKKDK KASKRTRISL QLLKNPAYRV FFSWEDEDFE RLKNLLEHSE TIFTPYLGVA SFIARLNYVG KYEATRVADF PCEVHTVVPN TVKLLPEPSH YLIFERVTRK MDKERNMLES AVYIFKRDLS PVKVEGGEVW RVGEQNIVWM // ID Q9WZ42_THEMA Unreviewed; 383 AA. AC Q9WZ42; G4FDP8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Lipopolysaccharide biosynthesis protein, putative {ECO:0000313|EMBL:AAD35657.1}; DE SubName: Full=Putative aminotransferase, DegT family {ECO:0000313|EMBL:AGL49495.1}; GN OrderedLocusNames=TM_0572 {ECO:0000313|EMBL:AAD35657.1}; GN ORFNames=Tmari_0570 {ECO:0000313|EMBL:AGL49495.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35657.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35657.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35657.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49495.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49495.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. CC {ECO:0000256|RuleBase:RU004508}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35657.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49495.1; -; Genomic_DNA. DR PIR; G72359; G72359. DR RefSeq; NP_228382.1; NC_000853.1. DR RefSeq; WP_004081290.1; NZ_CP011107.1. DR STRING; 243274.TM0572; -. DR EnsemblBacteria; AAD35657; AAD35657; TM_0572. DR EnsemblBacteria; AGL49495; AGL49495; Tmari_0570. DR GeneID; 897637; -. DR KEGG; tma:TM0572; -. DR KEGG; tmi:THEMA_01810; -. DR KEGG; tmm:Tmari_0570; -. DR KEGG; tmw:THMA_0586; -. DR PATRIC; 23936053; VBITheMar51294_0581. DR eggNOG; ENOG4105CF4; Bacteria. DR eggNOG; COG0399; LUCA. DR OMA; GHPLDWD; -. DR OrthoDB; EOG6JQH30; -. DR BioCyc; TMAR243274:GC6P-596-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000653; DegT/StrS_aminotransferase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF01041; DegT_DnrJ_EryC1; 1. DR PIRSF; PIRSF000390; PLP_StrS; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000313|EMBL:AGL49495.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-1, KW ECO:0000256|RuleBase:RU004508, ECO:0000256|SAAS:SAAS00486653}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49495.1}. FT MOD_RES 194 194 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR000390-1}. SQ SEQUENCE 383 AA; 43417 MW; 1CA944CA25BBD44E CRC64; MIPLSRPDIN EQDIERVVEV LKSGRLSLGE YTKRFGEMVA EYTGARFGWA VSSGTAALHL ILESLDIDEG DLILVPSFTF IASVNVILMK RAIPVFVDVD ERTLNVSPET LEEAVKRCLK GFKQGNIEIK GKPRLFMAVD VFGHPLDWDG ILDVCQRYGI AVVEDSCEAL GSEYKGRKVG TFGVAGAFAF YPNKQITTGE GGVVVTNDEK IHTAVKSMSN QGRGEGDEWL YHVRFGYNYR IDEMSAALGC SQMERIDEIV EKRAEAAERY SKMLKEFSWV KVPVVEDYVT KMSWFVYVVR LEGPDRNRVM RYMEEKGVQV RNYFYPVHFQ PFYEKLFGSM KGLLPVTERE SEKTLAIPFF TSITESEQKT VVEILREAVE RVG // ID Q9WXQ8_THEMA Unreviewed; 669 AA. AC Q9WXQ8; G4FGW6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 110. DE RecName: Full=Ferrous iron transport protein B {ECO:0000256|RuleBase:RU362098}; GN OrderedLocusNames=TM_0051 {ECO:0000313|EMBL:AAD35145.1}; GN ORFNames=Tmari_0048 {ECO:0000313|EMBL:AGL48974.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35145.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35145.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35145.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48974.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48974.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Fe(2+) uptake system, probably driven by GTP. CC {ECO:0000256|RuleBase:RU362098}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU362098}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. FeoB GTPase (TC 9.A.8) family. CC {ECO:0000256|RuleBase:RU362098}. CC -!- SIMILARITY: Contains 1 FeoB-type G (guanine nucleotide-binding) CC domain. {ECO:0000256|RuleBase:RU362098}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35145.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48974.1; -; Genomic_DNA. DR PIR; D72423; D72423. DR RefSeq; NP_227867.1; NC_000853.1. DR RefSeq; WP_004082534.1; NZ_CP011107.1. DR PDB; 3A1S; X-ray; 1.50 A; A/B=17-269. DR PDB; 3A1T; X-ray; 1.80 A; A=17-269. DR PDB; 3A1U; X-ray; 1.80 A; A/B=17-269. DR PDB; 3A1V; X-ray; 2.40 A; A/B=17-269. DR PDB; 3A1W; X-ray; 1.90 A; A=17-179. DR PDBsum; 3A1S; -. DR PDBsum; 3A1T; -. DR PDBsum; 3A1U; -. DR PDBsum; 3A1V; -. DR PDBsum; 3A1W; -. DR STRING; 243274.TM0051; -. DR EnsemblBacteria; AAD35145; AAD35145; TM_0051. DR EnsemblBacteria; AGL48974; AGL48974; Tmari_0048. DR GeneID; 896875; -. DR KEGG; tma:TM0051; -. DR KEGG; tmm:Tmari_0048; -. DR KEGG; tmw:THMA_0047; -. DR PATRIC; 23934942; VBITheMar51294_0049. DR eggNOG; ENOG4105CE1; Bacteria. DR eggNOG; COG0370; LUCA. DR KO; K04759; -. DR OMA; IWYLSSY; -. DR OrthoDB; EOG6JQH16; -. DR BioCyc; TMAR243274:GC6P-51-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003373; Fe2_transport_prot-B. DR InterPro; IPR011640; Fe2_transport_prot_B_C. DR InterPro; IPR011619; Fe2_transport_prot_B_N. DR InterPro; IPR030389; G_FEOB_dom. DR InterPro; IPR011642; Gate_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR11649:SF37; PTHR11649:SF37; 2. DR Pfam; PF07664; FeoB_C; 1. DR Pfam; PF02421; FeoB_N; 1. DR Pfam; PF07670; Gate; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00437; feoB; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51711; G_FEOB; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3A1S, ECO:0000213|PDB:3A1T, KW ECO:0000213|PDB:3A1U, ECO:0000213|PDB:3A1V}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW GTP-binding {ECO:0000256|RuleBase:RU362098}; KW Ion transport {ECO:0000256|RuleBase:RU362098}; KW Iron {ECO:0000256|RuleBase:RU362098}; KW Iron transport {ECO:0000256|RuleBase:RU362098}; KW Membrane {ECO:0000256|RuleBase:RU362098}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362098}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU362098}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362098}; KW Transport {ECO:0000256|RuleBase:RU362098}. FT TRANSMEM 289 307 Helical. {ECO:0000256|RuleBase:RU362098}. FT TRANSMEM 345 369 Helical. {ECO:0000256|RuleBase:RU362098}. FT TRANSMEM 389 411 Helical. {ECO:0000256|RuleBase:RU362098}. FT TRANSMEM 423 449 Helical. {ECO:0000256|RuleBase:RU362098}. FT TRANSMEM 455 479 Helical. {ECO:0000256|RuleBase:RU362098}. FT TRANSMEM 517 536 Helical. {ECO:0000256|RuleBase:RU362098}. FT TRANSMEM 610 632 Helical. {ECO:0000256|RuleBase:RU362098}. FT TRANSMEM 644 666 Helical. {ECO:0000256|RuleBase:RU362098}. FT DOMAIN 16 178 FeoB-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51711}. SQ SEQUENCE 669 AA; 75140 MW; 4B040B460C19A760 CRC64; MPVKSLTRRS EISQKIVKVA LAGCPNVGKT SLFNALTGTK QYVANWPGVT VEKKEGVFTY KGYTINLIDL PGTYSLGYSS IDEKIARDYL LKGDADLVIL VADSVNPEQS LYLLLEILEM EKKVILAMTA IDEAKKTGMK IDRYELQKHL GIPVVFTSSV TGEGLEELKE KIVEYAQKNT ILHRMILDYG EKVESEIKKV ENFLRDKKLR INPRYFALKY LSGDPEFYSE GVKLGLPELS EEERIGYRLL IAKRKREYVE NVVKEAFADA GSKSLSLSEA IDHVLTHKFL SFPLFFALMY LVFKFTFDIA QVFSDLLDLL FSQLGSAVVN TFGENAFTSL ISDGIIGGVG SVLVFTPNIF AMFLALGFLE ESGYLPRAAF VMDRIMEKFK LSGRAFMSLI LGFGCNVPSI MATRAIDDPR ERLVTILITP FISCSARLPV YLLILRIFFP ESSAAMLFII YSLSILITLL SSVVINWLFY RGRTSPLILE LPRYRMPTLK NLYIYTWNRG KHFLKKAGTI IFVSAILIWV LSYFPAAGDI ENSFSAMIGK SLEWIFKPFG YSWKIVTSLF YGAVAKEVVV STMSMLYGFE EETFLGAKEA LSAEMDPVSA IAFLIFVMAY IPCFATIATI YSETGSLKWT LFSIGYSLSI AYVLSLIVFY VGKLVVMLI // ID Q9X0R2_THEMA Unreviewed; 197 AA. AC Q9X0R2; G4FEG6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36255.1}; GN OrderedLocusNames=TM_1180 {ECO:0000313|EMBL:AAD36255.1}; GN ORFNames=Tmari_1187 {ECO:0000313|EMBL:AGL50111.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36255.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36255.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36255.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50111.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50111.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36255.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50111.1; -; Genomic_DNA. DR PIR; G72286; G72286. DR RefSeq; NP_228985.1; NC_000853.1. DR RefSeq; WP_004080178.1; NZ_CP011107.1. DR STRING; 243274.TM1180; -. DR EnsemblBacteria; AAD36255; AAD36255; TM_1180. DR EnsemblBacteria; AGL50111; AGL50111; Tmari_1187. DR GeneID; 898306; -. DR KEGG; tma:TM1180; -. DR KEGG; tmi:THEMA_08435; -. DR KEGG; tmm:Tmari_1187; -. DR KEGG; tmw:THMA_1205; -. DR PATRIC; 23937300; VBITheMar51294_1198. DR eggNOG; ENOG4106IHY; Bacteria. DR eggNOG; ENOG410Y60F; LUCA. DR OMA; FVPLQEF; -. DR OrthoDB; EOG6XSZV7; -. DR BioCyc; TMAR243274:GC6P-1209-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 197 AA; 22569 MW; 423CDE946E5E9DCD CRC64; MKVIVNGEEI VVEGVQTLGE LLNRVRENKG NLVVKRIVID HEEQPLSRLE DLKQMEINEE MEIELELSPL KDFLLETIEE VLRYIERVKP LLGKVADAVV AGTTEGYRSI NDLAEGLNAM ENVRMNTVRI TGINSKELGL KVEEENLVRI LTDFVNALQS KDLVKIADLI DGELKDVFEY YEEFFKRVEE LLQKEPS // ID Q9X1X5_THEMA Unreviewed; 468 AA. AC Q9X1X5; G4FG29; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 106. DE SubName: Full=Glutamate synthase [NADPH] small chain {ECO:0000313|EMBL:AGL50573.1}; DE EC=1.4.1.13 {ECO:0000313|EMBL:AGL50573.1}; DE SubName: Full=Glutamate synthase, beta subunit {ECO:0000313|EMBL:AAD36707.1}; GN OrderedLocusNames=TM_1640 {ECO:0000313|EMBL:AAD36707.1}; GN ORFNames=Tmari_1649 {ECO:0000313|EMBL:AGL50573.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36707.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36707.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36707.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50573.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50573.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36707.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50573.1; -; Genomic_DNA. DR PIR; H72230; H72230. DR RefSeq; NP_229440.1; NC_000853.1. DR RefSeq; WP_004082125.1; NZ_CP011107.1. DR PDB; 4YLF; X-ray; 2.30 A; B/D=1-468. DR PDB; 4YRY; X-ray; 2.40 A; B/D=1-468. DR PDBsum; 4YLF; -. DR PDBsum; 4YRY; -. DR STRING; 243274.TM1640; -. DR EnsemblBacteria; AAD36707; AAD36707; TM_1640. DR EnsemblBacteria; AGL50573; AGL50573; Tmari_1649. DR GeneID; 897921; -. DR KEGG; tma:TM1640; -. DR KEGG; tmm:Tmari_1649; -. DR KEGG; tmw:THMA_1681; -. DR PATRIC; 23938254; VBITheMar51294_1659. DR eggNOG; ENOG4107QZ5; Bacteria. DR eggNOG; COG0493; LUCA. DR KO; K00266; -. DR OMA; LMKAYDF; -. DR OrthoDB; EOG6XSZQF; -. DR BioCyc; TMAR243274:GC6P-1686-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR Gene3D; 3.50.50.60; -; 4. DR InterPro; IPR028261; DPD_II. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR006004; Glut_synth_NADPH. DR InterPro; IPR009051; Helical_ferredxn. DR Pfam; PF14691; Fer4_20; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR TIGRFAMs; TIGR01316; gltA; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4YLF, ECO:0000213|PDB:4YRY}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50573.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 16 127 Fer4_20. {ECO:0000259|Pfam:PF14691}. FT DOMAIN 142 448 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. SQ SEQUENCE 468 AA; 51613 MW; 062E26E1F28D07EA CRC64; MKNRKTPMKE QSPESRRRNF EEVALGYTLE EALEEAQRCL QCPTHPCVSG CPVEIDIPGF IRKLRDGKLE ESYRILKSYN NLPAVCGRVC PQEVQCESRC VVGKMKDSEP VAIGRLERFV ADWAAENLEE DVKPLAGSKK EKVAVVGSGP AGLTAAADLA KMGYHVDIFE AFHKPGGVLV YGIPEFRLPK RIVEREVSYI RKLGVNFHLN TVVGKTVKVK ELLSEYDAVF IGTGAGTPKF MGIPGTNLNG VYSANEFLTR VNLMKAYLFP EYDTPIRVGK KVAVIGAGNT AMDAARSALR LGAEKVYIVY RRTEREMPAR REEYHHALEE GIEFLWLTLP IRYIGDANGN VEAMECVRME LKEADGSGRP RPVPIEGSNF VLEVDMVIEA IGQGPNRVLL SEFPGLELNE RGYIKADEDT GATSVKGVFA GGDIVTGAAT VIKAMGAGKK AAQFIHSYLT GEWNPWQK // ID Q9WZB8_THEMA Unreviewed; 256 AA. AC Q9WZB8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35734.1}; GN OrderedLocusNames=TM_0650 {ECO:0000313|EMBL:AAD35734.1}; GN ORFNames=Tmari_0650 {ECO:0000313|EMBL:AGL49575.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35734.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35734.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35734.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49575.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49575.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35734.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49575.1; -; Genomic_DNA. DR PIR; A72352; A72352. DR RefSeq; NP_228459.1; NC_000853.1. DR RefSeq; WP_010865175.1; NZ_CP011107.1. DR STRING; 243274.TM0650; -. DR DNASU; 897755; -. DR EnsemblBacteria; AAD35734; AAD35734; TM_0650. DR EnsemblBacteria; AGL49575; AGL49575; Tmari_0650. DR GeneID; 897755; -. DR KEGG; tma:TM0650; -. DR KEGG; tmm:Tmari_0650; -. DR KEGG; tmw:THMA_0665; -. DR PATRIC; 23936214; VBITheMar51294_0660. DR eggNOG; ENOG4105QNS; Bacteria. DR eggNOG; ENOG4111Z2P; LUCA. DR OMA; ISVNDPW; -. DR OrthoDB; EOG60PHFT; -. DR BioCyc; TMAR243274:GC6P-675-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 256 AA; 28044 MW; D6FC7DBE65B41384 CRC64; MSRSLTTILV CLMFLSAFPQ IVLMSEIPES TSTSVAVSVP LQSILKDVSL LCLGSSGNLN LSRDVGIAVG KILKERGVSY YVFGSFDVLR RTDPDPLLKV SSSPYITAQV LSLLAEGLSI AGVVPVFNAT GPVNDQVVTA LITRKATYPV MVEDMEKYEY LKKLGYTTTF VMDTKGNVLV GRPVRFSWAY GKEIDYEDLR REVLESSVVL LDKDTKKISV NDPWGGGVLV FSDEEWLLKI AQAVLNGKRN PTGRVP // ID Q9X117_THEMA Unreviewed; 288 AA. AC Q9X117; G4FE58; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 107. DE SubName: Full=Iron-sulfur cluster-binding protein {ECO:0000313|EMBL:AAD36365.1}; DE SubName: Full=MinD superfamily P-loop ATPase containing an inserted ferredoxin domain {ECO:0000313|EMBL:AGL50223.1}; GN OrderedLocusNames=TM_1291 {ECO:0000313|EMBL:AAD36365.1}; GN ORFNames=Tmari_1299 {ECO:0000313|EMBL:AGL50223.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36365.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36365.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36365.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50223.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50223.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36365.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50223.1; -; Genomic_DNA. DR PIR; B72272; B72272. DR RefSeq; NP_229095.1; NC_000853.1. DR RefSeq; WP_004079937.1; NZ_CP011107.1. DR STRING; 243274.TM1291; -. DR EnsemblBacteria; AAD36365; AAD36365; TM_1291. DR EnsemblBacteria; AGL50223; AGL50223; Tmari_1299. DR GeneID; 898192; -. DR KEGG; tma:TM1291; -. DR KEGG; tmi:THEMA_07880; -. DR KEGG; tmm:Tmari_1299; -. DR KEGG; tmw:THMA_1317; -. DR PATRIC; 23937522; VBITheMar51294_1307. DR eggNOG; ENOG4105FTH; Bacteria. DR eggNOG; COG1149; LUCA. DR OMA; CEGCAVC; -. DR OrthoDB; EOG66TG44; -. DR BioCyc; TMAR243274:GC6P-1322-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR Pfam; PF00037; Fer4; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|RuleBase:RU003429}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|RuleBase:RU003429}; KW Iron-sulfur {ECO:0000256|RuleBase:RU003429}; KW Metal-binding {ECO:0000256|RuleBase:RU003429}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 59 88 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 91 116 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 288 AA; 31349 MW; 0A3CC97A3F37E2BA CRC64; MKQIAVVSGK GGTGKTTFTA SLGVLLENSL LADCDVDASN LYILFPGDPV EEHEYYRGKK AVIDQEKCDR CGICERVCRF DAIIPGEKYG VDQYACEGCN ACVVSCPRNA ITLVQSLAGR YFFAWSGGKP IVYARLSPGE ENSGGLVAEV RKLALEKAKE LKRDYVIIDG APGIGCSATS SIVGVNYVVV VTEPTMSGLH DLKRIVETLK CLKREFGIVI NKYDINSVVS REIEDYCLSE GLDLLGKIPF DETVVRASVE CKPVVTYENS PAAESIKKIV EKIIEKIS // ID Q9X173_THEMA Unreviewed; 232 AA. AC Q9X173; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Polymerase/histidinol phosphatase {ECO:0000313|EMBL:AGL50283.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36423.1}; GN OrderedLocusNames=TM_1352 {ECO:0000313|EMBL:AAD36423.1}; GN ORFNames=Tmari_1359 {ECO:0000313|EMBL:AGL50283.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36423.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36423.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36423.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50283.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50283.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36423.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50283.1; -; Genomic_DNA. DR PIR; H72264; H72264. DR RefSeq; NP_229153.1; NC_000853.1. DR RefSeq; WP_010865325.1; NZ_CP011107.1. DR STRING; 243274.TM1352; -. DR EnsemblBacteria; AAD36423; AAD36423; TM_1352. DR EnsemblBacteria; AGL50283; AGL50283; Tmari_1359. DR GeneID; 898128; -. DR KEGG; tma:TM1352; -. DR KEGG; tmi:THEMA_07580; -. DR KEGG; tmm:Tmari_1359; -. DR KEGG; tmw:THMA_1377; -. DR PATRIC; 23937642; VBITheMar51294_1364. DR eggNOG; ENOG41090YJ; Bacteria. DR eggNOG; COG0613; LUCA. DR KO; K07053; -. DR OMA; DDMTPNN; -. DR OrthoDB; EOG6KMB5P; -. DR BioCyc; TMAR243274:GC6P-1385-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; SSF89550; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 65 POLIIIAc. {ECO:0000259|SMART:SM00481}. SQ SEQUENCE 232 AA; 25752 MW; 36CCC997AD056D89 CRC64; MKADLHVHTC LSPCADLLMI PPVVERASGD VQILGIVDHN SAKNVPAFLK MKKLVVPGIE IQTVEDVHVL GFFSDIESAL KVTKIVYEHL PSVKHDHEKM GYQLFVDEKG NYTGYEDVPL GFPSDLTLSQ AVELIRSFGG IPVYAHVEKR FGVLYQLGFF PDLEIPVAEV VSREGKENAQ KKNLRVIVTS DAHFPSDIGR RYIDISGAPN SPEEVLKKIL NSEYTLGGVL NW // ID Q9WZ36_THEMA Unreviewed; 64 AA. AC Q9WZ36; G4FDQ4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35651.1}; GN OrderedLocusNames=TM_0566 {ECO:0000313|EMBL:AAD35651.1}; GN ORFNames=Tmari_0564 {ECO:0000313|EMBL:AGL49489.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35651.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35651.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35651.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49489.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49489.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35651.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49489.1; -; Genomic_DNA. DR PIR; E72361; E72361. DR RefSeq; NP_228376.1; NC_000853.1. DR RefSeq; WP_004081301.1; NZ_CP011107.1. DR STRING; 243274.TM0566; -. DR EnsemblBacteria; AAD35651; AAD35651; TM_0566. DR EnsemblBacteria; AGL49489; AGL49489; Tmari_0564. DR GeneID; 897630; -. DR KEGG; tma:TM0566; -. DR KEGG; tmi:THEMA_01840; -. DR KEGG; tmm:Tmari_0564; -. DR KEGG; tmw:THMA_0580; -. DR PATRIC; 23936041; VBITheMar51294_0575. DR OMA; EEMIVEF; -. DR OrthoDB; EOG65N1H6; -. DR BioCyc; TMAR243274:GC6P-590-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 6 40 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 64 AA; 7730 MW; 836416CD19AA83C3 CRC64; MENPTIEQLV KRYVEIKDLM KELRAEKKEI EEVLREYAQR TGIKEFKVDG KKVFFEEKLS LKVK // ID Q9WYM4_THEMA Unreviewed; 371 AA. AC Q9WYM4; G4FHV2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Regulator of trehalose utilization, ROK family {ECO:0000313|EMBL:AGL49315.1}; DE SubName: Full=Transcriptional regulator, XylR-related {ECO:0000313|EMBL:AAD35478.1}; GN OrderedLocusNames=TM_0393 {ECO:0000313|EMBL:AAD35478.1}; GN ORFNames=Tmari_0390 {ECO:0000313|EMBL:AGL49315.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35478.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35478.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35478.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49315.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49315.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35478.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49315.1; -; Genomic_DNA. DR PIR; B72382; B72382. DR RefSeq; NP_228203.1; NC_000853.1. DR RefSeq; WP_004083219.1; NZ_CP011107.1. DR STRING; 243274.TM0393; -. DR EnsemblBacteria; AAD35478; AAD35478; TM_0393. DR EnsemblBacteria; AGL49315; AGL49315; Tmari_0390. DR GeneID; 897382; -. DR KEGG; tma:TM0393; -. DR KEGG; tmi:THEMA_02765; -. DR KEGG; tmm:Tmari_0390; -. DR KEGG; tmw:THMA_0398; -. DR PATRIC; 23935667; VBITheMar51294_0398. DR eggNOG; ENOG4105UXZ; Bacteria. DR eggNOG; COG1940; LUCA. DR OMA; QTGCLEY; -. DR OrthoDB; EOG654P0T; -. DR BioCyc; TMAR243274:GC6P-407-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR000600; ROK. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00480; ROK; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 257 280 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 371 AA; 42323 MW; DD781707DF830480 CRC64; MPSPLLRREN KIKILRYILK NGKTTRNQLA SNLNLAHSTL SYIIDELLDE GFLVFEEIKK KRGRPYQILS VNPEKFTAIG VKVGREEVRG VLFDARMNPL KEHRVQILSG MRNNDGYTRA LRETIEQLRS ENLLGVGICS SGIVKEGRVV VSHVMNVKDW DPRKVLKDLE RILVMNDSDA LCREISQRVN TDFLLVSYGV GIGASLWKDK KIHHIEMGHM LAASEGKCYC GQTGCLEYHS SEYAVLKSYL GKEIDFEDFI TSEEEKYRQT IEELREKARE DFDSVKVHYE KAFKTFSVVL GNVIMGSGVS RVFFAGEGVV SEEMVKILEE LVKVRFNRDF VGEVQFQVAD ANWMLGAARA VVDKYLPYIV K // ID Q9WZD2_THEMA Unreviewed; 143 AA. AC Q9WZD2; G4FDG0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 76. DE SubName: Full=Putative endonuclease {ECO:0000313|EMBL:AGL49589.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35753.1}; GN OrderedLocusNames=TM_0664 {ECO:0000313|EMBL:AAD35753.1}; GN ORFNames=Tmari_0664 {ECO:0000313|EMBL:AGL49589.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35753.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35753.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35753.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49589.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49589.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35753.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49589.1; -; Genomic_DNA. DR PIR; E72349; E72349. DR RefSeq; NP_228473.1; NC_000853.1. DR RefSeq; WP_004081109.1; NZ_CP011107.1. DR STRING; 243274.TM0664; -. DR EnsemblBacteria; AAD35753; AAD35753; TM_0664. DR EnsemblBacteria; AGL49589; AGL49589; Tmari_0664. DR GeneID; 897779; -. DR KEGG; tma:TM0664; -. DR KEGG; tmi:THEMA_01345; -. DR KEGG; tmm:Tmari_0664; -. DR KEGG; tmw:THMA_0679; -. DR PATRIC; 23936242; VBITheMar51294_0674. DR eggNOG; ENOG410867N; Bacteria. DR eggNOG; COG1833; LUCA. DR OMA; IPRYFLG; -. DR OrthoDB; EOG6QZMTM; -. DR BioCyc; TMAR243274:GC6P-689-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR InterPro; IPR002837; DUF123. DR InterPro; IPR000305; GIY-YIG_SF. DR Pfam; PF01986; DUF123; 1. DR SMART; SM00465; GIYc; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Endonuclease {ECO:0000313|EMBL:AGL49589.1}; KW Hydrolase {ECO:0000313|EMBL:AGL49589.1}; KW Nuclease {ECO:0000313|EMBL:AGL49589.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 12 112 GIY-YIG. {ECO:0000259|SMART:SM00465}. SQ SEQUENCE 143 AA; 16524 MW; DDD268D6B6C5E8A4 CRC64; MKGTYVLLLK LEESVALRYG KKASHLEPGY YAYVGSAMGG FFKRIPRYFL GSRKRHWHID YLLDHAQIAG LIMFSGKRIE EEISNVLSYH FEGIEDFGAS DLRVKTNLYH VDPDKLFSLL GGFRENRDIR RAQKHRGKQN QSG // ID Q9WZM0_THEMA Unreviewed; 415 AA. AC Q9WZM0; G4FD62; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Permeases of the major facilitator superfamily {ECO:0000313|EMBL:AGL49687.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35843.1}; GN OrderedLocusNames=TM_0761 {ECO:0000313|EMBL:AAD35843.1}; GN ORFNames=Tmari_0762 {ECO:0000313|EMBL:AGL49687.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35843.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35843.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35843.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49687.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49687.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35843.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49687.1; -; Genomic_DNA. DR PIR; G72335; G72335. DR RefSeq; NP_228570.1; NC_000853.1. DR RefSeq; WP_004080938.1; NZ_CP011107.1. DR STRING; 243274.TM0761; -. DR EnsemblBacteria; AAD35843; AAD35843; TM_0761. DR EnsemblBacteria; AGL49687; AGL49687; Tmari_0762. DR GeneID; 898429; -. DR KEGG; tma:TM0761; -. DR KEGG; tmi:THEMA_00845; -. DR KEGG; tmm:Tmari_0762; -. DR KEGG; tmw:THMA_0780; -. DR PATRIC; 23936444; VBITheMar51294_0774. DR eggNOG; ENOG4108KCF; Bacteria. DR eggNOG; COG0477; LUCA. DR OMA; INSAFWV; -. DR OrthoDB; EOG69WFGP; -. DR BioCyc; TMAR243274:GC6P-788-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 69 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 81 104 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 110 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 149 168 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 180 201 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 240 257 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 269 289 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 296 315 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 321 342 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 354 374 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 380 406 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 183 415 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 415 AA; 46026 MW; 2C472BBD22F652EA CRC64; MKRLTEKDYR WNFIVNSLDY AFFSLGMTLG SIFTLFPVFA RNLGASNLEL GLIPAIANLG WGIPAIWGAK YAERSPKKLN LVLKVTLGER LPYLFMALIS FYLAVPSPRL ALYLSILMVG IATFSMGFLG PPWMSMIEKV IDPRRRGTFF AMGNGLGAIL GVGGSVIARE LLSSYPFPVN FGYVFLTAFV FFMVSFVFLA LTREVPDHTL PEDEPIWNYI KNMKNVFLDR HFRNFLIERI ITSFMFASSG FITVYLLEKF SLPDESAAVF TAIVLVSQGL SSFLFGPLGD RKGHKLNLLL SKIFYSGAVI LAFLSTSPVH AYPVFALMGL VNTTNNVGNM AITLDFVSGK RKELYMGSLY FSIAPFSFVA PLIGGKIADL SGYGVLMVLT GLIGVFGIFY VVKFIVDPRV SNKNN // ID Q9X1N8_THEMA Unreviewed; 331 AA. AC Q9X1N8; G4FFU0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Pyruvate formate-lyase activating enzyme, putative {ECO:0000313|EMBL:AAD36618.1}; DE SubName: Full=Radical SAM, Pyruvate-formate lyase-activating enzyme like protein {ECO:0000313|EMBL:AGL50484.1}; GN OrderedLocusNames=TM_1552 {ECO:0000313|EMBL:AAD36618.1}; GN ORFNames=Tmari_1560 {ECO:0000313|EMBL:AGL50484.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36618.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36618.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36618.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50484.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50484.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|PIRSR:PIRSR004869-50}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|PIRSR:PIRSR004869-50}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36618.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50484.1; -; Genomic_DNA. DR PIR; C72239; C72239. DR RefSeq; NP_229352.1; NC_000853.1. DR RefSeq; WP_004081949.1; NZ_CP011107.1. DR STRING; 243274.TM1552; -. DR DNASU; 897970; -. DR EnsemblBacteria; AAD36618; AAD36618; TM_1552. DR EnsemblBacteria; AGL50484; AGL50484; Tmari_1560. DR GeneID; 897970; -. DR KEGG; tma:TM1552; -. DR KEGG; tmi:THEMA_06520; -. DR KEGG; tmm:Tmari_1560; -. DR KEGG; tmw:THMA_1587; -. DR PATRIC; 23938066; VBITheMar51294_1570. DR eggNOG; ENOG4107R69; Bacteria. DR eggNOG; COG1180; LUCA. DR KO; K04069; -. DR OMA; PYIDAMN; -. DR OrthoDB; EOG693GK5; -. DR BioCyc; TMAR243274:GC6P-1593-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR027596; AmmeMemoSam_rS. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004869; PflX_prd; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR04337; AmmeMemoSam_rS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|PIRSR:PIRSR004869-50}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR004869-50}; KW Lyase {ECO:0000313|EMBL:AAD36618.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR004869-50}; KW Pyruvate {ECO:0000313|EMBL:AAD36618.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR004869-50}. FT DOMAIN 73 270 Elp3. {ECO:0000259|SMART:SM00729}. FT METAL 83 83 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. FT METAL 87 87 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. FT METAL 90 90 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. SQ SEQUENCE 331 AA; 38051 MW; FC9F7CC131C7FAA0 CRC64; MERMALHFEI LENGKVKCLL CPHECVLDNG QIGLCGVRKN KNGSLVSLNY GEVTAIAMDP IEKKPLFHFN PGEQIFSVGT FGCNFKCGFC QNWEISQAKP ETKRVTPEQL VKIAQMNRNS KGIAFTYNEP LVWYEFVLDT SRVAVREGMY CVLVTNGFIN EEPLELLFQS VHAMNIDLKG FNRDFYREIG GDLDVVLRNI EKVYNAGIHV ELTTLIIPGK NDDKEDLRRE FEWIADLDKD IPLHISRYFP NYKYTIPPTP IEELIEIYEM AREYLNFVYL GNVWDERYES TFCPDCGNLV IRRQGYEVEK VGLDEEGKCT KCGRQIATII G // ID Q9WZX8_THEMA Unreviewed; 158 AA. AC Q9WZX8; G4FCV0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35956.1}; GN OrderedLocusNames=TM_0875 {ECO:0000313|EMBL:AAD35956.1}; GN ORFNames=Tmari_0877 {ECO:0000313|EMBL:AGL49802.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35956.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35956.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35956.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49802.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49802.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35956.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49802.1; -; Genomic_DNA. DR PIR; E72323; E72323. DR RefSeq; NP_228683.1; NC_000853.1. DR RefSeq; WP_004080723.1; NZ_CP011107.1. DR PDB; 1O22; X-ray; 2.00 A; A=1-158. DR PDBsum; 1O22; -. DR STRING; 243274.TM0875; -. DR EnsemblBacteria; AAD35956; AAD35956; TM_0875. DR EnsemblBacteria; AGL49802; AGL49802; Tmari_0877. DR GeneID; 898548; -. DR KEGG; tma:TM0875; -. DR KEGG; tmi:THEMA_00260; -. DR KEGG; tmm:Tmari_0877; -. DR KEGG; tmw:THMA_0897; -. DR PATRIC; 23936681; VBITheMar51294_0889. DR OMA; FVEEASY; -. DR OrthoDB; EOG61P6RB; -. DR BioCyc; TMAR243274:GC6P-905-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.90.1000.10; -; 1. DR InterPro; IPR024482; DUF3855. DR Pfam; PF12967; DUF3855; 1. DR SUPFAM; SSF90064; SSF90064; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O22}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 158 DUF3855. {ECO:0000259|Pfam:PF12967}. SQ SEQUENCE 158 AA; 18579 MW; 0E21794921530F73 CRC64; MRLMDILEIL YYKKGKEFGI LEKKMKEIFN ETGVSLEPVN SELIGRIFLK ISVLEEGEEV PSFAIKALTP KENAVDLPLG DWTDLKNVFV EEIDYLDSYG DMKILSEKNW YKIYVPYSSV KKKNRNELVE EFMKYFFESK GWNPGEYTFS VQEIDNLF // ID Q9WZ11_THEMA Unreviewed; 164 AA. AC Q9WZ11; G4FDT0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Fumarate hydratase class I, aerobic L(+)-tartrate dehydratase beta subunit {ECO:0000313|EMBL:AGL49463.1}; DE EC=4.2.1.2 {ECO:0000313|EMBL:AGL49463.1}; DE EC=4.2.1.32 {ECO:0000313|EMBL:AGL49463.1}; DE SubName: Full=Fumarate hydratase, C-terminal subunit {ECO:0000313|EMBL:AAD35626.1}; GN OrderedLocusNames=TM_0541 {ECO:0000313|EMBL:AAD35626.1}; GN ORFNames=Tmari_0538 {ECO:0000313|EMBL:AGL49463.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35626.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35626.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35626.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49463.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49463.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35626.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49463.1; -; Genomic_DNA. DR PIR; B72364; B72364. DR RefSeq; NP_228351.1; NC_000853.1. DR RefSeq; WP_004081363.1; NZ_CP011107.1. DR STRING; 243274.TM0541; -. DR EnsemblBacteria; AAD35626; AAD35626; TM_0541. DR EnsemblBacteria; AGL49463; AGL49463; Tmari_0538. DR GeneID; 897595; -. DR KEGG; tma:TM0541; -. DR KEGG; tmi:THEMA_01970; -. DR KEGG; tmm:Tmari_0538; -. DR KEGG; tmw:THMA_0554; -. DR PATRIC; 23935989; VBITheMar51294_0549. DR eggNOG; ENOG4107GFK; Bacteria. DR eggNOG; COG1838; LUCA. DR KO; K01678; -. DR OMA; RVYFITP; -. DR OrthoDB; EOG6KWZ3F; -. DR BioCyc; TMAR243274:GC6P-565-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0008730; F:L(+)-tartrate dehydratase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.130.10; -; 1. DR InterPro; IPR004647; Fe-S_hydro-lyase_TtdB-typ_cat. DR Pfam; PF05683; Fumerase_C; 1. DR SUPFAM; SSF117457; SSF117457; 1. DR TIGRFAMs; TIGR00723; ttdB_fumA_fumB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000313|EMBL:AGL49463.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 163 Fumerase_C. {ECO:0000259|Pfam:PF05683}. SQ SEQUENCE 164 AA; 18173 MW; 319D8B28A8A2E9D1 CRC64; MRIEDLKAGQ EIRYSGKLIV MRDQAQRRLK EIVDRGEEPP VDLRGQIVFY AGPAKTPSGK PVGAIGPTTS ARMDDYLEML FKLGAIATIG KGKRSKKAIE ACKKWKRVYF VTPSGTAAAL SKRVKKSRVL AFEDLGPEAI YEIEVEDFPL IVAIDSNGNT IFKE // ID Q9WZ19_THEMA Unreviewed; 171 AA. AC Q9WZ19; G4FDS2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 111. DE SubName: Full=Acetolactate synthase small subunit {ECO:0000313|EMBL:AGL49471.1}; DE EC=2.2.1.6 {ECO:0000313|EMBL:AGL49471.1}; DE SubName: Full=Acetolactate synthase, small subunit {ECO:0000313|EMBL:AAD35634.1}; GN OrderedLocusNames=TM_0549 {ECO:0000313|EMBL:AAD35634.1}; GN ORFNames=Tmari_0546 {ECO:0000313|EMBL:AGL49471.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35634.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35634.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35634.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49471.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49471.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35634.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49471.1; -; Genomic_DNA. DR PIR; C72362; C72362. DR RefSeq; NP_228359.1; NC_000853.1. DR RefSeq; WP_004081340.1; NZ_CP011107.1. DR PDB; 2FGC; X-ray; 2.30 A; A=1-171. DR PDBsum; 2FGC; -. DR STRING; 243274.TM0549; -. DR EnsemblBacteria; AAD35634; AAD35634; TM_0549. DR EnsemblBacteria; AGL49471; AGL49471; Tmari_0546. DR GeneID; 897604; -. DR KEGG; tma:TM0549; -. DR KEGG; tmi:THEMA_01930; -. DR KEGG; tmm:Tmari_0546; -. DR KEGG; tmw:THMA_0562; -. DR PATRIC; 23936005; VBITheMar51294_0557. DR eggNOG; ENOG4108ZP8; Bacteria. DR eggNOG; COG0440; LUCA. DR KO; K01653; -. DR OMA; PYGIREI; -. DR OrthoDB; EOG6X3W8W; -. DR BioCyc; TMAR243274:GC6P-573-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:InterPro. DR InterPro; IPR004789; Acetalactate_synth_ssu. DR InterPro; IPR019455; Acetolactate_synth_ssu_C. DR InterPro; IPR002912; ACT_dom. DR Pfam; PF01842; ACT; 1. DR Pfam; PF10369; ALS_ss_C; 1. DR TIGRFAMs; TIGR00119; acolac_sm; 1. DR PROSITE; PS51671; ACT; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2FGC}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49471.1}. FT DOMAIN 9 83 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 171 AA; 19443 MW; 09A9ED5B9B9A0EBD CRC64; MTDQIREHLV SMLVHNKPGV MRKVANLFAR RGFNISSITV GESETPGLSR LVIMVKGDDK TIEQIEKQAY KLVEVVKVTP IDPLPENRVE REMALIKVRF DEDKQEIFQL VEIFRGKIID VSREGAIIEI TGARSKVEAF INLLPQKQVE EIARTGIVAM NRWNVKEGEG F // ID Q9X035_THEMA Unreviewed; 118 AA. AC Q9X035; G4FF53; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Transcriptional regulator, PadR family {ECO:0000313|EMBL:AGL49864.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36018.1}; GN OrderedLocusNames=TM_0937 {ECO:0000313|EMBL:AAD36018.1}; GN ORFNames=Tmari_0939 {ECO:0000313|EMBL:AGL49864.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36018.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36018.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36018.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49864.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49864.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36018.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49864.1; -; Genomic_DNA. DR PIR; A72316; A72316. DR RefSeq; NP_228745.1; NC_000853.1. DR RefSeq; WP_004080625.1; NZ_CP011107.1. DR PDB; 2ESH; X-ray; 2.30 A; A=1-118. DR PDBsum; 2ESH; -. DR STRING; 243274.TM0937; -. DR EnsemblBacteria; AAD36018; AAD36018; TM_0937. DR EnsemblBacteria; AGL49864; AGL49864; Tmari_0939. DR GeneID; 898611; -. DR KEGG; tma:TM0937; -. DR KEGG; tmi:THEMA_09665; -. DR KEGG; tmm:Tmari_0939; -. DR KEGG; tmw:THMA_0959; -. DR PATRIC; 23936805; VBITheMar51294_0951. DR eggNOG; ENOG4105Y3R; Bacteria. DR eggNOG; ENOG41122W3; LUCA. DR OMA; RGWWLAS; -. DR OrthoDB; EOG6BGP6V; -. DR BioCyc; TMAR243274:GC6P-967-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005149; Tscrpt_reg_PadR_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF03551; PadR; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2ESH}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 18 92 PadR. {ECO:0000259|Pfam:PF03551}. FT COILED 90 117 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 118 AA; 13779 MW; 4357D1DA2339FD30 CRC64; MRHRGGRGFR GWWLASTILL LVAEKPSHGY ELAERLAEFG IEIPGIGHMG NIYRVLADLE ESGFLSTEWD TTVSPPRKIY RITPQGKLYL REILRSLEDM KRRIETLEER IKRVLQEE // ID Q9WXM3_THEMA Unreviewed; 224 AA. AC Q9WXM3; G4FGS4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Cyclase family protein {ECO:0000313|EMBL:AGL48931.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35102.1}; GN OrderedLocusNames=TM_0008 {ECO:0000313|EMBL:AAD35102.1}; GN ORFNames=Tmari_0005 {ECO:0000313|EMBL:AGL48931.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35102.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35102.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35102.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48931.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48931.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35102.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48931.1; -; Genomic_DNA. DR PIR; B72430; B72430. DR RefSeq; NP_227824.1; NC_000853.1. DR RefSeq; WP_004082445.1; NZ_CP011107.1. DR STRING; 243274.TM0008; -. DR EnsemblBacteria; AAD35102; AAD35102; TM_0008. DR EnsemblBacteria; AGL48931; AGL48931; Tmari_0005. DR GeneID; 896817; -. DR KEGG; tma:TM0008; -. DR KEGG; tmi:THEMA_04760; -. DR KEGG; tmm:Tmari_0005; -. DR KEGG; tmw:THMA_0004; -. DR PATRIC; 23934856; VBITheMar51294_0006. DR eggNOG; ENOG4107URK; Bacteria. DR eggNOG; COG1878; LUCA. DR OMA; APKHFNP; -. DR OrthoDB; EOG6KMB57; -. DR BioCyc; TMAR243274:GC6P-8-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004061; F:arylformamidase activity; IBA:GO_Central. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IBA:GO_Central. DR InterPro; IPR007325; KFase. DR Pfam; PF04199; Cyclase; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 224 AA; 25925 MW; D15F40453C0F9150 CRC64; MFIELSYPIE ERMLTYPDNP PDYFEPKSRI EQGDAANTMM IHHFSHTGTH VDAPYHFCEE GWTLDQIPLE YFIFEKPLLV DREKKPMELF TIEDIEELDL NGVDLLMFRS GFAKLRRTDP ATYRYMFPGI SKELARFLRE SVLSLKAVML DFLSADPIVL GEKENYPAHR WLLSKKFSSK RPIIIFEDVN LEPVAGKKIK RVIALPLRFK GLDGGPVSVL AEVE // ID Q9X167_THEMA Unreviewed; 412 AA. AC Q9X167; G4FF82; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Peptidase, M16 family {ECO:0000313|EMBL:AGL50277.1}; DE SubName: Full=Processing protease, putative {ECO:0000313|EMBL:AAD36417.1}; GN OrderedLocusNames=TM_1346 {ECO:0000313|EMBL:AAD36417.1}; GN ORFNames=Tmari_1353 {ECO:0000313|EMBL:AGL50277.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36417.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36417.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36417.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50277.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50277.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the peptidase M16 family. CC {ECO:0000256|RuleBase:RU004447}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36417.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50277.1; -; Genomic_DNA. DR PIR; B72264; B72264. DR RefSeq; NP_229147.1; NC_000853.1. DR RefSeq; WP_004081542.1; NZ_CP011107.1. DR STRING; 243274.TM1346; -. DR EnsemblBacteria; AAD36417; AAD36417; TM_1346. DR EnsemblBacteria; AGL50277; AGL50277; Tmari_1353. DR GeneID; 898134; -. DR KEGG; tma:TM1346; -. DR KEGG; tmi:THEMA_07610; -. DR KEGG; tmm:Tmari_1353; -. DR KEGG; tmw:THMA_1371; -. DR PATRIC; 23937630; VBITheMar51294_1358. DR eggNOG; ENOG4107SW5; Bacteria. DR eggNOG; COG0612; LUCA. DR OMA; VMEAARY; -. DR OrthoDB; EOG689HSK; -. DR BioCyc; TMAR243274:GC6P-1379-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. DR Gene3D; 3.30.830.10; -; 2. DR InterPro; IPR011249; Metalloenz_LuxS/M16. DR InterPro; IPR011237; Pept_M16_dom. DR InterPro; IPR011765; Pept_M16_N. DR InterPro; IPR001431; Pept_M16_Zn_BS. DR InterPro; IPR007863; Peptidase_M16_C. DR Pfam; PF00675; Peptidase_M16; 1. DR Pfam; PF05193; Peptidase_M16_C; 1. DR SUPFAM; SSF63411; SSF63411; 2. DR PROSITE; PS00143; INSULINASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD36417.1}; KW Protease {ECO:0000313|EMBL:AAD36417.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 18 154 Peptidase_M16. FT {ECO:0000259|Pfam:PF00675}. FT DOMAIN 162 318 Peptidase_M16_C. FT {ECO:0000259|Pfam:PF05193}. SQ SEQUENCE 412 AA; 47413 MW; 960FEFA37AD310E2 CRC64; MERHTVNEIE IFTIPFDKAR TISCAFLIKK GSAHEPEELA GISHFIEHMA FRGTKSYDHF SLKYTVEVVG GTLNAFTDKL ATAYYAKVPE FHFGKTLNVL KEITFYPIFS PEDTEIERKI ILEEYKMSQD DPTSKLFDTL VETVWPGPYG RPIIGRKETI EKISSEDLRE YHRKNYNLPD TKIILAGKVN DDYLSLLEKE LSELERNKPG DPLPPPPSFE HTEPRYIVRN DLEQVHIAMA RPICGRISED IYPLYALNTA LGSGMSSILF HEIREKEGFV YDVFSQIYAL KETGIIIVYA ALSPEKIDEF FSKMKDVLSN ESLFMKNFEY GKMRYLGKLD MVTDNPAGMM SFVIDDLSND SLETIEERVE RIKNVSKEDY RRAYERFIAG NWSVFGIGPE SGKIIEKHEM IV // ID Q9X021_THEMA Unreviewed; 138 AA. AC Q9X021; G4FF71; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=OsmC/Ohr family protein {ECO:0000313|EMBL:AGL49846.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36000.1}; GN OrderedLocusNames=TM_0919 {ECO:0000313|EMBL:AAD36000.1}; GN ORFNames=Tmari_0921 {ECO:0000313|EMBL:AGL49846.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36000.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36000.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36000.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49846.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49846.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36000.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49846.1; -; Genomic_DNA. DR PIR; H72316; H72316. DR RefSeq; NP_228727.1; NC_000853.1. DR RefSeq; WP_004080643.1; NZ_CP011107.1. DR PDB; 1VLA; X-ray; 1.80 A; A/B/C/D=1-138. DR PDBsum; 1VLA; -. DR STRING; 243274.TM0919; -. DR EnsemblBacteria; AAD36000; AAD36000; TM_0919. DR EnsemblBacteria; AGL49846; AGL49846; Tmari_0921. DR GeneID; 898593; -. DR KEGG; tma:TM0919; -. DR KEGG; tmi:THEMA_00040; -. DR KEGG; tmm:Tmari_0921; -. DR KEGG; tmw:THMA_0941; -. DR PATRIC; 23936769; VBITheMar51294_0933. DR eggNOG; ENOG4108UKZ; Bacteria. DR eggNOG; COG1765; LUCA. DR KO; K07397; -. DR OMA; GPRPMEM; -. DR OrthoDB; EOG6R2H4J; -. DR BioCyc; TMAR243274:GC6P-949-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.30.300.20; -; 1. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR003718; OsmC/Ohr_fam. DR Pfam; PF02566; OsmC; 1. DR SUPFAM; SSF82784; SSF82784; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VLA}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 138 AA; 16004 MW; 33E10F0D7EC9DEFD CRC64; MQARWIGNMM FHVRTDSNHD VLMDTKEEVG GKDAAPRPLE LVLTGLMGCT GMDVVSILRK MKVIDQMKDF RIEIEYERTE EHPRIFTKVH LKYIFKFDGE PPKDKVEKAV QLSQEKYCSV SAILKCSSKV TYEIVYEN // ID Q9WZH2_THEMA Unreviewed; 231 AA. AC Q9WZH2; G4FDB1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35795.1}; GN OrderedLocusNames=TM_0713 {ECO:0000313|EMBL:AAD35795.1}; GN ORFNames=Tmari_0713 {ECO:0000313|EMBL:AGL49638.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35795.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35795.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35795.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49638.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49638.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35795.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49638.1; -; Genomic_DNA. DR PIR; H72343; H72343. DR RefSeq; NP_228522.1; NC_000853.1. DR RefSeq; WP_004081024.1; NZ_CP011107.1. DR STRING; 243274.TM0713; -. DR EnsemblBacteria; AAD35795; AAD35795; TM_0713. DR EnsemblBacteria; AGL49638; AGL49638; Tmari_0713. DR GeneID; 898380; -. DR KEGG; tma:TM0713; -. DR KEGG; tmi:THEMA_01100; -. DR KEGG; tmm:Tmari_0713; -. DR KEGG; tmw:THMA_0728; -. DR PATRIC; 23936344; VBITheMar51294_0725. DR eggNOG; ENOG4105SFJ; Bacteria. DR eggNOG; ENOG4111XSN; LUCA. DR OMA; KIHAFNI; -. DR OrthoDB; EOG6WQD78; -. DR BioCyc; TMAR243274:GC6P-739-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008152; P:metabolic process; IEA:InterPro. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR SUPFAM; SSF52151; SSF52151; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 231 AA; 26919 MW; 57D6E79C3A787C6E CRC64; MLKFLKDSKV DFTVRCCGVS SIPCALFFLT RSTNRTYSIL VKEWKNIEKL LDPFFTKGID QLSMVDALRI LMRIGDTLNG VRNHERLYRY IDSLFPAQKI PGGLEIWAFD LFEGKEVVFK EGDDLRRALK ISLSFPILYR PYEDRYVPIT WITGVPEGEL TVLFDVKKEK NPPRNALEYL FLSTTARTKH LERERIKKAK SLRIACTSLS PVSTTRRAYE EFSRFFEEVV L // ID Q9WY71_THEMA Unreviewed; 285 AA. AC Q9WY71; G4FHE3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Transporter {ECO:0000313|EMBL:AGL49153.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35320.1}; GN OrderedLocusNames=TM_0229 {ECO:0000313|EMBL:AAD35320.1}; GN ORFNames=Tmari_0227 {ECO:0000313|EMBL:AGL49153.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35320.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35320.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35320.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49153.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49153.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35320.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49153.1; -; Genomic_DNA. DR PIR; G72401; G72401. DR RefSeq; NP_228043.1; NC_000853.1. DR RefSeq; WP_004082920.1; NZ_CP011107.1. DR STRING; 243274.TM0229; -. DR EnsemblBacteria; AAD35320; AAD35320; TM_0229. DR EnsemblBacteria; AGL49153; AGL49153; Tmari_0227. DR GeneID; 897128; -. DR KEGG; tma:TM0229; -. DR KEGG; tmi:THEMA_03580; -. DR KEGG; tmm:Tmari_0227; -. DR KEGG; tmw:THMA_0236; -. DR PATRIC; 23935333; VBITheMar51294_0232. DR eggNOG; ENOG4108SQR; Bacteria. DR eggNOG; COG0679; LUCA. DR KO; K07088; -. DR OMA; RTIKNAN; -. DR OrthoDB; EOG6KWXVV; -. DR BioCyc; TMAR243274:GC6P-242-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004776; Auxin_eff. DR Pfam; PF03547; Mem_trans; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 24 42 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 102 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 133 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 140 159 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 179 197 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 209 228 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 234 253 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 284 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 285 AA; 31815 MW; 1B145E756259B198 CRC64; MEFSVIILIG YLTKKFFERD TGKILSKLVV NFTLPAAIFY SFSTSRFHFS KFAFTATGIL SNLLLIFLAF LFFSRIKDPR VRIPIILSFV GFNTGLFMYP LAESLWGEAS VVNFALFDLG NSFFIFGVGK AVAEQNKKGI LKVFTFPPFL FLLVGITMNS LKVVPPGIVL DVARTIKNAN AFLVFFLVGY YLSFRSVYEK FRLILMAGLV KYAAGLLVAL IAVKIFSLSS FEEMNLFLSP LLPSAIMTLV YSVEKGYDAE LASGLITFFT IVSTSIIMAV NYTWG // ID Q9X083_THEMA Unreviewed; 1123 AA. AC Q9X083; G4FF07; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36067.1}; GN OrderedLocusNames=TM_0988 {ECO:0000313|EMBL:AAD36067.1}; GN ORFNames=Tmari_0991 {ECO:0000313|EMBL:AGL49916.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36067.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36067.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36067.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49916.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49916.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36067.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49916.1; -; Genomic_DNA. DR PIR; A72311; A72311. DR RefSeq; NP_228796.1; NC_000853.1. DR RefSeq; WP_004080572.1; NZ_CP011107.1. DR STRING; 243274.TM0988; -. DR EnsemblBacteria; AAD36067; AAD36067; TM_0988. DR EnsemblBacteria; AGL49916; AGL49916; Tmari_0991. DR GeneID; 898716; -. DR KEGG; tma:TM0988; -. DR KEGG; tmi:THEMA_09410; -. DR KEGG; tmm:Tmari_0991; -. DR KEGG; tmw:THMA_1010; -. DR PATRIC; 23936905; VBITheMar51294_1001. DR eggNOG; ENOG41073NT; Bacteria. DR eggNOG; COG1483; LUCA. DR KO; K06922; -. DR OMA; FKRTYFT; -. DR OrthoDB; EOG6BGNWF; -. DR BioCyc; TMAR243274:GC6P-1018-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR007555; DUF499. DR Pfam; PF04465; DUF499; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 1123 AA; 129351 MW; 06D76F6EECD67890 CRC64; MKFGPYEVWE DVLDESFDSQ VAPELGDVYT GEAPEIYRDP KEFFKRTYFT DATVEILKRI LDTFEGKERR NIFLIYSLFG GGKTHLLLTL YHAFKTPEAL EDPEVLEGYI PEKRETIREL AERIKLLGES VKVVPVYGKG RVGQPSIPLN VDPYSVKTIW GYIAHSLGKY SIVEKNDKNL TVPDIETLRD LFKGERVLLL IDEIADYVDN LHNSGAEEDR RYAGNVDNFI DRLSSALSNS TSSMVITLPM TEERGNLRTQ EEYNHSVVRA LWDAVRRVGG ADSYTPVRTV GINDELVEVL KKRIFKHVDP DIRRRTLERI RSETNDVEIF GHGGFAQEIP RTYPFHPEYI QILRTIIEKT DLQRTRDMIR ITRIVVRNLI DRYEKEGFAP AIILPIHIDL TNDRIRGMLF GEKSKFADYA SIIDAELVND EKYRAFRHPE LARMILTYIF LRTYPFDAPT PLNDFPTLTT ISRAIYDPET FSKKQWIPAD IKDTVEEIES HPHFVFLNRK DGVFWFWRVA NVTKMVDSKT EELIQSNYGE IWNQLVRYVD QLVREKKSIA TTRGKGSTVE EHVRFFEQVI VSKEPQELMD NEMYKLFVLV SEDVDEKLLK GIVFQIGSGS RTYKNTVVVC YPIPGTMKHL IMTTARDMAC QRVMDTVKEM YGKYGEDVVK IQLNQLRDIR NRALEDLENQ IVGSFRKVAY PVKDGIDTAD APASSKSVVE NVYSALKGRG KIAEEFDFIE FANWLKENIG LNILKPEGYC VSELRKIICS NPSAPMVDFE NLKKSIKEAV RKLKIGLERK GKILFKRVYS EIPDFAQESG VEISKVEPDD IILPANEALR RQVCELLKQE KDEIRDGKRY RVWYEIYLPS SEFSELLKNL VTVENEECQI GDEEAVMYGL ILEKKEEVEI KKGEFDLEVA RRSVEGKPGE KVEIPVRITA FGDAEIELSS EYGELSYQNV FLREGESLEI LWNMTIPSEK KVVKIEAKSE EKMIPKEIVL VPKVESSVLE TNTLDETHKG MFLVSVKSIR DLDTLKSLPE DFEGVVSGRL ETEKPEWKVQ FSETDRKTFE YIAGELEDFL GTKALLDVNF RLSEPQMIND LIFEKLKPLN GKVSFILKKG DQK // ID Q9X0B5_THEMA Unreviewed; 32 AA. AC Q9X0B5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36102.1}; GN OrderedLocusNames=TM_1025 {ECO:0000313|EMBL:AAD36102.1}; GN ORFNames=Tmari_1027 {ECO:0000313|EMBL:AGL49951.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36102.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36102.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36102.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49951.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49951.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36102.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49951.1; -; Genomic_DNA. DR PIR; H72302; H72302. DR RefSeq; NP_228831.1; NC_000853.1. DR RefSeq; WP_010865246.1; NZ_CP011107.1. DR STRING; 243274.TM1025; -. DR EnsemblBacteria; AAD36102; AAD36102; TM_1025. DR EnsemblBacteria; AGL49951; AGL49951; Tmari_1027. DR GeneID; 897702; -. DR KEGG; tma:TM1025; -. DR KEGG; tmm:Tmari_1027; -. DR KEGG; tmw:THMA_1046; -. DR BioCyc; TMAR243274:GC6P-1054-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 32 AA; 3898 MW; EE9C827F3A6DFC4B CRC64; MRQKPSPSLW FPERKLTNEN LARKNHPVFD FL // ID Q9WZZ4_THEMA Unreviewed; 201 AA. AC Q9WZZ4; G4FCT3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=CBS domain containing protein {ECO:0000313|EMBL:AGL49819.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35973.1}; GN OrderedLocusNames=TM_0892 {ECO:0000313|EMBL:AAD35973.1}; GN ORFNames=Tmari_0894 {ECO:0000313|EMBL:AGL49819.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35973.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35973.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35973.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49819.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49819.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35973.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49819.1; -; Genomic_DNA. DR PIR; E72321; E72321. DR RefSeq; NP_228700.1; NC_000853.1. DR RefSeq; WP_004080692.1; NZ_CP011107.1. DR PDB; 1VR9; X-ray; 1.70 A; A/B=1-201. DR PDBsum; 1VR9; -. DR STRING; 243274.TM0892; -. DR EnsemblBacteria; AAD35973; AAD35973; TM_0892. DR EnsemblBacteria; AGL49819; AGL49819; Tmari_0894. DR GeneID; 898566; -. DR KEGG; tma:TM0892; -. DR KEGG; tmi:THEMA_00175; -. DR KEGG; tmm:Tmari_0894; -. DR KEGG; tmw:THMA_0914; -. DR PATRIC; 23936715; VBITheMar51294_0906. DR eggNOG; ENOG4108V83; Bacteria. DR eggNOG; COG0517; LUCA. DR KO; K04767; -. DR OMA; FLEHQEP; -. DR OrthoDB; EOG64V2CM; -. DR BioCyc; TMAR243274:GC6P-922-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008152; P:metabolic process; IEA:InterPro. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF01842; ACT; 1. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS51371; CBS; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VR9}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 62 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 63 122 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 128 201 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 201 AA; 22892 MW; 3A8B426BFBD2A382 CRC64; MKVKKWVTQD FPMVEESATV RECLHRMRQY QTNECIVKDR EGHFRGVVNK EDLLDLDLDS SVFNKVSLPD FFVHEEDNIT HALLLFLEHQ EPYLPVVDEE MRLKGAVSLH DFLEALIEAL AMDVPGIRFS VLLEDKPGEL RKVVDALALS NINILSVITT RSGDGKREVL IKVDAVDEGT LIKLFESLGI KIESIEKEEG F // ID Q9X0A6_THEMA Unreviewed; 835 AA. AC Q9X0A6; G4FEY4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36090.1}; GN OrderedLocusNames=TM_1013 {ECO:0000313|EMBL:AAD36090.1}; GN ORFNames=Tmari_1016 {ECO:0000313|EMBL:AGL49940.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36090.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36090.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36090.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49940.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49940.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36090.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49940.1; -; Genomic_DNA. DR PIR; E72305; E72305. DR RefSeq; NP_228819.1; NC_000853.1. DR RefSeq; WP_004080523.1; NZ_CP011107.1. DR STRING; 243274.TM1013; -. DR EnsemblBacteria; AAD36090; AAD36090; TM_1013. DR EnsemblBacteria; AGL49940; AGL49940; Tmari_1016. DR GeneID; 897156; -. DR KEGG; tma:TM1013; -. DR KEGG; tmi:THEMA_09290; -. DR KEGG; tmm:Tmari_1016; -. DR KEGG; tmw:THMA_1035; -. DR PATRIC; 23936955; VBITheMar51294_1026. DR eggNOG; ENOG41090BK; Bacteria. DR eggNOG; ENOG4111Q1C; LUCA. DR OMA; EFFRETS; -. DR OrthoDB; EOG6FRCRT; -. DR BioCyc; TMAR243274:GC6P-1042-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 835 AA; 95101 MW; 828A361521FA0847 CRC64; MIKRLFFAVV LLLVAELFSG VLHFEHADVV YPEGYFENAV LVGNIFEAIR PKVIELVGND PGRITIVLKD RGTISNGYTM PFFHKTIVVY LWPPESWLSF RLSLEDWYAY VLIHEFSHMC HLTYQDEIGK TVTKLTGIPL YPQLFSDLVE GVTVFNESSF SISSGRLNNP FFSNGLFYYS LPNFPSPGYI KVAPDDDYRD GLLYYNFTAG FYSYLVETYG LEKVKEFFRE TSKTFSTFAF EGFKDPYEKV FGKTREEIYT DWIYSLTKHE YPQGDLVYSA KNTWLHKIDL YGDHLVVLSE EYGPSTSYTG MKKQILKILD LDGKEVQKIP VRNVLDVKID GEKIYVLTKE KSFNRYENVL WDVKGGRQIS KGNISAFDVE NGKVYLAFYD TKTGKATIEG SEFHTTLDEF IRYMDVSDRF VALFTEKNDI IVLKTNGEVI LELKNETMKG PYVKFWKDGI IFVQVEGEHT VPCYYDLEKK ELHRLSSKSL VEDFVIQGSE IYYISYIPYG QTGGTGVYRK DLSMEPVVVE VKKSEPFVIE GKKFSTGNEF GFRLRKFFQP AMWFPVYFDN AFSLFLMFSN VENNTFLFLM PSVDLKGNFN QYTGFVASRD NFTAYGEYSS SGDYSFGLTG VLGDFPVSAN TRLDVTFEMN FSSTQTSLNS EAGAANNIGV GVDLRTYLLD MPSSLKVSLN LLNDDLSHLF DLNSLFCFAG LTSALGKDGS FSANIKFQLL NSEDFSYDVS FAQTLFKNSA ELFDGFILLR NTGNTLGIAR LRFSNGEEEH VIYDHLFQEV YMEGLKFYIT VGGFLNMNDI SSGSFYVGIS TSPNGLPSIS LFIRN // ID Q9X0Q6_THEMA Unreviewed; 117 AA. AC Q9X0Q6; G4FEH2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36249.1}; GN OrderedLocusNames=TM_1174 {ECO:0000313|EMBL:AAD36249.1}; GN ORFNames=Tmari_1181 {ECO:0000313|EMBL:AGL50105.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36249.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36249.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36249.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50105.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50105.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36249.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50105.1; -; Genomic_DNA. DR PIR; A72286; A72286. DR RefSeq; NP_228979.1; NC_000853.1. DR RefSeq; WP_004080190.1; NZ_CP011107.1. DR STRING; 243274.TM1174; -. DR EnsemblBacteria; AAD36249; AAD36249; TM_1174. DR EnsemblBacteria; AGL50105; AGL50105; Tmari_1181. DR GeneID; 898312; -. DR KEGG; tma:TM1174; -. DR KEGG; tmi:THEMA_08465; -. DR KEGG; tmm:Tmari_1181; -. DR KEGG; tmw:THMA_1199; -. DR PATRIC; 23937288; VBITheMar51294_1192. DR eggNOG; ENOG4108YKY; Bacteria. DR eggNOG; COG1148; LUCA. DR OMA; IRNMNTE; -. DR OrthoDB; EOG64XXPR; -. DR BioCyc; TMAR243274:GC6P-1203-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 117 AA; 13155 MW; CE56FB4295A4CCA9 CRC64; MGKKGLLLCV CQGTCPSFQK MNIFEVLNTL RREKVVDFVA IHPQLCSDDG DVFLQELLKG ADVEKLYVAG CDPTMQRKMF RDAFEAAGFD KEKHVGVDIR NMTTDEAVKA IKEVLEK // ID Q9X2F5_THEMA Unreviewed; 833 AA. AC Q9X2F5; G4FGM2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE SubName: Full=Maltose ABC transporter, permease protein {ECO:0000313|EMBL:AAD36899.1}; DE SubName: Full=Maltose/maltodextrin ABC transporter, permease protein MalG {ECO:0000313|EMBL:AGL50769.1}; GN OrderedLocusNames=TM_1836 {ECO:0000313|EMBL:AAD36899.1}; GN ORFNames=Tmari_1845 {ECO:0000313|EMBL:AGL50769.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36899.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36899.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36899.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50769.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50769.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36899.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50769.1; -; Genomic_DNA. DR PIR; H72205; H72205. DR RefSeq; NP_229633.1; NC_000853.1. DR RefSeq; WP_004082381.1; NZ_CP011107.1. DR STRING; 243274.TM1836; -. DR TCDB; 3.A.1.1.22; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36899; AAD36899; TM_1836. DR EnsemblBacteria; AGL50769; AGL50769; Tmari_1845. DR GeneID; 897399; -. DR KEGG; tma:TM1836; -. DR KEGG; tmm:Tmari_1845; -. DR KEGG; tmw:THMA_1880; -. DR PATRIC; 23938659; VBITheMar51294_1856. DR eggNOG; ENOG4105EG2; Bacteria. DR eggNOG; COG3833; LUCA. DR KO; K10110; -. DR OMA; FPAIMYM; -. DR OrthoDB; EOG60PHFH; -. DR BioCyc; TMAR243274:GC6P-1887-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0015609; F:maltooligosaccharide-importing ATPase activity; IBA:GO_Central. DR GO; GO:0015423; F:maltose-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0042956; P:maltodextrin transport; IBA:GO_Central. DR GO; GO:0015768; P:maltose transport; IBA:GOC. DR GO; GO:0015772; P:oligosaccharide transport; IBA:GOC. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 620 644 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 656 680 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 686 708 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 739 760 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 797 818 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 621 818 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. FT COILED 98 125 {ECO:0000256|SAM:Coils}. FT COILED 217 258 {ECO:0000256|SAM:Coils}. FT COILED 391 425 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 833 AA; 94862 MW; E85DAA174FD92854 CRC64; MMVRKKNRWL THVLLTLLVV VVLFPIVWVV STSFRRDEAA FSPKLFSSRL TLQHYKDLVA PEKNLPVLIQ EMQSLVSRVE PFDNVSREKA DRLIEDRIRR FENYLAETKK LLEDVNARNS KIEETLSQRF SDVLSYTKDV LEEAKKLTQE QMDKTPLPDS QRIAVALYEK LKGKNFRSAE FQALKDVIEK VVGYSVENQD TLNDALSELG LVYEKEVGTL MKEIEKLEGE IEILQREIAV LEKQKETLEK EILEKQKVLE VLKPDIDSVS EVLVKLKEMV HSVRNSKVET AFPYEDSRLK SSLEKLLSEL NTLYDKISAF SDLSDLSEKI FAMKSSLEEI NNVVSEDGDI SKKALYGSFV QSFEETVPII EGIVEKVSDG IDDFVQKIKD LKDIENEIMV LTAKLDGLEK SLNNVRSSLS EKEKEISSAK MYLDLKIFNH QIQSRIDSLE SMKSFNNAAQ IKLLSIYKTL KNFVSSYVSE YGGDDFIGKI RKLAAKLSWI EDYRDLNRRI ETGYKNAVEI VEKAQNILDD FKGSYSNLLD LSFKGLYVSS EHLEMLYDLV KMNFVQEVLT NTAVASRKAG TLMDTIPLKE LKSDLKKIDG DLYRLAQIWE QKTKHYFLRW VMNSVIVAGL VSLITTAVCA LAAYPFSRMR FWGRQYGIMA LLLIQMFPAI MYMVAIYGLL KLIGQFLPFL GLDSLGGLIF AYLGNIAYNM YLIKGFYDTI PSSLEEAAMI DGATRFQTFY KIVVPLALPI LTVIVILTFI GTFNEFVLAR IILQDVKNYT YALGLWTFST GAYETEWGLF TAAALLGMTP MVILFLSLQK YIVGGLTKGS VKG // ID Q9WY17_THEMA Unreviewed; 73 AA. AC Q9WY17; G4FH84; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35263.1}; GN OrderedLocusNames=TM_0170 {ECO:0000313|EMBL:AAD35263.1}; GN ORFNames=Tmari_0168 {ECO:0000313|EMBL:AGL49094.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35263.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35263.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35263.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49094.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49094.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35263.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49094.1; -; Genomic_DNA. DR PIR; H72408; H72408. DR RefSeq; NP_227985.1; NC_000853.1. DR RefSeq; WP_004082801.1; NZ_CP011107.1. DR STRING; 243274.TM0170; -. DR EnsemblBacteria; AAD35263; AAD35263; TM_0170. DR EnsemblBacteria; AGL49094; AGL49094; Tmari_0168. DR GeneID; 897009; -. DR KEGG; tma:TM0170; -. DR KEGG; tmi:THEMA_03950; -. DR KEGG; tmm:Tmari_0168; -. DR KEGG; tmw:THMA_0166; -. DR PATRIC; 23935188; VBITheMar51294_0171. DR eggNOG; ENOG4106EZY; Bacteria. DR eggNOG; ENOG410Y2BK; LUCA. DR OMA; EDVHILN; -. DR OrthoDB; EOG6C8N4H; -. DR BioCyc; TMAR243274:GC6P-171-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR032587; DUF4911. DR Pfam; PF16256; DUF4911; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 73 AA; 8598 MW; 6E91344DE6571D73 CRC64; MEYDVYVRVS KEDVHLLNYL LEVEEHMFNI RKYEDGVLKI ITPFPEEAIK LLEGCKEMVD LEILEVKENP GEA // ID Q9X2E7_THEMA Unreviewed; 190 AA. AC Q9X2E7; G4FGL4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Riboflavin synthase alpha chain {ECO:0000313|EMBL:AGL50761.1}; DE EC=2.5.1.9 {ECO:0000313|EMBL:AGL50761.1}; DE SubName: Full=Riboflavin synthase, alpha subunit {ECO:0000313|EMBL:AAD36890.1}; GN OrderedLocusNames=TM_1827 {ECO:0000313|EMBL:AAD36890.1}; GN ORFNames=Tmari_1837 {ECO:0000313|EMBL:AGL50761.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36890.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36890.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36890.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50761.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50761.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36890.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50761.1; -; Genomic_DNA. DR PIR; F72207; F72207. DR RefSeq; NP_229624.1; NC_000853.1. DR RefSeq; WP_004082373.1; NZ_CP011107.1. DR STRING; 243274.TM1827; -. DR DNASU; 897821; -. DR EnsemblBacteria; AAD36890; AAD36890; TM_1827. DR EnsemblBacteria; AGL50761; AGL50761; Tmari_1837. DR GeneID; 897821; -. DR KEGG; tma:TM1827; -. DR KEGG; tmi:THEMA_05060; -. DR KEGG; tmm:Tmari_1837; -. DR KEGG; tmw:THMA_1872; -. DR PATRIC; 23938641; VBITheMar51294_1847. DR eggNOG; ENOG4108R6K; Bacteria. DR eggNOG; COG0307; LUCA. DR KO; K00793; -. DR OMA; PHTAHAT; -. DR OrthoDB; EOG6VMTQH; -. DR BioCyc; TMAR243274:GC6P-1878-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-EC. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro. DR Gene3D; 2.40.30.20; -; 2. DR InterPro; IPR023366; ATPase_asu-like. DR InterPro; IPR001783; Lumazine-bd. DR InterPro; IPR026017; Lumazine-bd_dom. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR21098; PTHR21098; 1. DR Pfam; PF00677; Lum_binding; 2. DR PIRSF; PIRSF000498; Riboflavin_syn_A; 1. DR SUPFAM; SSF63380; SSF63380; 2. DR PROSITE; PS51177; LUMAZINE_BIND; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL50761.1}. FT DOMAIN 1 85 Lumazine-binding. FT {ECO:0000259|PROSITE:PS51177}. FT DOMAIN 86 181 Lumazine-binding. FT {ECO:0000259|PROSITE:PS51177}. FT REGION 4 6 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000498-1}. FT REGION 39 41 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000498-1}. FT REGION 53 58 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000498-1}. SQ SEQUENCE 190 AA; 21678 MW; 3E20EEA174E9989D CRC64; MFTGIVQKVE RGHIRGERIF FKRTWEVKLG ESIAVNGVCL TVSGLSEEEY WFDVGEETRR RTNLFVSRFY NLEKSLALGS RVEGHLVTGH VDGTVRFVGM ERRGNSYFMF FSMPSERWAI VPKGSITLNG ISLTVVETSL DTFSVQVIPH TFENTNLQYL VPGDPVNYEI DIIARYLKGV IDRGRTERGF // ID Q9WZI6_THEMA Unreviewed; 435 AA. AC Q9WZI6; G4FD96; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=PmbA-related protein {ECO:0000313|EMBL:AAD35809.1}; DE SubName: Full=TldE/PmbA protein, part of proposed TldE/TldD proteolytic complex {ECO:0000313|EMBL:AGL49653.1}; GN OrderedLocusNames=TM_0727 {ECO:0000313|EMBL:AAD35809.1}; GN ORFNames=Tmari_0728 {ECO:0000313|EMBL:AGL49653.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35809.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35809.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35809.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49653.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49653.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35809.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49653.1; -; Genomic_DNA. DR PIR; E72342; E72342. DR RefSeq; NP_228536.1; NC_000853.1. DR RefSeq; WP_004081001.1; NZ_CP011107.1. DR PDB; 1VL4; X-ray; 1.95 A; A/B=1-435. DR PDBsum; 1VL4; -. DR STRING; 243274.TM0727; -. DR MEROPS; U62.004; -. DR EnsemblBacteria; AAD35809; AAD35809; TM_0727. DR EnsemblBacteria; AGL49653; AGL49653; Tmari_0728. DR GeneID; 898394; -. DR KEGG; tma:TM0727; -. DR KEGG; tmi:THEMA_01025; -. DR KEGG; tmm:Tmari_0728; -. DR KEGG; tmw:THMA_0743; -. DR PATRIC; 23936374; VBITheMar51294_0740. DR eggNOG; ENOG4105CMS; Bacteria. DR eggNOG; COG0312; LUCA. DR KO; K03592; -. DR OMA; YSYTEKL; -. DR OrthoDB; EOG65J4ZF; -. DR BioCyc; TMAR243274:GC6P-753-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR InterPro; IPR002510; TldD/PmbA. DR Pfam; PF01523; PmbA_TldD; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VL4}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 435 AA; 48306 MW; C8764A342A975819 CRC64; MTFEEFKDRL FALAKKNGVE VQISFLETRE FSLRLANGDL DQYTDAGKFN VEIKVLKDGK TGTFRTQVLE NPEKCFEEAL SNLQVKDSEE KEYFFEGGKE YREMETYVGR FEKLSVKEKM DMAKKAHESA AKDERVVMVP TVMYKDMVIK KIITNTLGLD VESQMDGGFL FAMAIARDAN PRSGSWYELA RTPEDLNPEE IGKRAAEEAI SLIGSKTIPS GKYPVLMRNT ALLDLMEMFI PMISAENVQK NLSPLKGKLG EQVGNPAVSI KDLPYHPKGL SSTPFDDEGV PTTEKFVLEN GVLKTFLHNL KTARKEGVEP TGNGFVGGIR PVNLMLMPGE KSFEELLKEM DRGVVITEVE GMHAGANSIS GEFSLFAKGY WVENGEIAHG VEDITISGNF LDLLRKIVLV GNDVKVSQHT IAPSVLVEVL DVAGK // ID Q9X2J1_THEMA Unreviewed; 508 AA. AC Q9X2J1; G4FGS0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 106. DE SubName: Full=UDP-sugar hydrolase {ECO:0000313|EMBL:AAD36940.1}; DE SubName: Full=UDP-sugar hydrolase 5-nucleotidase {ECO:0000313|EMBL:AGL50817.1}; DE EC=3.1.3.5 {ECO:0000313|EMBL:AGL50817.1}; DE EC=3.6.1.45 {ECO:0000313|EMBL:AGL50817.1}; GN OrderedLocusNames=TM_1878 {ECO:0000313|EMBL:AAD36940.1}; GN ORFNames=Tmari_1893 {ECO:0000313|EMBL:AGL50817.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36940.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36940.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36940.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50817.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50817.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. CC {ECO:0000256|RuleBase:RU362119}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36940.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50817.1; -; Genomic_DNA. DR PIR; A72201; A72201. DR RefSeq; NP_229674.1; NC_000853.1. DR RefSeq; WP_004082429.1; NZ_CP011107.1. DR STRING; 243274.TM1878; -. DR EnsemblBacteria; AAD36940; AAD36940; TM_1878. DR EnsemblBacteria; AGL50817; AGL50817; Tmari_1893. DR GeneID; 897447; -. DR KEGG; tma:TM1878; -. DR KEGG; tmi:THEMA_04780; -. DR KEGG; tmm:Tmari_1893; -. DR KEGG; tmw:THMA_1928; -. DR PATRIC; 23938745; VBITheMar51294_1899. DR eggNOG; ENOG4105CGH; Bacteria. DR eggNOG; COG0737; LUCA. DR KO; K11751; -. DR OMA; AADYEPK; -. DR OrthoDB; EOG696BW0; -. DR BioCyc; TMAR243274:GC6P-1929-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProtKB-EC. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro. DR Gene3D; 3.60.21.10; -; 1. DR Gene3D; 3.90.780.10; -; 1. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006179; 5_nucleotidase/apyrase. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR PANTHER; PTHR11575; PTHR11575; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR SUPFAM; SSF55816; SSF55816; 1. DR SUPFAM; SSF56300; SSF56300; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|RuleBase:RU362119, KW ECO:0000313|EMBL:AAD36940.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 22 238 Metallophos. {ECO:0000259|Pfam:PF00149}. FT DOMAIN 322 470 5_nucleotid_C. FT {ECO:0000259|Pfam:PF02872}. SQ SEQUENCE 508 AA; 56490 MW; CB6C97ADDE8CBB6F CRC64; MRKFLVILLA LLITALLLGA RLTILHVNDT HGHAWAFDEY RNPGIGGLAT IATIVEEVKR EVESQGGYVI FLHAGDLNTG VPESDLQDAI PDIVGFNMMG LKAMAVGNHE FDNPREVLEK QMKFADFPFL SANIVKEDGE PFFNPYIVED LGELKIAIIG FTTEETEILE PLYLEGLKFE NALKVAQKIA PELKKQADVV IALAHLDWGE PKKEDITTTH QLAGVEGIDV VIAGHSHVLG SDVVDGKIIA SAGEYGKYVG RLDLDIEDGK IVAWHWEAIP VNLKVYENEK YRYLGKPYLE NRYVAKALEY FKKVGNEKLD TVIGETKIYL DGEREHVRSK STNLANLIVD AMRWKVGADI AFTNGGGIRA SIKPGKITVR DILTVLPFGN TLYVLELTGE QIMKVLEYAA TIPEGKGAFL QVSGLTWKSK DGKVVEVLVN GEPLDPEKKY KVVTNNYMAG GGDGYVMFKE WDGYDTGYLM SDAVIEYIQN VLNGKIEEYD DSQRYVRE // ID Q9WZX3_THEMA Unreviewed; 317 AA. AC Q9WZX3; G4FCV5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 112. DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003881}; DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003881}; GN OrderedLocusNames=TM_0869 {ECO:0000313|EMBL:AAD35951.1}; GN ORFNames=Tmari_0871 {ECO:0000313|EMBL:AGL49796.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35951.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35951.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35951.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49796.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49796.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide CC + NADPH. {ECO:0000256|RuleBase:RU003881}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003881}; CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881}; CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000256|RuleBase:RU003880}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35951.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49796.1; -; Genomic_DNA. DR PIR; H72322; H72322. DR RefSeq; NP_228678.1; NC_000853.1. DR RefSeq; WP_004080734.1; NZ_CP011107.1. DR STRING; 243274.TM0869; -. DR EnsemblBacteria; AAD35951; AAD35951; TM_0869. DR EnsemblBacteria; AGL49796; AGL49796; Tmari_0871. DR GeneID; 898542; -. DR KEGG; tma:TM0869; -. DR KEGG; tmi:THEMA_00290; -. DR KEGG; tmm:Tmari_0871; -. DR KEGG; tmw:THMA_0891; -. DR PATRIC; 23936666; VBITheMar51294_0882. DR eggNOG; ENOG4105C3M; Bacteria. DR eggNOG; COG0492; LUCA. DR KO; K00384; -. DR OMA; TDSGQVW; -. DR OrthoDB; EOG65XN2W; -. DR BioCyc; TMAR243274:GC6P-899-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS. DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2. DR InterPro; IPR005982; Thioredox_Rdtase. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00469; PNDRDTASEII. DR SUPFAM; SSF51905; SSF51905; 1. DR TIGRFAMs; TIGR01292; TRX_reduct; 1. DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW FAD {ECO:0000256|RuleBase:RU003880}; KW Flavoprotein {ECO:0000256|RuleBase:RU003880}; KW NADP {ECO:0000256|RuleBase:RU003881}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003880, KW ECO:0000313|EMBL:AGL49796.1}; KW Redox-active center {ECO:0000256|RuleBase:RU003880}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 18 305 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. SQ SEQUENCE 317 AA; 34348 MW; 11E19E491A8B580D CRC64; MVFFDTGSLK KKEIKDKYDI VVVGGGPAGL TSAIYARRAG LSVLVVEKAI EGGYVNLTHL VENYPGFPAI SGEELASKFK EHAEKFGADI YNAEVVKLEV QGDKKVVELD DGKRIEAPVV IVATGANPKK LNVPGEKEFF GKGVSYCATC DGYLFAGKDV IVVGGGDSAC DESIFLSNIV NKITMIQLLE TLTAAKVLQE RVLNNPKIEV IYNSTVREIR GKDKVEEVVI ENVKTGETKV LKADGVFIFI GLDPNSKLLE GLVELDPYGY VITDENMETS VKGIYAVGDV RKKNLRQIVT AVADGAIAVE HAAKHYF // ID Q9X0T8_THEMA Unreviewed; 466 AA. AC Q9X0T8; G4FED5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 105. DE SubName: Full=NADH dehydrogenase, putative {ECO:0000313|EMBL:AAD36286.1}; GN OrderedLocusNames=TM_1211 {ECO:0000313|EMBL:AAD36286.1}; GN ORFNames=Tmari_1218 {ECO:0000313|EMBL:AGL50142.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36286.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36286.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36286.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50142.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50142.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000320}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU000320}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36286.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50142.1; -; Genomic_DNA. DR PIR; A72281; A72281. DR RefSeq; NP_229016.1; NC_000853.1. DR RefSeq; WP_004080096.1; NZ_CP011107.1. DR STRING; 243274.TM1211; -. DR DNASU; 898273; -. DR EnsemblBacteria; AAD36286; AAD36286; TM_1211. DR EnsemblBacteria; AGL50142; AGL50142; Tmari_1218. DR GeneID; 898273; -. DR KEGG; tma:TM1211; -. DR KEGG; tmi:THEMA_08275; -. DR KEGG; tmm:Tmari_1218; -. DR KEGG; tmw:THMA_1237; -. DR PATRIC; 23937364; VBITheMar51294_1229. DR eggNOG; ENOG4107T0M; Bacteria. DR eggNOG; COG0651; LUCA. DR KO; K00343; -. DR KO; K05568; -. DR OMA; CGFFSKW; -. DR OrthoDB; EOG6S267X; -. DR BioCyc; TMAR243274:GC6P-1241-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR001750; ND/Mrp_mem. DR Pfam; PF00361; Proton_antipo_M; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 47 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 68 88 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 108 132 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 165 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 171 197 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 217 235 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 241 259 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 310 326 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 338 359 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 375 393 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 414 432 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 113 386 Proton_antipo_M. FT {ECO:0000259|Pfam:PF00361}. SQ SEQUENCE 466 AA; 50844 MW; C5C5C074281B9588 CRC64; MISLLVAVPL LAAFVSLFWK KASDVLFSLV ALFNVIVVLS KWFPGVVEIH AMGNWKPPFG INLVLDDASF YAALIVNLIF LMVSFLPVET KKGYETSLML LLGATNGFVL TGDLFNSFVF MEIITITAVT TAAKRENFYN AYKYLILGGI AGSFYLLATI FAYGATGSLN MAHIAMVGLS GSSLLAVTML YTIGLGVEAK LFPLNGWVPG VYGGNEVSPI VLGTAVSFAA LYMLGRLFGT VFHGSGLNTL YVLSLVTILT GEMAALRESR LLRTFAYSSV AQAGVVAAMI SKGTENALNL AYFHLTNDVI AKFVIFLVAG FLVYSYRDLN GVFRKHKLLG ISFSMATFSL VGFPMFAGFQ SKIRMIMEAF STKDFLFPAV LLIATAIEVG YVIRWNVRLW FEEETFEERS KVPLTIGFFS FALAILLVVV FLQPDVFLEG TQKMAKALLD TESYVNGVFS AVKGGM // ID Q9WYS5_THEMA Unreviewed; 458 AA. AC Q9WYS5; G4FE26; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:AAD35529.1}; DE EC=4.3.1.1 {ECO:0000313|EMBL:AGL49366.1}; GN OrderedLocusNames=TM_0444 {ECO:0000313|EMBL:AAD35529.1}; GN ORFNames=Tmari_0441 {ECO:0000313|EMBL:AGL49366.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35529.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35529.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35529.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49366.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49366.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35529.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49366.1; -; Genomic_DNA. DR PIR; G72377; G72377. DR RefSeq; NP_228254.1; NC_000853.1. DR RefSeq; WP_004081522.1; NZ_CP011107.1. DR STRING; 243274.TM0444; -. DR EnsemblBacteria; AAD35529; AAD35529; TM_0444. DR EnsemblBacteria; AGL49366; AGL49366; Tmari_0441. DR GeneID; 897462; -. DR KEGG; tma:TM0444; -. DR KEGG; tmi:THEMA_02505; -. DR KEGG; tmm:Tmari_0441; -. DR KEGG; tmw:THMA_0450; -. DR PATRIC; 23935773; VBITheMar51294_0450. DR eggNOG; ENOG4108IJ0; Bacteria. DR eggNOG; COG1027; LUCA. DR KO; K01744; -. DR OMA; PEAMNQT; -. DR OrthoDB; EOG6V1M4M; -. DR BioCyc; TMAR243274:GC6P-459-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC. DR GO; GO:0006106; P:fumarate metabolic process; IBA:GO_Central. DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central. DR GO; GO:0051262; P:protein tetramerization; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR Gene3D; 1.10.275.10; -; 1. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR PANTHER; PTHR11444; PTHR11444; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000313|EMBL:AAD35529.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 10 335 Lyase_1. {ECO:0000259|Pfam:PF00206}. FT COILED 147 170 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 458 AA; 51128 MW; E00593A3AC69AEE2 CRC64; MRKERDYLGK LEIEGEVYYG IHTKRALMNF PSTGEKLDET FIWAYFMVKK ACALLNTELG YLDERTGNAI VKACDEWEDL KKHVVVDPLS GGAGTSINMN VNEVIANRAT EILGGKKGEY LVDPIDHVNL HQSTNDTFPT SAKIATIVKL RRLIDEVINL QEKIQEKEKE FYSIRKPGRT QLMDGPPIML GQEFGAFADA LARDRWRLYK VEERIRSVNI GGTAIGTGVG APKDYILKIV EKVREVTKVK IAKAENLIDA TQNWDVFAEV HGLLKSLAVN LYKISNDIRL LGSGPNTVIG ELILPAVQAG SSIMPGKINP VVSEYVMQIC HMVFGHDMIL NHACALGNLE LNQFAPLIVH LTLKSLTLLT NACRSLASYI SKIKANNERC EEHLRRSVSN LTPLIKLFGY EAVSEAIKKA NWDIKKAVEI LSQEKNIPVE EILKVLNLKK MTGLGYSL // ID Q9X0B3_THEMA Unreviewed; 173 AA. AC Q9X0B3; G4FEX5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Putative phosphotransbutyrylase {ECO:0000313|EMBL:AGL49949.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36100.1}; GN OrderedLocusNames=TM_1023 {ECO:0000313|EMBL:AAD36100.1}; GN ORFNames=Tmari_1025 {ECO:0000313|EMBL:AGL49949.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36100.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36100.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36100.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49949.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49949.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36100.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49949.1; -; Genomic_DNA. DR PIR; F72302; F72302. DR RefSeq; NP_228829.1; NC_000853.1. DR RefSeq; WP_004080506.1; NZ_CP011107.1. DR STRING; 243274.TM1023; -. DR EnsemblBacteria; AAD36100; AAD36100; TM_1023. DR EnsemblBacteria; AGL49949; AGL49949; Tmari_1025. DR GeneID; 898733; -. DR KEGG; tma:TM1023; -. DR KEGG; tmi:THEMA_09245; -. DR KEGG; tmm:Tmari_1025; -. DR KEGG; tmw:THMA_1044; -. DR PATRIC; 23936975; VBITheMar51294_1036. DR eggNOG; ENOG4105S2W; Bacteria. DR eggNOG; COG5652; LUCA. DR OMA; KTAHFGL; -. DR OrthoDB; EOG6C5RTH; -. DR BioCyc; TMAR243274:GC6P-1052-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR016747; Phosphotransbutyrylase. DR InterPro; IPR006976; VanZ-like. DR Pfam; PF04892; VanZ; 1. DR PIRSF; PIRSF019083; UCP019083_VanZ; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 81 98 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 163 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 9 156 VanZ. {ECO:0000259|Pfam:PF04892}. SQ SEQUENCE 173 AA; 20275 MW; 594F78645FF65422 CRC64; MKRSFLVLTL ILMWIGLVFF FSSQPPDVSG RQSGNVYKFL KKVDNVLDFT QTRWYRNLRS LLEKWWFPDK KPTGEDLVRK SAHFGLYFIM GILSFTFSYT YLRKYVFSIL MGVSLPTLIA VLDEYNQSFR GRGASLYDVI VDMNGAVIGT VLIFLFLLTL KLFKRRGLRR RIL // ID Q9X0W8_THEMA Unreviewed; 144 AA. AC Q9X0W8; G4FEA6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36316.1}; GN OrderedLocusNames=TM_1241 {ECO:0000313|EMBL:AAD36316.1}; GN ORFNames=Tmari_1247 {ECO:0000313|EMBL:AGL50171.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36316.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36316.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36316.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50171.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50171.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36316.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50171.1; -; Genomic_DNA. DR PIR; B72280; B72280. DR RefSeq; NP_229046.1; NC_000853.1. DR RefSeq; WP_004080031.1; NZ_CP011107.1. DR STRING; 243274.TM1241; -. DR EnsemblBacteria; AAD36316; AAD36316; TM_1241. DR EnsemblBacteria; AGL50171; AGL50171; Tmari_1247. DR GeneID; 898243; -. DR KEGG; tma:TM1241; -. DR KEGG; tmi:THEMA_08130; -. DR KEGG; tmm:Tmari_1247; -. DR KEGG; tmw:THMA_1266; -. DR PATRIC; 23937422; VBITheMar51294_1258. DR eggNOG; ENOG4106C8J; Bacteria. DR eggNOG; ENOG410Y3IH; LUCA. DR OMA; FHYTIEM; -. DR OrthoDB; EOG61046H; -. DR BioCyc; TMAR243274:GC6P-1271-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 96 117 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 144 AA; 17225 MW; 7A42540002DEC4FB CRC64; MDFRYILRIH ISEEAAEEIL NNSKIQKRAS EVKNKLYYDN ALVIESEPGY DVDEDLIMMV ITAYGKPAKA EGYLVVNGKE RKVFDGMLDP RKPLSIHQTE TERKHEEEEE EEEYDEDEDF DLFNEEDFFE EEEEEDFFDE EDEY // ID Q9X2G5_THEMA Unreviewed; 59 AA. AC Q9X2G5; G4FGP2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36912.1}; GN OrderedLocusNames=TM_1850 {ECO:0000313|EMBL:AAD36912.1}; GN ORFNames=Tmari_1865 {ECO:0000313|EMBL:AGL50789.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36912.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36912.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36912.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50789.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50789.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36912.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50789.1; -; Genomic_DNA. DR PIR; C72203; C72203. DR RefSeq; NP_229646.1; NC_000853.1. DR RefSeq; WP_004082401.1; NZ_CP011107.1. DR STRING; 243274.TM1850; -. DR EnsemblBacteria; AAD36912; AAD36912; TM_1850. DR EnsemblBacteria; AGL50789; AGL50789; Tmari_1865. DR GeneID; 897809; -. DR KEGG; tma:TM1850; -. DR KEGG; tmi:THEMA_04920; -. DR KEGG; tmm:Tmari_1865; -. DR KEGG; tmw:THMA_1900; -. DR PATRIC; 23938689; VBITheMar51294_1871. DR BioCyc; TMAR243274:GC6P-1901-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 11 45 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 59 AA; 7174 MW; E9DA081E6F188A48 CRC64; MMMFLPPEVV REIHEERVKK ALENLKAIEL EKELLEKVVK EEKKVSSRRR RREKETVEV // ID Q9WY20_THEMA Unreviewed; 293 AA. AC Q9WY20; G4FH90; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35269.1}; GN OrderedLocusNames=TM_0176 {ECO:0000313|EMBL:AAD35269.1}; GN ORFNames=Tmari_0174 {ECO:0000313|EMBL:AGL49100.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35269.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35269.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35269.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49100.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49100.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35269.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49100.1; -; Genomic_DNA. DR PIR; F72409; F72409. DR RefSeq; NP_227991.1; NC_000853.1. DR RefSeq; WP_004082811.1; NZ_CP011107.1. DR STRING; 243274.TM0176; -. DR EnsemblBacteria; AAD35269; AAD35269; TM_0176. DR EnsemblBacteria; AGL49100; AGL49100; Tmari_0174. DR GeneID; 897016; -. DR KEGG; tma:TM0176; -. DR KEGG; tmi:THEMA_03920; -. DR KEGG; tmm:Tmari_0174; -. DR KEGG; tmw:THMA_0172; -. DR PATRIC; 23935200; VBITheMar51294_0177. DR eggNOG; ENOG41090IC; Bacteria. DR eggNOG; COG1578; LUCA. DR KO; K09116; -. DR OMA; YILKAKC; -. DR OrthoDB; EOG6JX7GX; -. DR BioCyc; TMAR243274:GC6P-177-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR002791; DUF89. DR InterPro; IPR014444; UCP006593. DR Pfam; PF01937; DUF89; 1. DR PIRSF; PIRSF006593; UCP006593; 1. DR SUPFAM; SSF111321; SSF111321; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 8 285 DUF89. {ECO:0000259|Pfam:PF01937}. SQ SEQUENCE 293 AA; 33715 MW; 58259378A666C2CF CRC64; MRYLRADERC LICSLRQAEN LLKKTITSPE KRWVIFREVF RIMSEMKWGM KPLEVNGEVH RFIMEYIKEE DPFKEEKRRS NDMAIKLVEM FRPEILNSPD PVYSAAKLAV SGNLIDLGIP GWSVDEIFEK LHEVYERPFD REDFEKFRNV LMNASTLFYV ADNAGEIVFD KFFIEVLKME NPSLEVVVAV RGKPIINDAT IEDAKYIGLE EIATVISSGV DEPGVMLDKA SEEFRKAFFE FDVVISKGQG NFEGLYEEEK KNLFFLLTAK CDFVAEVLNV PLGGKVFISS SSL // ID Q9WZN6_THEMA Unreviewed; 247 AA. AC Q9WZN6; G4FD44; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=DUF82 domain-containing protein {ECO:0000313|EMBL:AGL49705.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35861.1}; GN OrderedLocusNames=TM_0779 {ECO:0000313|EMBL:AAD35861.1}; GN ORFNames=Tmari_0780 {ECO:0000313|EMBL:AGL49705.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35861.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35861.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35861.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49705.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49705.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35861.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49705.1; -; Genomic_DNA. DR PIR; D72332; D72332. DR RefSeq; NP_228588.1; NC_000853.1. DR RefSeq; WP_004080909.1; NZ_CP011107.1. DR STRING; 243274.TM0779; -. DR EnsemblBacteria; AAD35861; AAD35861; TM_0779. DR EnsemblBacteria; AGL49705; AGL49705; Tmari_0780. DR GeneID; 898447; -. DR KEGG; tma:TM0779; -. DR KEGG; tmi:THEMA_00755; -. DR KEGG; tmm:Tmari_0780; -. DR KEGG; tmw:THMA_0798; -. DR PATRIC; 23936480; VBITheMar51294_0792. DR eggNOG; ENOG4108KR2; Bacteria. DR eggNOG; COG1656; LUCA. DR KO; K09122; -. DR OMA; ATFRFYE; -. DR OrthoDB; EOG69GZMT; -. DR BioCyc; TMAR243274:GC6P-806-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR002782; Mut7-C_RNAse_dom. DR InterPro; IPR027798; Ub_Mut7C. DR Pfam; PF01927; Mut7-C; 1. DR Pfam; PF14451; Ub-Mut7C; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 81 Ub-Mut7C. {ECO:0000259|Pfam:PF14451}. FT DOMAIN 97 239 Mut7-C. {ECO:0000259|Pfam:PF01927}. SQ SEQUENCE 247 AA; 29147 MW; 6BAB1795B1029B36 CRC64; MKYEKIAFFR FFGRLNDFFR NSERIKTHRF TGFQTVKDRI EALGVPHVEV SLITLNGKPV GFDHMVEDGE LFFVYPEFQN IEIPEDWLVT PRYIGEPRFV LDIHLGKLAR LLRMLGFEAV FGEESDEKLC WMAVKKKAIL LSRDTGLLKR KELVFGYYVR NTDPKEQLVE VVERYDLKKW MKPFTRCIEC GVELEEVPKE AVKNRVPPKV YGFFNEFARC PVCGRIYWKG SHYDHMVEFI KSNINKG // ID Q9X1P9_THEMA Unreviewed; 268 AA. AC Q9X1P9; G4FFV1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Small-conductance mechanosensitive channel {ECO:0000313|EMBL:AGL50495.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36629.1}; GN OrderedLocusNames=TM_1563 {ECO:0000313|EMBL:AAD36629.1}; GN ORFNames=Tmari_1571 {ECO:0000313|EMBL:AGL50495.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36629.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36629.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36629.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50495.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50495.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36629.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50495.1; -; Genomic_DNA. DR PIR; F72240; F72240. DR RefSeq; NP_229363.1; NC_000853.1. DR RefSeq; WP_004081973.1; NZ_CP011107.1. DR STRING; 243274.TM1563; -. DR EnsemblBacteria; AAD36629; AAD36629; TM_1563. DR EnsemblBacteria; AGL50495; AGL50495; Tmari_1571. DR GeneID; 897964; -. DR KEGG; tma:TM1563; -. DR KEGG; tmi:THEMA_06465; -. DR KEGG; tmm:Tmari_1571; -. DR KEGG; tmw:THMA_1598; -. DR PATRIC; 23938088; VBITheMar51294_1581. DR eggNOG; ENOG4107V51; Bacteria. DR eggNOG; COG0668; LUCA. DR KO; K03442; -. DR OMA; RTLDFGI; -. DR OrthoDB; EOG61GG69; -. DR BioCyc; TMAR243274:GC6P-1604-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005623; C:cell; IBA:GOC. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0008381; F:mechanically-gated ion channel activity; IBA:GO_Central. DR GO; GO:0009992; P:cellular water homeostasis; IBA:GO_Central. DR GO; GO:0034220; P:ion transmembrane transport; IBA:GOC. DR InterPro; IPR010920; LSM_dom. DR InterPro; IPR011066; MscC_channel_C. DR InterPro; IPR006685; MscS_channel. DR InterPro; IPR011014; MscS_channel_TM-2. DR Pfam; PF00924; MS_channel; 1. DR SUPFAM; SSF50182; SSF50182; 1. DR SUPFAM; SSF82689; SSF82689; 1. DR SUPFAM; SSF82861; SSF82861; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 60 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 268 AA; 30448 MW; B8FA169D7FACE143 CRC64; MLAKLILTAV TVVVSYLVFK WLFKLIEKSV EKLGKELQMR NTIRFFLGLI ISVIAVMIIL DIWDLSLAPL LAGVGIGGLV IGLALQEPLA NFFSGLFLLV SRAVKEGEAL EAGGVSGTVE VVNLNHTVIR TWDGRRVMIP NKAVWNDKII HFWPSNVRRQ EIVVGVPYSA DLRKVVEIFQ KALEDEETVE KDPAPAIVFS AFNSSSIDFI IRFWVNRDNF FEGVKRLAFR IKDYLEKEGI YIPFPQLDVH FDEEFIRVWK HEGSENKS // ID Q9WZT6_THEMA Unreviewed; 150 AA. AC Q9WZT6; G4FCZ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35911.1}; GN OrderedLocusNames=TM_0829 {ECO:0000313|EMBL:AAD35911.1}; GN ORFNames=Tmari_0831 {ECO:0000313|EMBL:AGL49756.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35911.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35911.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35911.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49756.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49756.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35911.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49756.1; -; Genomic_DNA. DR PIR; A72328; A72328. DR RefSeq; NP_228638.1; NC_000853.1. DR RefSeq; WP_004080815.1; NZ_CP011107.1. DR STRING; 243274.TM0829; -. DR EnsemblBacteria; AAD35911; AAD35911; TM_0829. DR EnsemblBacteria; AGL49756; AGL49756; Tmari_0831. DR GeneID; 898499; -. DR KEGG; tma:TM0829; -. DR KEGG; tmi:THEMA_00495; -. DR KEGG; tmm:Tmari_0831; -. DR KEGG; tmw:THMA_0850; -. DR PATRIC; 23936584; VBITheMar51294_0842. DR eggNOG; ENOG410824K; Bacteria. DR eggNOG; COG0517; LUCA. DR OMA; IRTMNSV; -. DR OrthoDB; EOG6KWXZQ; -. DR BioCyc; TMAR243274:GC6P-858-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 64 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 93 150 CBS. {ECO:0000259|PROSITE:PS51371}. SQ SEQUENCE 150 AA; 16846 MW; FD4CEFD29C6C321B CRC64; MRVKDAVIYD ISAVFEDETV ETVIKLLSRQ NLSGVPVVDH DMRVVGFVSE SDLIKALVPS YFSLLRSASF IPDTNQLIRN VVKIKDRPVS EFMNKPPVVV KEDDPLIVAA DYLIRHGFKS LPVVDEAMQL VGIVRRIDIL RVVSEGKLEI // ID Q9X0E2_THEMA Unreviewed; 181 AA. AC Q9X0E2; G4FEU6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=ComEA protein-related protein {ECO:0000313|EMBL:AAD36129.1}; DE SubName: Full=Late competence protein ComEA, DNA receptor {ECO:0000313|EMBL:AGL49980.1}; GN OrderedLocusNames=TM_1052 {ECO:0000313|EMBL:AAD36129.1}; GN ORFNames=Tmari_1056 {ECO:0000313|EMBL:AGL49980.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36129.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36129.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36129.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49980.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49980.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36129.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49980.1; -; Genomic_DNA. DR PIR; F72301; F72301. DR RefSeq; NP_228858.1; NC_000853.1. DR RefSeq; WP_004080456.1; NZ_CP011107.1. DR STRING; 243274.TM1052; -. DR EnsemblBacteria; AAD36129; AAD36129; TM_1052. DR EnsemblBacteria; AGL49980; AGL49980; Tmari_1056. DR GeneID; 896994; -. DR KEGG; tma:TM1052; -. DR KEGG; tmi:THEMA_09100; -. DR KEGG; tmm:Tmari_1056; -. DR KEGG; tmw:THMA_1074; -. DR PATRIC; 23937033; VBITheMar51294_1065. DR eggNOG; ENOG4105KQC; Bacteria. DR eggNOG; COG1555; LUCA. DR KO; K02237; -. DR OMA; IVMERET; -. DR OrthoDB; EOG6GFGQQ; -. DR BioCyc; TMAR243274:GC6P-1081-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR InterPro; IPR004509; Competence_ComEA_HhH. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR010994; RuvA_2-like. DR SMART; SM00278; HhH1; 4. DR SUPFAM; SSF47781; SSF47781; 2. DR TIGRFAMs; TIGR00426; TIGR00426; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Receptor {ECO:0000313|EMBL:AGL49980.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 55 74 HhH1. {ECO:0000259|SMART:SM00278}. FT DOMAIN 85 104 HhH1. {ECO:0000259|SMART:SM00278}. FT DOMAIN 129 148 HhH1. {ECO:0000259|SMART:SM00278}. FT DOMAIN 159 178 HhH1. {ECO:0000259|SMART:SM00278}. SQ SEQUENCE 181 AA; 20399 MW; D7713DCE05A9C573 CRC64; MRLRKQHQRT ILFVALVFFI LLGIVMERET RTEEDTTASQ KVVAFPVELN TASLEDLMSI PGIGPVKAQR IIDYRESHGG FSSVEELKNV SGIGEKTLEK ISRYVTVEGV EQHIKREVTK LNVNTASVEE LETLPYIGEV KAKAIVEYRE KNGPFRSPED LLDVPGIGEK TLEKIRGKIT F // ID Q9WYM3_THEMA Unreviewed; 406 AA. AC Q9WYM3; G4FHV1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Trehalose synthase {ECO:0000313|EMBL:AGL49314.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35477.1}; GN OrderedLocusNames=TM_0392 {ECO:0000313|EMBL:AAD35477.1}; GN ORFNames=Tmari_0389 {ECO:0000313|EMBL:AGL49314.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35477.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35477.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35477.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49314.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49314.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35477.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49314.1; -; Genomic_DNA. DR PIR; A72382; A72382. DR RefSeq; NP_228202.1; NC_000853.1. DR RefSeq; WP_004083215.1; NZ_CP011107.1. DR STRING; 243274.TM0392; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR DNASU; 897379; -. DR EnsemblBacteria; AAD35477; AAD35477; TM_0392. DR EnsemblBacteria; AGL49314; AGL49314; Tmari_0389. DR GeneID; 897379; -. DR KEGG; tma:TM0392; -. DR KEGG; tmi:THEMA_02770; -. DR KEGG; tmm:Tmari_0389; -. DR KEGG; tmw:THMA_0397; -. DR PATRIC; 23935665; VBITheMar51294_0397. DR eggNOG; ENOG41088YS; Bacteria. DR eggNOG; ENOG410XQX3; LUCA. DR KO; K13057; -. DR OMA; ITVVARF; -. DR OrthoDB; EOG6PP9ND; -. DR BioCyc; TMAR243274:GC6P-406-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR001296; Glyco_trans_1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 210 382 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 406 AA; 47023 MW; DA75238D947B3202 CRC64; MDVVLRERSI EEYRTIIGNE VDEIKKLAEP LKGKKVLHVN ATAYGGGVAE ILHNLVPLMR SVGLDARWRV IEAPDEFFNV TKKFHNTLQG ADIEISEEEW NLYEEVCRKN AELIQDEELF VIHDSQPAAV RKFVDLNDRK WIWRCHIDLS TPNMKVWQKF SQYLEGYNRL VFHLEEYFPQ GWKERSIAFP PSIDPLSEKN RDLDEDTIRK TLERLEIDPE RPLITVVARF DPWKDLFSAI DVYRLVKKEI PEVQLAVVSA MAADDPEGWF FFEKVLRYAG TDEDIKFCTN LKGVGNKEVN AIQRATTVAL HTATREGFGL VISEALYKRV PVVARPVGGV KIQVKHGENG YLAWEREDLA GYVVKLIKDE ELRRKMGEKG RQTVVENFII TVHLKNYLKL FLDLLR // ID Q9X198_THEMA Unreviewed; 256 AA. AC Q9X198; G4FFB4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE SubName: Full=Spermidine Putrescine ABC transporter permease component potC {ECO:0000313|EMBL:AGL50309.1}; DE SubName: Full=Spermidine/putrescine ABC transporter, permease protein {ECO:0000313|EMBL:AAD36448.1}; GN OrderedLocusNames=TM_1378 {ECO:0000313|EMBL:AAD36448.1}; GN ORFNames=Tmari_1385 {ECO:0000313|EMBL:AGL50309.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36448.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36448.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36448.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50309.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50309.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36448.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50309.1; -; Genomic_DNA. DR PIR; C72261; C72261. DR RefSeq; NP_229179.1; NC_000853.1. DR RefSeq; WP_004081576.1; NZ_CP011107.1. DR STRING; 243274.TM1378; -. DR DNASU; 898100; -. DR EnsemblBacteria; AAD36448; AAD36448; TM_1378. DR EnsemblBacteria; AGL50309; AGL50309; Tmari_1385. DR GeneID; 898100; -. DR KEGG; tma:TM1378; -. DR KEGG; tmi:THEMA_07435; -. DR KEGG; tmm:Tmari_1385; -. DR KEGG; tmw:THMA_1405; -. DR PATRIC; 23937698; VBITheMar51294_1390. DR eggNOG; ENOG4105D38; Bacteria. DR eggNOG; COG1177; LUCA. DR KO; K11070; -. DR OMA; KPWKVFF; -. DR OrthoDB; EOG66XBH9; -. DR BioCyc; TMAR243274:GC6P-1413-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 30 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 64 87 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 99 122 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 128 147 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 181 206 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 226 248 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 60 248 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 256 AA; 29091 MW; 5A26A28DC6E5B983 CRC64; MKPGRFIKTI VILTMVFFYL PLFIVVLMSF NSAKSPVWSG FTLKWYLELF TREYSVWHAF RNSLIVAIVS STVSTAIGTL TAIELFWKKS RLENSIWFLT YLPFVVPDVI IGISLLLLFS MFKVQLGLFT ITLAHITFSI PYTMMIVHSR LQDFDKSIIE AAYDLGSTDF QVFYRVIIPN LVPGIVAAFL LAFTLSIDDF VITFFVAGPG STTLPIQIYS MIRFGISPTV NAISTFMIAG TILIGFVLRR FVRYIF // ID Q9X2D5_THEMA Unreviewed; 139 AA. AC Q9X2D5; G4FGK2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:AAD36878.1}; GN OrderedLocusNames=TM_1815 {ECO:0000313|EMBL:AAD36878.1}; GN ORFNames=Tmari_1825 {ECO:0000313|EMBL:AGL50749.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36878.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36878.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36878.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50749.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50749.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36878.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50749.1; -; Genomic_DNA. DR PIR; B72206; B72206. DR RefSeq; NP_229612.1; NC_000853.1. DR RefSeq; WP_004082361.1; NZ_CP011107.1. DR STRING; 243274.TM1815; -. DR EnsemblBacteria; AAD36878; AAD36878; TM_1815. DR EnsemblBacteria; AGL50749; AGL50749; Tmari_1825. DR GeneID; 897827; -. DR KEGG; tma:TM1815; -. DR KEGG; tmi:THEMA_05120; -. DR KEGG; tmm:Tmari_1825; -. DR KEGG; tmw:THMA_1860; -. DR PATRIC; 23938617; VBITheMar51294_1835. DR eggNOG; ENOG4105S8M; Bacteria. DR eggNOG; COG1146; LUCA. DR OMA; DLSVIPW; -. DR OrthoDB; EOG6NKR17; -. DR BioCyc; TMAR243274:GC6P-1866-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF12838; Fer4_7; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 37 66 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 68 99 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 139 AA; 15684 MW; F3F38088412E336A CRC64; MAEAKNAPLI GKDALGREVR DLSKVPWWGV DRKEIEWYPT IDYDKCVTCG ICFVTCGRRV FDFDKKEGKV IVARPYNCMV ACQTCMNLCP TGAISFPDAS YIKKLVAQNK IVKKAFEIIK PLLAEDHLSP KETETKPEP // ID Q9X2C9_THEMA Unreviewed; 247 AA. AC Q9X2C9; G4FGJ7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=CRISPR-associated RAMP Csm3 {ECO:0000313|EMBL:AGL50744.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36872.1}; GN OrderedLocusNames=TM_1809 {ECO:0000313|EMBL:AAD36872.1}; GN ORFNames=Tmari_1820 {ECO:0000313|EMBL:AGL50744.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36872.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36872.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36872.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50744.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50744.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36872.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50744.1; -; Genomic_DNA. DR PIR; F72208; F72208. DR RefSeq; NP_229606.1; NC_000853.1. DR RefSeq; WP_004082356.1; NZ_CP011107.1. DR STRING; 243274.TM1809; -. DR EnsemblBacteria; AAD36872; AAD36872; TM_1809. DR EnsemblBacteria; AGL50744; AGL50744; Tmari_1820. DR GeneID; 897830; -. DR KEGG; tma:TM1809; -. DR KEGG; tmi:THEMA_05145; -. DR KEGG; tmm:Tmari_1820; -. DR KEGG; tmw:THMA_1855; -. DR PATRIC; 23938607; VBITheMar51294_1830. DR eggNOG; ENOG4108W8W; Bacteria. DR eggNOG; COG1337; LUCA. DR KO; K09002; -. DR OMA; KFENTIN; -. DR OrthoDB; EOG6C2WKD; -. DR BioCyc; TMAR243274:GC6P-1860-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR013412; CRISPR-assoc_RAMP_Csm3. DR InterPro; IPR005537; RAMP_III_fam. DR Pfam; PF03787; RAMPs; 1. DR TIGRFAMs; TIGR02582; cas7_TM1809; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 247 AA; 27589 MW; 48E91FF729C22D70 CRC64; MERPILGKYI IKGKIILETG LRIGGQELGV NIGGIDNPVI RNPLTGEPYI PGSSVKGKMR SLMERLLNLD ISGNKVRRHE CEERECKVCR VFGSTSKEGN NIPSRLLVRD AFLTEDSKTK LLSMETDLPY TEWKTENALD RVTCKADPRS FERIPAGAEF EFEIIYTAEN EKHIKEDLEN IATALELLED DYLGGNGSRG YGKVKFSIEK VIFKSADYYK GEGTPVEKEV KGGVEGFKKA IPEIVKG // ID Q9WZI4_THEMA Unreviewed; 285 AA. AC Q9WZI4; G4FD98; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35807.1}; GN OrderedLocusNames=TM_0725 {ECO:0000313|EMBL:AAD35807.1}; GN ORFNames=Tmari_0726 {ECO:0000313|EMBL:AGL49651.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35807.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35807.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35807.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49651.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49651.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35807.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49651.1; -; Genomic_DNA. DR PIR; C72342; C72342. DR RefSeq; NP_228534.1; NC_000853.1. DR RefSeq; WP_004081005.1; NZ_CP011107.1. DR STRING; 243274.TM0725; -. DR EnsemblBacteria; AAD35807; AAD35807; TM_0725. DR EnsemblBacteria; AGL49651; AGL49651; Tmari_0726. DR GeneID; 898392; -. DR KEGG; tma:TM0725; -. DR KEGG; tmi:THEMA_01035; -. DR KEGG; tmm:Tmari_0726; -. DR KEGG; tmw:THMA_0741; -. DR PATRIC; 23936370; VBITheMar51294_0738. DR eggNOG; ENOG4105P93; Bacteria. DR eggNOG; ENOG4111XHN; LUCA. DR OMA; WSININL; -. DR OrthoDB; EOG66TG2M; -. DR BioCyc; TMAR243274:GC6P-751-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.60.40.1120; -; 1. DR InterPro; IPR014766; CarboxyPept_regulatory_dom. DR InterPro; IPR025965; FlgD_Ig. DR InterPro; IPR013229; PEGA. DR Pfam; PF13860; FlgD_ig; 1. DR Pfam; PF08308; PEGA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 93 162 PEGA. {ECO:0000259|Pfam:PF08308}. FT DOMAIN 186 246 FlgD_ig. {ECO:0000259|Pfam:PF13860}. SQ SEQUENCE 285 AA; 32108 MW; D81520437B4F38CC CRC64; MRRFLPILFL LIASAVLAGD YVLIVYSEPL SQVFINGNYV GTVDVTGQMI LTLNSSGKFT ITVRKSWYIP FESEIIVSSP GEFVIFANLK EAGALRVFSN VYPVEVFAEG MYLGKIRSVK DVLYVPAGTV TLTFKAPGYK EETVTVQVKP RSENTINIYL EEKALVLDLK VEPERFSPNG DWYNDKTTFY IYLSKPADLS VEVLNDRGET IWFRQLKGSE GTNKVIWDGK GTSDGRYRVR VTASTDDEMQ SVEKEVIVDR SEYTYFKELF IGSVLALAVL LILVH // ID Q9X135_THEMA Unreviewed; 68 AA. AC Q9X135; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=ABC-2 type transporter {ECO:0000313|EMBL:AGL50239.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36383.1}; GN OrderedLocusNames=TM_1309 {ECO:0000313|EMBL:AAD36383.1}; GN ORFNames=Tmari_1315 {ECO:0000313|EMBL:AGL50239.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36383.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36383.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36383.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50239.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50239.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36383.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50239.1; -; Genomic_DNA. DR PIR; G72270; G72270. DR RefSeq; NP_229113.1; NC_000853.1. DR RefSeq; WP_010865305.1; NZ_CP011107.1. DR STRING; 243274.TM1309; -. DR EnsemblBacteria; AAD36383; AAD36383; TM_1309. DR EnsemblBacteria; AGL50239; AGL50239; Tmari_1315. DR GeneID; 898173; -. DR KEGG; tma:TM1309; -. DR KEGG; tmi:THEMA_07800; -. DR KEGG; tmm:Tmari_1315; -. DR KEGG; tmw:THMA_1333; -. DR PATRIC; 23937556; VBITheMar51294_1324. DR BioCyc; TMAR243274:GC6P-1340-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 52 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 68 AA; 7930 MW; C105DCAF2C344CA4 CRC64; MFFRWLSQLL PLSRSVESII YALQGFKMKA WISSAWEAAV GLAYLVLAYF TLRLIEFAAR KYGNIDMY // ID Q9X042_THEMA Unreviewed; 422 AA. AC Q9X042; G4FF45; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=PhoP/Q-regulated protein PqaA {ECO:0000313|EMBL:AGL49872.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36026.1}; GN OrderedLocusNames=TM_0945 {ECO:0000313|EMBL:AAD36026.1}; GN ORFNames=Tmari_0947 {ECO:0000313|EMBL:AGL49872.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36026.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36026.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36026.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49872.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49872.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36026.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49872.1; -; Genomic_DNA. DR PIR; D72313; D72313. DR RefSeq; NP_228753.1; NC_000853.1. DR RefSeq; WP_004080617.1; NZ_CP011107.1. DR STRING; 243274.TM0945; -. DR ESTHER; thema-q9x042; PhoPQ_related. DR EnsemblBacteria; AAD36026; AAD36026; TM_0945. DR EnsemblBacteria; AGL49872; AGL49872; Tmari_0947. DR GeneID; 898682; -. DR KEGG; tma:TM0945; -. DR KEGG; tmi:THEMA_09620; -. DR KEGG; tmm:Tmari_0947; -. DR KEGG; tmw:THMA_0968; -. DR PATRIC; 23936821; VBITheMar51294_0959. DR eggNOG; ENOG4108M7N; Bacteria. DR eggNOG; COG4287; LUCA. DR OMA; NATNDEY; -. DR OrthoDB; EOG693GJK; -. DR BioCyc; TMAR243274:GC6P-975-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR009199; PhoPQ-act_pathogen-rel_PqaA. DR Pfam; PF10142; PhoPQ_related; 1. DR PIRSF; PIRSF014728; PqaA; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 422 AA; 49136 MW; 064C1B52844B808C CRC64; MKRFLAILLI LPVMVLAIHP LDLLVRARGN PVYETIIATT TQDGDEIYIL KSYGMNWQNI QWFHRVGIIL PSNLNYKDRA FFFITGGSRK EENERYYDSF LEDVKENLWV AKEFEAPFIV VGDVPNQPIF GLREDALIAE TFKMFLENPD PFLPLLVPMT YGVIKAMDTA QDFLEKKGVE IKGFMVSGAS KRGWTTYLTA IFDPRVFAIA PMVYDNLNIE AQLLHQKEYY GTYSEKLRDY QERGLFEILE NDLGKRLLEI VDPYAMRLRL SLPKILVLGT NDEYWTVDSA NLYVDDLPGE TFLFYSPNDP HNLKNVKEII ETLSSFFKMY PKLPKVEFFY RDGKIFVERI PEIVDAELWF ARSKSRDFRK AVWLRRGVEE TDDSLIGVPP EKPEGFHQAY FLRVTLEING LRMKLCSKMM VE // ID Q9X1J4_THEMA Unreviewed; 139 AA. AC Q9X1J4; G4FFP3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=DUF1893 domain-containing protein {ECO:0000313|EMBL:AGL50438.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36573.1}; GN OrderedLocusNames=TM_1506 {ECO:0000313|EMBL:AAD36573.1}; GN ORFNames=Tmari_1514 {ECO:0000313|EMBL:AGL50438.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36573.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36573.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36573.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50438.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50438.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36573.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50438.1; -; Genomic_DNA. DR PIR; C72244; C72244. DR RefSeq; NP_229306.1; NC_000853.1. DR RefSeq; WP_004081848.1; NZ_CP011107.1. DR PDB; 1VK9; X-ray; 2.70 A; A=1-139. DR PDBsum; 1VK9; -. DR STRING; 243274.TM1506; -. DR EnsemblBacteria; AAD36573; AAD36573; TM_1506. DR EnsemblBacteria; AGL50438; AGL50438; Tmari_1514. DR GeneID; 897993; -. DR KEGG; tma:TM1506; -. DR KEGG; tmi:THEMA_06770; -. DR KEGG; tmm:Tmari_1514; -. DR KEGG; tmw:THMA_1538; -. DR PATRIC; 23937970; VBITheMar51294_1523. DR eggNOG; ENOG41064ZH; Bacteria. DR eggNOG; ENOG41123Z7; LUCA. DR OMA; DGKSMCP; -. DR OrthoDB; EOG64BQ7R; -. DR BioCyc; TMAR243274:GC6P-1546-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.140.30; -; 1. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR015067; DUF1893. DR Pfam; PF08973; TM1506; 1. DR SUPFAM; SSF53927; SSF53927; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VK9}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000213|PDB:1VK9}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000213|PDB:1VK9}. FT METAL 76 76 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:1VK9}. FT METAL 98 98 Zinc. {ECO:0000213|PDB:1VK9}. SQ SEQUENCE 139 AA; 15745 MW; E8F86DAEE7F10E30 CRC64; MEKNLLRSAL KIFEKKDLSL LAYSGRSIFE SKDSGLKPVV ELFKRFDNLE GSLVIDKMVG KAAASFLLKM KPDHIHAKVI SKPALKLMNE YGQSFSYDEK IPFVLGKDGK SMCPFEKLVL EMDDPEEIIR IVLSKFTSL // ID Q9WYE3_THEMA Unreviewed; 473 AA. AC Q9WYE3; G4FHM1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=L-fucose isomerase {ECO:0000313|EMBL:AGL49231.1}; DE EC=5.3.1.25 {ECO:0000313|EMBL:AGL49231.1}; DE SubName: Full=L-fucose isomerase, putative {ECO:0000313|EMBL:AAD35395.1}; GN OrderedLocusNames=TM_0307 {ECO:0000313|EMBL:AAD35395.1}; GN ORFNames=Tmari_0305 {ECO:0000313|EMBL:AGL49231.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35395.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35395.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35395.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49231.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49231.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35395.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49231.1; -; Genomic_DNA. DR PIR; H72393; H72393. DR RefSeq; NP_228119.1; NC_000853.1. DR RefSeq; WP_004083033.1; NZ_CP011107.1. DR STRING; 243274.TM0307; -. DR EnsemblBacteria; AAD35395; AAD35395; TM_0307. DR EnsemblBacteria; AGL49231; AGL49231; Tmari_0305. DR GeneID; 897241; -. DR KEGG; tma:TM0307; -. DR KEGG; tmi:THEMA_03190; -. DR KEGG; tmm:Tmari_0305; -. DR KEGG; tmw:THMA_0314; -. DR PATRIC; 23935493; VBITheMar51294_0312. DR eggNOG; ENOG4105EHF; Bacteria. DR eggNOG; COG2407; LUCA. DR KO; K01818; -. DR OMA; VWAFPHF; -. DR OrthoDB; EOG6FJNCF; -. DR BioCyc; TMAR243274:GC6P-320-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0008736; F:L-fucose isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro. DR Gene3D; 3.20.14.10; -; 1. DR Gene3D; 3.40.275.10; -; 1. DR Gene3D; 3.40.50.1070; -; 1. DR InterPro; IPR015888; Fuc_isomerase_C. DR InterPro; IPR012888; Fucose_iso_N1. DR InterPro; IPR009015; Fucose_isomerase_N/cen. DR InterPro; IPR012889; Fucose_isomerase_N2. DR Pfam; PF02952; Fucose_iso_C; 1. DR Pfam; PF07881; Fucose_iso_N1; 1. DR Pfam; PF07882; Fucose_iso_N2; 1. DR SUPFAM; SSF53743; SSF53743; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000313|EMBL:AAD35395.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 159 Fucose_iso_N1. FT {ECO:0000259|Pfam:PF07881}. FT DOMAIN 258 314 Fucose_iso_N2. FT {ECO:0000259|Pfam:PF07882}. FT DOMAIN 335 472 Fucose_iso_C. {ECO:0000259|Pfam:PF02952}. SQ SEQUENCE 473 AA; 54193 MW; B68FA0FA91FE152E CRC64; MKGKYRVGLI SFSDGREYVH RELEGIVKKF EDEIAKTLEE TGEVEVIRAK EIVWKPSIAK REARRLAEEG AEVTIFNYAV WAFPHFTVLA SKFAPGPFLL FSNINPQYPG MVAMLSAAGA LEQDGTKHYR MWGNIKDEKV LRKVMAFIRA GSTYKKLRGQ RYGVFGGRSM GMYTAVPNVD LWNKIFGVDV EHIDQFEIVR RSQLIPDERA RKGRLWIEEK AKAVHYDGKY LTPEKLELQI KSYHAVREIV EEMELDFVGI KGQLELTEHF VTMDVTETFL NDPYDWEGEH EPIVCATEAD SDGALTMQIF KLIAKTPVLF ADVRHYVEEY DVLDLCNSGN HATYFAARSF DPDENMKKVE FYPQTFYFPA GGAAVKHIAA PGKVTLGRLT REDGRYRFTV VPGEFVDFGE EKNYEIADSI QNNWPHAFLK METPIDEFLA KYSSNHIHGV YGDYVEEIKT FCEIASIDFV LMK // ID Q9WYT6_THEMA Unreviewed; 238 AA. AC Q9WYT6; G4FE05; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35549.1}; GN OrderedLocusNames=TM_0465 {ECO:0000313|EMBL:AAD35549.1}; GN ORFNames=Tmari_0462 {ECO:0000313|EMBL:AGL49387.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35549.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35549.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35549.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49387.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49387.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35549.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49387.1; -; Genomic_DNA. DR PIR; A72374; A72374. DR RefSeq; NP_228275.1; NC_000853.1. DR RefSeq; WP_004081501.1; NZ_CP011107.1. DR STRING; 243274.TM0465; -. DR EnsemblBacteria; AAD35549; AAD35549; TM_0465. DR EnsemblBacteria; AGL49387; AGL49387; Tmari_0462. DR GeneID; 897496; -. DR KEGG; tma:TM0465; -. DR KEGG; tmi:THEMA_02365; -. DR KEGG; tmm:Tmari_0462; -. DR KEGG; tmw:THMA_0474; -. DR PATRIC; 23935827; VBITheMar51294_0472. DR OMA; GKENWAF; -. DR OrthoDB; EOG6G20JT; -. DR BioCyc; TMAR243274:GC6P-485-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 238 AA; 27107 MW; 9C6D313524222FEA CRC64; MFILATVPAY AGFIEVGAGV YDETPIVGFV LSPELKTDFI EGKFRFDFFA SFSEGEPSLL PFIYDNPVYF RFGIDDFSFE YHAPAVLKAT FVPFKKSWNV RLGFMGGIWN GENVFFFTEK PVFLVLSNDD NYHIGLNFKV FDTGLELFVE NEKPGVWLEL GSLKVGVSNW IGLIFEHKKT VVRFLYDGEF KPGLALLEEN GWIFINSDYV EGSWKVGRFH AGGKIGKENW AFQISVEF // ID Q9X0Q0_THEMA Unreviewed; 190 AA. AC Q9X0Q0; G4FEH9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36243.1}; GN OrderedLocusNames=TM_1167 {ECO:0000313|EMBL:AAD36243.1}; GN ORFNames=Tmari_1174 {ECO:0000313|EMBL:AGL50098.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36243.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36243.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36243.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50098.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50098.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36243.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50098.1; -; Genomic_DNA. DR PIR; E72288; E72288. DR RefSeq; NP_228973.1; NC_000853.1. DR RefSeq; WP_004080202.1; NZ_CP011107.1. DR STRING; 243274.TM1167; -. DR EnsemblBacteria; AAD36243; AAD36243; TM_1167. DR EnsemblBacteria; AGL50098; AGL50098; Tmari_1174. DR GeneID; 898319; -. DR KEGG; tma:TM1167; -. DR KEGG; tmi:THEMA_08500; -. DR KEGG; tmm:Tmari_1174; -. DR KEGG; tmw:THMA_1192; -. DR PATRIC; 23937271; VBITheMar51294_1184. DR OMA; HEIAYKF; -. DR OrthoDB; EOG6Z9B0V; -. DR BioCyc; TMAR243274:GC6P-1196-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 190 AA; 22438 MW; C57C752DF3472DA6 CRC64; MTHIVHKGLD FFVKPQKVSL NLNMKIGSLK VHPEDLKLLM KKVPVFMMSY YDNKAFMERE LEISSADFPN GVVFFSYYEP VPAELNWDVD KKLISQLTKY FHLYDLVHSI NSLIDETEGS SLHIGVYEEW LDRIMVKVPS ENTEELRNML SRFSLLYTTK ILWKIFRGNF EELKKRTHEI AYKLYEVAGF // ID Q9WZ53_THEMA Unreviewed; 235 AA. AC Q9WZ53; G4FDN6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35669.1}; GN OrderedLocusNames=TM_0584 {ECO:0000313|EMBL:AAD35669.1}; GN ORFNames=Tmari_0582 {ECO:0000313|EMBL:AGL49507.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35669.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35669.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35669.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49507.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49507.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35669.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49507.1; -; Genomic_DNA. DR PIR; A72359; A72359. DR RefSeq; NP_228394.1; NC_000853.1. DR RefSeq; WP_004081273.1; NZ_CP011107.1. DR STRING; 243274.TM0584; -. DR EnsemblBacteria; AAD35669; AAD35669; TM_0584. DR EnsemblBacteria; AGL49507; AGL49507; Tmari_0582. DR GeneID; 897654; -. DR KEGG; tma:TM0584; -. DR KEGG; tmi:THEMA_01745; -. DR KEGG; tmm:Tmari_0582; -. DR KEGG; tmw:THMA_0599; -. DR PATRIC; 23936079; VBITheMar51294_0593. DR eggNOG; ENOG4105NDA; Bacteria. DR eggNOG; COG0705; LUCA. DR OMA; FLHIGIM; -. DR OrthoDB; EOG6QCDF6; -. DR BioCyc; TMAR243274:GC6P-609-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. DR Gene3D; 1.20.1540.10; -; 1. DR InterPro; IPR002610; Peptidase_S54_rhomboid. DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom. DR PANTHER; PTHR22936; PTHR22936; 1. DR Pfam; PF01694; Rhomboid; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 118 136 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 164 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 199 218 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 50 192 Rhomboid. {ECO:0000259|Pfam:PF01694}. SQ SEQUENCE 235 AA; 26394 MW; 510932CC6E7723D7 CRC64; MRKRAVYFIL LFNAFIFVMM TFSGVFSTRD PVLQMLLLLR YGAQYGPRVD AGDWFRLITA LFVHGGILHI LFNSYALYYF GLIVEDIYGT EKFLVGYFFT GIVGNLATHV FYHDTISVGA SGAIFGLIGI LFAAGFRKDT PFFMKPVTGV SLLPIILINV VYGFLPGTNI NNAAHLGGFL SGMLLGYTMS PFSWKRRTLW RVLAIAVVLL VVLSYIFLIR QIPEIDEAIR RFKAG // ID Q9X1Y9_THEMA Unreviewed; 108 AA. AC Q9X1Y9; G4FG48; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36726.1}; GN OrderedLocusNames=TM_1659 {ECO:0000313|EMBL:AAD36726.1}; GN ORFNames=Tmari_1668 {ECO:0000313|EMBL:AGL50592.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36726.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36726.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36726.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50592.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50592.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36726.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50592.1; -; Genomic_DNA. DR PIR; A72224; A72224. DR RefSeq; NP_229459.1; NC_000853.1. DR RefSeq; WP_004082172.1; NZ_CP011107.1. DR STRING; 243274.TM1659; -. DR EnsemblBacteria; AAD36726; AAD36726; TM_1659. DR EnsemblBacteria; AGL50592; AGL50592; Tmari_1668. DR GeneID; 897910; -. DR KEGG; tma:TM1659; -. DR KEGG; tmi:THEMA_05950; -. DR KEGG; tmm:Tmari_1668; -. DR KEGG; tmw:THMA_1700; -. DR PATRIC; 23938292; VBITheMar51294_1678. DR eggNOG; ENOG4105N6E; Bacteria. DR eggNOG; ENOG4111W8Q; LUCA. DR OMA; LVVYIKC; -. DR OrthoDB; EOG62C9HB; -. DR BioCyc; TMAR243274:GC6P-1705-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 108 AA; 12532 MW; 754DB9757C43836F CRC64; MLFLFFGKKK KDLNKNPFYR EKGSLVVYIK CDRCGEVFRS HLRTGYDFIV DYDNPGVPYK IDKLYVGSKC PNKIHLVATF TSSYKPVSVS LEGGTFITRE EFEESQKQ // ID Q9WXP7_THEMA Unreviewed; 278 AA. AC Q9WXP7; G4FGV7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=Dihydropteroate synthase {ECO:0000313|EMBL:AAD35134.1}; DE EC=2.5.1.15 {ECO:0000313|EMBL:AGL48963.1}; GN OrderedLocusNames=TM_0040 {ECO:0000313|EMBL:AAD35134.1}; GN ORFNames=Tmari_0037 {ECO:0000313|EMBL:AGL48963.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35134.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35134.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35134.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48963.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48963.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains pterin-binding domain. CC {ECO:0000256|SAAS:SAAS00062578}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35134.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48963.1; -; Genomic_DNA. DR PIR; E72425; E72425. DR RefSeq; NP_227856.1; NC_000853.1. DR RefSeq; WP_004082506.1; NZ_CP011107.1. DR STRING; 243274.TM0040; -. DR EnsemblBacteria; AAD35134; AAD35134; TM_0040. DR EnsemblBacteria; AGL48963; AGL48963; Tmari_0037. DR GeneID; 896864; -. DR KEGG; tma:TM0040; -. DR KEGG; tmi:THEMA_04600; -. DR KEGG; tmm:Tmari_0037; -. DR KEGG; tmw:THMA_0036; -. DR PATRIC; 23934920; VBITheMar51294_0038. DR eggNOG; ENOG4105EEI; Bacteria. DR eggNOG; COG0294; LUCA. DR KO; K00796; -. DR OMA; SIDTYHA; -. DR OrthoDB; EOG67T5P5; -. DR BioCyc; TMAR243274:GC6P-40-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR InterPro; IPR006390; DHP_synth. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding_dom. DR Pfam; PF00809; Pterin_bind; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR TIGRFAMs; TIGR01496; DHPS; 1. DR PROSITE; PS00793; DHPS_2; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL48963.1}. FT DOMAIN 16 268 Pterin-binding. FT {ECO:0000259|PROSITE:PS50972}. SQ SEQUENCE 278 AA; 31639 MW; A39D2DAB98EA91E2 CRC64; MVYTTPWNRK IEFGRTMVMG IINVTPDSFF ADSRKQSVLE AVETAKKMIE EGADIIDVGG MSTRPGSDPV DEEEELNRVI PVIRAIRSIT DVPISVDTYR WRVALKALEA GADIVNDISG YQFEPDIVRV VSENNVPYVL MHIKGTPKTM QENPHYEDVV KEIKEYFTEK IEYLKEKGVN QIVLDPGIGF GKRYEDNLEI LRRIDEFKEL KLPILIGASR KSFIGITLGN VPPEERLEGT LAVTAYCTMK GVDIIRVHDV LPNKRVIRMM EAILWQRL // ID Q9X265_THEMA Unreviewed; 274 AA. AC Q9X265; G4FGC9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=2,5-diketo-D-gluconic acid reductase {ECO:0000313|EMBL:AGL50675.1}; DE EC=1.1.1.- {ECO:0000313|EMBL:AGL50675.1}; DE SubName: Full=Oxidoreductase, aldo/keto reductase family {ECO:0000313|EMBL:AAD36808.1}; GN OrderedLocusNames=TM_1743 {ECO:0000313|EMBL:AAD36808.1}; GN ORFNames=Tmari_1751 {ECO:0000313|EMBL:AGL50675.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36808.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36808.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36808.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50675.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50675.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36808.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50675.1; -; Genomic_DNA. DR PIR; F72218; F72218. DR RefSeq; NP_229541.1; NC_000853.1. DR RefSeq; WP_004082270.1; NZ_CP011107.1. DR STRING; 243274.TM1743; -. DR EnsemblBacteria; AAD36808; AAD36808; TM_1743. DR EnsemblBacteria; AGL50675; AGL50675; Tmari_1751. DR GeneID; 897867; -. DR KEGG; tma:TM1743; -. DR KEGG; tmi:THEMA_05520; -. DR KEGG; tmm:Tmari_1751; -. DR KEGG; tmw:THMA_1785; -. DR PATRIC; 23938462; VBITheMar51294_1761. DR eggNOG; ENOG4105CV8; Bacteria. DR eggNOG; COG0656; LUCA. DR OMA; YHLFRRD; -. DR OrthoDB; EOG6NGVXP; -. DR BioCyc; TMAR243274:GC6P-1791-MONOMER; -. DR BRENDA; 1.1.1.184; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red/Kv-b. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PIRSF; PIRSF000097; AKR; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50675.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 16 273 Aldo_ket_red. {ECO:0000259|Pfam:PF00248}. FT ACT_SITE 58 58 Proton donor. FT {ECO:0000256|PIRSR:PIRSR000097-1}. FT BINDING 117 117 Substrate. FT {ECO:0000256|PIRSR:PIRSR000097-2}. FT SITE 84 84 Lowers pKa of active site Tyr. FT {ECO:0000256|PIRSR:PIRSR000097-3}. SQ SEQUENCE 274 AA; 31360 MW; 7757FF1BCCCBD5E1 CRC64; MLYKELGRTG EEIPALGLGT WGIGGFETPD YSRDEEMVEL LKTAIKMGYT HIDTAEYYGG GHTEELIGKA IKDFRREDLF IVSKVWPTHL RRDDLLRSLE NTLKRLDTDY VDLYLIHWPN PEIPLEETLS AMAEGVRQGL IRYIGVSNFD RRLLEEAISK SQEPIVCDQV KYNIEDRDPE RDGLLEFCQK NGVTLVAYSP LRRTLLSEKT KRTLEEIAKN HGATIYQIML AWLLAKPNVV AIPKAGRVEH LRENLKATEI KLSEEEMKLL DSLG // ID Q9X0U1_THEMA Unreviewed; 178 AA. AC Q9X0U1; G4FED2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 103. DE SubName: Full=NADH dehydrogenase, putative {ECO:0000313|EMBL:AAD36289.1}; DE SubName: Full=NADH-ubiquinone oxidoreductase chain B {ECO:0000313|EMBL:AGL50145.1}; DE EC=1.6.5.3 {ECO:0000313|EMBL:AGL50145.1}; GN OrderedLocusNames=TM_1214 {ECO:0000313|EMBL:AAD36289.1}; GN ORFNames=Tmari_1221 {ECO:0000313|EMBL:AGL50145.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36289.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36289.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36289.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50145.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50145.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC {ECO:0000256|RuleBase:RU004464}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36289.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50145.1; -; Genomic_DNA. DR PIR; D72281; D72281. DR RefSeq; NP_229019.1; NC_000853.1. DR RefSeq; WP_004080086.1; NZ_CP011107.1. DR STRING; 243274.TM1214; -. DR EnsemblBacteria; AAD36289; AAD36289; TM_1214. DR EnsemblBacteria; AGL50145; AGL50145; Tmari_1221. DR GeneID; 898270; -. DR KEGG; tma:TM1214; -. DR KEGG; tmi:THEMA_08260; -. DR KEGG; tmm:Tmari_1221; -. DR KEGG; tmw:THMA_1240; -. DR PATRIC; 23937370; VBITheMar51294_1232. DR eggNOG; ENOG4105ES3; Bacteria. DR eggNOG; COG0377; LUCA. DR KO; K00331; -. DR OMA; RLDYYIP; -. DR OrthoDB; EOG62K20C; -. DR BioCyc; TMAR243274:GC6P-1244-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR Gene3D; 3.40.50.700; -; 1. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su. DR Pfam; PF01058; Oxidored_q6; 1. DR TIGRFAMs; TIGR01957; nuoB_fam; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|RuleBase:RU004464}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|RuleBase:RU004464}; KW Iron-sulfur {ECO:0000256|RuleBase:RU004464}; KW Metal-binding {ECO:0000256|RuleBase:RU004464}; KW NAD {ECO:0000256|RuleBase:RU004464}; KW Oxidoreductase {ECO:0000256|RuleBase:RU004464, KW ECO:0000313|EMBL:AGL50145.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Ubiquinone {ECO:0000313|EMBL:AGL50145.1}. FT DOMAIN 25 136 Oxidored_q6. {ECO:0000259|Pfam:PF01058}. SQ SEQUENCE 178 AA; 20959 MW; 57A3F89D80B1218F CRC64; MKERSIWERI ADNLRSRSIW MLHYCTGCGA VELPPSMTSR FDMERFGIAP MATPRQADIL LITGYLNTKT LRRVIYTYEQ MPDPKYVVGF GSCTINGGIY FDSYATVNRL DYYIPVDVYI AGCMPRPEAI LEAFNYLMEK IRKGEADGWK RYRENYEWYK QNQIRSLGEV YVHDEFHE // ID Q9X032_THEMA Unreviewed; 425 AA. AC Q9X032; G4FF56; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Arsenical pump membrane protein {ECO:0000313|EMBL:AGL49861.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36015.1}; GN OrderedLocusNames=TM_0934 {ECO:0000313|EMBL:AAD36015.1}; GN ORFNames=Tmari_0936 {ECO:0000313|EMBL:AGL49861.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36015.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36015.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36015.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49861.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49861.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36015.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49861.1; -; Genomic_DNA. DR PIR; F72315; F72315. DR RefSeq; NP_228742.1; NC_000853.1. DR RefSeq; WP_004080628.1; NZ_CP011107.1. DR STRING; 243274.TM0934; -. DR DNASU; 898608; -. DR EnsemblBacteria; AAD36015; AAD36015; TM_0934. DR EnsemblBacteria; AGL49861; AGL49861; Tmari_0936. DR GeneID; 898608; -. DR KEGG; tma:TM0934; -. DR KEGG; tmi:THEMA_09680; -. DR KEGG; tmm:Tmari_0936; -. DR KEGG; tmw:THMA_0956; -. DR PATRIC; 23936799; VBITheMar51294_0948. DR eggNOG; ENOG4107R3E; Bacteria. DR eggNOG; COG1055; LUCA. DR OMA; EIEWGVI; -. DR OrthoDB; EOG6VXF6K; -. DR BioCyc; TMAR243274:GC6P-964-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0015105; F:arsenite transmembrane transporter activity; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR GO; GO:0098656; P:anion transmembrane transport; IBA:GO_Central. DR GO; GO:0015700; P:arsenite transport; IEA:InterPro. DR InterPro; IPR000802; Arsenical_pump_ArsB. DR InterPro; IPR004680; Cit_transptr-like_dom. DR Pfam; PF03600; CitMHS; 1. DR PRINTS; PR00758; ARSENICPUMP. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 21 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 28 46 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 71 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 196 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 223 240 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 275 293 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 318 342 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 362 385 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 405 423 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 16 369 CitMHS. {ECO:0000259|Pfam:PF03600}. SQ SEQUENCE 425 AA; 46771 MW; 69AB2A3163F8EE2E CRC64; MFEDAVVSLL IFIIVYLFII LEKHHRAVIT MLGGSAALFL VFKDPIEALV RYVDFNTIFL LIGMMIFVSV TKRSGLFHFL GLYSVKLSGG NVFLFFIAIN TLVALLSSFL DNVTTILVFV PVTLVVCDTV DLDPVPFVIS EIISSNIGGT ATMIGDPPNI MIASAAKLHF LDFVVNVAPA AVLTLIVTLI FLSAVYRRVI FRKIPVEVVK DFDPRRAIVD KKLFYLSIIL TLVVLVLFSL QKPLGLESFE VALLAGFLSL AFLKKKDIED VFKEIEWGVI FFFIGLFLVV GALEEAGVLE RISELVIRLS KGKMESTLIS VLGISGLSSA FVDNIPFTAT MIPVIKKLAV LAPETFSDLR PLWWALSLGA CFGGNGTLIG ASANVVGTSL IADRKHITFW EYFKIGFPVL ILSLLVSGVY LLIRY // ID Q9X206_THEMA Unreviewed; 160 AA. AC Q9X206; G4FG65; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36745.1}; GN OrderedLocusNames=TM_1678 {ECO:0000313|EMBL:AAD36745.1}; GN ORFNames=Tmari_1686 {ECO:0000313|EMBL:AGL50610.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36745.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36745.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36745.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50610.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50610.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36745.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50610.1; -; Genomic_DNA. DR PIR; D72226; D72226. DR RefSeq; NP_229478.1; NC_000853.1. DR RefSeq; WP_004082194.1; NZ_CP011107.1. DR STRING; 243274.TM1678; -. DR EnsemblBacteria; AAD36745; AAD36745; TM_1678. DR EnsemblBacteria; AGL50610; AGL50610; Tmari_1686. DR GeneID; 897258; -. DR KEGG; tma:TM1678; -. DR KEGG; tmi:THEMA_05850; -. DR KEGG; tmm:Tmari_1686; -. DR KEGG; tmw:THMA_1720; -. DR PATRIC; 23938330; VBITheMar51294_1695. DR eggNOG; ENOG4108YFP; Bacteria. DR eggNOG; COG2206; LUCA. DR OMA; KKHSIVG; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1726-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR006674; HD_domain. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 160 AA; 17634 MW; D1C21F06B9048675 CRC64; MEGGLRATKN PIPFRGLGGG QIGKIAVPEH ILNKPGKLTD EEFEEIKKHS IVGADILREY PELSFAVPVV LYHHERVDGS GYPFGLKDGE IPLLARILAV ADVFDALTSD RPYRKAMKPE DAAALMKKMP LDQEIVGILE KHLSEFVSLK PQVSNPRSNP // ID Q9WYK7_THEMA Unreviewed; 147 AA. AC Q9WYK7; G4FHT6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Heat shock protein, class I {ECO:0000313|EMBL:AAD35461.1}; DE SubName: Full=Small heat shock protein {ECO:0000313|EMBL:AGL49297.1}; GN OrderedLocusNames=TM_0374 {ECO:0000313|EMBL:AAD35461.1}; GN ORFNames=Tmari_0372 {ECO:0000313|EMBL:AGL49297.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35461.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35461.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35461.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49297.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49297.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) CC family. {ECO:0000256|RuleBase:RU003616}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35461.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49297.1; -; Genomic_DNA. DR PIR; D72385; D72385. DR RefSeq; NP_228185.1; NC_000853.1. DR RefSeq; WP_004083188.1; NZ_CP011107.1. DR STRING; 243274.TM0374; -. DR EnsemblBacteria; AAD35461; AAD35461; TM_0374. DR EnsemblBacteria; AGL49297; AGL49297; Tmari_0372. DR GeneID; 897333; -. DR KEGG; tma:TM0374; -. DR KEGG; tmi:THEMA_02845; -. DR KEGG; tmm:Tmari_0372; -. DR KEGG; tmw:THMA_0382; -. DR PATRIC; 23935629; VBITheMar51294_0379. DR eggNOG; ENOG4105VN1; Bacteria. DR eggNOG; COG0071; LUCA. DR KO; K13993; -. DR OMA; VRWEPFR; -. DR OrthoDB; EOG6PZXGF; -. DR BioCyc; TMAR243274:GC6P-388-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.60.40.790; -; 1. DR InterPro; IPR002068; A-crystallin/Hsp20_dom. DR InterPro; IPR031107; HSP20. DR InterPro; IPR008978; HSP20-like_chaperone. DR PANTHER; PTHR11527; PTHR11527; 1. DR Pfam; PF00011; HSP20; 1. DR SUPFAM; SSF49764; SSF49764; 1. DR PROSITE; PS01031; HSP20; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Stress response {ECO:0000313|EMBL:AAD35461.1}. FT DOMAIN 44 132 HSP20. {ECO:0000259|PROSITE:PS01031}. SQ SEQUENCE 147 AA; 17645 MW; 2B514C6820357E7C CRC64; MLLGRREDIF RPFRELQREI DRLFDDFFRT EVRPAKEFFA PDMDVYETDD EVVIEVEIPG IDRKDVKITV EENILKISGE KKLEREQKGK NYYYVERSAG KFERAIRLPD YVDVEKIKAE YKNGVLTIRV PKKEERKKKV IEVEVQE // ID Q9WZ33_THEMA Unreviewed; 459 AA. AC Q9WZ33; G4FDQ7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Permease of the major facilitator superfamily {ECO:0000313|EMBL:AGL49486.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35648.1}; GN OrderedLocusNames=TM_0563 {ECO:0000313|EMBL:AAD35648.1}; GN ORFNames=Tmari_0561 {ECO:0000313|EMBL:AGL49486.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35648.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35648.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35648.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49486.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49486.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35648.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49486.1; -; Genomic_DNA. DR PIR; B72361; B72361. DR RefSeq; NP_228373.1; NC_000853.1. DR RefSeq; WP_004081307.1; NZ_CP011107.1. DR STRING; 243274.TM0563; -. DR DNASU; 897624; -. DR EnsemblBacteria; AAD35648; AAD35648; TM_0563. DR EnsemblBacteria; AGL49486; AGL49486; Tmari_0561. DR GeneID; 897624; -. DR KEGG; tma:TM0563; -. DR KEGG; tmi:THEMA_01855; -. DR KEGG; tmm:Tmari_0561; -. DR KEGG; tmw:THMA_0577; -. DR PATRIC; 23936035; VBITheMar51294_0572. DR eggNOG; ENOG4108JN7; Bacteria. DR eggNOG; COG0477; LUCA. DR OMA; IAGPYFN; -. DR OrthoDB; EOG69WFGP; -. DR BioCyc; TMAR243274:GC6P-587-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 92 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 118 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 139 157 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 163 182 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 211 231 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 243 262 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 292 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 298 322 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 334 360 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 372 393 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 4 400 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 459 AA; 52218 MW; C19C3FC977D9C27E CRC64; MKKAYLFLTL EGVFSLFYAL LIQGPVFTGL AMLFNLDEFL LSVAAAIPPM MQFFQLFASF FVQKYRKRRF LVNVFNAFSR FSFAFLIVFL LLGKTEPLIF IVALVISQIF AALSSSTWNS WMRDLVPPEE RGRVFGNRNM FLSIGNALII YLYSSIVDHF SSGFVLVLLI STVGTVLSIL AMNKIPDVPV KETGTGIPLK VVFKDENFMK FVFFTFYWNM AVTFSSAFYH YHLLKNLGVD YTYIAYMMIV NNFVAMLVYR ILGKVSDRVG HKTIAEFGII LASFVSGMWF FMNTNTYRTL MVADAFLSSI AWSAINLSLA ILPMEVAFES DPVFFGLNAS FASAGSLIGS FAGGITAKFL SDIYVNLHGF EIFGLQLLFL MAGIFRFSAV FFLRKVKVKK YIPFRAFMLS TLSVTLRRPV YRILDVYLLL KRGNERVRRL VRRSKRRKSN TDEQGGEQG // ID Q9WZN0_THEMA Unreviewed; 271 AA. AC Q9WZN0; G4FD51; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Signal peptidase-like protein {ECO:0000313|EMBL:AGL49698.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35854.1}; GN OrderedLocusNames=TM_0772 {ECO:0000313|EMBL:AAD35854.1}; GN ORFNames=Tmari_0773 {ECO:0000313|EMBL:AGL49698.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35854.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35854.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35854.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49698.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49698.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35854.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49698.1; -; Genomic_DNA. DR PIR; B72337; B72337. DR RefSeq; NP_228581.1; NC_000853.1. DR RefSeq; WP_004080919.1; NZ_CP011107.1. DR STRING; 243274.TM0772; -. DR DNASU; 898440; -. DR EnsemblBacteria; AAD35854; AAD35854; TM_0772. DR EnsemblBacteria; AGL49698; AGL49698; Tmari_0773. DR GeneID; 898440; -. DR KEGG; tma:TM0772; -. DR KEGG; tmi:THEMA_00790; -. DR KEGG; tmm:Tmari_0773; -. DR KEGG; tmw:THMA_0791; -. DR PATRIC; 23936466; VBITheMar51294_0785. DR eggNOG; ENOG4105MA4; Bacteria. DR eggNOG; COG1774; LUCA. DR OMA; DPVSIKM; -. DR OrthoDB; EOG6W45VP; -. DR BioCyc; TMAR243274:GC6P-799-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central. DR InterPro; IPR007557; PSP1_C. DR Pfam; PF04468; PSP1; 1. DR PROSITE; PS51411; PSP1_C; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 65 150 PSP1 C-terminal. FT {ECO:0000259|PROSITE:PS51411}. FT COILED 69 96 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 271 AA; 31352 MW; E050D22438132E74 CRC64; MELKARAVGV EIIPKGKIIY YSVPNGDEYE RGDLVLVLGD FGLEVGKVLI PPREVVIDEV GYELKAVIRK LTDEDLEQYR KNVEDALKAF QICKQKIKEH GLPMKLLYAK YTFDRTRLIF FFSAEGRVDF RELVRDLAKI FKTRIELRQV GVRDEMKFFG GLGLCGLPTC CSTFLREFTS VTLKHAKKQQ MMINPAKISG PCRRLLCCLT YEYDFYEKEL EGIPDEGSTI TYEGKRYKVV NVNVFLRTVT LFSEQEGEMI KLPFDYFRKG E // ID Q9X0B9_THEMA Unreviewed; 263 AA. AC Q9X0B9; G4FEW9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=ABC transporter, permease protein, putative {ECO:0000313|EMBL:AAD36106.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL49957.1}; GN OrderedLocusNames=TM_1029 {ECO:0000313|EMBL:AAD36106.1}; GN ORFNames=Tmari_1033 {ECO:0000313|EMBL:AGL49957.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36106.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36106.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36106.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49957.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49957.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36106.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49957.1; -; Genomic_DNA. DR PIR; D72303; D72303. DR RefSeq; NP_228835.1; NC_000853.1. DR RefSeq; WP_004080494.1; NZ_CP011107.1. DR STRING; 243274.TM1029; -. DR EnsemblBacteria; AAD36106; AAD36106; TM_1029. DR EnsemblBacteria; AGL49957; AGL49957; Tmari_1033. DR GeneID; 897059; -. DR KEGG; tma:TM1029; -. DR KEGG; tmi:THEMA_09215; -. DR KEGG; tmm:Tmari_1033; -. DR KEGG; tmw:THMA_1051; -. DR PATRIC; 23936987; VBITheMar51294_1042. DR eggNOG; ENOG4105MVR; Bacteria. DR eggNOG; COG1277; LUCA. DR KO; K01992; -. DR OMA; KYVTPFY; -. DR OrthoDB; EOG6NWBSM; -. DR BioCyc; TMAR243274:GC6P-1058-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032688; ABC2_membrane_2. DR Pfam; PF12679; ABC2_membrane_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 68 93 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 123 146 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 179 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 236 256 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 263 AA; 29969 MW; F0A6535CCD354666 CRC64; MNIFRWDMKR YMKSTIAWTV VLILLQLMYA AFYPSMAKET EFITKWMKVM PKAFVKLFGL EDMDFSNIMN YLAMVSSIYV TLVGGVFASL VGVRSVSREE NEKTVEFLLS KPVSRFEVVI SKFFSSLVHV LIFDALLFSS LFMFANIYSS SPVEVEKFVV FAFSQVFLHF TLMNISFFVG TLRSDGALSL GLGTVFVLYV LNMISKITDK AEFLKYFTPF SYADPSTVIR HGFPEFSGLF FALVNIALLI SSIVLFSKKD ILV // ID Q9WXV8_THEMA Unreviewed; 507 AA. AC Q9WXV8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 119. DE SubName: Full=Sugar ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35197.1}; GN OrderedLocusNames=TM_0103 {ECO:0000313|EMBL:AAD35197.1}; GN ORFNames=Tmari_0100 {ECO:0000313|EMBL:AGL49026.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35197.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35197.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35197.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49026.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49026.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35197.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49026.1; -; Genomic_DNA. DR PIR; G72418; G72418. DR RefSeq; NP_227919.1; NC_000853.1. DR RefSeq; WP_010865052.1; NZ_CP011107.1. DR STRING; 243274.TM0103; -. DR DNASU; 896930; -. DR EnsemblBacteria; AAD35197; AAD35197; TM_0103. DR EnsemblBacteria; AGL49026; AGL49026; Tmari_0100. DR GeneID; 896930; -. DR KEGG; tma:TM0103; -. DR KEGG; tmi:THEMA_04290; -. DR KEGG; tmm:Tmari_0100; -. DR KEGG; tmw:THMA_0099; -. DR PATRIC; 23935046; VBITheMar51294_0101. DR eggNOG; ENOG4108JQ9; Bacteria. DR eggNOG; COG3845; LUCA. DR KO; K02056; -. DR OMA; YIPADRQ; -. DR OrthoDB; EOG6QK4RR; -. DR BioCyc; TMAR243274:GC6P-103-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35197.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35197.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 240 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT DOMAIN 257 501 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 507 AA; 57065 MW; F1BFC61593EB739D CRC64; MEYAVVMKRI VKRFPGVLAN DHVDLFVEKG EIHAIVGENG AGKTTLMKQL YGLLKPDEGE IYINGKRVEF SGPADAIKSG IGMVHQHFML VDNLTAYENV IIGMEPRKGI LLDRKKARKE VKRLSEEYGL TIDVDMKIED MPVGLQQRVE IIKTLYRGAE ILILDEPTAV LTPQETEELF EVLKRLKKSG KTIIFISHKL NEVMEISDRI TVMRQGRVTG NLITSQTTPQ EIARLMVGRD VVLTVEKKPK EAGETLLKIE DLWVKDNRKL DAVKGVSFEV KRGEIVGIAG VAGNGQSELV EAITGLRGAE RGRVYFKGED ITGYDPKRLR DLGMFHVPED RLKRGLIVDF PAYFNTILGR HMIEPFVKSG FLNMKEIKRF SKQLFEKFDI RPRNIELLAG SFSGGNQQKI IVAREMSFSP ELLVVAQPTR GLDVGAIEFI HKTLVSMRDA GVGVLLISME LDEIFSLSDR ILVMYEGQIM GEVKPEETTP EEVGLMMAGK RLEEIRR // ID Q9X0Z2_THEMA Unreviewed; 387 AA. AC Q9X0Z2; G4FE83; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 104. DE SubName: Full=ATPase {ECO:0000313|EMBL:AGL50194.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36340.1}; GN OrderedLocusNames=TM_1265 {ECO:0000313|EMBL:AAD36340.1}; GN ORFNames=Tmari_1270 {ECO:0000313|EMBL:AGL50194.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36340.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36340.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36340.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50194.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50194.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36340.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50194.1; -; Genomic_DNA. DR PIR; H72273; H72273. DR RefSeq; NP_229070.1; NC_000853.1. DR RefSeq; WP_004079989.1; NZ_CP011107.1. DR STRING; 243274.TM1265; -. DR EnsemblBacteria; AAD36340; AAD36340; TM_1265. DR EnsemblBacteria; AGL50194; AGL50194; Tmari_1270. DR GeneID; 898218; -. DR KEGG; tma:TM1265; -. DR KEGG; tmi:THEMA_08010; -. DR KEGG; tmm:Tmari_1270; -. DR KEGG; tmw:THMA_1290; -. DR PATRIC; 23937470; VBITheMar51294_1281. DR eggNOG; ENOG4105CHX; Bacteria. DR eggNOG; COG1373; LUCA. DR KO; K07133; -. DR OMA; ESMCREW; -. DR OrthoDB; EOG64FKFQ; -. DR BioCyc; TMAR243274:GC6P-1296-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 36 149 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 387 AA; 45157 MW; CDDDE83AD88C2802 CRC64; MYEEIIEKLD LQMNRMISFL SKKMRLFFQD LEKRFTNRAI LLYGPRGAGK TTFLLSMARK HGFLYVSGDE ILLLDVPLHD LFQEIMKNYP GIIIDEVHLL KNWSTILKVL YDSFPDKVIW TSDSSSVLLR KGISDLSRRF VLIRMPLMSF REFIHFETGK TLRKLSSPFE VSIDYAAEAL KEVDLMSLFR KYRETGTRPF YVEGNFREKL MNILQKAIYY DVPHFLGTVT ENHLGVMKAI VGHLLHSKIP TINVESMCRE WGVGKQKFYQ LLQTMEEIEL VNIVRKKRVE KPFSKGEKIF LSDPAMYYAF EGEIGNFREA FVVFALKEIG KIYAVKNEEE GDYVFEGIKI EVGGKSKKKK SSDFVIRDDV DLPVRNVIPM WMLGMLW // ID Q9WZB7_THEMA Unreviewed; 162 AA. AC Q9WZB7; G4FDH5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35733.1}; GN OrderedLocusNames=TM_0649 {ECO:0000313|EMBL:AAD35733.1}; GN ORFNames=Tmari_0649 {ECO:0000313|EMBL:AGL49574.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35733.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35733.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35733.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49574.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49574.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35733.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49574.1; -; Genomic_DNA. DR PIR; H72351; H72351. DR RefSeq; NP_228458.1; NC_000853.1. DR RefSeq; WP_004081148.1; NZ_CP011107.1. DR STRING; 243274.TM0649; -. DR DNASU; 897754; -. DR EnsemblBacteria; AAD35733; AAD35733; TM_0649. DR EnsemblBacteria; AGL49574; AGL49574; Tmari_0649. DR GeneID; 897754; -. DR KEGG; tma:TM0649; -. DR KEGG; tmi:THEMA_01420; -. DR KEGG; tmm:Tmari_0649; -. DR KEGG; tmw:THMA_0664; -. DR PATRIC; 23936212; VBITheMar51294_0659. DR eggNOG; ENOG41066SJ; Bacteria. DR eggNOG; ENOG4112D2Z; LUCA. DR OMA; RNIYGFE; -. DR OrthoDB; EOG6SFPF8; -. DR BioCyc; TMAR243274:GC6P-674-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 10 37 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 162 AA; 19558 MW; E4C8FD51A2243EC2 CRC64; MKREQILSLI AEIDDLLNAL NMVVKEIEEK KREFSDKEPD QFILRALGSL LHDFYTIIED IFELISSEMN GVRLDSFDWH KRLLNKMTLE IPGLRPAVIS KRLKEMLDEY LRFRHVFRNV YGYLLQWERM KPLLEKAGAV YERFEEEIER FKDFLRELAE KM // ID Q9X1C6_THEMA Unreviewed; 246 AA. AC Q9X1C6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36477.1}; GN OrderedLocusNames=TM_1406 {ECO:0000313|EMBL:AAD36477.1}; GN ORFNames=Tmari_1413 {ECO:0000313|EMBL:AGL50337.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36477.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36477.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36477.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50337.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50337.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36477.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50337.1; -; Genomic_DNA. DR PIR; G72257; G72257. DR RefSeq; NP_229207.1; NC_000853.1. DR RefSeq; WP_010865331.1; NZ_CP011107.1. DR STRING; 243274.TM1406; -. DR EnsemblBacteria; AAD36477; AAD36477; TM_1406. DR EnsemblBacteria; AGL50337; AGL50337; Tmari_1413. DR GeneID; 898070; -. DR KEGG; tma:TM1406; -. DR KEGG; tmm:Tmari_1413; -. DR KEGG; tmw:THMA_1435; -. DR PATRIC; 23937758; VBITheMar51294_1418. DR eggNOG; ENOG4107AV4; Bacteria. DR eggNOG; ENOG410ZGFT; LUCA. DR OMA; DERYFIM; -. DR OrthoDB; EOG6FBX5Z; -. DR BioCyc; TMAR243274:GC6P-1443-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 246 AA; 29146 MW; A1FD6F9002289201 CRC64; MILCLNLVIS FLVNRDVSQI VIAIMTYPLG LVVPLKKKKL RFEGVGKPQK VERINLMKRS FKEAIFFGQD EDKKRSILRL SEDVEKGKVP PERLISASKR LMKNSGVDVG LYTTESIERV EKSFEKEEEI LLNIENLDDK SEELYERVWD YLEADFVSGK LKEYYRFLLL DRLKLLGKDE RYFIMKYRVE RNLEVLWEGL KQTRSPLIYR TLLFELLKRR NYPELRQLKL FFSKSEKDKD SGTSQS // ID Q9WZQ2_THEMA Unreviewed; 270 AA. AC Q9WZQ2; G4FD29; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=PfkB family sugar kinase {ECO:0000313|EMBL:AGL49721.1}; DE SubName: Full=Sugar kinase, pfkB family {ECO:0000313|EMBL:AAD35877.1}; GN OrderedLocusNames=TM_0795 {ECO:0000313|EMBL:AAD35877.1}; GN ORFNames=Tmari_0796 {ECO:0000313|EMBL:AGL49721.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35877.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35877.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35877.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49721.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49721.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35877.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49721.1; -; Genomic_DNA. DR PIR; D72334; D72334. DR RefSeq; NP_228604.1; NC_000853.1. DR RefSeq; WP_004080876.1; NZ_CP011107.1. DR STRING; 243274.TM0795; -. DR EnsemblBacteria; AAD35877; AAD35877; TM_0795. DR EnsemblBacteria; AGL49721; AGL49721; Tmari_0796. DR GeneID; 898463; -. DR KEGG; tma:TM0795; -. DR KEGG; tmi:THEMA_00675; -. DR KEGG; tmm:Tmari_0796; -. DR KEGG; tmw:THMA_0814; -. DR PATRIC; 23936510; VBITheMar51294_0807. DR eggNOG; ENOG4105MYA; Bacteria. DR eggNOG; COG0524; LUCA. DR OMA; FGGTFWD; -. DR OrthoDB; EOG63FVZW; -. DR BioCyc; TMAR243274:GC6P-822-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF00294; PfkB; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR PROSITE; PS00583; PFKB_KINASES_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|SAAS:SAAS00446051, ECO:0000313|EMBL:AAD35877.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00446051, KW ECO:0000313|EMBL:AAD35877.1}. FT DOMAIN 2 131 PfkB. {ECO:0000259|Pfam:PF00294}. SQ SEQUENCE 270 AA; 29625 MW; 6D48BEB47BF5A0BB CRC64; MKIAVVGGTF WDIFIFGENP HSSTIRESPG GSGLNVAYGL FLLGHTVDFY SNIGDDWRGK QIVELLEKAS FDTSHMSTIQ GGKTGIFIAH NDKPLAVDPG VNRKEMKLPS LSEYDLVFVT GEIPEKTIRK ICENTKNVIL DVGPGARFDT SDLNALVIGN ERECSFRKCD VVKMGSKGAR WGEVYVPGNG ISYPHSIGLG DLFDIVFVHH LPLGKSKKEI LEEAVKCSQI LGQKENVTPF ERISFLEPLS TKDDTLECPD ESKDASHHGG // ID Q9X127_THEMA Unreviewed; 442 AA. AC Q9X127; G4FE48; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 104. DE SubName: Full=Arylsulfatase regulator (Fe-S oxidoreductase) {ECO:0000313|EMBL:AGL50232.1}; DE SubName: Full=AstB/chuR-related protein {ECO:0000313|EMBL:AAD36375.1}; GN OrderedLocusNames=TM_1301 {ECO:0000313|EMBL:AAD36375.1}; GN ORFNames=Tmari_1308 {ECO:0000313|EMBL:AGL50232.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36375.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36375.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36375.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50232.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50232.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36375.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50232.1; -; Genomic_DNA. DR PIR; G72269; G72269. DR RefSeq; NP_229105.1; NC_000853.1. DR RefSeq; WP_004079919.1; NZ_CP011107.1. DR STRING; 243274.TM1301; -. DR EnsemblBacteria; AAD36375; AAD36375; TM_1301. DR EnsemblBacteria; AGL50232; AGL50232; Tmari_1308. DR GeneID; 898181; -. DR KEGG; tma:TM1301; -. DR KEGG; tmi:THEMA_07835; -. DR KEGG; tmm:Tmari_1308; -. DR KEGG; tmw:THMA_1326; -. DR PATRIC; 23937542; VBITheMar51294_1317. DR eggNOG; ENOG4105C4X; Bacteria. DR eggNOG; COG0641; LUCA. DR KO; K06871; -. DR OMA; HECFINS; -. DR OrthoDB; EOG60PH7N; -. DR BioCyc; TMAR243274:GC6P-1332-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1. DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00489002}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|SAAS:SAAS00489002}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00489002}; KW Metal-binding {ECO:0000256|SAAS:SAAS00489002}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00488995}. FT DOMAIN 93 254 Radical_SAM. {ECO:0000259|Pfam:PF04055}. SQ SEQUENCE 442 AA; 51523 MW; E1E076E5D17875EC CRC64; MSGYKFSDFL IKVQEKNRIL LYNVLLRSYA ETNVDELRRL QAALNGANEE FLLSTFVDRG IVLENHINEY ALFKYISNKI KYDRSVLSIT DVITLNCNLN CIYCMQQGIK PHNKERNGSL SPQDRVNLWL ALMDLFDTKT IAVTFFGGEP SLYPEKLSEI IRIAEKEQVP IKQYNIITNG VSFSNHMFEV LSNSKFRFIQ ITIDGPKNIH DKRRISQNYD GTWEVIIDNI NKLLNKTNLT IVIHTVLDRM NSEEKYGMMI DELIDIFGKN TIKERFLFNI GLLSHPNSSC AYTIENIPDI AEYANIYVNT IKVALERDIF LLDFLNIWPC TYHKETDLVV APNGDLYNCI SGVGREEFRI CSYSEFLNSP IDFLRRYSQF MENDNTDNEC KDCIYLPICN GGCRFNAYIL KTKKDCWKVF HQNSYPELLR LFSKFRERVK LV // ID Q9X1U3_THEMA Unreviewed; 178 AA. AC Q9X1U3; G4FFZ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Ribosomal subunit interface protein {ECO:0000313|EMBL:AGL50539.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36674.1}; GN OrderedLocusNames=TM_1607 {ECO:0000313|EMBL:AAD36674.1}; GN ORFNames=Tmari_1615 {ECO:0000313|EMBL:AGL50539.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36674.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36674.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36674.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50539.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50539.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36674.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50539.1; -; Genomic_DNA. DR PIR; C72235; C72235. DR RefSeq; NP_229407.1; NC_000853.1. DR RefSeq; WP_004082054.1; NZ_CP011107.1. DR STRING; 243274.TM1607; -. DR EnsemblBacteria; AAD36674; AAD36674; TM_1607. DR EnsemblBacteria; AGL50539; AGL50539; Tmari_1615. DR GeneID; 897668; -. DR KEGG; tma:TM1607; -. DR KEGG; tmi:THEMA_06215; -. DR KEGG; tmm:Tmari_1615; -. DR KEGG; tmw:THMA_1647; -. DR PATRIC; 23938188; VBITheMar51294_1626. DR eggNOG; ENOG41082TV; Bacteria. DR eggNOG; COG1544; LUCA. DR KO; K05808; -. DR OMA; DYGDENQ; -. DR OrthoDB; EOG618R0J; -. DR BioCyc; TMAR243274:GC6P-1653-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0044238; P:primary metabolic process; IEA:InterPro. DR Gene3D; 3.30.160.100; -; 1. DR InterPro; IPR032528; Ribosom_S30AE_C. DR InterPro; IPR003489; Ribosomal_S30Ae/sigma54_mod. DR Pfam; PF16321; Ribosom_S30AE_C; 1. DR Pfam; PF02482; Ribosomal_S30AE; 1. DR SUPFAM; SSF69754; SSF69754; 1. DR TIGRFAMs; TIGR00741; yfiA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 119 171 Ribosom_S30AE_C. FT {ECO:0000259|Pfam:PF16321}. SQ SEQUENCE 178 AA; 20704 MW; 4ACD1C3FE24A79F5 CRC64; MEYRITGKGV EISEAIKNYL EKRLDKIDRV IYDDDLVSFN VRIEKDGKNQ YVVKFNMNLK GNIINVEERH PDIYTAIDFA SDALEKQVKR LKERLKNHPH RSSALVETPL EEPGEFSPSD KVSSVKRVSL LNLDLDEAVM QMDELNHRFL VFRNVNTGEI NLLYRDENGD IHLIEMAE // ID Q9WXM4_THEMA Unreviewed; 142 AA. AC Q9WXM4; G4FGS5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Rubrerythrin {ECO:0000313|EMBL:AGL48932.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35103.1}; GN OrderedLocusNames=TM_0009 {ECO:0000313|EMBL:AAD35103.1}; GN ORFNames=Tmari_0006 {ECO:0000313|EMBL:AGL48932.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35103.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35103.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35103.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48932.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48932.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35103.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48932.1; -; Genomic_DNA. DR PIR; C72430; C72430. DR RefSeq; NP_227825.1; NC_000853.1. DR RefSeq; WP_004082446.1; NZ_CP011107.1. DR STRING; 243274.TM0009; -. DR EnsemblBacteria; AAD35103; AAD35103; TM_0009. DR EnsemblBacteria; AGL48932; AGL48932; Tmari_0006. DR GeneID; 896818; -. DR KEGG; tma:TM0009; -. DR KEGG; tmi:THEMA_04755; -. DR KEGG; tmm:Tmari_0006; -. DR KEGG; tmw:THMA_0005; -. DR PATRIC; 23934858; VBITheMar51294_0007. DR eggNOG; ENOG41062ND; Bacteria. DR eggNOG; COG1633; LUCA. DR OMA; QERDHSR; -. DR OrthoDB; EOG6KQ6GS; -. DR BioCyc; TMAR243274:GC6P-9-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR003251; Rubrerythrin. DR Pfam; PF02915; Rubrerythrin; 1. DR SUPFAM; SSF47240; SSF47240; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 6 140 Rubrerythrin. {ECO:0000259|Pfam:PF02915}. SQ SEQUENCE 142 AA; 16672 MW; D918BE2DCF6E90C1 CRC64; MIGPRDLLNI ALRIESTGYS YYKNLTEKTE GETKALFERL AEQERDHSRK FKEILEKYEQ DLNPSDEVLG YLEALAEISI FPKLEETPPD DLREAVRRAI EVEKDSIVFY SEILSYVPEK EPVQTIIDEE KKHLRDLLRL EV // ID Q9X0A2_THEMA Unreviewed; 286 AA. AC Q9X0A2; G4FEY8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=Oxidoreductase, aldo/keto reductase family {ECO:0000313|EMBL:AAD36074.1}; GN OrderedLocusNames=TM_1009 {ECO:0000313|EMBL:AAD36074.1}; GN ORFNames=Tmari_1012 {ECO:0000313|EMBL:AGL49936.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36074.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36074.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36074.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49936.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49936.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36074.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49936.1; -; Genomic_DNA. DR PIR; A72308; A72308. DR RefSeq; NP_228815.1; NC_000853.1. DR RefSeq; WP_004080532.1; NZ_CP011107.1. DR PDB; 1VP5; X-ray; 2.40 A; A/B=1-286. DR PDBsum; 1VP5; -. DR EnsemblBacteria; AAD36074; AAD36074; TM_1009. DR EnsemblBacteria; AGL49936; AGL49936; Tmari_1012. DR GeneID; 896824; -. DR KEGG; tma:TM1009; -. DR KEGG; tmi:THEMA_09310; -. DR KEGG; tmm:Tmari_1012; -. DR KEGG; tmw:THMA_1031; -. DR PATRIC; 23936947; VBITheMar51294_1022. DR eggNOG; ENOG4105CV8; Bacteria. DR eggNOG; COG0656; LUCA. DR OMA; TTKIWIS; -. DR OrthoDB; EOG68H8C2; -. DR BioCyc; TMAR243274:GC6P-1038-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red/Kv-b. DR InterPro; IPR018170; Aldo/ket_reductase_CS. DR InterPro; IPR020471; Aldo/keto_reductase. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1. DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VP5}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW NADP {ECO:0000213|PDB:1VP5}; KW Nucleotide-binding {ECO:0000213|PDB:1VP5}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 23 262 Aldo_ket_red. {ECO:0000259|Pfam:PF00248}. FT NP_BIND 21 22 NADP. {ECO:0000213|PDB:1VP5}. FT NP_BIND 140 141 NADP. {ECO:0000213|PDB:1VP5}. FT NP_BIND 188 193 NADP. {ECO:0000213|PDB:1VP5}. FT NP_BIND 233 235 NADP. {ECO:0000213|PDB:1VP5}. FT NP_BIND 239 243 NADP. {ECO:0000213|PDB:1VP5}. FT BINDING 45 45 NADP. {ECO:0000213|PDB:1VP5}. FT BINDING 162 162 NADP. {ECO:0000213|PDB:1VP5}. FT BINDING 199 199 NADP. {ECO:0000213|PDB:1VP5}. SQ SEQUENCE 286 AA; 33244 MW; E8A95EF2AC44FCEB CRC64; MQVPKVTLNN GVEMPILGYG VFQIPPEKTE ECVYEAIKVG YRLIDTAASY MNEEGVGRAI KRAIDEGIVR REELFVTTKL WVSDVGYEST KKAFEKSLKK LQLEYIDLYL IHQPFGDVHC AWKAMEEMYK DGLVRAIGVS NFYPDRLMDL MVHHEIVPAV NQIEIHPFYQ RQEEIEFMRN YNIQPEAWGP FAEGRKNIFQ NGVLRSIAEK YGKTVAQVIL RWLTQKGIVA IPKTVRRERM KENISIFDFE LTQEDMEKIA TLDEGQSAFF SHRDPEVVKW ICSLKR // ID Q9WZM5_THEMA Unreviewed; 121 AA. AC Q9WZM5; G4FD57; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 100. DE SubName: Full=Transcriptional regulator, GntR family {ECO:0000313|EMBL:AAD35848.1}; GN OrderedLocusNames=TM_0766 {ECO:0000313|EMBL:AAD35848.1}; GN ORFNames=Tmari_0767 {ECO:0000313|EMBL:AGL49692.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35848.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35848.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35848.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49692.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49692.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 HTH gntR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000706}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35848.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49692.1; -; Genomic_DNA. DR PIR; D72336; D72336. DR RefSeq; NP_228575.1; NC_000853.1. DR RefSeq; WP_004080932.1; NZ_CP011107.1. DR STRING; 243274.TM0766; -. DR EnsemblBacteria; AAD35848; AAD35848; TM_0766. DR EnsemblBacteria; AGL49692; AGL49692; Tmari_0767. DR GeneID; 898434; -. DR KEGG; tma:TM0766; -. DR KEGG; tmi:THEMA_00820; -. DR KEGG; tmm:Tmari_0767; -. DR KEGG; tmw:THMA_0785; -. DR PATRIC; 23936454; VBITheMar51294_0779. DR eggNOG; ENOG4105W8V; Bacteria. DR eggNOG; COG1725; LUCA. DR KO; K07979; -. DR OMA; RDMASSI; -. DR OrthoDB; EOG699754; -. DR BioCyc; TMAR243274:GC6P-793-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00392; GntR; 1. DR SMART; SM00345; HTH_GNTR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50949; HTH_GNTR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000706}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU000706}; KW Transcription regulation {ECO:0000256|RuleBase:RU000706}. FT DOMAIN 11 79 HTH gntR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50949}. SQ SEQUENCE 121 AA; 14057 MW; 1F281D949F4913F6 CRC64; MWFRIDFHSS KPIYEQIKER IKLLILSGKL KEGEFVPSIR SLAEDLGVNL NTVARAYREL VQEGVLEVRR GEGYVVSKVN VEKIRTQLET ELRKKIEDCK KAGIPLERIL KIAEEIYRGD E // ID Q9X1M0_THEMA Unreviewed; 113 AA. AC Q9X1M0; G4FFS2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36601.1}; GN OrderedLocusNames=TM_1534 {ECO:0000313|EMBL:AAD36601.1}; GN ORFNames=Tmari_1542 {ECO:0000313|EMBL:AGL50466.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36601.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36601.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36601.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50466.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50466.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36601.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50466.1; -; Genomic_DNA. DR PIR; B72242; B72242. DR RefSeq; NP_229334.1; NC_000853.1. DR RefSeq; WP_004081912.1; NZ_CP011107.1. DR STRING; 243274.TM1534; -. DR EnsemblBacteria; AAD36601; AAD36601; TM_1534. DR EnsemblBacteria; AGL50466; AGL50466; Tmari_1542. DR GeneID; 897979; -. DR KEGG; tma:TM1534; -. DR KEGG; tmi:THEMA_06615; -. DR KEGG; tmm:Tmari_1542; -. DR KEGG; tmw:THMA_1568; -. DR PATRIC; 23938028; VBITheMar51294_1552. DR OMA; VRIDRRK; -. DR OrthoDB; EOG6WHNSP; -. DR BioCyc; TMAR243274:GC6P-1574-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 62 89 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 113 AA; 13006 MW; 30817A3BC97A83E1 CRC64; MYVKIDRKKL PCVETEGTVL CTTCGNSYQI EPRQKLHSII VTTCPHCGHQ NINVVTNSVK FIEEVLSKID RLRKDLMELK KSLEIELQQN GFVDNYPEVF KADDEKQAEP KLL // ID Q9WYL5_THEMA Unreviewed; 183 AA. AC Q9WYL5; G4FHU5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Anaerobic ribonucleoside-triphosphate reductase-related protein {ECO:0000313|EMBL:AAD35469.1}; DE SubName: Full=Ribonucleotide reductase of class III (Anaerobic), activating protein {ECO:0000313|EMBL:AGL49307.1}; DE EC=1.97.1.4 {ECO:0000313|EMBL:AGL49307.1}; GN OrderedLocusNames=TM_0384 {ECO:0000313|EMBL:AAD35469.1}; GN ORFNames=Tmari_0382 {ECO:0000313|EMBL:AGL49307.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35469.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35469.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35469.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49307.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49307.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35469.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49307.1; -; Genomic_DNA. DR PIR; H72383; H72383. DR RefSeq; NP_228194.1; NC_000853.1. DR RefSeq; WP_004083204.1; NZ_CP011107.1. DR STRING; 243274.TM0384; -. DR EnsemblBacteria; AAD35469; AAD35469; TM_0384. DR EnsemblBacteria; AGL49307; AGL49307; Tmari_0382. DR GeneID; 897361; -. DR KEGG; tma:TM0384; -. DR KEGG; tmi:THEMA_02800; -. DR KEGG; tmm:Tmari_0382; -. DR KEGG; tmw:THMA_0391; -. DR PATRIC; 23935651; VBITheMar51294_0390. DR eggNOG; ENOG4107HIH; Bacteria. DR eggNOG; ENOG410YPIY; LUCA. DR KO; K04068; -. DR OMA; EPLAPYN; -. DR OrthoDB; EOG686NKZ; -. DR BioCyc; TMAR243274:GC6P-398-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR014191; Anaer_RNR_activator. DR TIGRFAMs; TIGR02826; RNR_activ_nrdG3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49307.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 183 AA; 21843 MW; AA3943698795DE45 CRC64; MYVNRIGTFR DHPDLYGVSV YFQGCDAKPK CYMCHNPETW HLSEEYKRPS EVVTKIIDEK LSSLLRYFPK AALVFLGGEP LAPYNREEML SLSKMFKEKY GERLTVVLFT WRLPKDIVKE NLLKYVQYVD EFVMGRYLHT YRRDGFPASK NQIHIDRRTF ERMIEAVLRR GHYEGSVFVR KRI // ID Q9X250_THEMA Unreviewed; 264 AA. AC Q9X250; G4FGB3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Chalcone/stilbene synthase family protein {ECO:0000313|EMBL:AGL50659.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36792.1}; GN OrderedLocusNames=TM_1727 {ECO:0000313|EMBL:AAD36792.1}; GN ORFNames=Tmari_1735 {ECO:0000313|EMBL:AGL50659.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36792.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36792.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36792.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50659.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50659.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36792.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50659.1; -; Genomic_DNA. DR PIR; F72216; F72216. DR RefSeq; NP_229525.1; NC_000853.1. DR RefSeq; WP_004082242.1; NZ_CP011107.1. DR PDB; 2I76; X-ray; 3.00 A; A/B=2-264. DR PDBsum; 2I76; -. DR STRING; 243274.TM1727; -. DR EnsemblBacteria; AAD36792; AAD36792; TM_1727. DR EnsemblBacteria; AGL50659; AGL50659; Tmari_1735. DR GeneID; 897875; -. DR KEGG; tma:TM1727; -. DR KEGG; tmi:THEMA_05600; -. DR KEGG; tmm:Tmari_1735; -. DR KEGG; tmw:THMA_1769; -. DR PATRIC; 23938430; VBITheMar51294_1745. DR eggNOG; ENOG41082QP; Bacteria. DR eggNOG; COG5495; LUCA. DR OMA; PELLIHT; -. DR OrthoDB; EOG6GFGQ2; -. DR BioCyc; TMAR243274:GC6P-1775-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro. DR Gene3D; 1.10.1040.20; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR018931; DUF2520. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF10728; DUF2520; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2I76}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW NADP {ECO:0000213|PDB:2I76}; KW Nucleotide-binding {ECO:0000213|PDB:2I76}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 122 231 DUF2520. {ECO:0000259|Pfam:PF10728}. FT NP_BIND 30 31 NADP. {ECO:0000213|PDB:2I76}. FT NP_BIND 66 68 NADP. {ECO:0000213|PDB:2I76}. FT BINDING 8 8 NADP. {ECO:0000213|PDB:2I76}. FT BINDING 35 35 NADP. {ECO:0000213|PDB:2I76}. FT BINDING 213 213 NADP. {ECO:0000213|PDB:2I76}. FT BINDING 218 218 NADP. {ECO:0000213|PDB:2I76}. SQ SEQUENCE 264 AA; 29884 MW; 3ABD9A420A4E7FE7 CRC64; MVLNFVGTGT LTRFFLECLK DRYEIGYILS RSIDRARNLA EVYGGKAATL EKHPELNGVV FVIVPDRYIK TVANHLNLGD AVLVHCSGFL SSEIFKKSGR ASIHPNFSFS SLEKALEMKD QIVFGLEGDE RGLPIVKKIA EEISGKYFVI PSEKKKAYHL AAVIASNFPV ALAYLSKRIY TLLGLDEPEL LIHTLMKGVA DNIKKMRVEC SLTGPVKRGD WQVVEEERRE YEKIFGNTVL YDEIVKLLRE VAESERREAQ EDER // ID Q9X1L8_THEMA Unreviewed; 438 AA. AC Q9X1L8; G4FFS0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 102. DE SubName: Full=FixC protein {ECO:0000313|EMBL:AAD36599.1}; DE SubName: Full=Putative electron transfer flavoprotein-quinone oxidoreductase FixC {ECO:0000313|EMBL:AGL50464.1}; DE EC=1.5.5.- {ECO:0000313|EMBL:AGL50464.1}; GN OrderedLocusNames=TM_1532 {ECO:0000313|EMBL:AAD36599.1}; GN ORFNames=Tmari_1540 {ECO:0000313|EMBL:AGL50464.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36599.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36599.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36599.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50464.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50464.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36599.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50464.1; -; Genomic_DNA. DR PIR; H72241; H72241. DR RefSeq; NP_229332.1; NC_000853.1. DR RefSeq; WP_004081907.1; NZ_CP011107.1. DR STRING; 243274.TM1532; -. DR EnsemblBacteria; AAD36599; AAD36599; TM_1532. DR EnsemblBacteria; AGL50464; AGL50464; Tmari_1540. DR GeneID; 897980; -. DR KEGG; tma:TM1532; -. DR KEGG; tmi:THEMA_06625; -. DR KEGG; tmm:Tmari_1540; -. DR KEGG; tmw:THMA_1566; -. DR PATRIC; 23938024; VBITheMar51294_1550. DR eggNOG; ENOG4105DWH; Bacteria. DR eggNOG; COG0644; LUCA. DR KO; K00313; -. DR OMA; HREGSNM; -. DR OrthoDB; EOG6716K7; -. DR BioCyc; TMAR243274:GC6P-1572-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR002938; FAD-bd. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF01494; FAD_binding_3; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50464.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 354 FAD_binding_3. FT {ECO:0000259|Pfam:PF01494}. SQ SEQUENCE 438 AA; 48974 MW; 3F8AE42C24DB5E0A CRC64; MKIEFDVVVV GAGPSGLSCA YVLAKNGLKV AVVEKGEYPG SKNVMGGVLY VHPLKEIMPD FLEKAANSKA LERNVIEQNL WLLGNEGVIK IGHRNVEWKE NPNAFTVLRA NFDRWFAQEV EKAGALIIPK TKVEDFLRNE KGEIAGVVTS RPKGEIHSKA VVIAEGVNPI LTMKAGLRKE DLKPHMVAVA VKEVISVPED VVNRVFGVEG NDGATIELLG SWSEGMFGMG FLYANRSSVS LGCGVLLEDL RKKKIKPYQL LENLKNHPVI SDMLGEYRNN TMEYLAHLIP EGGYYAMPKV YGDRVLVCGD AAMLVNSIHR EGSNHAITSG RLAAETLLEA FEKGDFSEKI LKNYYLRLKE SFILKDLEKY KDLMPTMEKN HQFVEIYPDL ANDALKRFLQ VDGTPKWDVQ KQIADMVLSR RSLIGISLDL LRFWRAVR // ID Q9WZP9_THEMA Unreviewed; 212 AA. AC Q9WZP9; G4FD32; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Putative preQ0 transporter {ECO:0000313|EMBL:AGL49718.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35874.1}; GN OrderedLocusNames=TM_0792 {ECO:0000313|EMBL:AAD35874.1}; GN ORFNames=Tmari_0793 {ECO:0000313|EMBL:AGL49718.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35874.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35874.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35874.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49718.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49718.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35874.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49718.1; -; Genomic_DNA. DR PIR; A72334; A72334. DR RefSeq; NP_228601.1; NC_000853.1. DR RefSeq; WP_004080883.1; NZ_CP011107.1. DR STRING; 243274.TM0792; -. DR EnsemblBacteria; AAD35874; AAD35874; TM_0792. DR EnsemblBacteria; AGL49718; AGL49718; Tmari_0793. DR GeneID; 898460; -. DR KEGG; tma:TM0792; -. DR KEGG; tmi:THEMA_00690; -. DR KEGG; tmm:Tmari_0793; -. DR KEGG; tmw:THMA_0811; -. DR PATRIC; 23936504; VBITheMar51294_0804. DR eggNOG; ENOG4108PKW; Bacteria. DR eggNOG; COG1738; LUCA. DR KO; K09125; -. DR OMA; YEIEERN; -. DR OrthoDB; EOG60CWR6; -. DR BioCyc; TMAR243274:GC6P-819-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003744; DUF165. DR Pfam; PF02592; Vut_1; 1. DR TIGRFAMs; TIGR00697; TIGR00697; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 89 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 152 172 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 178 199 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 212 AA; 23537 MW; D3D8182EDAD73710 CRC64; MEKSNEKLIL LTGIFVSALT ISNVIAGKLV NIGPFLVPVA VLCYPITFAV TDIVSEVYGK RTAQKMVWTG FFTSLILVIY SQIAVFYPPA SIFANNEAFV KVFGSTPRIV LASILAYILS QTHDVWAFHF WKKITRGSHL WLRNNLSTMV SQFIDTLTFI TVAFAGTIPG NVLVQMIFSQ YVVKLIMALI DTPFVYLGVK LVSGQWTVKE GS // ID Q9WZR8_THEMA Unreviewed; 300 AA. AC Q9WZR8; G4FD13; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE SubName: Full=Chitobiose ABC transport system, permease protein 1 {ECO:0000313|EMBL:AGL49737.1}; DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35893.1}; GN OrderedLocusNames=TM_0811 {ECO:0000313|EMBL:AAD35893.1}; GN ORFNames=Tmari_0812 {ECO:0000313|EMBL:AGL49737.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35893.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35893.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35893.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49737.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49737.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35893.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49737.1; -; Genomic_DNA. DR PIR; D72331; D72331. DR RefSeq; NP_228620.1; NC_000853.1. DR RefSeq; WP_004080851.1; NZ_CP011107.1. DR STRING; 243274.TM0811; -. DR DNASU; 898479; -. DR EnsemblBacteria; AAD35893; AAD35893; TM_0811. DR EnsemblBacteria; AGL49737; AGL49737; Tmari_0812. DR GeneID; 898479; -. DR KEGG; tma:TM0811; -. DR KEGG; tmm:Tmari_0812; -. DR KEGG; tmw:THMA_0830; -. DR PATRIC; 23936542; VBITheMar51294_0823. DR eggNOG; ENOG4105DB9; Bacteria. DR eggNOG; COG1175; LUCA. DR KO; K17245; -. DR OMA; TPVDWFA; -. DR OrthoDB; EOG69SKBS; -. DR BioCyc; TMAR243274:GC6P-838-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 14 34 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 78 98 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 110 130 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 159 182 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 217 238 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 270 290 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 73 286 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 300 AA; 34482 MW; 9DEBA709C29DAB0A CRC64; MPGRYYKSLR KKQLLLAFFF ITIPTLLMVL FIYYPLVFGI KISFYQYDIV GESLYIGLKN YVDLLRDPLF WNAFKNSLLY LLVVPPLQLI SILLAVLLDR AIRGRNLFRT LIFLPVVTPI TIAAITWQWM YREKGFINFL LQSLHIIDEP IAFLSDPKIA LFAIMFVTMW KGFGYYMVIY LAGLQSIPRE LIEAARVDGA KPSQVFFKVT IPLLKPYILF CSTMSSIAAL NVFGEIYAMT KGGPVHATET MGIFIYNRAF EYLQFGYSNA AAVLFSFVVI AFSLLNFYLF REGGLKSYYA // ID G4FFR3_THEMA Unreviewed; 274 AA. AC G4FFR3; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 13-APR-2016, entry version 42. DE SubName: Full=Endo-1,4-beta-glucanase {ECO:0000313|EMBL:AGL50457.1}; DE EC=3.2.1.4 {ECO:0000313|EMBL:AGL50457.1}; DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:AAD36592.1}; GN OrderedLocusNames=TM_1525 {ECO:0000313|EMBL:AAD36592.1}; GN ORFNames=Tmari_1533 {ECO:0000313|EMBL:AGL50457.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AGL50457.1, ECO:0000313|Proteomes:UP000013901}; RN [1] {ECO:0000313|EMBL:AAD36592.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36592.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50457.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50457.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) CC family. {ECO:0000256|RuleBase:RU361163}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36592.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50457.1; -; Genomic_DNA. DR PIR; A72241; A72241. DR RefSeq; NP_229325.1; NC_000853.1. DR RefSeq; WP_004081891.1; NZ_CP011107.1. DR STRING; 243274.TM1525; -. DR CAZy; GH12; Glycoside Hydrolase Family 12. DR EnsemblBacteria; AAD36592; AAD36592; TM_1525. DR EnsemblBacteria; AGL50457; AGL50457; Tmari_1533. DR GeneID; 897395; -. DR KEGG; tma:TM1525; -. DR KEGG; tmi:THEMA_06665; -. DR KEGG; tmm:Tmari_1533; -. DR KEGG; tmw:THMA_1559; -. DR eggNOG; ENOG4111VJ0; LUCA. DR OMA; LVIPIYI; -. DR BioCyc; TMAR243274:GC6P-1565-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.180; -; 1. DR InterPro; IPR013320; ConA-like_dom. DR InterPro; IPR013319; GH11/12. DR InterPro; IPR002594; GH12. DR Pfam; PF01670; Glyco_hydro_12; 1. DR SUPFAM; SSF49899; SSF49899; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361163}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361163, KW ECO:0000313|EMBL:AGL50457.1}; KW Hydrolase {ECO:0000256|RuleBase:RU361163, KW ECO:0000313|EMBL:AGL50457.1}; KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361163}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 274 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006953697. SQ SEQUENCE 274 AA; 31734 MW; 72C0A5ACAD7BA358 CRC64; MRWAVLLMVV FSALLFSSEV VLTSVGATDI SFNGFPVTME LNFWNVKSYE GETWLKFDGE KVEFYADLYN IVLQNPDSWV HGYPEIYYGY KPWAGHNSGV EFLPVKVKDL PDFYVTLDYS IWYENNLPIN LAMETWITRS PDQTSVSSGD AEIMVWFYNN VLMPGGQKVD EFTTTVEING VKQETKWDVY FAPWGWDYLA FRLTTPMKEG KVKINVKDFV QKAAEVVKKH STRIDNFEEL YFCVWEIGTE FGDPNTTAAK FGWTFRDFSV EVVK // ID Q9WZC8_THEMA Unreviewed; 263 AA. AC Q9WZC8; G4FDG4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35744.1}; GN OrderedLocusNames=TM_0660 {ECO:0000313|EMBL:AAD35744.1}; GN ORFNames=Tmari_0660 {ECO:0000313|EMBL:AGL49585.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35744.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35744.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35744.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49585.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49585.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35744.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49585.1; -; Genomic_DNA. DR PIR; A72349; A72349. DR RefSeq; NP_228469.1; NC_000853.1. DR RefSeq; WP_004081113.1; NZ_CP011107.1. DR PDB; 2ZBU; X-ray; 2.10 A; A/B/C/D=1-263. DR PDB; 2ZBV; X-ray; 2.05 A; A/B/C=1-263. DR PDBsum; 2ZBU; -. DR PDBsum; 2ZBV; -. DR STRING; 243274.TM0660; -. DR EnsemblBacteria; AAD35744; AAD35744; TM_0660. DR EnsemblBacteria; AGL49585; AGL49585; Tmari_0660. DR GeneID; 897772; -. DR KEGG; tma:TM0660; -. DR KEGG; tmi:THEMA_01365; -. DR KEGG; tmm:Tmari_0660; -. DR KEGG; tmw:THMA_0675; -. DR PATRIC; 23936234; VBITheMar51294_0670. DR eggNOG; ENOG4105VDU; Bacteria. DR eggNOG; COG1912; LUCA. DR KO; K09134; -. DR OMA; GSFVMEQ; -. DR OrthoDB; EOG63FW3R; -. DR BioCyc; TMAR243274:GC6P-685-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.40.30.90; -; 1. DR InterPro; IPR002747; SAM_Chlor/Fluor. DR InterPro; IPR023227; SAM_OH_AdoTrfase_C. DR InterPro; IPR023228; SAM_OH_AdoTrfase_N. DR Pfam; PF01887; SAM_adeno_trans; 1. DR PIRSF; PIRSF006779; UCP006779; 1. DR SUPFAM; SSF101852; SSF101852; 1. DR SUPFAM; SSF102522; SSF102522; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2ZBU, ECO:0000213|PDB:2ZBV}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 263 AA; 29199 MW; 0F96FB6DCA918AE1 CRC64; MIGFLTDWGL KSHYVGVAKA VIKRINPSAE IIDITHEVEP FNVRKASHVL YRASLDFPPS TVFLVVVDYG VGTSRKAIVM KTKNDQYFVA PDNGVLTVVA EEYGVAEIRE IENRELFYKK NPSFTFHGRD IFAPVAAHLD MGLPLERVGD RLLSYEVLKM RKPVVENEKV IGEVAIVDTF GNVSTNIPFD LFLKLSVDFD DVVRVRVGRK EFKAAVAKAF GDVDTGELLV HPDSAGFLEI AVNLGDASQV LSVKEGDEIE ICR // ID Q9WY53_THEMA Unreviewed; 69 AA. AC Q9WY53; G4FHC4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35302.1}; GN OrderedLocusNames=TM_0210 {ECO:0000313|EMBL:AAD35302.1}; GN ORFNames=Tmari_0208 {ECO:0000313|EMBL:AGL49134.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35302.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35302.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35302.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49134.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49134.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35302.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49134.1; -; Genomic_DNA. DR PIR; D72403; D72403. DR RefSeq; NP_228025.1; NC_000853.1. DR RefSeq; WP_004082882.1; NZ_CP011107.1. DR STRING; 243274.TM0210; -. DR EnsemblBacteria; AAD35302; AAD35302; TM_0210. DR EnsemblBacteria; AGL49134; AGL49134; Tmari_0208. DR GeneID; 897082; -. DR KEGG; tma:TM0210; -. DR KEGG; tmi:THEMA_03675; -. DR KEGG; tmm:Tmari_0208; -. DR KEGG; tmw:THMA_0217; -. DR PATRIC; 23935292; VBITheMar51294_0212. DR OMA; ENDIPYV; -. DR OrthoDB; EOG6C5RTS; -. DR BioCyc; TMAR243274:GC6P-223-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR018551; DUF2007. DR Pfam; PF09413; DUF2007; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 68 DUF2007. {ECO:0000259|Pfam:PF09413}. SQ SEQUENCE 69 AA; 7956 MW; AAF9CBDFFED9FB90 CRC64; MKWKTLIEGS ELEVKMIEDI LKENGVPYVV ETCDDVTPRA IFGSSALMVI KVPEKFLEEA KRILEEMRE // ID Q9WXW5_THEMA Unreviewed; 378 AA. AC Q9WXW5; G4FH25; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE SubName: Full=Transcriptional regulator, XylR-related {ECO:0000313|EMBL:AAD35204.1}; DE SubName: Full=Xylose repressor XylR (ROK family) {ECO:0000313|EMBL:AGL49033.1}; GN OrderedLocusNames=TM_0110 {ECO:0000313|EMBL:AAD35204.1}; GN ORFNames=Tmari_0107 {ECO:0000313|EMBL:AGL49033.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35204.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35204.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35204.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49033.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49033.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35204.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49033.1; -; Genomic_DNA. DR PIR; E72416; E72416. DR RefSeq; NP_227926.1; NC_000853.1. DR RefSeq; WP_004082680.1; NZ_CP011107.1. DR STRING; 243274.TM0110; -. DR EnsemblBacteria; AAD35204; AAD35204; TM_0110. DR EnsemblBacteria; AGL49033; AGL49033; Tmari_0107. DR GeneID; 896937; -. DR KEGG; tma:TM0110; -. DR KEGG; tmi:THEMA_04255; -. DR KEGG; tmm:Tmari_0107; -. DR KEGG; tmw:THMA_0106; -. DR PATRIC; 23935060; VBITheMar51294_0108. DR eggNOG; ENOG4105E2R; Bacteria. DR eggNOG; COG1940; LUCA. DR OMA; IRRNICK; -. DR OrthoDB; EOG64R61Z; -. DR BioCyc; TMAR243274:GC6P-110-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR012318; HTH_CRP. DR InterPro; IPR000600; ROK. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00480; ROK; 1. DR SMART; SM00419; HTH_CRP; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS01125; ROK; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 18 74 HTH crp-type DNA-binding. FT {ECO:0000259|SMART:SM00419}. SQ SEQUENCE 378 AA; 42573 MW; C2925BAC15F42A56 CRC64; MKYNSPRIKI LNKKSILKVI HENHPISRSD ISEVTGLTPS SVTRLTKELI DEGYIREIGT MGKNSPGRRR ILLDLRKNAF LSLVFDIGVN ITTYGIGFFD GEVEPRGTFN TPKEPVEFFN IVKEIYERIS GEYRISRISL SVPGMVDMEE KKILLAPNLE WENVNIKELL KVDVPVLADN EANLSMLAEK YHSEDLRNVK EAVFIIIREG VGTGLMIDGK IFRGPSFTAG EAGHMTVNMY SDRQCHCSNW GCWELVSSIN WTIEQYGKEL PGKNAIEKFQ ALKQRNDAKR ILMKFAENIA VGIVNLVNIL NPELVILGGE VVDLGENFLD IIKDFVHQRA LKAAVKDLKI RTTEFRNISS NLVGAAVLAV EDIIEEVK // ID Q9X2B2_THEMA Unreviewed; 288 AA. AC Q9X2B2; G4FGI0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=CRISPR-associated RAMP Cmr4 {ECO:0000313|EMBL:AGL50726.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36855.1}; GN OrderedLocusNames=TM_1792 {ECO:0000313|EMBL:AAD36855.1}; GN ORFNames=Tmari_1802 {ECO:0000313|EMBL:AGL50726.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36855.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36855.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36855.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50726.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50726.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36855.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50726.1; -; Genomic_DNA. DR PIR; E72209; E72209. DR RefSeq; NP_229589.1; NC_000853.1. DR RefSeq; WP_004082339.1; NZ_CP011107.1. DR STRING; 243274.TM1792; -. DR EnsemblBacteria; AAD36855; AAD36855; TM_1792. DR EnsemblBacteria; AGL50726; AGL50726; Tmari_1802. DR GeneID; 897725; -. DR KEGG; tma:TM1792; -. DR KEGG; tmi:THEMA_05230; -. DR KEGG; tmm:Tmari_1802; -. DR KEGG; tmw:THMA_1838; -. DR PATRIC; 23938573; VBITheMar51294_1813. DR eggNOG; ENOG4108PDN; Bacteria. DR eggNOG; COG1336; LUCA. DR KO; K09000; -. DR OMA; KGALWYE; -. DR OrthoDB; EOG67DPJP; -. DR BioCyc; TMAR243274:GC6P-1843-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR013410; CRISPR-assoc_RAMP_Cmr4. DR InterPro; IPR005537; RAMP_III_fam. DR Pfam; PF03787; RAMPs; 1. DR TIGRFAMs; TIGR02580; cas_RAMP_Cmr4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 288 AA; 32759 MW; AFB9E69AF4FB0B5C CRC64; MEGRVFLLYA ETQVHAGTGF EIGVVDLPIQ RERTTKFPII HGIKGALRAY FRSLIKEDKI DEKKIEEIFG SEPKSDKGTV PGSLSFSEAR ILLFPVRNPD RLFVWVTCPL VLIKFAKSVG DNDVVKELEE ANIDYGKAVS FYGSGEVFLE EVKLEPFVGE LPRTRELISK ISNCAPVDYL KKKMESDVVV VNDVLFSEIV QAMTEVVPRV RINREKKTVE EGGLWYEEYL PQDTVMYFVV RKTYYGNKED SGKDSLMEVF ENEVNGELIN IGGKETVGKG MMWVHAWR // ID Q9X168_THEMA Unreviewed; 482 AA. AC Q9X168; G4FF83; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 117. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|RuleBase:RU003928}; DE EC=1.1.1.205 {ECO:0000256|RuleBase:RU003928}; GN OrderedLocusNames=TM_1347 {ECO:0000313|EMBL:AAD36418.1}; GN ORFNames=Tmari_1354 {ECO:0000313|EMBL:AGL50278.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36418.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36418.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36418.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50278.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50278.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O = CC xanthosine 5'-phosphate + NADH. {ECO:0000256|RuleBase:RU003928}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; CC XMP from IMP: step 1/1. {ECO:0000256|RuleBase:RU003928}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC {ECO:0000256|RuleBase:RU003927}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36418.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50278.1; -; Genomic_DNA. DR PIR; C72264; C72264. DR RefSeq; NP_229148.1; NC_000853.1. DR RefSeq; WP_004081543.1; NZ_CP011107.1. DR PDB; 1VRD; X-ray; 2.18 A; A/B=1-482. DR PDBsum; 1VRD; -. DR STRING; 243274.TM1347; -. DR EnsemblBacteria; AAD36418; AAD36418; TM_1347. DR EnsemblBacteria; AGL50278; AGL50278; Tmari_1354. DR GeneID; 898133; -. DR KEGG; tma:TM1347; -. DR KEGG; tmi:THEMA_07605; -. DR KEGG; tmm:Tmari_1354; -. DR KEGG; tmw:THMA_1372; -. DR PATRIC; 23937632; VBITheMar51294_1359. DR eggNOG; ENOG4105CP4; Bacteria. DR eggNOG; COG0516; LUCA. DR eggNOG; COG0517; LUCA. DR KO; K00088; -. DR OMA; SSMGYCG; -. DR OrthoDB; EOG6GTZPV; -. DR BioCyc; TMAR243274:GC6P-1380-MONOMER; -. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01964; IMPDH; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR005990; IMP_DH. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR PANTHER; PTHR11911:SF6; PTHR11911:SF6; 2. DR Pfam; PF00571; CBS; 2. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000130; IMPDH; 1. DR SMART; SM00116; CBS; 2. DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VRD}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW GMP biosynthesis {ECO:0000256|RuleBase:RU003928}; KW Metal-binding {ECO:0000256|RuleBase:RU003928}; KW NAD {ECO:0000256|PIRSR:PIRSR000130-3, ECO:0000256|RuleBase:RU003928}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003927, KW ECO:0000313|EMBL:AGL50278.1}; KW Potassium {ECO:0000256|PIRSR:PIRSR000130-4, KW ECO:0000256|RuleBase:RU003928}; KW Purine biosynthesis {ECO:0000256|RuleBase:RU003928}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 89 148 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 149 210 CBS. {ECO:0000259|PROSITE:PS51371}. FT NP_BIND 244 246 NAD. {ECO:0000256|PIRSR:PIRSR000130-3}. FT NP_BIND 294 296 NAD. {ECO:0000256|PIRSR:PIRSR000130-3}. FT REGION 334 336 IMP binding. FT {ECO:0000256|PIRSR:PIRSR000130-2}. FT REGION 357 358 IMP binding. FT {ECO:0000256|PIRSR:PIRSR000130-2}. FT REGION 381 385 IMP binding. FT {ECO:0000256|PIRSR:PIRSR000130-2}. FT ACT_SITE 301 301 Thioimidate intermediate. FT {ECO:0000256|PIRSR:PIRSR000130-1}. FT ACT_SITE 397 397 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR000130-1}. FT METAL 296 296 Potassium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 298 298 Potassium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000130-4}. FT METAL 301 301 Potassium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000130-4}. FT BINDING 299 299 IMP. {ECO:0000256|PIRSR:PIRSR000130-2}. FT BINDING 409 409 IMP. {ECO:0000256|PIRSR:PIRSR000130-2}. SQ SEQUENCE 482 AA; 52014 MW; 4E08237F69D909FA CRC64; MKEALTFDDV LLVPQYSEVL PKDVKIDTRL TRQIRINIPL VSAAMDTVTE AALAKALARE GGIGIIHKNL TPDEQARQVS IVKKTENGII YDPITVTPDM TVKEAIDLMA EYKIGGLPVV DEEGRLVGLL TNRDVRFEKN LSKKIKDLMT PREKLIVAPP DISLEKAKEI LHQHRIEKLP LVSKDNKLVG LITIKDIMSV IEHPNAARDE KGRLLVGAAV GTSPETMERV EKLVKAGVDV IVIDTAHGHS RRVIETLEMI KADYPDLPVV AGNVATPEGT EALIKAGADA VKVGVGPGSI CTTRVVAGVG VPQLTAVMEC SEVARKYDVP IIADGGIRYS GDIVKALAAG AESVMVGSIF AGTEEAPGET ILYQGRKYKA YRGMGSLGAM RSGSADRYGQ EGENKFVPEG IEGMVPYKGT VKDVVHQLVG GLRSGMGYIG ARTIKELQEK AVFVKITPAG VKESHPHDII ITKESPNYWV QA // ID Q9X285_THEMA Unreviewed; 121 AA. AC Q9X285; G4FGF1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36828.1}; GN OrderedLocusNames=TM_1764 {ECO:0000313|EMBL:AAD36828.1}; GN ORFNames=Tmari_1773 {ECO:0000313|EMBL:AGL50697.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36828.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36828.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36828.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50697.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50697.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36828.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50697.1; -; Genomic_DNA. DR PIR; C72212; C72212. DR RefSeq; NP_229561.1; NC_000853.1. DR RefSeq; WP_004082310.1; NZ_CP011107.1. DR STRING; 243274.TM1764; -. DR EnsemblBacteria; AAD36828; AAD36828; TM_1764. DR EnsemblBacteria; AGL50697; AGL50697; Tmari_1773. DR GeneID; 897739; -. DR KEGG; tma:TM1764; -. DR KEGG; tmi:THEMA_05405; -. DR KEGG; tmm:Tmari_1773; -. DR KEGG; tmw:THMA_1808; -. DR PATRIC; 23938508; VBITheMar51294_1783. DR eggNOG; ENOG4107136; Bacteria. DR eggNOG; ENOG410YY4A; LUCA. DR OMA; IEIERTP; -. DR OrthoDB; EOG6GFGP8; -. DR BioCyc; TMAR243274:GC6P-1813-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR005531; Asp23. DR Pfam; PF03780; Asp23; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 121 AA; 14049 MW; 92DF73AD61FFB472 CRC64; MAEEYKNIEI SDGVIKEIAI RSIEEFLGDV SSKVIKKIRK SLDVTRNPDD SLVIEFKIDV PYGEPIPEYV SKLTEKVKHD VEMMTSMKVE SINVTVENVF EKEEELEEEP EEIKEDEEKK E // ID Q9X0R5_THEMA Unreviewed; 379 AA. AC Q9X0R5; G4FEG3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 98. DE SubName: Full=Aldo/keto reductase {ECO:0000313|EMBL:AGL50114.1}; DE SubName: Full=Oxidoreductase, aldo/keto reductase family {ECO:0000313|EMBL:AAD36258.1}; GN OrderedLocusNames=TM_1183 {ECO:0000313|EMBL:AAD36258.1}; GN ORFNames=Tmari_1190 {ECO:0000313|EMBL:AGL50114.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36258.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36258.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36258.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50114.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50114.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36258.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50114.1; -; Genomic_DNA. DR PIR; E72284; E72284. DR RefSeq; NP_228988.1; NC_000853.1. DR RefSeq; WP_004080165.1; NZ_CP011107.1. DR STRING; 243274.TM1183; -. DR EnsemblBacteria; AAD36258; AAD36258; TM_1183. DR EnsemblBacteria; AGL50114; AGL50114; Tmari_1190. DR GeneID; 898302; -. DR KEGG; tma:TM1183; -. DR KEGG; tmi:THEMA_08420; -. DR KEGG; tmm:Tmari_1190; -. DR KEGG; tmw:THMA_1208; -. DR PATRIC; 23937306; VBITheMar51294_1201. DR eggNOG; ENOG4107QJX; Bacteria. DR eggNOG; COG1453; LUCA. DR KO; K07079; -. DR OMA; NVRIAST; -. DR OrthoDB; EOG6384H0; -. DR BioCyc; TMAR243274:GC6P-1212-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR001395; Aldo/ket_red/Kv-b. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR SUPFAM; SSF51430; SSF51430; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 16 286 Aldo_ket_red. {ECO:0000259|Pfam:PF00248}. SQ SEQUENCE 379 AA; 43719 MW; A74E99EF40B3E789 CRC64; MQYREFGRTG VKTSLLGFGA MRLPVIGEDH SNIDEEKAIE MIRYAIDHGV NYVDTAYPYH GGNSEKVVGK ALKDGYREKV FLATKSPVWQ VEKHEDFERI LDEQLEKLQT DHVDMYLMHA LNKERWEKIK NLRFSDFFEK AKAKGKIRFA GFSFHDSYPV FKEIVDGYDW DFCQIQLNYM DVNYQAGLRG LKYAGSKGLA VVIMEPLKGG KLARLPEKVM EILRKYNKNW SPVELSFRWI GHHPEVSTIL SGMSTLEQVK QNIDIMSKIT PGNLTDEDMK MIEEIRKTLE SFAVINCTQC GYCMPCPNGV DIPGNFRLYN ETVMFEDWEG GRRTYKWLES QKSAASFCVE CGECLSKCPQ KLDIPNLLKK VHRELAEVK // ID Q9WZP3_THEMA Unreviewed; 114 AA. AC Q9WZP3; G4FD38; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Ferritin/ribonucleotide reductase-like protein {ECO:0000313|EMBL:AGL49712.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35868.1}; GN OrderedLocusNames=TM_0786 {ECO:0000313|EMBL:AAD35868.1}; GN ORFNames=Tmari_0787 {ECO:0000313|EMBL:AGL49712.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35868.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35868.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35868.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49712.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49712.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35868.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49712.1; -; Genomic_DNA. DR PIR; C72333; C72333. DR RefSeq; NP_228595.1; NC_000853.1. DR RefSeq; WP_004080895.1; NZ_CP011107.1. DR PDB; 3DKT; X-ray; 3.10 A; K/L/M/N/O/P/Q/R/S/T=106-113. DR PDBsum; 3DKT; -. DR STRING; 243274.TM0786; -. DR EnsemblBacteria; AAD35868; AAD35868; TM_0786. DR EnsemblBacteria; AGL49712; AGL49712; Tmari_0787. DR GeneID; 898454; -. DR KEGG; tma:TM0786; -. DR KEGG; tmi:THEMA_00720; -. DR KEGG; tmm:Tmari_0787; -. DR KEGG; tmw:THMA_0805; -. DR PATRIC; 23936492; VBITheMar51294_0798. DR eggNOG; ENOG4105P1F; Bacteria. DR eggNOG; COG3461; LUCA. DR KO; K09700; -. DR OMA; NEGYHEP; -. DR OrthoDB; EOG62VNPS; -. DR BioCyc; TMAR243274:GC6P-813-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR030907; Ferrit_encaps. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR SUPFAM; SSF47240; SSF47240; 1. DR TIGRFAMs; TIGR04535; ferrit_encaps; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3DKT}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 114 AA; 13289 MW; BD3DF9F2E69D98BE CRC64; MADQYHEPVS ELTGKDRDFV RALNSLKEEI EAVAWYHQRV VTTKDETVRK ILEHNRDEEM EHAAMLLEWL RRNMPGWDEA LRTYLFTDKP ITEIEEETSG GSENTGGDLG IRKL // ID Q9WYE6_THEMA Unreviewed; 672 AA. AC Q9WYE6; G4FHM4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE RecName: Full=Beta-galactosidase {ECO:0000256|PIRNR:PIRNR001084}; DE Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084}; DE EC=3.2.1.23 {ECO:0000256|PIRNR:PIRNR001084}; GN OrderedLocusNames=TM_0310 {ECO:0000313|EMBL:AAD35398.1}; GN ORFNames=Tmari_0308 {ECO:0000313|EMBL:AGL49234.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35398.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35398.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35398.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49234.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49234.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D- CC galactose residues in beta-D-galactosides. CC {ECO:0000256|PIRNR:PIRNR001084}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. CC {ECO:0000256|PIRNR:PIRNR001084}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35398.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49234.1; -; Genomic_DNA. DR PIR; E72391; E72391. DR RefSeq; NP_228122.1; NC_000853.1. DR RefSeq; WP_004083040.1; NZ_CP011107.1. DR STRING; 243274.TM0310; -. DR CAZy; GH42; Glycoside Hydrolase Family 42. DR EnsemblBacteria; AAD35398; AAD35398; TM_0310. DR EnsemblBacteria; AGL49234; AGL49234; Tmari_0308. DR GeneID; 897246; -. DR KEGG; tma:TM0310; -. DR KEGG; tmi:THEMA_03175; -. DR KEGG; tmm:Tmari_0308; -. DR KEGG; tmw:THMA_0317; -. DR PATRIC; 23935499; VBITheMar51294_0315. DR eggNOG; ENOG4105C4C; Bacteria. DR eggNOG; COG1874; LUCA. DR KO; K12308; -. DR OMA; DWENWWA; -. DR OrthoDB; EOG6GTZGG; -. DR BioCyc; TMAR243274:GC6P-323-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro. DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.80; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR013739; Beta_galactosidase_C. DR InterPro; IPR013738; Beta_galactosidase_Trimer. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR003476; Glyco_hydro_42. DR InterPro; IPR013529; Glyco_hydro_42_N. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF02449; Glyco_hydro_42; 1. DR Pfam; PF08533; Glyco_hydro_42C; 1. DR Pfam; PF08532; Glyco_hydro_42M; 1. DR PIRSF; PIRSF001084; B-galactosidase; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR SUPFAM; SSF52317; SSF52317; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084, KW ECO:0000313|EMBL:AGL49234.1}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, KW ECO:0000313|EMBL:AGL49234.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}. FT DOMAIN 14 390 Glyco_hydro_42. FT {ECO:0000259|Pfam:PF02449}. FT DOMAIN 401 604 Glyco_hydro_42M. FT {ECO:0000259|Pfam:PF08532}. FT DOMAIN 613 670 Glyco_hydro_42C. FT {ECO:0000259|Pfam:PF08533}. FT ACT_SITE 150 150 Proton donor. FT {ECO:0000256|PIRSR:PIRSR001084-1}. FT ACT_SITE 311 311 Nucleophile. FT {ECO:0000256|PIRSR:PIRSR001084-1}. FT METAL 115 115 Zinc. {ECO:0000256|PIRSR:PIRSR001084-3}. FT METAL 155 155 Zinc. {ECO:0000256|PIRSR:PIRSR001084-3}. FT METAL 157 157 Zinc. {ECO:0000256|PIRSR:PIRSR001084-3}. FT METAL 160 160 Zinc. {ECO:0000256|PIRSR:PIRSR001084-3}. FT BINDING 111 111 Substrate. FT {ECO:0000256|PIRSR:PIRSR001084-2}. FT BINDING 149 149 Substrate. FT {ECO:0000256|PIRSR:PIRSR001084-2}. FT BINDING 319 319 Substrate. FT {ECO:0000256|PIRSR:PIRSR001084-2}. SQ SEQUENCE 672 AA; 79113 MW; E7F2FFB2ED1D916C CRC64; MVNPKLPVIW YGGDYYPEQW DEETFERDIR MFKEAGINVV TIGVFSWSLI QPDENTYDFS FFEKVMDRLY KEGIYVCLAT PTSAPPHWMT QKYPEILFTD VNGVKREKGG RQNFCPNSEK YRYFARNIAE KLAEHFKDHP ALVLWHVNNE YLNYCYCDIC RGKFQNWLKE KYGTLDELNR RWNTRFWSQT FTAWEEIPVP TTRSVLVWRK DRYQSVLPEL YLDYRRFMTQ SMLECFLEEY RAIKKHTPDI PVTTNLIAAT FKEWNYFEWA KHMDVAAWDN YPGYKEDFSV ISLRHSLIRC LKEGKPFVLM EQSPSQACWR WYNPQKRPGE MRLWSYHALA HGAETLMFFQ LRQSKGGVEK FHGAVITHVD SPNTRVFQEV KRVGEEIKSL SDILDARVVS QTALLFDWES WWAMEDTLTP SVDFRYLNEV QKYFKALVKT GLGVDVVGKD QNFERYRVLV APVLYMVGKE LAQKLKDYVS NGGILILTTM SGIVDEDDQV VLGGYPGYLR DLMGGYVEEI DALPPEEKNE ILMFGKRYEC SLVFDYIKTT TAEVLGRFGR DYYMNEPAVL RNNYGKGWVY YVGSSTSFDL VWDLVKFMER EHNLRAEIAP PDDVEVIKKI KGEKIFYFLF NHSHELQIVD LPEGMFRDLI KGNLYEKKVK LQPLDVLILL KE // ID Q9WY72_THEMA Unreviewed; 158 AA. AC Q9WY72; G4FHE4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039}; DE EC=3.1.4.- {ECO:0000256|RuleBase:RU362039}; GN OrderedLocusNames=TM_0230 {ECO:0000313|EMBL:AAD35321.1}; GN ORFNames=Tmari_0228 {ECO:0000313|EMBL:AGL49154.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35321.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35321.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35321.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49154.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49154.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|RuleBase:RU362039}; CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CC YfcE family. {ECO:0000256|RuleBase:RU362039}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35321.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49154.1; -; Genomic_DNA. DR PIR; H72401; H72401. DR RefSeq; NP_228044.1; NC_000853.1. DR RefSeq; WP_004082922.1; NZ_CP011107.1. DR STRING; 243274.TM0230; -. DR EnsemblBacteria; AAD35321; AAD35321; TM_0230. DR EnsemblBacteria; AGL49154; AGL49154; Tmari_0228. DR GeneID; 897129; -. DR KEGG; tma:TM0230; -. DR KEGG; tmi:THEMA_03575; -. DR KEGG; tmm:Tmari_0228; -. DR KEGG; tmw:THMA_0237; -. DR PATRIC; 23935335; VBITheMar51294_0233. DR eggNOG; ENOG4105QI5; Bacteria. DR eggNOG; COG0622; LUCA. DR KO; K07095; -. DR OMA; VIHCGDF; -. DR OrthoDB; EOG68DD3N; -. DR BioCyc; TMAR243274:GC6P-243-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29. DR PANTHER; PTHR11124; PTHR11124; 1. DR Pfam; PF12850; Metallophos_2; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00040; yfcE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000256|RuleBase:RU362039}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 147 Metallophos_2. FT {ECO:0000259|Pfam:PF12850}. SQ SEQUENCE 158 AA; 17828 MW; 26ABDF36E86A2820 CRC64; MWLILSDTHD NMEVLKKVEE LVSEKNIEKI FHCGDFVAPF TLGRLIKEGV DFYGVFGNND GEVLLLDKRS GGRIKKPPIS LEVDGLRIAM MHEPVLLDAI VRSQEFDLVL YGHTHKVDVR KEGKTLVVNP GEACGYLSGR STVYLFDPRT REGELLEL // ID Q9X2G1_THEMA Unreviewed; 580 AA. AC Q9X2G1; G4FGN1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 112. DE SubName: Full=Beta transducin-related protein {ECO:0000313|EMBL:AAD36908.1}; DE SubName: Full=WD-40 repeat protein {ECO:0000313|EMBL:AGL50778.1}; GN OrderedLocusNames=TM_1846 {ECO:0000313|EMBL:AAD36908.1}; GN ORFNames=Tmari_1854 {ECO:0000313|EMBL:AGL50778.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36908.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36908.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36908.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50778.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50778.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36908.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50778.1; -; Genomic_DNA. DR PIR; G72202; G72202. DR RefSeq; NP_229642.1; NC_000853.1. DR RefSeq; WP_004082390.1; NZ_CP011107.1. DR STRING; 243274.TM1846; -. DR EnsemblBacteria; AAD36908; AAD36908; TM_1846. DR EnsemblBacteria; AGL50778; AGL50778; Tmari_1854. DR GeneID; 897749; -. DR KEGG; tma:TM1846; -. DR KEGG; tmi:THEMA_04975; -. DR KEGG; tmm:Tmari_1854; -. DR KEGG; tmw:THMA_1889; -. DR PATRIC; 23938681; VBITheMar51294_1867. DR eggNOG; ENOG4108602; Bacteria. DR eggNOG; COG2319; LUCA. DR OMA; VGTWNGN; -. DR OrthoDB; EOG6742RR; -. DR BioCyc; TMAR243274:GC6P-1897-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.130.10.10; -; 2. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_dom. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 10. DR SUPFAM; SSF50978; SSF50978; 1. DR SUPFAM; SSF50998; SSF50998; 1. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 4. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Repeat {ECO:0000256|RuleBase:RU003532}; KW WD repeat {ECO:0000256|RuleBase:RU000362}. FT DOMAIN 102 508 WD_REPEATS_REGION. FT {ECO:0000259|PROSITE:PS50294}. SQ SEQUENCE 580 AA; 63788 MW; 8B493C8FB5C82BAE CRC64; MKKSLTLVLV VVSILIFSQT FKLEKVLGFS DISSLAFKDG YLLLGTGNGE IIVYKDGSYY RAFKVHDNRV NEVTFENGFI VSASDDKTVG VTNLETGEIK LLKGHMKGVS SVAVAGSKIL SASFDGTVRV WSFPDGGEIS SQKLGPSVVQ IAAHENRYVV GLANGLALIR DLSNQSFSIP LKAHPEGIKK IVFSENGQLI ATCGGNTVKV WNASNGNLVL QYDHVITVND VAFLENDSLI FVADDYKAVV LNIQKNEVVK SIDAHNNFVL FVSSDDGSIA TYGMDKTVKV WNANLELQYS LYGHQLSVNT VALSSDRKFI VSGSDDREIL IWNTEKGIAE HRIKALSGVR KLLTVENNII SCLDSNQLKI YNLENGKLVK RIKVGTTSTM DIALQNDRMA VGFYDGSVAL FRYPSFEEIW RKDTEHEMIQ TIDMNNKFIA FGVSYSDPKD KIGYVEVLSA DTGERVFLLE GHRGNVNAVK FAGDFLVSGG EDGKVILWNL DTGSKVKEIY LNEPVSSLFV DEKELFVGTW NGSIKIFAFP DLTLKTSLKA SDQKIGHLIK VGNHLVVPCG DGKIRILVEK // ID Q9X266_THEMA Unreviewed; 343 AA. AC Q9X266; G4FGD0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 107. DE SubName: Full=L-allo-threonine aldolase {ECO:0000313|EMBL:AAD36809.1}; DE SubName: Full=Low-specificity L-threonine aldolase {ECO:0000313|EMBL:AGL50676.1}; DE EC=4.1.2.5 {ECO:0000313|EMBL:AGL50676.1}; GN OrderedLocusNames=TM_1744 {ECO:0000313|EMBL:AAD36809.1}; GN ORFNames=Tmari_1752 {ECO:0000313|EMBL:AGL50676.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36809.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36809.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36809.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50676.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50676.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36809.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50676.1; -; Genomic_DNA. DR PIR; C72215; C72215. DR RefSeq; NP_229542.1; NC_000853.1. DR RefSeq; WP_004082276.1; NZ_CP011107.1. DR PDB; 1JG8; X-ray; 1.80 A; A/B/C/D=1-343. DR PDB; 1LW4; X-ray; 1.90 A; A/B/C/D=1-343. DR PDB; 1LW5; X-ray; 2.05 A; A/B/C/D=1-343. DR PDB; 1M6S; X-ray; 1.80 A; A/B/C/D=1-343. DR PDB; 2FM1; X-ray; 2.25 A; A/B/C/D=1-343. DR PDBsum; 1JG8; -. DR PDBsum; 1LW4; -. DR PDBsum; 1LW5; -. DR PDBsum; 1M6S; -. DR PDBsum; 2FM1; -. DR STRING; 243274.TM1744; -. DR EnsemblBacteria; AAD36809; AAD36809; TM_1744. DR EnsemblBacteria; AGL50676; AGL50676; Tmari_1752. DR GeneID; 897167; -. DR KEGG; tma:TM1744; -. DR KEGG; tmm:Tmari_1752; -. DR KEGG; tmw:THMA_1786; -. DR PATRIC; 23938464; VBITheMar51294_1762. DR eggNOG; ENOG4105C5W; Bacteria. DR eggNOG; COG2008; LUCA. DR KO; K01620; -. DR OMA; TMTNQVA; -. DR OrthoDB; EOG65N16K; -. DR BioCyc; TMAR243274:GC6P-1792-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006545; P:glycine biosynthetic process; IBA:GO_Central. DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR InterPro; IPR023603; Threonine_aldolase. DR Pfam; PF01212; Beta_elim_lyase; 1. DR PIRSF; PIRSF017617; Thr_aldolase; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1JG8, ECO:0000213|PDB:1LW4, KW ECO:0000213|PDB:1LW5, ECO:0000213|PDB:1M6S}; KW Calcium {ECO:0000213|PDB:1JG8, ECO:0000213|PDB:1LW4, KW ECO:0000213|PDB:1LW5, ECO:0000213|PDB:1M6S}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000313|EMBL:AGL50676.1}; KW Metal-binding {ECO:0000213|PDB:1JG8, ECO:0000213|PDB:1LW4, KW ECO:0000213|PDB:1LW5, ECO:0000213|PDB:1M6S}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 284 Beta_elim_lyase. FT {ECO:0000259|Pfam:PF01212}. FT METAL 8 8 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:1JG8, FT ECO:0000213|PDB:1LW4, FT ECO:0000213|PDB:1LW5}. FT METAL 10 10 Calcium 1. {ECO:0000213|PDB:1JG8, FT ECO:0000213|PDB:1LW4, FT ECO:0000213|PDB:1LW5}. FT METAL 198 198 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:1JG8, FT ECO:0000213|PDB:1LW4, FT ECO:0000213|PDB:1LW5}. FT METAL 203 203 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:1JG8, FT ECO:0000213|PDB:1LW4, FT ECO:0000213|PDB:1LW5}. FT METAL 326 326 Calcium 2. {ECO:0000213|PDB:1JG8}. FT METAL 329 329 Calcium 2. {ECO:0000213|PDB:1JG8}. FT MOD_RES 199 199 N6-(pyridoxal phosphate)lysine. FT {ECO:0000213|PDB:1LW4, FT ECO:0000213|PDB:1LW5}. SQ SEQUENCE 343 AA; 37574 MW; E72FB364989F0554 CRC64; MIDLRSDTVT KPTEEMRKAM AQAEVGDDVY GEDPTINELE RLAAETFGKE AALFVPSGTM GNQVSIMAHT QRGDEVILEA DSHIFWYEVG AMAVLSGVMP HPVPGKNGAM DPDDVRKAIR PRNIHFPRTS LIAIENTHNR SGGRVVPLEN IKEICTIAKE HGINVHIDGA RIFNASIASG VPVKEYAGYA DSVMFCLSKG LCAPVGSVVV GDRDFIERAR KARKMLGGGM RQAGVLAAAG IIALTKMVDR LKEDHENARF LALKLKEIGY SVNPEDVKTN MVILRTDNLK VNAHGFIEAL RNSGVLANAV SDTEIRLVTH KDVSRNDIEE ALNIFEKLFR KFS // ID Q9WZ65_THEMA Unreviewed; 420 AA. AC Q9WZ65; G4FDM3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE SubName: Full=N-Acetyl-D-glucosamine ABC transport system, permease protein 1 {ECO:0000313|EMBL:AGL49520.1}; DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35681.1}; GN OrderedLocusNames=TM_0596 {ECO:0000313|EMBL:AAD35681.1}; GN ORFNames=Tmari_0595 {ECO:0000313|EMBL:AGL49520.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35681.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35681.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35681.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49520.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49520.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35681.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49520.1; -; Genomic_DNA. DR PIR; E72357; E72357. DR RefSeq; NP_228406.1; NC_000853.1. DR RefSeq; WP_004081251.1; NZ_CP011107.1. DR STRING; 243274.TM0596; -. DR EnsemblBacteria; AAD35681; AAD35681; TM_0596. DR EnsemblBacteria; AGL49520; AGL49520; Tmari_0595. DR GeneID; 897672; -. DR KEGG; tma:TM0596; -. DR KEGG; tmi:THEMA_01680; -. DR KEGG; tmm:Tmari_0595; -. DR KEGG; tmw:THMA_0612; -. DR PATRIC; 23936107; VBITheMar51294_0607. DR eggNOG; ENOG4105E4X; Bacteria. DR eggNOG; COG1175; LUCA. DR KO; K02025; -. DR OMA; GMTMVYY; -. DR OrthoDB; EOG69SKBS; -. DR BioCyc; TMAR243274:GC6P-621-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 41 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 73 95 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 102 122 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 128 145 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 154 177 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 197 218 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 230 250 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 365 382 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 389 409 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 193 408 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 420 AA; 48552 MW; 58EF81939FE04CE3 CRC64; MKPSKKLREA VLAYLFLLPS LVVLGMFVFW PVGFSFVLSF FKWDFRNMKN PYFTGLDNYI EIFKFDYPPK YSFVFTVLNT FFHLAVAGAI VMLIVHLIKK RTLSGIISNA AVVLVYIALN LFNVENPILS FLVAAISWSW LVYDFKRVEF KNTWLWFILF LAVFVFVELN SSLPGLVNFL LDAKDKNLFL KALTNTLYYV ILSVPSQIFI SLMIALLLNS NVKFRVFFRT AYFIPFVTSV VAISLVWKWI FNDEFGLLNY ILSLFNIEPI SWLKDERWTI PTIAIVSVWK TVGYDAVIFL AGLQNIDRSY YEAAEVDGAS SLQKFFYITW PLLSPTTFFL LIVSLIGAFK VFAEVYVLYD GLPGPYNNSG MTLVYYVFDL FYRQQRMGIA SAAAYILFAI ILIFTFIQYR VGRRAVEYVS // ID Q9WXV6_THEMA Unreviewed; 622 AA. AC Q9WXV6; G4FH16; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35195.1}; GN OrderedLocusNames=TM_0101 {ECO:0000313|EMBL:AAD35195.1}; GN ORFNames=Tmari_0098 {ECO:0000313|EMBL:AGL49024.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35195.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35195.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35195.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49024.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49024.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35195.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49024.1; -; Genomic_DNA. DR PIR; E72418; E72418. DR RefSeq; NP_227917.1; NC_000853.1. DR RefSeq; WP_004082649.1; NZ_CP011107.1. DR STRING; 243274.TM0101; -. DR EnsemblBacteria; AAD35195; AAD35195; TM_0101. DR EnsemblBacteria; AGL49024; AGL49024; Tmari_0098. DR GeneID; 896928; -. DR KEGG; tma:TM0101; -. DR KEGG; tmi:THEMA_04300; -. DR KEGG; tmm:Tmari_0098; -. DR KEGG; tmw:THMA_0097; -. DR PATRIC; 23935042; VBITheMar51294_0099. DR eggNOG; ENOG4105JS1; Bacteria. DR eggNOG; ENOG4111PVF; LUCA. DR OMA; RWILAYY; -. DR OrthoDB; EOG62VNJD; -. DR BioCyc; TMAR243274:GC6P-101-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256 272 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 279 298 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 304 323 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 328 348 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 532 550 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 593 612 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 622 AA; 72593 MW; B0D801CBB7BDF741 CRC64; MKKWIFLFLL FLVVPVLSYA IDLENVTAQF QKLVEDYESG FPQDPFVSYV KENIPQLQKY RIFRRFLAGS VEKTEFAKTP GDYLFVLYQN WKETNWERKL SNVLFLSYLQ SMMSGSKPSE SVLKNSPAFN SFFAEYRMFV RSNALNLLRW ILAYYTGGTN TPPPVEFNLG IRNTGFSFNV NHDVHPDILK VLPEDLEAKL KEAIEEIASS KNQAEYTRNI NRQASLLWKE FESNISALQN EVADVFENTS PSISNFWWIR FVVYGILLVI FLRKYRTILQ FIIAAEILFI WVTKSLYLNT VENMIFSTVV VFMFIFFNFI LLVRRRYLYP LLSLIFVFLL FIPSYISIRE MGMDSAFENS PYYDQLKFEV FEGSDSPVKT AIRRMNTIAL SSKEHTKQIV ETLGSLPEEL LKIGALKSIE PTKNGLFFLL NERSKFFTTA GFEDRLDLTG KIEGDLSDYL SQEKSRYRKY RREINSLDQL IKKITSYTSE KFSQDFEREL TNTIERYPLI AGVSFSYSTE KSYLSLKPYR TMNGLIGIFT FFLLFFSAVL GGRYLLFPAA ATLFTSILSM IKWKHLEVFV ESGIFPLIIE TSSTHTFHIE VFLIFVSLFL LYKNFMKRRV KA // ID Q9WXY1_THEMA Unreviewed; 285 AA. AC Q9WXY1; G4FH42; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 104. DE SubName: Full=Sensor histidine kinase {ECO:0000313|EMBL:AAD35221.1}; GN OrderedLocusNames=TM_0127 {ECO:0000313|EMBL:AAD35221.1}; GN ORFNames=Tmari_0125 {ECO:0000313|EMBL:AGL49051.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35221.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35221.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35221.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49051.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49051.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35221.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49051.1; -; Genomic_DNA. DR PIR; G72415; G72415. DR RefSeq; NP_227943.1; NC_000853.1. DR RefSeq; WP_004082713.1; NZ_CP011107.1. DR STRING; 243274.TM0127; -. DR DNASU; 896954; -. DR EnsemblBacteria; AAD35221; AAD35221; TM_0127. DR EnsemblBacteria; AGL49051; AGL49051; Tmari_0125. DR GeneID; 896954; -. DR KEGG; tma:TM0127; -. DR KEGG; tmi:THEMA_04170; -. DR KEGG; tmm:Tmari_0125; -. DR KEGG; tmw:THMA_0123; -. DR eggNOG; COG0642; LUCA. DR KO; K02484; -. DR OMA; HVKKDRI; -. DR OrthoDB; EOG661H6M; -. DR BioCyc; TMAR243274:GC6P-127-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR Pfam; PF02518; HATPase_c; 1. DR SMART; SM00387; HATPase_c; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000313|EMBL:AAD35221.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35221.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 31 50 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 121 274 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. SQ SEQUENCE 285 AA; 32992 MW; A895C6910057425E CRC64; MISLRTFLIT FLVNIALLGI FWGNRMNFVD VVIFSFFSAL FVSLATHILV TSRLRKLREA VARKSRFEDF LNDEITKLAE EVNSVVENSL IQEKETEKLK DIVTGFVHDV KSLVWNEVED ENLQKIIEEF YEFAKLEAGL ERLRKEPVNL VELVNDVVEK FPGKVIFKYD DVVEVEADPM KLFRAFYNVI ENAVKYSSGP VEVHVKKDRI IVKGPGPEIP YEVRANLFEK KKKSKGTGLG LYLAREFFEM HGFRIAYRRE GNHNVFEIYT GYTGMSSVKS ERDSR // ID Q9X2H8_THEMA Unreviewed; 191 AA. AC Q9X2H8; G4FGQ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36926.1}; GN OrderedLocusNames=TM_1864 {ECO:0000313|EMBL:AAD36926.1}; GN ORFNames=Tmari_1879 {ECO:0000313|EMBL:AGL50803.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36926.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36926.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36926.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50803.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50803.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- INTERACTION: CC Q9WZ57:TM_0588; NbExp=11; IntAct=EBI-7816285, EBI-7816271; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36926.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50803.1; -; Genomic_DNA. DR PIR; A72202; A72202. DR RefSeq; NP_229660.1; NC_000853.1. DR RefSeq; WP_004082415.1; NZ_CP011107.1. DR PDB; 2WUS; X-ray; 2.90 A; R/S=1-104. DR PDBsum; 2WUS; -. DR MINT; MINT-7893483; -. DR STRING; 243274.TM1864; -. DR EnsemblBacteria; AAD36926; AAD36926; TM_1864. DR EnsemblBacteria; AGL50803; AGL50803; Tmari_1879. DR GeneID; 897460; -. DR KEGG; tma:TM1864; -. DR KEGG; tmi:THEMA_04850; -. DR KEGG; tmm:Tmari_1879; -. DR KEGG; tmw:THMA_1914; -. DR PATRIC; 23938717; VBITheMar51294_1885. DR eggNOG; ENOG41068HP; Bacteria. DR eggNOG; COG1426; LUCA. DR OMA; KTASEEW; -. DR OrthoDB; EOG618QQ4; -. DR BioCyc; TMAR243274:GC6P-1915-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF13413; HTH_25; 1. DR SUPFAM; SSF47413; SSF47413; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2WUS}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 104 122 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 12 72 HTH_25. {ECO:0000259|Pfam:PF13413}. SQ SEQUENCE 191 AA; 22331 MW; BF3DE3BDBB773F08 CRC64; MSEKWKELGE TFRKKREERR ITLLDASLFT NINPSKLKRI EEGDLKGLDA EVYIKSYIKR YSEFLELSPD EMLKLYEEGK EEVAEEVEEK KPRKKKEKEK TRDLVMFFFL IAGLVFLLFS AVENLKLRQT PPAYLVAPEE TIVNGKSVSG EIPLQEGEYI VESRSDVVLK TASEEWTVKI RKFEVSVSWE K // ID Q9WZ66_THEMA Unreviewed; 150 AA. AC Q9WZ66; G4FDM2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Monosaccharide-transporting ATPase {ECO:0000313|EMBL:AGL49521.1}; DE EC=3.6.3.17 {ECO:0000313|EMBL:AGL49521.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35682.1}; GN OrderedLocusNames=TM_0597 {ECO:0000313|EMBL:AAD35682.1}; GN ORFNames=Tmari_0596 {ECO:0000313|EMBL:AGL49521.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35682.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35682.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35682.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49521.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49521.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35682.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49521.1; -; Genomic_DNA. DR PIR; F72357; F72357. DR RefSeq; NP_228407.1; NC_000853.1. DR RefSeq; WP_004081249.1; NZ_CP011107.1. DR STRING; 243274.TM0597; -. DR EnsemblBacteria; AAD35682; AAD35682; TM_0597. DR EnsemblBacteria; AGL49521; AGL49521; Tmari_0596. DR GeneID; 897673; -. DR KEGG; tma:TM0597; -. DR KEGG; tmm:Tmari_0596; -. DR KEGG; tmw:THMA_0613; -. DR PATRIC; 23936109; VBITheMar51294_0608. DR eggNOG; ENOG4105EX2; Bacteria. DR eggNOG; COG0395; LUCA. DR OrthoDB; EOG6C01G6; -. DR BioCyc; TMAR243274:GC6P-622-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0015407; F:monosaccharide-transporting ATPase activity; IEA:UniProtKB-EC. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR SUPFAM; SSF161098; SSF161098; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49521.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 150 AA; 17182 MW; 378540A7D16226FB CRC64; MKKLVVYILL IFGAVVMLGP FIWMLLTSFK APSEVQQWPP SFYTKNFAFS RDVKVILKPG VQRVAKGVSL REAYALKTAE ENLLTITVND DPFHRGTMTI PLKGAKYTTG VDVERVKELS SKSPVEFSWK TPEEFFEQFF IYYKSGGQNW // ID Q9X118_THEMA Unreviewed; 283 AA. AC Q9X118; G4FE57; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 105. DE SubName: Full=Iron-sulfur cluster-binding protein, putative {ECO:0000313|EMBL:AAD36366.1}; DE SubName: Full=MinD superfamily P-loop ATPase containing an inserted ferredoxin domain {ECO:0000313|EMBL:AGL50224.1}; GN OrderedLocusNames=TM_1292 {ECO:0000313|EMBL:AAD36366.1}; GN ORFNames=Tmari_1300 {ECO:0000313|EMBL:AGL50224.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36366.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36366.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36366.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50224.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50224.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36366.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50224.1; -; Genomic_DNA. DR PIR; C72272; C72272. DR RefSeq; NP_229096.1; NC_000853.1. DR RefSeq; WP_004079932.1; NZ_CP011107.1. DR STRING; 243274.TM1292; -. DR DNASU; 898191; -. DR EnsemblBacteria; AAD36366; AAD36366; TM_1292. DR EnsemblBacteria; AGL50224; AGL50224; Tmari_1300. DR GeneID; 898191; -. DR KEGG; tma:TM1292; -. DR KEGG; tmm:Tmari_1300; -. DR KEGG; tmw:THMA_1318; -. DR PATRIC; 23937524; VBITheMar51294_1308. DR eggNOG; ENOG4105D0G; Bacteria. DR eggNOG; COG1149; LUCA. DR OMA; DVEEPNC; -. DR OrthoDB; EOG6H1PXV; -. DR BioCyc; TMAR243274:GC6P-1323-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR Pfam; PF00037; Fer4; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|RuleBase:RU003429}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|RuleBase:RU003429}; KW Iron-sulfur {ECO:0000256|RuleBase:RU003429}; KW Metal-binding {ECO:0000256|RuleBase:RU003429}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 61 90 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 91 119 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 283 AA; 30754 MW; 7EF58168BCD8E73F CRC64; MTKITVLSGK GGTGKTTVSV NMAKALSESY RVQLLDADVE EPNDHIFFNV DVSFEEPVHL MIPVVDNSVC IRCGECASTC QFGAISVFPS GTFVFESLCH GCGACSIMCP VNAISERPKE IGKIRFGTAD GNISFGMGIL NIGERTGVPV IRKLKKHIDE KADVVIVDAP PGTSCPVVES LRNTDFALLV TEPTAFGLHD LKLAVELTKE MGIPSGIVVN RYIPGNTIIE EFADEEGIPV LLKIPFKREI ASLCAEGKLI VEAFQDMKKD FLELFEKIEV MVR // ID Q9X0J0_THEMA Unreviewed; 123 AA. AC Q9X0J0; G4FEP2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36182.1}; GN OrderedLocusNames=TM_1106 {ECO:0000313|EMBL:AAD36182.1}; GN ORFNames=Tmari_1112 {ECO:0000313|EMBL:AGL50036.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36182.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36182.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36182.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50036.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50036.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36182.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50036.1; -; Genomic_DNA. DR PIR; D72295; D72295. DR RefSeq; NP_228912.1; NC_000853.1. DR RefSeq; WP_004080328.1; NZ_CP011107.1. DR STRING; 243274.TM1106; -. DR EnsemblBacteria; AAD36182; AAD36182; TM_1106. DR EnsemblBacteria; AGL50036; AGL50036; Tmari_1112. DR GeneID; 898659; -. DR KEGG; tma:TM1106; -. DR KEGG; tmi:THEMA_08815; -. DR KEGG; tmm:Tmari_1112; -. DR KEGG; tmw:THMA_1129; -. DR PATRIC; 23937145; VBITheMar51294_1121. DR KO; K05569; -. DR OMA; PVKDEWE; -. DR OrthoDB; EOG6B09X2; -. DR BioCyc; TMAR243274:GC6P-1135-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002758; Cation_antiport_E. DR Pfam; PF01899; MNHE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 123 AA; 13937 MW; 7FAB625D60FFF535 CRC64; MSFLVAVITG TVFFMVLSQK ATLTTIVLGA VMSVVTYIFT RPIHFEKFPV LVLKLFYNVP KAVFESILVL LFHNGAKRAY EVPVKDEWEE LEKTLTITLT PKTLVIVSEE GYMVVHQVGE RKT // ID Q9WZM8_THEMA Unreviewed; 599 AA. AC Q9WZM8; G4FD53; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 106. DE SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:AGL49696.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35852.1}; GN OrderedLocusNames=TM_0770 {ECO:0000313|EMBL:AAD35852.1}; GN ORFNames=Tmari_0771 {ECO:0000313|EMBL:AGL49696.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35852.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35852.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35852.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49696.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49696.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35852.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49696.1; -; Genomic_DNA. DR PIR; H72336; H72336. DR RefSeq; NP_228579.1; NC_000853.1. DR RefSeq; WP_004080923.1; NZ_CP011107.1. DR STRING; 243274.TM0770; -. DR EnsemblBacteria; AAD35852; AAD35852; TM_0770. DR EnsemblBacteria; AGL49696; AGL49696; Tmari_0771. DR GeneID; 898438; -. DR KEGG; tma:TM0770; -. DR KEGG; tmi:THEMA_00800; -. DR KEGG; tmm:Tmari_0771; -. DR KEGG; tmw:THMA_0789; -. DR PATRIC; 23936462; VBITheMar51294_0783. DR eggNOG; ENOG4105CBE; Bacteria. DR eggNOG; COG1032; LUCA. DR OMA; PFQWEPQ; -. DR OrthoDB; EOG683S6D; -. DR BioCyc; TMAR243274:GC6P-797-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR023862; CHP03960_rSAM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR PANTHER; PTHR11918; PTHR11918; 2. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR03960; rSAM_fuse_unch; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 250 465 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 599 AA; 69315 MW; B8CA2D8FF05593F6 CRC64; MILKFLNETL PWVRKPSRYI GREINSVVKD PEEISLRIAL VFPDTYEVGT SNHGLEILYH ILNEQPDVWA ERSYLPWIDM IERMKEKDIP LYTMESYTPL YQMDAVGISL EYELSYTNVV EVLKLSKIPI FFWERKRRDP IVLGGGPCSS NPEPIYGFFD AILIGDGEEA ILEIAQVLKE TKGEERETIW KELSRIEGVY VPAFYEQKGR KIVPVSPEYP RTIKRRIVKD LNSQPVPVKK IVPNVESVHD RAVIEVARGC TRGCRFCHAS VYYRPVRERS LENILENVEE MLKNTGYEEV SLLSLSTMDH TQIGEIVSEL LKRYSEKKIA VSIPSTRMDR FGVEIAGRIA SVRKTGLTFA PEAATQRLRN IINKNISEED IFATLEAAKK SGWRRVKLYF MMGLPGETNE DLEEMVKLLE RVKRLGFKEV SASVSVFVPK PHTPFQFARQ ISPEEAYEKI KTLKRAKRSA RISYHDPRMS LLEGVFSRGD RKLLDLIVKA HELGALFDEW SEMFRFDLWE KAFDETGIDP NDYLREIDPS EDFPWDHIDM GVTKEFLKEE YRKALKGETT DDCRWNRCYL CGVCFRFGVK NVLFGGERG // ID Q9X0V5_THEMA Unreviewed; 266 AA. AC Q9X0V5; G4FEB8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Putative regulator for cell wall polysaccharide synthesis gene cluster, RpiR family {ECO:0000313|EMBL:AGL50159.1}; DE SubName: Full=Transcriptional regulator, RpiR family {ECO:0000313|EMBL:AAD36303.1}; GN OrderedLocusNames=TM_1228 {ECO:0000313|EMBL:AAD36303.1}; GN ORFNames=Tmari_1235 {ECO:0000313|EMBL:AGL50159.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36303.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36303.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36303.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50159.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50159.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36303.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50159.1; -; Genomic_DNA. DR PIR; E72278; E72278. DR RefSeq; NP_229033.1; NC_000853.1. DR RefSeq; WP_004080056.1; NZ_CP011107.1. DR STRING; 243274.TM1228; -. DR EnsemblBacteria; AAD36303; AAD36303; TM_1228. DR EnsemblBacteria; AGL50159; AGL50159; Tmari_1235. DR GeneID; 898256; -. DR KEGG; tma:TM1228; -. DR KEGG; tmi:THEMA_08190; -. DR KEGG; tmm:Tmari_1235; -. DR KEGG; tmw:THMA_1254; -. DR PATRIC; 23937398; VBITheMar51294_1246. DR eggNOG; ENOG4106KNT; Bacteria. DR eggNOG; COG1737; LUCA. DR OMA; VSTDAHQ; -. DR OrthoDB; EOG6HMXHM; -. DR BioCyc; TMAR243274:GC6P-1258-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR000281; HTH_RpiR. DR InterPro; IPR001347; SIS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01418; HTH_6; 1. DR Pfam; PF01380; SIS; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS51071; HTH_RPIR; 1. DR PROSITE; PS51464; SIS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 77 HTH rpiR-type DNA-binding. FT {ECO:0000259|PROSITE:PS51071}. FT DOMAIN 109 248 SIS. {ECO:0000259|PROSITE:PS51464}. SQ SEQUENCE 266 AA; 30671 MW; 54A9F627B5FBCC0C CRC64; MKIRDKILNV YTQFSPAERK VADYVLERPD DVIHYSITEF AKIVGVSETT IHRMIKKLDF EGYQAFKIAL ARELSGLEET IERRDFIDEE IDILRRLKDT LDMKNVEKAV EWILSAHRIL FFGVGLSGVV SEYASLKFSL LGFHTFFSND PHVQVIEAVN LTGEDLVISI SHTGNIRDTV KSTQVAKDMG AKTIAITTNR QSELAKVVHL VLQSPPVKYD TYEFLRENIG EIAVVDVLFK ETFQRIYRER KKHFENLEGV FKPKRF // ID Q9WXN4_THEMA Unreviewed; 268 AA. AC Q9WXN4; G4FGU4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 123. DE SubName: Full=Beta-glucoside ABC transport system, ATP-binding protein 2 {ECO:0000313|EMBL:AGL48950.1}; DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35121.1}; GN OrderedLocusNames=TM_0027 {ECO:0000313|EMBL:AAD35121.1}; GN ORFNames=Tmari_0024 {ECO:0000313|EMBL:AGL48950.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35121.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35121.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35121.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48950.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48950.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35121.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48950.1; -; Genomic_DNA. DR PIR; E72428; E72428. DR RefSeq; NP_227843.1; NC_000853.1. DR RefSeq; WP_004082480.1; NZ_CP011107.1. DR STRING; 243274.TM0027; -. DR TCDB; 3.A.1.5.16; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35121; AAD35121; TM_0027. DR EnsemblBacteria; AGL48950; AGL48950; Tmari_0024. DR GeneID; 896845; -. DR KEGG; tma:TM0027; -. DR KEGG; tmi:THEMA_04665; -. DR KEGG; tmm:Tmari_0024; -. DR KEGG; tmw:THMA_0023; -. DR PATRIC; 23934894; VBITheMar51294_0025. DR eggNOG; ENOG4108EBF; Bacteria. DR eggNOG; ENOG410XR2R; LUCA. DR KO; K02032; -. DR OMA; AMPRCKE; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-27-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35121.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35121.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 255 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 268 AA; 30621 MW; 97649FFF921C5015 CRC64; MSRLVVKNLT KIFSLGFFSK RRIEAVKNVS FEVKEKEIVS LVGESGSGKT TTAKMILRLL PPTSGEIYFE GKDIWKDIKD RESLVEFRRK VHAVFQDPFA SYNPFYPVER TLWQAISLLE NKPSNKKEAL ELIKESLFRV GIDPKDVLGK YPHQISGGQK QRIMIARCWI LRPLLIVADE PTSMIDASSR GGIIKLLEEL REEQGTSIIF ITHDLGLAYY VSDNIFVMKN GEIVERGHPD KVVLEPTHEY TKLLVGSIPK LYRKLEDL // ID Q9X1J9_THEMA Unreviewed; 230 AA. AC Q9X1J9; G4FFP8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Putative metal-dependent peptidase {ECO:0000313|EMBL:AGL50443.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36578.1}; GN OrderedLocusNames=TM_1511 {ECO:0000313|EMBL:AAD36578.1}; GN ORFNames=Tmari_1519 {ECO:0000313|EMBL:AGL50443.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36578.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36578.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36578.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50443.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50443.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36578.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50443.1; -; Genomic_DNA. DR PIR; H72244; H72244. DR RefSeq; NP_229311.1; NC_000853.1. DR RefSeq; WP_004081858.1; NZ_CP011107.1. DR STRING; 243274.TM1511; -. DR EnsemblBacteria; AAD36578; AAD36578; TM_1511. DR EnsemblBacteria; AGL50443; AGL50443; Tmari_1519. DR GeneID; 896965; -. DR KEGG; tma:TM1511; -. DR KEGG; tmi:THEMA_06745; -. DR KEGG; tmm:Tmari_1519; -. DR KEGG; tmw:THMA_1543; -. DR PATRIC; 23937980; VBITheMar51294_1528. DR eggNOG; ENOG4108R8F; Bacteria. DR eggNOG; COG2738; LUCA. DR KO; K06973; -. DR OMA; LWAQFRV; -. DR OrthoDB; EOG6CS037; -. DR BioCyc; TMAR243274:GC6P-1551-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007395; Zn_peptidase_2. DR Pfam; PF04298; Zn_peptidase_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 120 143 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 150 168 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 202 226 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 230 AA; 25816 MW; 30ED848611309951 CRC64; MFFLFDPTFI ILIPGILLAF WAQMRVQAAY NKYSQVRSSL GLTGYELAKR LLENAGIYNV KIEVVSGFLT DHYDPYRKVL RLSPQNFKGV SVASLGVVAH EVGHALQDAE KYPMLALRNL MVPAAITGSQ LAWIIFILGF IFYTPFLIRL GILLFSLVVL FTLITLPVEF DASRRAVKLL ETTMLMPEYE LKGVKEVLDA AALTYVASSL MAFLQLLRMI VIAGLFGDRR // ID Q9WZJ4_THEMA Unreviewed; 455 AA. AC Q9WZJ4; G4FD88; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35816.1}; GN OrderedLocusNames=TM_0735 {ECO:0000313|EMBL:AAD35816.1}; GN ORFNames=Tmari_0736 {ECO:0000313|EMBL:AGL49661.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35816.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35816.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35816.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49661.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49661.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35816.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49661.1; -; Genomic_DNA. DR PIR; B72339; B72339. DR RefSeq; NP_228544.1; NC_000853.1. DR RefSeq; WP_004080991.1; NZ_CP011107.1. DR STRING; 243274.TM0735; -. DR EnsemblBacteria; AAD35816; AAD35816; TM_0735. DR EnsemblBacteria; AGL49661; AGL49661; Tmari_0736. DR GeneID; 898402; -. DR KEGG; tma:TM0735; -. DR KEGG; tmi:THEMA_00980; -. DR KEGG; tmm:Tmari_0736; -. DR KEGG; tmw:THMA_0753; -. DR PATRIC; 23936390; VBITheMar51294_0748. DR eggNOG; ENOG4105FEG; Bacteria. DR eggNOG; COG1315; LUCA. DR KO; K09749; -. DR OMA; HFDIKRE; -. DR OrthoDB; EOG6JDWCD; -. DR BioCyc; TMAR243274:GC6P-761-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR005646; DUF342. DR Pfam; PF03961; DUF342; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 374 408 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 455 AA; 49894 MW; 4FED84BD526B4D8E CRC64; MKVEITVSED RMQAYVTLRK EGSSELPLTK EELLNALLSA GINHGIKEEI IEDLARSPVY NTPVLVAEGT PPVDGEDGRV ELLKKIEFSS HEGEKIDLRE IPAKQRVIVR KGETIARIIP PTPGKEGMDV FGNPVKPKPG RVPEYHLGYN VATKNNEIIA TKSGILVIEP NGTIHVYDTL EVDNVDYSTG NIDFPGKVVV KGDVKPDFVV KAQEDITVKG VIEAATVISF NGSITAGGIK GRGKAFVKAK KTVKAVFIES AEVEAEEVQV EKNIENSAVK AINVVVSGKG GSIRGGITIA QVKVETYFLG SPIGVKTRVE VGVDPEINEK IKLLSAQISL DRENVQKLTK LLVELRKLQG MLKDKFPPDK EALLNKVNNT LINLRDSIQK NEGELKRLKE IAEEMAKNAS VVVKEVVYSG VEIVMFERVF RVEKELAKAV FYYRDGEIRV GGYSA // ID Q9X1X9_THEMA Unreviewed; 152 AA. AC Q9X1X9; G4FG35; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=DUF327 domain-containing protein {ECO:0000313|EMBL:AGL50579.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36713.1}; GN OrderedLocusNames=TM_1646 {ECO:0000313|EMBL:AAD36713.1}; GN ORFNames=Tmari_1655 {ECO:0000313|EMBL:AGL50579.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36713.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36713.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36713.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50579.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50579.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36713.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50579.1; -; Genomic_DNA. DR PIR; C72227; C72227. DR RefSeq; NP_229446.1; NC_000853.1. DR RefSeq; WP_004082145.1; NZ_CP011107.1. DR PDB; 2P61; X-ray; 2.70 A; A=2-152. DR PDBsum; 2P61; -. DR STRING; 243274.TM1646; -. DR EnsemblBacteria; AAD36713; AAD36713; TM_1646. DR EnsemblBacteria; AGL50579; AGL50579; Tmari_1655. DR GeneID; 897918; -. DR KEGG; tma:TM1646; -. DR KEGG; tmi:THEMA_06015; -. DR KEGG; tmm:Tmari_1655; -. DR KEGG; tmw:THMA_1687; -. DR PATRIC; 23938266; VBITheMar51294_1665. DR eggNOG; ENOG4105T4D; Bacteria. DR eggNOG; COG1728; LUCA. DR KO; K09770; -. DR OMA; MNSGRAR; -. DR OrthoDB; EOG64JFP4; -. DR BioCyc; TMAR243274:GC6P-1692-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.20.120.490; -; 1. DR InterPro; IPR005585; DUF327. DR InterPro; IPR024042; TM1646-like_dom. DR Pfam; PF03885; DUF327; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2P61}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 105 132 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 152 AA; 17549 MW; D83CECD9791AB4B6 CRC64; MRIDPLGGES LKNQEVKGKK SGKTSRVGES KKKEFFDILE DVKEDHFEKL LEEAVEEVID SGNELVRSPT PSNLKRYKNA IKEFLKLIEK KIYKLAGSFD MNSGRARLHL VVEEVNEKLM DLTEKIMKNE WQTINLAARI EEINGLILNL YR // ID Q9X2D4_THEMA Unreviewed; 250 AA. AC Q9X2D4; G4FGK1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE RecName: Full=CRISPR-associated endoribonuclease {ECO:0000256|PIRNR:PIRNR005054}; GN OrderedLocusNames=TM_1814 {ECO:0000313|EMBL:AAD36877.1}; GN ORFNames=Tmari_1824 {ECO:0000313|EMBL:AGL50748.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36877.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36877.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36877.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50748.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50748.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat), is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC sequences complementary to antecedent mobile elements and target CC invading nucleic acids. CRISPR clusters are transcribed and CC processed into CRISPR RNA (crRNA). CC {ECO:0000256|PIRNR:PIRNR005054}. CC -!- SIMILARITY: Belongs to the CRISPR-associated protein CC Cas6/Cse3/CasE family. {ECO:0000256|PIRNR:PIRNR005054}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36877.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50748.1; -; Genomic_DNA. DR PIR; C72209; C72209. DR RefSeq; NP_229611.1; NC_000853.1. DR RefSeq; WP_004082360.1; NZ_CP011107.1. DR STRING; 243274.TM1814; -. DR EnsemblBacteria; AAD36877; AAD36877; TM_1814. DR EnsemblBacteria; AGL50748; AGL50748; Tmari_1824. DR GeneID; 897708; -. DR KEGG; tma:TM1814; -. DR KEGG; tmi:THEMA_05125; -. DR KEGG; tmm:Tmari_1824; -. DR KEGG; tmw:THMA_1859; -. DR PATRIC; 23938615; VBITheMar51294_1834. DR eggNOG; ENOG4105KW3; Bacteria. DR eggNOG; COG1583; LUCA. DR KO; K19091; -. DR OMA; IMEVAYY; -. DR OrthoDB; EOG683SC8; -. DR BioCyc; TMAR243274:GC6P-1865-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. DR InterPro; IPR010156; CRISPR-assoc_prot_Cas6. DR Pfam; PF01881; Cas_Cas6; 1. DR PIRSF; PIRSF005054; PF1131; 1. DR TIGRFAMs; TIGR01877; cas_cas6; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 250 AA; 29612 MW; 98AB9975FCA853E9 CRC64; MRLKVSFQAM ESTVPLNYNY FLSSFIYKRL ASQNENFARF LHEKGYGKRF KFFTFSQLFF ENSRVSGERI FIFPGKGWWY ISSPVVEFVR YMFSSLSEDP VIRVGKTEFI VKSIDIENSL PDQSEYHFVM LSPLVVSVPE ENNGKLYHRY LHPGEEEFYE VFRKNLMKKY RAFYGKDPEG TVEVIPDWDY IKSRHRITKR IKLKNAFVRA VVFPFKIRGE KKLVEIGYEA GFGEKNSMGF GMVALKKYER // ID Q9X0T6_THEMA Unreviewed; 254 AA. AC Q9X0T6; G4FED7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Na(+) H(+) antiporter subunit A Na(+) H(+) antiporter subunit B {ECO:0000313|EMBL:AGL50140.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36284.1}; GN OrderedLocusNames=TM_1209 {ECO:0000313|EMBL:AAD36284.1}; GN ORFNames=Tmari_1216 {ECO:0000313|EMBL:AGL50140.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36284.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36284.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36284.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50140.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50140.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36284.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50140.1; -; Genomic_DNA. DR PIR; G72280; G72280. DR RefSeq; NP_229014.1; NC_000853.1. DR RefSeq; WP_004080100.1; NZ_CP011107.1. DR STRING; 243274.TM1209; -. DR EnsemblBacteria; AAD36284; AAD36284; TM_1209. DR EnsemblBacteria; AGL50140; AGL50140; Tmari_1216. DR GeneID; 898275; -. DR KEGG; tma:TM1209; -. DR KEGG; tmi:THEMA_08285; -. DR KEGG; tmm:Tmari_1216; -. DR KEGG; tmw:THMA_1235; -. DR PATRIC; 23937360; VBITheMar51294_1227. DR eggNOG; ENOG4108PMQ; Bacteria. DR eggNOG; COG2111; LUCA. DR KO; K05566; -. DR OMA; SIVVNYR; -. DR OrthoDB; EOG6T7N8G; -. DR BioCyc; TMAR243274:GC6P-1239-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007182; MnhB. DR Pfam; PF04039; MnhB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 124 146 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 152 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 192 213 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 225 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 242 MnhB. {ECO:0000259|Pfam:PF04039}. SQ SEQUENCE 254 AA; 27591 MW; 3FB09A5442976D7B CRC64; MRRFFAILIS AAFVYVMLSF ITTLEPFGKI DLSRRVSVHY LAKDVNTVDS RKWIEGNLQV PSERRIYGES NLEDGSANVV TSIVVNYRSF DTLGEVTVLL AAAIGVGTIL RGSRRMKYRR EPNFILKVST GILLPLILMF GVYIFVHGHL SPGGGFPGGT VIAAAILLLY LSNEEFTLNE GRAKLLEGSM GALYVLVGLI GLLTGGAFLY NFLSTGRVGD LFSAGVVPVV YIIIGLKVGS ELSGVISEIH RKGE // ID Q9WZE0_THEMA Unreviewed; 647 AA. AC Q9WZE0; G4FDF2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35756.1}; GN OrderedLocusNames=TM_0672 {ECO:0000313|EMBL:AAD35756.1}; GN ORFNames=Tmari_0672 {ECO:0000313|EMBL:AGL49597.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35756.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35756.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35756.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49597.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49597.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35756.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49597.1; -; Genomic_DNA. DR PIR; G72346; G72346. DR RefSeq; NP_228481.1; NC_000853.1. DR RefSeq; WP_004081099.1; NZ_CP011107.1. DR STRING; 243274.TM0672; -. DR EnsemblBacteria; AAD35756; AAD35756; TM_0672. DR EnsemblBacteria; AGL49597; AGL49597; Tmari_0672. DR GeneID; 898340; -. DR KEGG; tma:TM0672; -. DR KEGG; tmi:THEMA_01305; -. DR KEGG; tmm:Tmari_0672; -. DR KEGG; tmw:THMA_0687; -. DR PATRIC; 23936258; VBITheMar51294_0682. DR eggNOG; ENOG4106IRI; Bacteria. DR eggNOG; ENOG410Y7AK; LUCA. DR OMA; STEHEEK; -. DR OrthoDB; EOG6N3CNZ; -. DR BioCyc; TMAR243274:GC6P-697-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR021136; Flagellar_hook_control-like_C. DR Pfam; PF02120; Flg_hook; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 531 604 Flg_hook. {ECO:0000259|Pfam:PF02120}. SQ SEQUENCE 647 AA; 74047 MW; 4CED35D0A761080A CRC64; MKVGQFSLFA MIKTAEEKGE LKKKSAAGLF SQSVKDLMKS LGSKGKVLGT TPGKKNVHRA ESSENRADGL KKTKRNVLDN LDGTSAQHIS MSAEENVKLE EMLGGQLSEK PQNVSEDQKE REEEAGRSSS SKLIKEIKTT DDKSSEKHVL EEVSKRDENH AEYRKSEQGI FKSRTHDIST EKLLTSTEHE EKKENGFLVK DSENKESASQ ISFEKKHSSI PYLESETSRS ESNKKLSSSF RTPAEPSLKS ESTKVFKEQP ISAQDKETKH SARQPIFNET RSLPQNSDAA KLSRDFEKTT GIKNELFEER ITGNTGNEIK MSKLSFVPLL PADEKQQSSN GDGERVLEVI NQRISQINFG NSGLKESLLV NENSENSKEN QKINSFTKRG DTHTEEQLEK TSSSLRETVL SIRNDGSSPE KNTRSVLNSR NEAPSVRRKT PANKFDGQKV VENNSKVSPE KTSEKPLFQN REKNQPMEMK MKYEEKGKIE SYREITNREA LEFLSQERAK QVYSLPELKR TETVHLPRFV EQMYYHKTER AVIDLEPPEL GKLEITITKE ENQLKIVFRV QTEEAKHVLE HDIPRLIERF NEKGFDVQVY VEKQEEDYLY QENQNKEGNQ RQQRESKNHK RETSGSLFEE FIQEVKT // ID Q9WZR6_THEMA Unreviewed; 467 AA. AC Q9WZR6; B6DVV2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Beta-N-acetylglucosaminidase {ECO:0000313|EMBL:ACI15900.1}; DE EC=3.2.1.52 {ECO:0000313|EMBL:ACI15900.1}; DE SubName: Full=Hydrolase, putative {ECO:0000313|EMBL:AAD35891.1}; GN Name=nagA {ECO:0000313|EMBL:ACI15900.1}; GN OrderedLocusNames=TM_0809 {ECO:0000313|EMBL:AAD35891.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35891.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35891.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35891.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:ACI15900.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MSB8 {ECO:0000313|EMBL:ACI15900.1}; RX PubMed=19914575; DOI=10.1016/j.jbiosc.2009.06.003; RA Choi K.-H., Seo J.Y., Park K.-M., Park C.-S., Cha J.; RT "Characterization of glycosyl hydrolase family 3 beta-N- RT acetylglucosaminidases from Thermotoga maritima and Thermotoga RT neapolitana."; RL J. Biosci. Bioeng. 108:455-459(2009). RN [3] {ECO:0000213|PDB:3WO8} RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS). RX PubMed=25227262; DOI=10.1111/febs.13049; RA Mine S., Kado Y., Watanabe M., Fukuda Y., Abe Y., Ueda T., RA Kawarabayasi Y., Inoue T., Ishikawa K.; RT "The structure of hyperthermophilic beta-N-acetylglucosaminidase RT reveals a novel dimer architecture associated with the active site."; RL FEBS J. 281:5092-5103(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35891.1; -; Genomic_DNA. DR EMBL; FJ172673; ACI15900.1; -; Genomic_DNA. DR PIR; B72331; B72331. DR RefSeq; NP_228618.1; NC_000853.1. DR RefSeq; WP_010865208.1; NC_000853.1. DR PDB; 3WO8; X-ray; 2.43 A; A/B=1-467. DR PDBsum; 3WO8; -. DR STRING; 243274.TM0809; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR EnsemblBacteria; AAD35891; AAD35891; TM_0809. DR GeneID; 898477; -. DR KEGG; tma:TM0809; -. DR KEGG; tmi:THEMA_00605; -. DR PATRIC; 23936538; VBITheMar51294_0821. DR eggNOG; ENOG4107QWM; Bacteria. DR eggNOG; COG1472; LUCA. DR KO; K01207; -. DR OMA; EDSHFTL; -. DR OrthoDB; EOG6X9MKR; -. DR BioCyc; TMAR243274:GC6P-836-MONOMER; -. DR BRENDA; 3.2.1.52; 10309. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central. DR Gene3D; 3.20.20.300; -; 1. DR InterPro; IPR001764; Glyco_hydro_3_N. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF00933; Glyco_hydro_3; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3WO8}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|SAAS:SAAS00475007, KW ECO:0000313|EMBL:ACI15900.1}; KW Hydrolase {ECO:0000256|SAAS:SAAS00475007, KW ECO:0000313|EMBL:ACI15900.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 309 Glyco_hydro_3. FT {ECO:0000259|Pfam:PF00933}. SQ SEQUENCE 467 AA; 52378 MW; 1EE6CE84A7BA344B CRC64; MDVDLGKLFF CGFNDFNEEV KEIIRKYRPT GILIYPGVLS KEYLLMDFMS FLSKEGDFLI SSDHEGGQLE VLKYVPSSPG NLAFGKNSPD VTYRYSRVAG KIMEIVGLNM VFAPVLDLLS EESSSVIDIR SYGSDPKIVA EHGARACEGY LEGGVIPCIK HFPGHGKARE DSHLTLPVVD APFEKLWEED LLPFRKVLER EKKVTVMTAH VRYSSIDSLP ATLSEKIITD VLREKIGFDG LVISDAMEMS AVSNNFSVEE IVSLFLNAGG NMILLGDYRN LPVYYETLVK LLEDGKVQKD KVERSIRTVE KYLAFAKKNS GVGFLADVSM KAVEFLGFEK IDHTSEVTLL VPSSENLSQA DTTGGDYDQI PEIVSRFFEV ENVVRYTVED GPEFVEGDLI FDFVADIPNE KALKAHLSLP AEKTVYFVLR NPFDVRYFEG RKIVVTRSTK PISIYKSLEH FLGRCDS // ID Q9X0P7_THEMA Unreviewed; 558 AA. AC Q9X0P7; G4FEI2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE SubName: Full=2-oxoacid ferredoxin oxidoreductase, alpha subunit {ECO:0000313|EMBL:AAD36240.1}; DE SubName: Full=2-oxoglutarate oxidoreductase, alpha subunit {ECO:0000313|EMBL:AGL50095.1}; DE EC=1.2.7.3 {ECO:0000313|EMBL:AGL50095.1}; GN OrderedLocusNames=TM_1164 {ECO:0000313|EMBL:AAD36240.1}; GN ORFNames=Tmari_1171 {ECO:0000313|EMBL:AGL50095.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36240.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36240.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36240.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50095.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50095.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36240.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50095.1; -; Genomic_DNA. DR PIR; B72288; B72288. DR RefSeq; NP_228970.1; NC_000853.1. DR RefSeq; WP_004080205.1; NZ_CP011107.1. DR STRING; 243274.TM1164; -. DR EnsemblBacteria; AAD36240; AAD36240; TM_1164. DR EnsemblBacteria; AGL50095; AGL50095; Tmari_1171. DR GeneID; 898322; -. DR KEGG; tma:TM1164; -. DR KEGG; tmi:THEMA_08515; -. DR KEGG; tmm:Tmari_1171; -. DR KEGG; tmw:THMA_1189; -. DR PATRIC; 23937265; VBITheMar51294_1181. DR eggNOG; ENOG4105DI2; Bacteria. DR eggNOG; COG0674; LUCA. DR eggNOG; COG1014; LUCA. DR KO; K00174; -. DR OMA; TGFPTRT; -. DR OrthoDB; EOG69PQ05; -. DR BioCyc; TMAR243274:GC6P-1193-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 1. DR Gene3D; 3.40.920.10; -; 1. DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu. DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat. DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N. DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR Pfam; PF01558; POR; 1. DR Pfam; PF01855; POR_N; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR SUPFAM; SSF52922; SSF52922; 1. DR SUPFAM; SSF53323; SSF53323; 1. DR TIGRFAMs; TIGR03710; OAFO_sf; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50095.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 12 169 POR. {ECO:0000259|Pfam:PF01558}. FT DOMAIN 204 437 POR_N. {ECO:0000259|Pfam:PF01855}. SQ SEQUENCE 558 AA; 61458 MW; E7BC53686E97F281 CRC64; MKDVSIVLSG EAGQGIQTVE NVLTRVLKDS GFHVFATKEY MSRVRGGNNT TEIRVSSRRV RSFVDRIDVL IPLGKGATER LKNRITEKTL VIGEEEFIKE SPGEKIVIPF LNIAKQIGKS IYANSVAIGF LSGLLGADES ALKDQITRQF SSKGEDIVND NIRAALEGYK KGQELSQKIE FDVEKDPSIK NEVLLNGAEA VGLGAIAGGC NFVSSYPMSP STSVLVFLAQ HKNDFGIVVE QAEDEIAAMN MIIGAWYAGA RGLVTTSGGG FALMEEALSL AGMIESPAVI HLAQRPGPAT GLPTRTEQGD LNLALYAGHG DFPRVIYAPG NVEEAFYLTQ KAFNVADKYQ VPVFVLTDQY LVDSYYNLPG FDLNELKVEK HFIKTTRDYI RYAITEDGIS PRGIPGYGEG LVRVDSDEHD EFGHITEDFN TRVRMVNKRL RKGETLKKEI VKPKLIGDEN YRVLLVAWGS TLEPIKEAIE GLDGVALLHF SQVWPIDESV ATYFEKAEKV VAVEGNATGQ FANLIRQVTG FHIKDRILKY NGLQFSVEEL KEKIAEVL // ID Q9WXY8_THEMA Unreviewed; 410 AA. AC Q9WXY8; G4FH49; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Transposase, putative {ECO:0000313|EMBL:AAD35228.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL49059.1}; GN OrderedLocusNames=TM_0135 {ECO:0000313|EMBL:AAD35228.1}; GN ORFNames=Tmari_0133 {ECO:0000313|EMBL:AGL49059.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35228.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35228.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35228.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49059.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49059.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35228.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49059.1; -; Genomic_DNA. DR PIR; E72413; E72413. DR RefSeq; NP_227950.1; NC_000853.1. DR RefSeq; WP_004082727.1; NZ_CP011107.1. DR STRING; 243274.TM0135; -. DR DNASU; 896962; -. DR EnsemblBacteria; AAD35228; AAD35228; TM_0135. DR EnsemblBacteria; AGL49059; AGL49059; Tmari_0133. DR GeneID; 896962; -. DR KEGG; tma:TM0135; -. DR KEGG; tmi:THEMA_04130; -. DR KEGG; tmm:Tmari_0133; -. DR KEGG; tmw:THMA_0130; -. DR PATRIC; 23935112; VBITheMar51294_0134. DR eggNOG; ENOG4108QGC; Bacteria. DR eggNOG; COG0675; LUCA. DR KO; K07496; -. DR OMA; TEKANRN; -. DR OrthoDB; EOG6D2KVG; -. DR BioCyc; TMAR243274:GC6P-135-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR001959; Transposase_2. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR InterPro; IPR010094; Transposase_put_N. DR Pfam; PF01385; OrfB_IS605; 1. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. DR TIGRFAMs; TIGR01765; tspaseT_teng_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 182 277 OrfB_IS605. {ECO:0000259|Pfam:PF01385}. FT DOMAIN 312 383 OrfB_Zn_ribbon. FT {ECO:0000259|Pfam:PF07282}. SQ SEQUENCE 410 AA; 47653 MW; B66EE2E9F5D1F1BF CRC64; MTVTLTCRFK LELSKDQKQQ FLDIATAYTN AVNYVLEQNL KDKSTNVKKL HRLYYKTIRE DFDLPAQMAI NVNRDVSAMY KTLWAQFKEL KRRKPDSKAV KKFWDKPPKR KSLIVKYTYN RTASFKKING EWHASLSTLQ GRIKWIPMKG WSKHFEYLKS CKIGDPILTY DKSSKTFFLL VPVTLEVQEH QPKEIVGVDV GERHIAAVAS TKGTRYLIDL PEEFKQRKQH YQRLRSELMS KGTRSAKRKL ARISRREKRF TENVLHIIAK KLTTSHPGAR FVLEDLTQIR ANRITYRGKD KEARRQSEQW PFASLQQKIE YKAKLYYGVQ SEKVDPSYTS QTCPRCGHVS KENRPDHGER FVCQSCGYEE HADIVGAINI ALRVLAKDQQ VNLEKLLGAV VSRPDAPRLG // ID Q9WYP8_THEMA Unreviewed; 273 AA. AC Q9WYP8; G4FHX6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Ferrous iron transport permease EfeU {ECO:0000313|EMBL:AGL49339.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35502.1}; GN OrderedLocusNames=TM_0417 {ECO:0000313|EMBL:AAD35502.1}; GN ORFNames=Tmari_0414 {ECO:0000313|EMBL:AGL49339.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35502.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35502.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35502.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49339.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49339.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35502.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49339.1; -; Genomic_DNA. DR PIR; A72378; A72378. DR RefSeq; NP_228227.1; NC_000853.1. DR RefSeq; WP_004083270.1; NZ_CP011107.1. DR STRING; 243274.TM0417; -. DR EnsemblBacteria; AAD35502; AAD35502; TM_0417. DR EnsemblBacteria; AGL49339; AGL49339; Tmari_0414. DR GeneID; 897419; -. DR KEGG; tma:TM0417; -. DR KEGG; tmi:THEMA_02640; -. DR KEGG; tmm:Tmari_0414; -. DR KEGG; tmw:THMA_0423; -. DR PATRIC; 23935717; VBITheMar51294_0422. DR eggNOG; ENOG4107T0N; Bacteria. DR eggNOG; COG0672; LUCA. DR KO; K07243; -. DR OMA; VGYGTHE; -. DR OrthoDB; EOG62ZHSM; -. DR BioCyc; TMAR243274:GC6P-432-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0033573; C:high-affinity iron permease complex; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006827; P:high-affinity iron ion transmembrane transport; IEA:InterPro. DR InterPro; IPR004923; FTR1/Fip1/EfeU. DR PANTHER; PTHR31632; PTHR31632; 1. DR Pfam; PF03239; FTR1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 61 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 132 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 166 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 193 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 250 268 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 273 AA; 30856 MW; DE4DB63DE7389E87 CRC64; MHLGALLITF REALEASVII AVILAYLKRT GRETQKREVW LGMFFSIFAS LVLGAIVIWF YGGIEEKELF ESVASYVAVV VLTSMIYWMA TKGKSIKSEI ERKVSKVISR WALIGFVFVV VFREGFETVL FVTPFMTQNL AGTVVGIVLG LIFAGAIAYT LYVVGVKINL RRFFYYSSIL LIFVAAGLVG YGTHEFIEWS EEKGFDLGFF EKEAYNLGIP ESSVWHHKGL IGSILMVLFG YSVKMEWGRV LVQFGYLVLA LILITRAYKR KEI // ID Q9X082_THEMA Unreviewed; 1008 AA. AC Q9X082; G4FF08; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36066.1}; GN OrderedLocusNames=TM_0987 {ECO:0000313|EMBL:AAD36066.1}; GN ORFNames=Tmari_0990 {ECO:0000313|EMBL:AGL49915.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36066.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36066.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36066.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49915.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49915.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36066.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49915.1; -; Genomic_DNA. DR PIR; H72310; H72310. DR RefSeq; NP_228795.1; NC_000853.1. DR RefSeq; WP_004080574.1; NZ_CP011107.1. DR STRING; 243274.TM0987; -. DR REBASE; 64913; M.TmaMSB8ORF990P. DR EnsemblBacteria; AAD36066; AAD36066; TM_0987. DR EnsemblBacteria; AGL49915; AGL49915; Tmari_0990. DR GeneID; 897013; -. DR KEGG; tma:TM0987; -. DR KEGG; tmi:THEMA_09415; -. DR KEGG; tmm:Tmari_0990; -. DR KEGG; tmw:THMA_1009; -. DR PATRIC; 23936903; VBITheMar51294_1000. DR eggNOG; COG1743; LUCA. DR KO; K07445; -. DR OMA; YKLFNPR; -. DR OrthoDB; EOG6QP0WF; -. DR BioCyc; TMAR243274:GC6P-1017-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 3. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR009537; DUF1156. DR InterPro; IPR014455; N6_adenine_Mtase_MK1259. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF06634; DUF1156; 1. DR PIRSF; PIRSF009427; UCP009427_DNAmts; 1. DR SUPFAM; SSF53335; SSF53335; 4. DR PROSITE; PS00092; N6_MTASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 10 56 DUF1156. {ECO:0000259|Pfam:PF06634}. SQ SEQUENCE 1008 AA; 115761 MW; 4D640F610123E614 CRC64; MKTFLESLKF PVQEVNKKSS GEKGPGRPPY WEMVFYWTRK PLVGARSVIA GALLPENVDE NLFKAAVRLS SPTPHRENPQ IPAEFAKYFE GKKLLDPFAG FGSIPLEGLR LGLDVTAVEL LPTTYIFLKA VLEYPKKFGK SLVKDVERWG EWITEQLKND PEIRELYDDD VAVYIGTWEI RCPHCGRWTP AIGNFWLARV KDGKGYKRLA YMKPERKGDE IEIRVIDLNE ILDDISKANV DGNEIIFEGE NYVKTVEEAV RDGKLKQSDV KIDGNTVIFE VPSANIESRR DQLTCLMCGN VIKYADENGN HHMKLKNGDF YVKFALRKYH EGDERFARQR LLVKVKVKDG DLIFEPATKE DSEKLWKAKE KVREMLEKGD LDVPSEAIPL YENRRITPIL SAEKWYQFFN PRQLLTLIKI VRLIREVGRK VEEEKIAEGW NKERAFEYAE AVATYLSTAM LKYAYYNSIV TRWDSTWWKI GETMSTRGIA MNWNWTESPW FSSFGGMIKT LLAILRGVKY LTSALSSSQR TLADFTENSV KVLQGDATSL NLGEKFDVIV TDPPYADDVP YTELSDFYYV WLKRALSDVE NGKLIPRFHK EAFFKRIGPK WVEIKTQWQE FAKKEVSTNP GRFMEDENKK EKAVQHFENL FSQAFVAMRE HLKDDGVLVT YYAHTDPGSW INLIEAGWRR ARLQITRAIP LTTESETSIV SRGKMSLDTS IVAVWRKQKE EKTVQISTLK EEIERKAKSS AREFIEYGYE GLDLLYGVMA AALEEVTKYR EISSLKGPLT TEEILNEYVY PATIRGIVNA IAEIEGTGTL HSGTAMFYTA YKILFGNASL SANDIVLLRL ATSTDPSELI SSGVLKEKRS SSSKEYTLYT PDLLGKKALD TKEFQKFLHE KKLDPVEPKP KNSVDVLQLL EYYSLLGRSR VKEEIEKLRK MWAGEVEEAL FIARLVSEYY AEIYIRKIDP VRRMKEEFAS EIDRELEKDG FLEVVLMRRL LGYVGGAV // ID Q9X0D5_THEMA Unreviewed; 421 AA. AC Q9X0D5; G4FEV3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Arsenical pump membrane protein {ECO:0000313|EMBL:AGL49973.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36122.1}; GN OrderedLocusNames=TM_1045 {ECO:0000313|EMBL:AAD36122.1}; GN ORFNames=Tmari_1049 {ECO:0000313|EMBL:AGL49973.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36122.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36122.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36122.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49973.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49973.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36122.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49973.1; -; Genomic_DNA. DR PIR; G72300; G72300. DR RefSeq; NP_228851.1; NC_000853.1. DR RefSeq; WP_004080471.1; NZ_CP011107.1. DR STRING; 243274.TM1045; -. DR EnsemblBacteria; AAD36122; AAD36122; TM_1045. DR EnsemblBacteria; AGL49973; AGL49973; Tmari_1049. DR GeneID; 898703; -. DR KEGG; tma:TM1045; -. DR KEGG; tmi:THEMA_09135; -. DR KEGG; tmm:Tmari_1049; -. DR KEGG; tmw:THMA_1067; -. DR PATRIC; 23937019; VBITheMar51294_1058. DR eggNOG; ENOG4105Z8X; Bacteria. DR eggNOG; COG1055; LUCA. DR OMA; GRVINTG; -. DR OrthoDB; EOG6VXF6K; -. DR BioCyc; TMAR243274:GC6P-1074-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0015105; F:arsenite transmembrane transporter activity; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR GO; GO:0098656; P:anion transmembrane transport; IBA:GO_Central. DR GO; GO:0015700; P:arsenite transport; IEA:InterPro. DR InterPro; IPR000802; Arsenical_pump_ArsB. DR InterPro; IPR004680; Cit_transptr-like_dom. DR Pfam; PF03600; CitMHS; 1. DR PRINTS; PR00758; ARSENICPUMP. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 39 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 126 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 162 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 174 193 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 224 242 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 249 268 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 280 302 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 314 344 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 356 380 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 401 420 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 15 363 CitMHS. {ECO:0000259|Pfam:PF03600}. SQ SEQUENCE 421 AA; 46868 MW; 517130A77BE19090 CRC64; MNEAMLVLLF AILAYYFIIF GKIAKSVVTL LIALVLMAIK VVEGLDLKNI GEVVDFNTLG LLLGMMIIVH ILKGTGFFEY LAISAIKISR GRFWLLFAFL MVLTAVTSAF LDNLITIILV SPILFLILDT MEVNPVPFFL FTIFIDNIGG MSTLIGSPLN IVLGSISGLS FNDFLKNMGL VTVLMFVVVF FLFKRYVRID EKAFEKLRNL LSVDPKRSIT DPVVLKKSLF VFLSTLVLFG LHSFVEVELS LIALIAACAL LLMLGKNFEK VSEGIDWDTL FFYTGLFIIS YSLEQIGVME VIASFLKALS FNRFLFVATV TWISILSTAF LSAVPATLII APTLKILVSQ GFPASLWWVY AVGANLGTNL TPLGAVQNIV GLSLLEKYTK HTVSFKEFFK VAWSFMFIPF IIATLYSLII Y // ID Q9WY04_THEMA Unreviewed; 149 AA. AC Q9WY04; G4FH70; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Actinorhodin polyketide dimerase-related protein {ECO:0000313|EMBL:AAD35250.1}; DE SubName: Full=Nitrilotriacetate monooxygenase component B {ECO:0000313|EMBL:AGL49080.1}; DE EC=1.14.13.- {ECO:0000313|EMBL:AGL49080.1}; GN OrderedLocusNames=TM_0157 {ECO:0000313|EMBL:AAD35250.1}; GN ORFNames=Tmari_0154 {ECO:0000313|EMBL:AGL49080.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35250.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35250.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35250.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49080.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49080.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35250.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49080.1; -; Genomic_DNA. DR PIR; C72410; C72410. DR RefSeq; NP_227972.1; NC_000853.1. DR RefSeq; WP_004082774.1; NZ_CP011107.1. DR STRING; 243274.TM0157; -. DR EnsemblBacteria; AAD35250; AAD35250; TM_0157. DR EnsemblBacteria; AGL49080; AGL49080; Tmari_0154. DR GeneID; 896995; -. DR KEGG; tma:TM0157; -. DR KEGG; tmi:THEMA_04020; -. DR KEGG; tmm:Tmari_0154; -. DR KEGG; tmw:THMA_0152; -. DR PATRIC; 23935156; VBITheMar51294_0155. DR eggNOG; ENOG41083YZ; Bacteria. DR eggNOG; COG1853; LUCA. DR OMA; WVMQASF; -. DR OrthoDB; EOG6GJBVP; -. DR BioCyc; TMAR243274:GC6P-158-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IBA:GO_Central. DR Gene3D; 2.30.110.10; -; 1. DR InterPro; IPR002563; Flavin_Rdtase-like_dom. DR InterPro; IPR012349; Split_barrel_FMN-bd. DR Pfam; PF01613; Flavin_Reduct; 1. DR SMART; SM00903; Flavin_Reduct; 1. DR SUPFAM; SSF50475; SSF50475; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Monooxygenase {ECO:0000313|EMBL:AGL49080.1}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49080.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 147 Flavin_Reduct. FT {ECO:0000259|SMART:SM00903}. SQ SEQUENCE 149 AA; 16623 MW; 9EF881B9DE5580A6 CRC64; MDALGKLYTS TAIVTVNVEG KLNGITVAWV TRVSWQPPMV AVSIGKTRYT RELMDRTDSF AVCILGKDAK EIAEYFGTVS GRNTDKFKKY PYTMSEGNLP IPEGTIAYIE CDKTGQFEAG DHIVYIGTVR RQKVLKDEPP LIFGEHELL // ID Q9X123_THEMA Unreviewed; 285 AA. AC Q9X123; G4FE52; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Oxidoreductase, putative {ECO:0000313|EMBL:AAD36371.1}; DE SubName: Full=Putative oxidoreductases (Related to aryl-alcohol dehydrogenases) {ECO:0000313|EMBL:AGL50229.1}; GN OrderedLocusNames=TM_1297 {ECO:0000313|EMBL:AAD36371.1}; GN ORFNames=Tmari_1305 {ECO:0000313|EMBL:AGL50229.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36371.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36371.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36371.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50229.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50229.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36371.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50229.1; -; Genomic_DNA. DR PIR; C72269; C72269. DR RefSeq; NP_229101.1; NC_000853.1. DR RefSeq; WP_004079927.1; NZ_CP011107.1. DR STRING; 243274.TM1297; -. DR EnsemblBacteria; AAD36371; AAD36371; TM_1297. DR EnsemblBacteria; AGL50229; AGL50229; Tmari_1305. DR GeneID; 898185; -. DR KEGG; tma:TM1297; -. DR KEGG; tmi:THEMA_07850; -. DR KEGG; tmm:Tmari_1305; -. DR KEGG; tmw:THMA_1323; -. DR PATRIC; 23937534; VBITheMar51294_1313. DR eggNOG; ENOG4107UNA; Bacteria. DR eggNOG; COG0667; LUCA. DR OMA; KPMADAR; -. DR OrthoDB; EOG60652R; -. DR BioCyc; TMAR243274:GC6P-1328-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red/Kv-b. DR InterPro; IPR020471; Aldo/keto_reductase. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR SUPFAM; SSF51430; SSF51430; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 23 263 Aldo_ket_red. {ECO:0000259|Pfam:PF00248}. SQ SEQUENCE 285 AA; 32487 MW; AC18EB00723DBBDC CRC64; MEKRVLGKTG EKLSVVGFGG IVVMNESVES AKKIVARAIE RGINYFDVAP SYGDAEEKLG PALKPYRDQV FLACKTMERT KEGAWKELNE SLKRLQTDHF DLYQFHAVTT LDEVEAIFSP NGAIEAFLKA KEEGLIRYIG FSAHSEEAAL SMLERFDFDT VLFPLNWASW LGKGFGKRLY SKAREKNMGI LAIKALAKRR LEEGEEKRWE KCWYHPVDDF EEASMALRFT LSLPVTAAVS PSHQEFLWWM CQIVENQGTK ISEEELQILK EKAQKLTPVF PLDHS // ID Q9WZG9_THEMA Unreviewed; 143 AA. AC Q9WZG9; G4FDB4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 110. DE SubName: Full=Transcriptional regulator, MarR family {ECO:0000313|EMBL:AAD35792.1}; GN OrderedLocusNames=TM_0710 {ECO:0000313|EMBL:AAD35792.1}; GN ORFNames=Tmari_0710 {ECO:0000313|EMBL:AGL49635.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35792.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35792.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35792.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:2A61} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND DISULFIDE BONDS. RA Lunin V.V., Evdokimova E., Kudritska M., Chang C., Joachimiak A., RA Edwards A., Savchenko A.; RT "The crystal structure of transcriptional regulator Tm0710 from RT Thermotoga maritima."; RL Submitted (JUL-2005) to the PDB data bank. RN [3] {ECO:0000313|EMBL:AGL49635.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49635.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 4 HTH marR-type DNA-binding domains. CC {ECO:0000256|RuleBase:RU000702}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35792.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49635.1; -; Genomic_DNA. DR PIR; E72343; E72343. DR RefSeq; NP_228519.1; NC_000853.1. DR RefSeq; WP_004081029.1; NZ_CP011107.1. DR PDB; 2A61; X-ray; 1.80 A; A/B/C/D=1-143. DR PDBsum; 2A61; -. DR SMR; Q9WZG9; 2-143. DR STRING; 243274.TM0710; -. DR EnsemblBacteria; AAD35792; AAD35792; TM_0710. DR EnsemblBacteria; AGL49635; AGL49635; Tmari_0710. DR GeneID; 898377; -. DR KEGG; tma:TM0710; -. DR KEGG; tmi:THEMA_01115; -. DR KEGG; tmm:Tmari_0710; -. DR KEGG; tmw:THMA_0725; -. DR PATRIC; 23936338; VBITheMar51294_0722. DR eggNOG; ENOG41067TZ; Bacteria. DR eggNOG; ENOG410XUB6; LUCA. DR OMA; MADYSPF; -. DR OrthoDB; EOG6B62DJ; -. DR BioCyc; TMAR243274:GC6P-736-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR000835; HTH_MarR-typ. DR InterPro; IPR023187; Tscrpt_reg_MarR-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01047; MarR; 1. DR PRINTS; PR00598; HTHMARR. DR SMART; SM00347; HTH_MARR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS01117; HTH_MARR_1; 1. DR PROSITE; PS50995; HTH_MARR_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2A61}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487313}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487138}; KW Transcription regulation {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487138}. FT DOMAIN 1 134 HTH marR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50995}. FT DISULFID 13 13 Interchain. {ECO:0000213|PDB:2A61}. SQ SEQUENCE 143 AA; 16567 MW; 93049E8958F3ADE2 CRC64; MKQPFERILR EICFMVKVEG RKVLRDFGIT PAQFDILQKI YFEGPKRPGE LSVLLGVAKS TVTGLVKRLE ADGYLTRTPD PADRRAYFLV ITRKGEEVIE KVIERRENFI EKITSDLGKE KSSKILDYLK ELKGVMERNF SKQ // ID Q9X2D9_THEMA Unreviewed; 190 AA. AC Q9X2D9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Chromate transport protein, putative {ECO:0000313|EMBL:AAD36882.1}; GN OrderedLocusNames=TM_1819 {ECO:0000313|EMBL:AAD36882.1}; GN ORFNames=Tmari_1829 {ECO:0000313|EMBL:AGL50753.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36882.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36882.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36882.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50753.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50753.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36882.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50753.1; -; Genomic_DNA. DR PIR; F72206; F72206. DR RefSeq; NP_229616.1; NC_000853.1. DR RefSeq; WP_010865410.1; NC_000853.1. DR STRING; 243274.TM1819; -. DR EnsemblBacteria; AAD36882; AAD36882; TM_1819. DR EnsemblBacteria; AGL50753; AGL50753; Tmari_1829. DR GeneID; 897825; -. DR KEGG; tma:TM1819; -. DR KEGG; tmm:Tmari_1829; -. DR PATRIC; 23938625; VBITheMar51294_1839. DR eggNOG; ENOG4108V6Y; Bacteria. DR eggNOG; COG2059; LUCA. DR KO; K07240; -. DR OMA; AYASIIG; -. DR OrthoDB; EOG6MWNGX; -. DR BioCyc; TMAR243274:GC6P-1870-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015109; F:chromate transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003370; Chromate_transpt. DR Pfam; PF02417; Chromate_transp; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 43 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64 84 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 90 115 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 127 146 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 187 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 190 AA; 20763 MW; 38769F51A5237E2B CRC64; MEICVEGKSS KIEVQEGSNL IGRLFFLFLR ISALTIGGGY AMIPVMKWEL ERSGLLTEKE FFRIMSTAQV VPGPIAFNTA VLVGRRLAGI YGAIASGLAV VLPPFFAIVA VAEVIRTLSG ISYVRSFLRG AYASIIGLVG SVLYRLVRNQ RWNLYRAIMI GVAVFVLLLN GSLVIPVVIL LVLLLYLKEV // ID Q9X260_THEMA Unreviewed; 245 AA. AC Q9X260; G4FGC4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=GufA protein {ECO:0000313|EMBL:AAD36803.1}; DE SubName: Full=Metal transporter, ZIP family {ECO:0000313|EMBL:AGL50670.1}; GN OrderedLocusNames=TM_1738 {ECO:0000313|EMBL:AAD36803.1}; GN ORFNames=Tmari_1746 {ECO:0000313|EMBL:AGL50670.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36803.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36803.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36803.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50670.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50670.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36803.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50670.1; -; Genomic_DNA. DR PIR; A72218; A72218. DR RefSeq; NP_229536.1; NC_000853.1. DR RefSeq; WP_004082259.1; NZ_CP011107.1. DR STRING; 243274.TM1738; -. DR DNASU; 897180; -. DR EnsemblBacteria; AAD36803; AAD36803; TM_1738. DR EnsemblBacteria; AGL50670; AGL50670; Tmari_1746. DR GeneID; 897180; -. DR KEGG; tma:TM1738; -. DR KEGG; tmi:THEMA_05545; -. DR KEGG; tmm:Tmari_1746; -. DR KEGG; tmw:THMA_1780; -. DR PATRIC; 23938452; VBITheMar51294_1756. DR eggNOG; ENOG4105DUN; Bacteria. DR eggNOG; COG0428; LUCA. DR KO; K07238; -. DR OMA; MIVASFT; -. DR OrthoDB; EOG6M3PH0; -. DR BioCyc; TMAR243274:GC6P-1786-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0071577; P:zinc II ion transmembrane transport; IBA:GO_Central. DR InterPro; IPR003689; ZIP. DR Pfam; PF02535; Zip; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64 82 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 125 145 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 165 187 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 193 214 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 244 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 245 AA; 25865 MW; 1FBAC67841ED2987 CRC64; MVLKGILYST IAGMATSLGA LPFLFLKPHH TSDKVIDSFL GFAAGVMLAA SAFSLVAPSL EMGGIVRFLI GFVLGGLFVN LADKLIPHEH LLKGHEGPDT KRLKGVWLFI IAITIHNFPE GMAVGVSAFT PQALAIAIAI GVQNIPEGAA VMASLIPMKY KKGKAFLITF LTGLVEAIGG LLGAGIVSIS QRLLPYMMAF AAGAMIYVVS DEVIPETHSK GNELLSTWWI MVGFLVMASL DVALG // ID Q9WY23_THEMA Unreviewed; 92 AA. AC Q9WY23; G4FH93; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35272.1}; GN OrderedLocusNames=TM_0179 {ECO:0000313|EMBL:AAD35272.1}; GN ORFNames=Tmari_0177 {ECO:0000313|EMBL:AGL49103.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35272.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35272.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35272.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49103.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49103.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35272.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49103.1; -; Genomic_DNA. DR PIR; F72407; F72407. DR RefSeq; NP_227994.1; NC_000853.1. DR RefSeq; WP_004082814.1; NZ_CP011107.1. DR STRING; 243274.TM0179; -. DR EnsemblBacteria; AAD35272; AAD35272; TM_0179. DR EnsemblBacteria; AGL49103; AGL49103; Tmari_0177. DR GeneID; 897025; -. DR KEGG; tma:TM0179; -. DR KEGG; tmi:THEMA_03880; -. DR KEGG; tmm:Tmari_0177; -. DR KEGG; tmw:THMA_0180; -. DR PATRIC; 23935214; VBITheMar51294_0180. DR eggNOG; ENOG41060VT; Bacteria. DR eggNOG; ENOG41127BP; LUCA. DR OMA; LTEYGCY; -. DR OrthoDB; EOG6KHG30; -. DR BioCyc; TMAR243274:GC6P-185-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 92 AA; 10336 MW; 2B3E5086856FA754 CRC64; MAEKLPIKTV MTILVENRRE TAEKVQKILT AWGCLIKTRL GLHDGVLDNC SEAGLIVLEL VGSPEQHREL CDKLNKLPGV KADYMELSFD EE // ID Q9X136_THEMA Unreviewed; 580 AA. AC Q9X136; G4FE41; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36384.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL50240.1}; GN OrderedLocusNames=TM_1310 {ECO:0000313|EMBL:AAD36384.1}; GN ORFNames=Tmari_1316 {ECO:0000313|EMBL:AGL50240.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36384.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36384.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36384.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50240.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50240.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36384.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50240.1; -; Genomic_DNA. DR PIR; H72270; H72270. DR RefSeq; NP_229114.1; NC_000853.1. DR RefSeq; WP_004079909.1; NZ_CP011107.1. DR STRING; 243274.TM1310; -. DR EnsemblBacteria; AAD36384; AAD36384; TM_1310. DR EnsemblBacteria; AGL50240; AGL50240; Tmari_1316. DR GeneID; 898172; -. DR KEGG; tma:TM1310; -. DR KEGG; tmi:THEMA_07795; -. DR KEGG; tmm:Tmari_1316; -. DR KEGG; tmw:THMA_1334; -. DR PATRIC; 23937558; VBITheMar51294_1325. DR eggNOG; ENOG4108KNM; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K06148; -. DR OMA; CISSIYR; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; TMAR243274:GC6P-1341-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0034040; F:lipid-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0006869; P:lipid transport; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD36384.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD36384.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 41 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 161 180 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 252 270 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 276 296 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 25 305 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 341 567 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 580 AA; 66433 MW; 44556E2E2A19CFA0 CRC64; MNLRSIQKIL RFYSLIRKRF LVLIVIGGFL ATSSVVFDFF IPLLVRDVID GLAGLELRLN TIYLLGFLYA LSFVLTYAGD QIYLKAKYRA VADLSSRIFS QSFFFPWQKL KQQGSAYYAT LINHQLNDAF FLLDYGFFQN VLVIIRSVFI LATVFVWNKA FFGLFVANAV IVGIYLNIIG RVTERPYAQM YEILRRVTGF ITETFENIHE VLAGEAQKKR QKECETMYQQ VADTVLKAEL PRSRFDKLMV NLPEYFTRLF ILTYGAYLVI DGKMTVGTIW ALWTYFSFVT APLYMFRELA RVITRVSANL DAVLDYFDEV KRAEETFKKR EIKPVPGSPV YELIDVTFGF EPGKPILKQV SFTIQPREIA AIVGLSGEGK STLLNILLGL EQNYEGVVKL FGNDLKQVMP SAVFEHVAFY SQNVGIFNDT LENNIVLGRE YDEKKLERII KELGIEHLRG RKLGEGGSFV SGGEKQRIQL ARLFYADKPV VVLDEPLTNL DTITEKFLLE KLIEFLKEKT AIMISHKPNI IRVASKIIFL ENGKVSSVGG FEELMQNNTT FRRIIETYVN ESKRIADKDV // ID Q9X0X9_THEMA Unreviewed; 191 AA. AC Q9X0X9; G4FE96; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36327.1}; GN OrderedLocusNames=TM_1252 {ECO:0000313|EMBL:AAD36327.1}; GN ORFNames=Tmari_1257 {ECO:0000313|EMBL:AGL50181.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36327.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36327.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36327.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50181.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50181.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36327.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50181.1; -; Genomic_DNA. DR PIR; F72277; F72277. DR RefSeq; NP_229057.1; NC_000853.1. DR RefSeq; WP_004080011.1; NZ_CP011107.1. DR STRING; 243274.TM1252; -. DR EnsemblBacteria; AAD36327; AAD36327; TM_1252. DR EnsemblBacteria; AGL50181; AGL50181; Tmari_1257. DR GeneID; 898231; -. DR KEGG; tma:TM1252; -. DR KEGG; tmi:THEMA_08075; -. DR KEGG; tmm:Tmari_1257; -. DR KEGG; tmw:THMA_1277; -. DR PATRIC; 23937444; VBITheMar51294_1268. DR OMA; SAFYGMA; -. DR OrthoDB; EOG6F81Q0; -. DR BioCyc; TMAR243274:GC6P-1283-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 18 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 50 69 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 76 109 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 141 165 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 191 AA; 21567 MW; 82A6ABCD45D08498 CRC64; MIESFVKGFR EIVQNTKLAV ISVMALVLGF VTEVLYIFAG KYDFLSFDFF VIKLFEEVLL ALLMGLLLVP RRRENLLSLL VFSAFYGLTV SAGFSLFVLP GFVAFMFLFF VPLLSAKDES PSSVLEKNYR MVFKGEKTVD VFLAAAVVFI VWFIPYLGSI ISNLLRVVLV YSMYRIMEGS YEKTESDTGS A // ID Q9WXZ4_THEMA Unreviewed; 110 AA. AC Q9WXZ4; G4FH61; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE RecName: Full=Ribosomal silencing factor RsfS {ECO:0000256|HAMAP-Rule:MF_01477}; GN Name=rsfS {ECO:0000256|HAMAP-Rule:MF_01477}; GN OrderedLocusNames=TM_0147 {ECO:0000313|EMBL:AAD35240.1}; GN ORFNames=Tmari_0145 {ECO:0000313|EMBL:AGL49071.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35240.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35240.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35240.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49071.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49071.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Functions as a ribosomal silencing factor. Interacts CC with ribosomal protein L14 (rplN), blocking formation of CC intersubunit bridge B8. Prevents association of the 30S and 50S CC ribosomal subunits and the formation of functional ribosomes, thus CC repressing translation. {ECO:0000256|HAMAP-Rule:MF_01477}. CC -!- SUBUNIT: Interacts with ribosomal protein L14 (rplN). CC {ECO:0000256|HAMAP-Rule:MF_01477}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01477}. CC -!- SIMILARITY: Belongs to the Iojap/RsfS family. {ECO:0000256|HAMAP- CC Rule:MF_01477}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35240.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49071.1; -; Genomic_DNA. DR PIR; A72412; A72412. DR RefSeq; NP_227962.1; NC_000853.1. DR RefSeq; WP_004082754.1; NZ_CP011107.1. DR STRING; 243274.TM0147; -. DR EnsemblBacteria; AAD35240; AAD35240; TM_0147. DR EnsemblBacteria; AGL49071; AGL49071; Tmari_0145. DR GeneID; 896980; -. DR KEGG; tma:TM0147; -. DR KEGG; tmi:THEMA_04065; -. DR KEGG; tmm:Tmari_0145; -. DR KEGG; tmw:THMA_0143; -. DR PATRIC; 23935138; VBITheMar51294_0146. DR eggNOG; ENOG41085A2; Bacteria. DR eggNOG; COG0799; LUCA. DR KO; K09710; -. DR OMA; CSANSER; -. DR OrthoDB; EOG6J48TR; -. DR BioCyc; TMAR243274:GC6P-148-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central. DR GO; GO:0042256; P:mature ribosome assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0090071; P:negative regulation of ribosome biogenesis; IBA:GO_Central. DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central. DR HAMAP; MF_01477; Iojap_RsfS; 1. DR InterPro; IPR004394; Iojap/RsfS/C7orf30. DR PANTHER; PTHR21043; PTHR21043; 1. DR TIGRFAMs; TIGR00090; rsfS_iojap_ybeB; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01477}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Repressor {ECO:0000256|HAMAP-Rule:MF_01477}; KW Translation regulation {ECO:0000256|HAMAP-Rule:MF_01477}. SQ SEQUENCE 110 AA; 12841 MW; AB3368CC887ADFFE CRC64; MIDVLRKILK KISEKGGENP VVLDMRKTPV PTDYFVIFTA NSYTHMRAMR DELIDLIKEL SLPLIYYDKG EEYEWLIIDA GSVVIHIFTE KGRDFYDLEG LWIDADRISV // ID Q9WZ13_THEMA Unreviewed; 412 AA. AC Q9WZ13; G4FDS8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=ABC transporter {ECO:0000313|EMBL:AGL49465.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35628.1}; GN OrderedLocusNames=TM_0543 {ECO:0000313|EMBL:AAD35628.1}; GN ORFNames=Tmari_0540 {ECO:0000313|EMBL:AGL49465.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35628.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35628.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35628.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49465.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49465.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35628.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49465.1; -; Genomic_DNA. DR PIR; D72364; D72364. DR RefSeq; NP_228353.1; NC_000853.1. DR RefSeq; WP_004081357.1; NZ_CP011107.1. DR PDB; 3CNI; X-ray; 2.30 A; A=37-192. DR PDBsum; 3CNI; -. DR STRING; 243274.TM0543; -. DR EnsemblBacteria; AAD35628; AAD35628; TM_0543. DR EnsemblBacteria; AGL49465; AGL49465; Tmari_0540. DR GeneID; 897597; -. DR KEGG; tma:TM0543; -. DR KEGG; tmi:THEMA_01960; -. DR KEGG; tmm:Tmari_0540; -. DR KEGG; tmw:THMA_0556; -. DR PATRIC; 23935993; VBITheMar51294_0551. DR eggNOG; ENOG4105IIQ; Bacteria. DR eggNOG; COG1668; LUCA. DR KO; K01992; -. DR OMA; IMMLIIM; -. DR OrthoDB; EOG6BCSPS; -. DR BioCyc; TMAR243274:GC6P-567-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR InterPro; IPR000412; ABC_2_transport. DR PROSITE; PS51012; ABC_TM2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3CNI}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 193 216 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 237 262 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 282 303 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 315 333 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 369 392 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 412 AA; 45292 MW; A44E3849BB700F7B CRC64; MFGKLLKKEI KELLNLGAIV SVIVVAVLYG SLGNVFKSTV EKSTVGQKVA IVREDTGTIA ELAEKALGNM VDIVYAGSDL KEAEEAVKKE KAPAIIVIPK GFSQSLESGE KARLEIVWYL RGTGLSEAVS TGTISSLIES LKVQLASFLL NDPKKAQLLF DPLEIVQHTY LRGSLFKNHS PEAIMNVFYS QNIMIPILIM MLIIMSGSSL ISSLAMEKEN KTLETLLTMP VKREHIALAK IVGSAIVGLI LAGIYMAGFY SYLNSLTQNV QGMGLNFKAV DFLLMGSSLF LSILAGLSLC MLLGMMAKDY RSAQLLTFPI SILALVPMIA NMIMDFSNLP GVLKVIVFLI PFSHPIMSPK LAFYGDYGLI VSGILYLLIF SIVTTVFVFR IFNSDYVVLG WQREKRLKFF SR // ID Q9WZN2_THEMA Unreviewed; 104 AA. AC Q9WZN2; G4FD49; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Ribosomal protein L7Ae family protein {ECO:0000313|EMBL:AGL49700.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35856.1}; GN OrderedLocusNames=TM_0774 {ECO:0000313|EMBL:AAD35856.1}; GN ORFNames=Tmari_0775 {ECO:0000313|EMBL:AGL49700.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35856.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35856.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35856.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49700.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49700.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35856.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49700.1; -; Genomic_DNA. DR PIR; D72337; D72337. DR RefSeq; NP_228583.1; NC_000853.1. DR RefSeq; WP_004080915.1; NZ_CP011107.1. DR STRING; 243274.TM0774; -. DR EnsemblBacteria; AAD35856; AAD35856; TM_0774. DR EnsemblBacteria; AGL49700; AGL49700; Tmari_0775. DR GeneID; 898442; -. DR KEGG; tma:TM0774; -. DR KEGG; tmi:THEMA_00780; -. DR KEGG; tmm:Tmari_0775; -. DR KEGG; tmw:THMA_0793; -. DR PATRIC; 23936470; VBITheMar51294_0787. DR eggNOG; ENOG41084PC; Bacteria. DR eggNOG; COG1358; LUCA. DR OMA; IRCEINN; -. DR OrthoDB; EOG6N0HS0; -. DR BioCyc; TMAR243274:GC6P-801-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro. DR Gene3D; 3.30.1330.30; -; 1. DR InterPro; IPR029064; L30e-like. DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45. DR InterPro; IPR004037; Ribosomal_L7Ae_CS. DR Pfam; PF01248; Ribosomal_L7Ae; 1. DR SUPFAM; SSF55315; SSF55315; 1. DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Ribonucleoprotein {ECO:0000313|EMBL:AGL49700.1}; KW Ribosomal protein {ECO:0000313|EMBL:AGL49700.1}. FT DOMAIN 8 90 Ribosomal_L7Ae. FT {ECO:0000259|Pfam:PF01248}. SQ SEQUENCE 104 AA; 12190 MW; 905302E322202A29 CRC64; MEDQIRRKVY SYIGFAVRAR KIVFGKERIR AYIRSPREKK LIIIAEDTSE RMKRDTIMRC ENKKVPYVIM FSKEELGRLL DKPAVSVIGL EEDNLIDAIL GMVK // ID Q9X221_THEMA Unreviewed; 357 AA. AC Q9X221; G4FG82; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36762.1}; GN OrderedLocusNames=TM_1695 {ECO:0000313|EMBL:AAD36762.1}; GN ORFNames=Tmari_1703 {ECO:0000313|EMBL:AGL50627.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36762.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36762.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36762.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50627.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50627.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36762.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50627.1; -; Genomic_DNA. DR PIR; A72220; A72220. DR RefSeq; NP_229495.1; NC_000853.1. DR RefSeq; WP_004082211.1; NZ_CP011107.1. DR STRING; 243274.TM1695; -. DR EnsemblBacteria; AAD36762; AAD36762; TM_1695. DR EnsemblBacteria; AGL50627; AGL50627; Tmari_1703. DR GeneID; 897891; -. DR KEGG; tma:TM1695; -. DR KEGG; tmm:Tmari_1703; -. DR KEGG; tmw:THMA_1737; -. DR PATRIC; 23938364; VBITheMar51294_1712. DR eggNOG; ENOG4107TAA; Bacteria. DR eggNOG; COG0457; LUCA. DR OMA; NYAPAYE; -. DR OrthoDB; EOG696BTV; -. DR BioCyc; TMAR243274:GC6P-1743-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF13414; TPR_11; 1. DR SMART; SM00028; TPR; 4. DR SUPFAM; SSF48452; SSF48452; 2. DR PROSITE; PS50005; TPR; 6. DR PROSITE; PS50293; TPR_REGION; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 97 334 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 357 AA; 42044 MW; B445307A1AE13F9B CRC64; MAEHIITLVL SGERLDVTTS TPFVVALRDL LYEGDWELLK EDMKKKENIM KEVQTCEKLE KVVHLDETVY EPLIFPEFQE WLREENITPK DFKNVSLKGL YDLALEYADR NLYDIAHDII KFMLDIDENY APAYELKGSL LVEQGKIEEG IKFLDKAVEI DPWLVQAYAS LGEAYYNLGD YEKAIHYWER ELEYNPNDKI TYFMITEAYY EMNRKDLAVK TLERLLEIDP DNIPALYQLS QLYRELGNEE KAREMEEKIM NCKPKYPTEL EPWARVMLKH GRYKEVAEEL EKIVESSPLN TLARLLLVVP YVKLGQIDKA REILDDIGQS NFWYYYGKKE ILDELLTEEE KRACGIS // ID Q9WYC6_THEMA Unreviewed; 367 AA. AC Q9WYC6; G4FHK4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 106. DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369}; GN OrderedLocusNames=TM_0290 {ECO:0000313|EMBL:AAD35378.1}; GN ORFNames=Tmari_0288 {ECO:0000313|EMBL:AGL49214.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35378.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35378.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35378.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49214.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49214.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the citrate synthase family. CC {ECO:0000256|PIRNR:PIRNR001369}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35378.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49214.1; -; Genomic_DNA. DR PIR; B72394; B72394. DR RefSeq; NP_228102.1; NC_000853.1. DR RefSeq; WP_004083006.1; NZ_CP011107.1. DR PDB; 2P2W; X-ray; 1.90 A; A=1-367. DR PDBsum; 2P2W; -. DR STRING; 243274.TM0290; -. DR DNASU; 897210; -. DR EnsemblBacteria; AAD35378; AAD35378; TM_0290. DR EnsemblBacteria; AGL49214; AGL49214; Tmari_0288. DR GeneID; 897210; -. DR KEGG; tma:TM0290; -. DR KEGG; tmi:THEMA_03275; -. DR KEGG; tmm:Tmari_0288; -. DR KEGG; tmw:THMA_0297; -. DR PATRIC; 23935459; VBITheMar51294_0295. DR eggNOG; ENOG4105BZN; Bacteria. DR eggNOG; COG0372; LUCA. DR KO; K01647; -. DR OMA; DNRLLRP; -. DR OrthoDB; EOG6P8TP4; -. DR BioCyc; TMAR243274:GC6P-303-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0046912; F:transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 1.10.230.10; -; 1. DR Gene3D; 1.10.580.10; -; 1. DR InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II. DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub. DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub. DR InterPro; IPR002020; Citrate_synthase. DR InterPro; IPR019810; Citrate_synthase_AS. DR InterPro; IPR024176; Citrate_synthase_bac-typ. DR PANTHER; PTHR11739; PTHR11739; 1. DR Pfam; PF00285; Citrate_synt; 1. DR PIRSF; PIRSF001369; Citrate_synth; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR SUPFAM; SSF48256; SSF48256; 1. DR TIGRFAMs; TIGR01800; cit_synth_II; 1. DR PROSITE; PS00480; CITRATE_SYNTHASE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2P2W}; KW Acyltransferase {ECO:0000313|EMBL:AGL49214.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49214.1}. FT REGION 250 251 Citrate 2 binding. FT {ECO:0000213|PDB:2P2W}. FT ACT_SITE 250 250 {ECO:0000256|PIRSR:PIRSR001369-1}. FT ACT_SITE 300 300 {ECO:0000256|PIRSR:PIRSR001369-1}. FT BINDING 176 176 Citrate 1. {ECO:0000213|PDB:2P2W}. FT BINDING 211 211 Citrate 1; via carbonyl oxygen. FT {ECO:0000213|PDB:2P2W}. FT BINDING 244 244 Citrate 2. {ECO:0000213|PDB:2P2W}. FT BINDING 250 250 Citrate 1. {ECO:0000213|PDB:2P2W}. FT BINDING 259 259 Citrate 1. {ECO:0000213|PDB:2P2W}. FT BINDING 300 300 Citrate 1. {ECO:0000213|PDB:2P2W}. FT BINDING 325 325 Citrate 1. {ECO:0000213|PDB:2P2W}. FT BINDING 344 344 Citrate 1. {ECO:0000213|PDB:2P2W}. SQ SEQUENCE 367 AA; 42305 MW; C95CDAFC6D3D7D8F CRC64; MIQKGLEGVK ICESSICYLD GINGRLYYRG IPVEELAEKS TFEETAYFLW YGKLPTKSEL EEFKRKMADY RELPAEALGI LYHLPKNLHY IDVLKIFLSI HGSMDGNDED LREKAIRVAS VFPTILAYYY RYSKGKELIR PRKDLSHVEN FYYMMFGERN EKIRLLESAF ILLMEQDINA STFAALVIAS TLSDLYSCIV GALGALKGPL HGGASEKVPP MLEEIGSEDR VEEFVQKCLK EKRKIMGFGH RVYKTYDPRA VFLKRVLQEH FPDSKLFRIA SKLEEYIVSN KIKNIYPNVD LYSSVLFEEL GFPRNMFTAL FATARVVGWT AHVIEYVSDN KLIRPTSEYV GPMDVEYIPI ERRDENG // ID Q9WZ93_THEMA Unreviewed; 383 AA. AC Q9WZ93; G4FDJ8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35709.1}; GN OrderedLocusNames=TM_0625 {ECO:0000313|EMBL:AAD35709.1}; GN ORFNames=Tmari_0626 {ECO:0000313|EMBL:AGL49551.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35709.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35709.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35709.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49551.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49551.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35709.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49551.1; -; Genomic_DNA. DR PIR; F72352; F72352. DR RefSeq; NP_228434.1; NC_000853.1. DR RefSeq; WP_004081183.1; NZ_CP011107.1. DR STRING; 243274.TM0625; -. DR EnsemblBacteria; AAD35709; AAD35709; TM_0625. DR EnsemblBacteria; AGL49551; AGL49551; Tmari_0626. DR GeneID; 897712; -. DR KEGG; tma:TM0625; -. DR KEGG; tmi:THEMA_01535; -. DR KEGG; tmm:Tmari_0626; -. DR KEGG; tmw:THMA_0641; -. DR PATRIC; 23936163; VBITheMar51294_0635. DR BioCyc; TMAR243274:GC6P-650-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 383 AA; 45509 MW; CA3ADCB26D2E79C0 CRC64; MFRLEELNYP DTLKDFIKQI AKVLLSACGK ENVVVLLLTG SGGRGELTIL ETPGGYEILG DLEFIVISTK RLSILRKNIL KWIIEDKIRH FPFLSESFHV DFSIVNPEVL KEANTVLMWE TLTNSCILYG NLPFDNIQKQ HLGERKIRLK DIHNILLYRH YSVFWGIRKC KTHQCRFYSV IRNSLDLLTA ILYKNGIFIP SYRKRYDYLK KHSFEILPHW KKEDIENFVS FIGKCTFLKL EPLYESFIND QALYDMLEKY LFFSEMILLD FLKDFFKCNN KIECFNKFLN TRGFFEKGIN GFGFLKFFIW NIKNIPVSFL ARSFPIELLY ALMHIQLCEK ANYKSELLQE ISGKNITLDE KMIERIYKYY FPYAQHLKIN KRN // ID Q9X091_THEMA Unreviewed; 80 AA. AC Q9X091; G4FF00; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 88. DE SubName: Full=Redox-active disulfide protein 2 {ECO:0000313|EMBL:AGL49925.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36078.1}; GN OrderedLocusNames=TM_0996 {ECO:0000313|EMBL:AAD36078.1}; GN ORFNames=Tmari_1000 {ECO:0000313|EMBL:AGL49925.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36078.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36078.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36078.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49925.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49925.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36078.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49925.1; -; Genomic_DNA. DR PIR; F72306; F72306. DR RefSeq; NP_228804.1; NC_000853.1. DR RefSeq; WP_004080561.1; NZ_CP011107.1. DR STRING; 243274.TM0996; -. DR EnsemblBacteria; AAD36078; AAD36078; TM_0996. DR EnsemblBacteria; AGL49925; AGL49925; Tmari_1000. DR GeneID; 896982; -. DR KEGG; tma:TM0996; -. DR KEGG; tmi:THEMA_09370; -. DR KEGG; tmm:Tmari_1000; -. DR KEGG; tmw:THMA_1018; -. DR PATRIC; 23936923; VBITheMar51294_1010. DR eggNOG; ENOG4105VGV; Bacteria. DR eggNOG; COG0526; LUCA. DR OMA; GCAKCKT; -. DR OrthoDB; EOG6QVRMV; -. DR BioCyc; TMAR243274:GC6P-1026-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR005243; Redox_disulphide_2. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF13192; Thioredoxin_3; 1. DR PIRSF; PIRSF037031; Redox_disulphide_2; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR00412; redox_disulf_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 78 Thioredoxin. {ECO:0000259|Pfam:PF13192}. SQ SEQUENCE 80 AA; 8568 MW; CB9AB639E9665C6E CRC64; MAKKVEILGK GCPRCKQTEK IVRMAIEELG IDAVVEKVQD INEIVSRGVV ATPAVAVDGK VVISGKIPSL DEVKKVLQQA // ID Q9WZF2_THEMA Unreviewed; 478 AA. AC Q9WZF2; G4FDD8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 103. DE SubName: Full=DNA polymerase III subunits gamma and tau {ECO:0000313|EMBL:AGL49611.1}; DE EC=2.7.7.7 {ECO:0000313|EMBL:AGL49611.1}; DE SubName: Full=DNA polymerase III, gamma and tau subunit {ECO:0000313|EMBL:AAD35768.1}; GN OrderedLocusNames=TM_0686 {ECO:0000313|EMBL:AAD35768.1}; GN ORFNames=Tmari_0686 {ECO:0000313|EMBL:AGL49611.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35768.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35768.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35768.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49611.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49611.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35768.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49611.1; -; Genomic_DNA. DR PIR; D72344; D72344. DR RefSeq; NP_228495.1; NC_000853.1. DR RefSeq; WP_004081077.1; NZ_CP011107.1. DR STRING; 243274.TM0686; -. DR EnsemblBacteria; AAD35768; AAD35768; TM_0686. DR EnsemblBacteria; AGL49611; AGL49611; Tmari_0686. DR GeneID; 898353; -. DR KEGG; tma:TM0686; -. DR KEGG; tmi:THEMA_01235; -. DR KEGG; tmm:Tmari_0686; -. DR KEGG; tmw:THMA_0701; -. DR PATRIC; 23936290; VBITheMar51294_0698. DR eggNOG; ENOG4105C6E; Bacteria. DR eggNOG; COG2812; LUCA. DR KO; K02343; -. DR OMA; HHCAAND; -. DR OrthoDB; EOG6WQD76; -. DR BioCyc; TMAR243274:GC6P-712-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0006261; P:DNA-dependent DNA replication; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR012763; DNA_pol_III_sug/sutau. DR InterPro; IPR027417; P-loop_NTPase. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF48019; SSF48019; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02397; dnaX_nterm; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AGL49611.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49611.1}. FT DOMAIN 35 177 AAA. {ECO:0000259|SMART:SM00382}. FT COILED 358 391 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 478 AA; 54817 MW; F26C584E01971690 CRC64; MEVLYRKYRP KTFSEVVNQD HVKKAIIGAI QKNSVAHGYI FAGPRGTGKT TLARILAKSL NCENRKGVEP CNSCRACREI DEGTFMDVIE LDAASNRGID EIRRIRDAVG YRPMEGKYKV YIIDEVHMLT KEAFNALLKT LEEPPSHVVF VLATTNLEKV PPTIISRCQV FEFRNIPDEL IEKRLQEVAE AEGIEIDREA LSFIAKRASG GLRDALTMLE QVWKFSEGKI DLETVHRALG LIPIQVVRDY VNAIFSGDVK RVFTVLDDVY YSGKDYEVLI QEAVEDLVED LERERGVYQV SANDIVQVSR QLLNLLREIK FAEEKRLVCK VGSAYIATRF STTNVQENDV REKNDNSNVQ QKEEKKETVK AKEEKQEDSE FEKRFKELME ELKEKGDLSI FVALSLSEVQ FDGEKVIISF DSSKAMHYEL MKKKLPELEN IFSRKLGKKV EVELRLMGKE ETIEKVSQKI LRLFEQEG // ID Q9X0I4_THEMA Unreviewed; 366 AA. AC Q9X0I4; G4FEP8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36176.1}; GN OrderedLocusNames=TM_1100 {ECO:0000313|EMBL:AAD36176.1}; GN ORFNames=Tmari_1106 {ECO:0000313|EMBL:AGL50030.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36176.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36176.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36176.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50030.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50030.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36176.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50030.1; -; Genomic_DNA. DR PIR; F72294; F72294. DR RefSeq; NP_228906.1; NC_000853.1. DR RefSeq; WP_004080339.1; NZ_CP011107.1. DR STRING; 243274.TM1100; -. DR EnsemblBacteria; AAD36176; AAD36176; TM_1100. DR EnsemblBacteria; AGL50030; AGL50030; Tmari_1106. DR GeneID; 898665; -. DR KEGG; tma:TM1100; -. DR KEGG; tmi:THEMA_08845; -. DR KEGG; tmm:Tmari_1106; -. DR KEGG; tmw:THMA_1123; -. DR PATRIC; 23937133; VBITheMar51294_1115. DR eggNOG; ENOG41082KH; Bacteria. DR eggNOG; COG0842; LUCA. DR KO; K01992; -. DR OMA; RIAMSTP; -. DR OrthoDB; EOG6SJJG1; -. DR BioCyc; TMAR243274:GC6P-1129-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 175 199 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 224 246 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 252 273 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 285 304 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 341 363 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 366 AA; 41094 MW; FA6B66611AD93004 CRC64; MFRIAIVELK RILKKRSSLM MIIAAPVLVV LISLLFMQGY NLQTMKLGIY NEDNSIWSSL VMRFIGTILR QENIVKVDQN YEKLLKEGKL NAVIVIPKGF AAKLYSKQPT QMIFIPSPID LHLAAAIYNV LDSVLADFQG SAFFDPKVLR YIFTESDYPV PRLKLKDSEL RFSDLISPFV VFFTAILITV SLASVSTFLD REKNLHEMFL VYNLPAWKYA CGKILAYTII GASVSFIAYS LTVILTGDSL DFFITSVLIL LNALLHTSVG FLVSSISPDK SLANILGVSV IGISLFSSGF AIPISNLPDI FRRIAMSTPV FRTMYALRVY QLEHTVDNRS IFVVLLWTVV LFSISILSGK FVIRRG // ID Q9WYB6_THEMA Unreviewed; 620 AA. AC Q9WYB6; G4FHJ4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Secreted protein {ECO:0000313|EMBL:AGL49204.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35368.1}; GN OrderedLocusNames=TM_0280 {ECO:0000313|EMBL:AAD35368.1}; GN ORFNames=Tmari_0278 {ECO:0000313|EMBL:AGL49204.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35368.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35368.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35368.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49204.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49204.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35368.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49204.1; -; Genomic_DNA. DR PIR; F72395; F72395. DR RefSeq; NP_228092.1; NC_000853.1. DR RefSeq; WP_004082989.1; NZ_CP011107.1. DR STRING; 243274.TM0280; -. DR EnsemblBacteria; AAD35368; AAD35368; TM_0280. DR EnsemblBacteria; AGL49204; AGL49204; Tmari_0278. DR GeneID; 897197; -. DR KEGG; tma:TM0280; -. DR KEGG; tmi:THEMA_03325; -. DR KEGG; tmm:Tmari_0278; -. DR KEGG; tmw:THMA_0287; -. DR PATRIC; 23935439; VBITheMar51294_0285. DR eggNOG; ENOG4105DQC; Bacteria. DR eggNOG; COG3533; LUCA. DR KO; K09955; -. DR OMA; LYCAGHM; -. DR OrthoDB; EOG6TR0C2; -. DR BioCyc; TMAR243274:GC6P-293-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 1.50.10.10; -; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase-like. DR InterPro; IPR012341; 6hp_glycosidase. DR InterPro; IPR012878; Glyco_hydro_127. DR Pfam; PF07944; Glyco_hydro_127; 1. DR SUPFAM; SSF48208; SSF48208; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 620 AA; 70954 MW; 3DBA6F1FE3B9C70F CRC64; MSKIVEVSKS PYAKLKTIPV GSVRVNGFMG KYFETLVNVT LPTQYDLLEN TGRLDNFRIA AGKMEGSYKT LFPFDDTDVY KWAETVSFAL ANRKLPELEK ILDSVIEEVK AAQDEDGYLG TYLSGDRKKE RWTNLAWNHE LYNAGHLIQA AVAHRRVTGK NTLFEVAKRF ADHIYNTFGP EKKEGAPGHP EVEMALVELY RETGDRKYLD LARYFIYARG KGLASVPRNP GPEYFIDHKP FVELEEITGH AVRALYLCSG ATDLYLETGD EKIWQALNRL WENFVTKKMY ITGGAGSRHD WESFGEEYEL PNRRSYAESC ASIANFMWNF RMLLATGDGK FADVMEQVLY NGLLSGISLD GKHYFYFNPL EDYGRTRRQK WFDCACCPPN LARFIVSFPG YMYTTSDDGV QVHLYEKSTA RLDFKGSVVE IEQETDYPWS GEVAFTIKTD IEEPFSIYLR LPSWADDFVL RVDGKAVIAK PQNGYVKLSQ SWKGKHTVEL SLPMKAVFIE AHPFVRDDLG KAAVKRGPVV YCIEQADNPD FHVWTLVLNS ESLKEEKGKI LDREAVFLKG TGRALDISEW EGKLYRKLSE VREKTVEFTL IPYHMWANRE PGAMAVWLKR // ID Q9WZW6_THEMA Unreviewed; 355 AA. AC Q9WZW6; G4FCW2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000313|EMBL:AAD35944.1}; DE EC=2.7.7.24 {ECO:0000313|EMBL:AGL49789.1}; GN OrderedLocusNames=TM_0862 {ECO:0000313|EMBL:AAD35944.1}; GN ORFNames=Tmari_0864 {ECO:0000313|EMBL:AGL49789.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35944.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35944.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35944.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49789.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49789.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35944.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49789.1; -; Genomic_DNA. DR PIR; G72325; G72325. DR RefSeq; NP_228671.1; NC_000853.1. DR RefSeq; WP_004080744.1; NZ_CP011107.1. DR STRING; 243274.TM0862; -. DR EnsemblBacteria; AAD35944; AAD35944; TM_0862. DR EnsemblBacteria; AGL49789; AGL49789; Tmari_0864. DR GeneID; 898535; -. DR KEGG; tma:TM0862; -. DR KEGG; tmi:THEMA_00325; -. DR KEGG; tmm:Tmari_0864; -. DR KEGG; tmw:THMA_0884; -. DR PATRIC; 23936652; VBITheMar51294_0875. DR eggNOG; ENOG4108I19; Bacteria. DR eggNOG; COG1209; LUCA. DR KO; K00973; -. DR OMA; CISHDYP; -. DR OrthoDB; EOG6RC3RN; -. DR BioCyc; TMAR243274:GC6P-892-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR005908; G1P_thy_trans_l. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00132; Hexapep; 1. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR01208; rmlA_long; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AGL49789.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49789.1}. FT DOMAIN 3 236 NTP_transferase. FT {ECO:0000259|Pfam:PF00483}. SQ SEQUENCE 355 AA; 39339 MW; 6219354995ED8BF0 CRC64; MKKAIVLCAG KGTRLRPLTF TTAKHLIPIA NKPILFYSLE NIARAGIEEV GIVVSPHNAE EFKSIVGTGE NFGLRISYII QEEPKGLAHA VWVSREFLGD EDFMMYLGDN LILEDLGKFV KDFENSDYAA SILLSPVKDP TRFGVAVMEG DRVIKVVEKP KTPPSNLAIV GLYLFRNKIF EGIKNIKPSW RGELEITDAI EYLIEKGEKV RGYIVYGWWK DTGKPEDLLE ANRKILMETT EELLGEMDDK SSIQGPVRIG KASKIVNSVI RGPAVIGENC FIKNSYVGPY SSIGNRVILE DCEVENSIVM DECSITGVEK RIDSSILGKG VSVKGSQKRP ASLNLILGNM SRVEL // ID Q9WYD7_THEMA Unreviewed; 334 AA. AC Q9WYD7; G4FHL5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 90. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35389.1}; DE SubName: Full=Xyloglucan ABC transport system, permease protein 1 {ECO:0000313|EMBL:AGL49225.1}; GN OrderedLocusNames=TM_0301 {ECO:0000313|EMBL:AAD35389.1}; GN ORFNames=Tmari_0299 {ECO:0000313|EMBL:AGL49225.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35389.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35389.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35389.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49225.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49225.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35389.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49225.1; -; Genomic_DNA. DR PIR; B72393; B72393. DR RefSeq; NP_228113.1; NC_000853.1. DR RefSeq; WP_004083023.1; NZ_CP011107.1. DR STRING; 243274.TM0301; -. DR TCDB; 3.A.1.5.30; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35389; AAD35389; TM_0301. DR EnsemblBacteria; AGL49225; AGL49225; Tmari_0299. DR GeneID; 897226; -. DR KEGG; tma:TM0301; -. DR KEGG; tmi:THEMA_03220; -. DR KEGG; tmm:Tmari_0299; -. DR KEGG; tmw:THMA_0308; -. DR PATRIC; 23935481; VBITheMar51294_0306. DR eggNOG; COG0601; LUCA. DR HOGENOM; HOG000170250; -. DR KO; K02033; -. DR OMA; GWILSMR; -. DR OrthoDB; EOG66F098; -. DR BioCyc; TMAR243274:GC6P-314-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 29 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 112 136 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 157 177 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 197 218 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 260 281 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 301 324 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 108 320 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 334 AA; 37490 MW; 75C8B068BE5467C8 CRC64; MKFIKSYLIP RLIQYVYMVV IGITLVFLIP RLSPVDPIEQ ILNTRLRIQN TTPEAVIKMR EVMEELYGLK GTLWEQYVNL WKRLLKGDFG PSMVYYPASV ISLIRNSLPW TIGLLTLTTL ISWVLGLVIG AILGYYKESF GSKILTGILM AINPIPYYIF ALTLLLLFCY VFPIFPLGGG FSVGQKISLS WSFILDVIKH GTLPALSLII LGFAGWGLGT KILVQNLREE DYVVYARMMG LRNSKILFSY VLRNAMLPQV TGLGLSLGGI FGGAMMTEIL FTYPGIGTLA YNAVRANDYN VMIAISFFSI IAVATALLIL DLLYPLIDPR IRYR // ID Q9X162_THEMA Unreviewed; 321 AA. AC Q9X162; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Oxidase-related protein {ECO:0000313|EMBL:AAD36412.1}; DE SubName: Full=Rieske (2Fe-2S) domain protein {ECO:0000313|EMBL:AGL50271.1}; GN OrderedLocusNames=TM_1340 {ECO:0000313|EMBL:AAD36412.1}; GN ORFNames=Tmari_1347 {ECO:0000313|EMBL:AGL50271.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36412.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36412.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36412.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50271.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50271.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 Rieske domain. CC {ECO:0000256|RuleBase:RU004493}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36412.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50271.1; -; Genomic_DNA. DR PIR; D72266; D72266. DR RefSeq; NP_229142.1; NC_000853.1. DR RefSeq; WP_010865320.1; NC_000853.1. DR STRING; 243274.TM1340; -. DR EnsemblBacteria; AAD36412; AAD36412; TM_1340. DR EnsemblBacteria; AGL50271; AGL50271; Tmari_1347. DR GeneID; 898142; -. DR KEGG; tma:TM1340; -. DR KEGG; tmi:THEMA_07645; -. DR KEGG; tmm:Tmari_1347; -. DR PATRIC; 23937611; VBITheMar51294_1351. DR eggNOG; ENOG4108KUH; Bacteria. DR eggNOG; COG4638; LUCA. DR OMA; SEYSEVW; -. DR OrthoDB; EOG6DNT94; -. DR BioCyc; TMAR243274:GC6P-1371-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR Gene3D; 2.102.10.10; -; 1. DR InterPro; IPR017941; Rieske_2Fe-2S. DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS. DR Pfam; PF00355; Rieske; 1. DR SUPFAM; SSF50022; SSF50022; 1. DR PROSITE; PS51296; RIESKE; 1. DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1. PE 4: Predicted; KW 2Fe-2S {ECO:0000256|RuleBase:RU004492}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|RuleBase:RU004492}; KW Iron-sulfur {ECO:0000256|RuleBase:RU004492}; KW Metal-binding {ECO:0000256|RuleBase:RU004492}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 106 Rieske. {ECO:0000259|PROSITE:PS51296}. SQ SEQUENCE 321 AA; 38015 MW; F5301ABFA915FAE7 CRC64; MWFAVLSSNE VRRKPVGVRR LGRDLVFWRD SLGKVYALED FCVHRRARLS AGKVINDRIQ CPFHGFEYDG NGRVRLIPAL GKNYKVPDRF RVNSYPVYEK NNIIWLWSGE GEPEKEPKFF DDIDEDFAYA EFRELWNVPF PRAVENQLDV MHLPFVHRTT IGRGNRTLVH GPVVKWIDED SFIFYVFNEV DRGQRVKRPE ELSGEESRVY LEFIFPNLWQ NHISEGTRVV AFFVPVDRQK TMIYLRFYVK MTGLKPVDSI IARLSMPLNR IILHQDRRVV ETQERDIRKD VLVQGDLPIM EFRKRLYKEK KLIDFLFGGG Q // ID Q9WZN8_THEMA Unreviewed; 71 AA. AC Q9WZN8; G4FD42; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35863.1}; GN OrderedLocusNames=TM_0781 {ECO:0000313|EMBL:AAD35863.1}; GN ORFNames=Tmari_0782 {ECO:0000313|EMBL:AGL49707.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35863.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35863.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35863.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49707.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49707.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35863.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49707.1; -; Genomic_DNA. DR PIR; F72332; F72332. DR RefSeq; NP_228590.1; NC_000853.1. DR RefSeq; WP_004080906.1; NZ_CP011107.1. DR STRING; 243274.TM0781; -. DR EnsemblBacteria; AAD35863; AAD35863; TM_0781. DR EnsemblBacteria; AGL49707; AGL49707; Tmari_0782. DR GeneID; 898449; -. DR KEGG; tma:TM0781; -. DR KEGG; tmi:THEMA_00745; -. DR KEGG; tmm:Tmari_0782; -. DR KEGG; tmw:THMA_0800; -. DR PATRIC; 23936484; VBITheMar51294_0794. DR eggNOG; ENOG4106HNW; Bacteria. DR eggNOG; ENOG410Y1ZQ; LUCA. DR OMA; MRVERIG; -. DR OrthoDB; EOG6W45X6; -. DR BioCyc; TMAR243274:GC6P-808-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 71 AA; 7994 MW; 1C623FFDF3906808 CRC64; MRVEGIGYNP VYQSYAQQRT TPVSTAGSSP VMTKEQMEQI LFFSLYQQTG LNVKLVRIAG ELYGKMMDQL A // ID Q9X1C4_THEMA Unreviewed; 256 AA. AC Q9X1C4; G4FFE0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE RecName: Full=Transport permease protein {ECO:0000256|RuleBase:RU361157}; GN OrderedLocusNames=TM_1404 {ECO:0000313|EMBL:AAD36475.1}; GN ORFNames=Tmari_1411 {ECO:0000313|EMBL:AGL50335.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36475.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36475.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36475.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50335.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50335.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU361157}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU361157}. CC -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family. CC {ECO:0000256|RuleBase:RU361157}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-2 domain. CC {ECO:0000256|RuleBase:RU361157}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36475.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50335.1; -; Genomic_DNA. DR PIR; E72257; E72257. DR RefSeq; NP_229205.1; NC_000853.1. DR RefSeq; WP_004081633.1; NZ_CP011107.1. DR STRING; 243274.TM1404; -. DR DNASU; 898072; -. DR EnsemblBacteria; AAD36475; AAD36475; TM_1404. DR EnsemblBacteria; AGL50335; AGL50335; Tmari_1411. DR GeneID; 898072; -. DR KEGG; tma:TM1404; -. DR KEGG; tmi:THEMA_07295; -. DR KEGG; tmm:Tmari_1411; -. DR KEGG; tmw:THMA_1433; -. DR PATRIC; 23937754; VBITheMar51294_1416. DR eggNOG; ENOG4105F7Z; Bacteria. DR eggNOG; COG0842; LUCA. DR KO; K01992; -. DR OMA; LIWDKQF; -. DR OrthoDB; EOG65J51T; -. DR BioCyc; TMAR243274:GC6P-1441-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR InterPro; IPR013525; ABC_2_trans. DR InterPro; IPR000412; ABC_2_transport. DR InterPro; IPR005942; Daunbcin-R_ABC-transpt. DR Pfam; PF01061; ABC2_membrane; 1. DR PIRSF; PIRSF006648; DrrB; 1. DR PRINTS; PR00164; ABC2TRNSPORT. DR TIGRFAMs; TIGR01247; drrB; 1. DR PROSITE; PS51012; ABC_TM2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU361157}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU361157}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU361157}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361157}; KW Transport {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 21 41 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 61 84 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 105 130 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 136 160 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 172 191 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 232 250 Helical. {ECO:0000256|RuleBase:RU361157}. FT DOMAIN 4 217 ABC2_membrane. FT {ECO:0000259|Pfam:PF01061}. SQ SEQUENCE 256 AA; 28665 MW; 7A4860D118AAC0ED CRC64; MAAFVTMIYR QFMRFLRSRS RVIGMIINPL IWIIFFGLGW SKVFDNPWAK MMFGGVDYLT YLAPGIFAMT VFNMSFISGV SLIWDKQFGF FKEVLVAPSS RRLSITGRIV GDAIVTVLQG LIILVFNYFL AESLKISGLL PALAVGFLMS VTIASFGIAL ALKMESTEGF QMIMMTLMMP LVFLSGAMYP IDSMPNWMKA LAYINPLTYA VDASRGYLVG EKVMKFSFGL DWGILSILML VGLILAMESF ERARIS // ID Q9X0E3_THEMA Unreviewed; 159 AA. AC Q9X0E3; G4FEU5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 87. DE SubName: Full=Cationic outer membrane protein {ECO:0000313|EMBL:AAD36130.1}; DE SubName: Full=Outer membrane protein H {ECO:0000313|EMBL:AGL49981.1}; GN OrderedLocusNames=TM_1053 {ECO:0000313|EMBL:AAD36130.1}; GN ORFNames=Tmari_1057 {ECO:0000313|EMBL:AGL49981.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36130.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36130.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36130.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49981.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49981.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36130.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49981.1; -; Genomic_DNA. DR PIR; G72301; G72301. DR RefSeq; NP_228859.1; NC_000853.1. DR RefSeq; WP_004080454.1; NZ_CP011107.1. DR STRING; 243274.TM1053; -. DR EnsemblBacteria; AAD36130; AAD36130; TM_1053. DR EnsemblBacteria; AGL49981; AGL49981; Tmari_1057. DR GeneID; 898715; -. DR KEGG; tma:TM1053; -. DR KEGG; tmi:THEMA_09095; -. DR KEGG; tmm:Tmari_1057; -. DR KEGG; tmw:THMA_1075; -. DR PATRIC; 23937035; VBITheMar51294_1066. DR eggNOG; ENOG4106088; Bacteria. DR eggNOG; COG2825; LUCA. DR KO; K06142; -. DR OMA; NSKYDIT; -. DR OrthoDB; EOG63NMKZ; -. DR BioCyc; TMAR243274:GC6P-1082-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR005632; Chaperone_Skp. DR InterPro; IPR024930; Skp_domain. DR Pfam; PF03938; OmpH; 1. DR SMART; SM00935; OmpH; 1. DR SUPFAM; SSF111384; SSF111384; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 159 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972310. FT COILED 50 104 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 159 AA; 18597 MW; 9AF1CF80F2A5D750 CRC64; MKKLLLPLVL AGVLLATLLV SQSSSSPSLR VAYVDVEKAT ESYYKWQDLN EKYKRDYSFY QNKLKEMEDE LKKMQEEGRS QEEIQAKQKE ILSKKAEYEN LLKTEYQQKI QEVMKEVVSK IQEYASVMGY DLVIAKQMVL YGKPSYDITD QVIAYINQK // ID Q9X2F9_THEMA Unreviewed; 380 AA. AC Q9X2F9; G4FGM8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36905.1}; GN OrderedLocusNames=TM_1843 {ECO:0000313|EMBL:AAD36905.1}; GN ORFNames=Tmari_1851 {ECO:0000313|EMBL:AGL50775.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36905.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36905.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36905.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50775.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50775.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36905.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50775.1; -; Genomic_DNA. DR PIR; F72204; F72204. DR RefSeq; NP_229639.1; NC_000853.1. DR RefSeq; WP_004082387.1; NZ_CP011107.1. DR STRING; 243274.TM1843; -. DR DNASU; 897813; -. DR EnsemblBacteria; AAD36905; AAD36905; TM_1843. DR EnsemblBacteria; AGL50775; AGL50775; Tmari_1851. DR GeneID; 897813; -. DR KEGG; tma:TM1843; -. DR KEGG; tmi:THEMA_04990; -. DR KEGG; tmm:Tmari_1851; -. DR KEGG; tmw:THMA_1886; -. DR PATRIC; 23938675; VBITheMar51294_1864. DR eggNOG; ENOG4106VP5; Bacteria. DR eggNOG; ENOG410YQ3N; LUCA. DR OMA; ETHLDYC; -. DR OrthoDB; EOG6TXQSR; -. DR BioCyc; TMAR243274:GC6P-1894-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 380 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972273. SQ SEQUENCE 380 AA; 43703 MW; 240BA357056F9CF9 CRC64; MKKLAVLIMC LLAFSYVFSF SPTGSLKVGY SYDLENQSGS SYTELYLSGN SLSGDFTTKD LKLDSGYIAL DTDLVDLKAY YNRVFGSTGD WLGIYSFNDS RNGLEIELFG FRGVTTGDVS YLQYRGNLSN FYFSAMLGKR STVNDMYFDF NWEPGLRYFG EFGVSYENEE KIGSNNFFYM FGISTADWKH GVKLTGVGSE TYLDYCDYVN DNDLEGEILA NLWTTFGDFK LWFDYKFTSK TPKYGVEYSS GDVWFKAWKE GTKFDSDILN WDDFGMEIGK NFSFIGFNGK ISYKFGKPAH DSTSAMGEVF YAELWKNFGS VNFFAKWQYL NTLYTEAYTA YYELKFTDEK SEFKLSLGDG DFSSQINFVK KISLEYSTWW // ID Q9WXX1_THEMA Unreviewed; 492 AA. AC Q9WXX1; G4FH31; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 101. DE SubName: Full=Sugar kinase, FGGY family {ECO:0000313|EMBL:AAD35210.1}; DE SubName: Full=Xylulose kinase {ECO:0000313|EMBL:AGL49039.1}; DE EC=2.7.1.17 {ECO:0000313|EMBL:AGL49039.1}; GN OrderedLocusNames=TM_0116 {ECO:0000313|EMBL:AAD35210.1}; GN ORFNames=Tmari_0113 {ECO:0000313|EMBL:AGL49039.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35210.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35210.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35210.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49039.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49039.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the FGGY kinase family. CC {ECO:0000256|RuleBase:RU003733}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35210.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49039.1; -; Genomic_DNA. DR PIR; C72417; C72417. DR RefSeq; NP_227932.1; NC_000853.1. DR RefSeq; WP_004082695.1; NZ_CP011107.1. DR STRING; 243274.TM0116; -. DR EnsemblBacteria; AAD35210; AAD35210; TM_0116. DR EnsemblBacteria; AGL49039; AGL49039; Tmari_0113. DR GeneID; 896943; -. DR KEGG; tma:TM0116; -. DR KEGG; tmi:THEMA_04225; -. DR KEGG; tmm:Tmari_0113; -. DR KEGG; tmw:THMA_0112; -. DR PATRIC; 23935072; VBITheMar51294_0114. DR eggNOG; ENOG4105CMG; Bacteria. DR eggNOG; COG1070; LUCA. DR KO; K00854; -. DR OMA; VIFAHSD; -. DR OrthoDB; EOG6S52KR; -. DR BioCyc; TMAR243274:GC6P-116-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central. DR GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR GO; GO:0005997; P:xylulose metabolic process; IEA:InterPro. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR InterPro; IPR006000; Xylulokinase. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR TIGRFAMs; TIGR01312; XylB; 1. DR PROSITE; PS00933; FGGY_KINASES_1; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000256|SAAS:SAAS00430777, KW ECO:0000313|EMBL:AAD35210.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU003733, KW ECO:0000256|SAAS:SAAS00430777, ECO:0000313|EMBL:AAD35210.1}. FT DOMAIN 3 248 FGGY_N. {ECO:0000259|Pfam:PF00370}. FT DOMAIN 258 440 FGGY_C. {ECO:0000259|Pfam:PF02782}. SQ SEQUENCE 492 AA; 54405 MW; 0F66A3AB451D88E1 CRC64; MNLYVGLDVG TTGVKGILVN EKGEILATAN ERLTMFTPQP AWAEQDPLSW WEAVKKILKN LSERSKEMGG KIRAISTSGQ MHSLVAIDDN GKVLRNAILW CDQRTYKECE EATQILGGEE NVLKLVGNPI LPGFTLPKIL WIRKHEPEIY GKISKIMLPK DFINYMLTGE VKTEHSDASG TVMYSVSKME WNKDVLKELN IPESVLPEII PSNGVVGNVK PEVASDLGLS EDTLVIGGGA DNACAALGIA VVEPGDVMVS LGTSGTVLAP TKGNQPDPKG RVHFFAHTVP ETRYHMGVML SATYSLEWFK EKFLSEDYET INEEVDKIPA GSNGIIFLPY LNGERTPHRD PFARGVFFGI SSYNTKWDMV RAIFEGVAFG IKDSFDILRE LKVVLNSVRI TGGGSKSRVW NKMLADMTGL RIQKPAVDEG ASYGAAILAV SGSMGENPAK ISKEWFRVKS YTDPAVENTE TYEKLHEKFK KLYTSLKEMF RS // ID Q9X0W6_THEMA Unreviewed; 122 AA. AC Q9X0W6; G4FEA8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36314.1}; GN OrderedLocusNames=TM_1239 {ECO:0000313|EMBL:AAD36314.1}; GN ORFNames=Tmari_1245 {ECO:0000313|EMBL:AGL50169.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36314.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36314.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36314.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50169.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50169.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36314.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50169.1; -; Genomic_DNA. DR PIR; H72279; H72279. DR RefSeq; NP_229044.1; NC_000853.1. DR RefSeq; WP_004080035.1; NZ_CP011107.1. DR STRING; 243274.TM1239; -. DR EnsemblBacteria; AAD36314; AAD36314; TM_1239. DR EnsemblBacteria; AGL50169; AGL50169; Tmari_1245. DR GeneID; 898245; -. DR KEGG; tma:TM1239; -. DR KEGG; tmi:THEMA_08140; -. DR KEGG; tmm:Tmari_1245; -. DR KEGG; tmw:THMA_1264; -. DR PATRIC; 23937418; VBITheMar51294_1256. DR eggNOG; ENOG41089Y9; Bacteria. DR eggNOG; COG1963; LUCA. DR KO; K09775; -. DR OMA; MPSAHVA; -. DR OrthoDB; EOG6CCH6S; -. DR BioCyc; TMAR243274:GC6P-1269-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003832; AP_V-HP-rel. DR Pfam; PF02681; DUF212; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 68 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 116 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 122 AA; 13467 MW; 97D570D607ED4AAC CRC64; MLDVWKIFRS TPFTTAVISF LTAQFIKFLI KRDVKMLKSY GGMPSGHVAT VSGLAWSLAR STGFDSPYTS IAAIFLVIIF MDAIVLRPAV KKDLGHNFLE ALAGLGLGML IAHIFPARLH LW // ID Q9WZP0_THEMA Unreviewed; 33 AA. AC Q9WZP0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35865.1}; GN OrderedLocusNames=TM_0783 {ECO:0000313|EMBL:AAD35865.1}; GN ORFNames=Tmari_0784 {ECO:0000313|EMBL:AGL49709.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35865.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35865.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35865.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49709.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49709.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35865.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49709.1; -; Genomic_DNA. DR PIR; H72332; H72332. DR RefSeq; NP_228592.1; NC_000853.1. DR RefSeq; WP_010865202.1; NZ_CP011107.1. DR STRING; 243274.TM0783; -. DR EnsemblBacteria; AAD35865; AAD35865; TM_0783. DR EnsemblBacteria; AGL49709; AGL49709; Tmari_0784. DR GeneID; 898451; -. DR KEGG; tma:TM0783; -. DR KEGG; tmi:THEMA_00735; -. DR KEGG; tmm:Tmari_0784; -. DR KEGG; tmw:THMA_0802; -. DR BioCyc; TMAR243274:GC6P-810-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 33 AA; 3662 MW; CF2A02B6C317B8FD CRC64; MDSFVLFEQG ILSDMIMCTT IKSRPLEGPG VFV // ID Q9X227_THEMA Unreviewed; 458 AA. AC Q9X227; G4FG88; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Multi antimicrobial extrusion protein (Na(+)/drug antiporter), MATE family of MDR efflux pumps {ECO:0000313|EMBL:AGL50633.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36768.1}; GN OrderedLocusNames=TM_1701 {ECO:0000313|EMBL:AAD36768.1}; GN ORFNames=Tmari_1709 {ECO:0000313|EMBL:AGL50633.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36768.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36768.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36768.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50633.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50633.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36768.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50633.1; -; Genomic_DNA. DR PIR; G72220; G72220. DR RefSeq; NP_229501.1; NC_000853.1. DR RefSeq; WP_004082217.1; NZ_CP011107.1. DR STRING; 243274.TM1701; -. DR EnsemblBacteria; AAD36768; AAD36768; TM_1701. DR EnsemblBacteria; AGL50633; AGL50633; Tmari_1709. DR GeneID; 897888; -. DR KEGG; tma:TM1701; -. DR KEGG; tmm:Tmari_1709; -. DR KEGG; tmw:THMA_1743; -. DR PATRIC; 23938376; VBITheMar51294_1718. DR eggNOG; ENOG4105C3S; Bacteria. DR eggNOG; COG0534; LUCA. DR OMA; NTIGYYV; -. DR OrthoDB; EOG6PZX7B; -. DR BioCyc; TMAR243274:GC6P-1749-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015297; F:antiporter activity; IEA:InterPro. DR GO; GO:0015238; F:drug transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0006855; P:drug transmembrane transport; IBA:GO_Central. DR InterPro; IPR002528; MATE_fam. DR Pfam; PF01554; MatE; 2. DR PIRSF; PIRSF006603; DinF; 1. DR TIGRFAMs; TIGR00797; matE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 41 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 76 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 97 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 140 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 193 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 199 219 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 240 264 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 284 307 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 319 343 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 363 382 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 458 AA; 49858 MW; 7C7E7D07F7DD4543 CRC64; MVLERETIGI KLLRGDPRKA IVKLSIPMML AMLVQTIYNL ADGIWVAGLG PYALAAIGLF FPVFMVIISL AAGIGVGASS VVSQKIGERD KEGADTAASV SILLSIVIGF LSIAVILPFI SDILIFAGAQ GETLRLALEY SVILVYFIPL IMFNNVANGV FRGEGDAKRA MVAITIGSLL NIGLDPVFIY VFGMGIRGAA YATVVSIAVS SLLIAYWMFF KKDTYVSFRL KWDGEILKRI LKIGIPASLA QISMSVAIYV LNVFAVRSGG DYGVAVFTSA WRVINFGTVP LIGMAMAVTS VTGAAFGERN GEKLETAHLY AVKLGFFVGL AVMFTILIFA PYIARLFTYS QEGEKLYSDL VKALRILSLF LPGVPFGMFT SSMFQGVGQG LKSLIVTIMR TVIMQVVFSW LFVFVLRIGL VGVWWGIVLG NTTSAFITFN WGRFTVKHLK RDFQKNIT // ID Q9X258_THEMA Unreviewed; 451 AA. AC Q9X258; G4FGC2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 118. DE RecName: Full=Replicative DNA helicase {ECO:0000256|RuleBase:RU362085}; DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU362085}; GN OrderedLocusNames=TM_1736 {ECO:0000313|EMBL:AAD36801.1}; GN ORFNames=Tmari_1744 {ECO:0000313|EMBL:AGL50668.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36801.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36801.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36801.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50668.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50668.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Participates in initiation and elongation during CC chromosome replication; it exhibits DNA-dependent ATPase activity. CC {ECO:0000256|RuleBase:RU362085}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|RuleBase:RU362085}. CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily. CC {ECO:0000256|RuleBase:RU362085}. CC -!- SIMILARITY: Contains 1 SF4 helicase domain. CC {ECO:0000256|RuleBase:RU362085}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36801.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50668.1; -; Genomic_DNA. DR PIR; G72217; G72217. DR RefSeq; NP_229534.1; NC_000853.1. DR RefSeq; WP_004082256.1; NZ_CP011107.1. DR STRING; 243274.TM1736; -. DR EnsemblBacteria; AAD36801; AAD36801; TM_1736. DR EnsemblBacteria; AGL50668; AGL50668; Tmari_1744. DR GeneID; 897724; -. DR KEGG; tma:TM1736; -. DR KEGG; tmi:THEMA_05555; -. DR KEGG; tmm:Tmari_1744; -. DR KEGG; tmw:THMA_1778; -. DR PATRIC; 23938448; VBITheMar51294_1754. DR eggNOG; ENOG4105CDU; Bacteria. DR eggNOG; COG0305; LUCA. DR KO; K02314; -. DR OMA; FQIAEAR; -. DR OrthoDB; EOG6T4RW5; -. DR BioCyc; TMAR243274:GC6P-1784-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central. DR Gene3D; 1.10.860.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR007692; DNA_helicase_DnaB. DR InterPro; IPR007694; DNA_helicase_DnaB-like_C. DR InterPro; IPR007693; DNA_helicase_DnaB-like_N. DR InterPro; IPR016136; DNA_helicase_N/primase_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00772; DnaB; 1. DR Pfam; PF03796; DnaB_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF48024; SSF48024; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00665; DnaB; 1. DR PROSITE; PS51199; SF4_HELICASE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU362085, KW ECO:0000313|EMBL:AAD36801.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA replication {ECO:0000256|RuleBase:RU362085, KW ECO:0000256|SAAS:SAAS00435671}; KW DNA-binding {ECO:0000256|RuleBase:RU362085, KW ECO:0000256|SAAS:SAAS00435659}; KW Helicase {ECO:0000256|RuleBase:RU362085, ECO:0000313|EMBL:AAD36801.1}; KW Hydrolase {ECO:0000256|RuleBase:RU362085, KW ECO:0000313|EMBL:AAD36801.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362085, KW ECO:0000313|EMBL:AAD36801.1}; KW Primosome {ECO:0000256|RuleBase:RU362085}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 178 450 SF4 helicase. FT {ECO:0000259|PROSITE:PS51199}. SQ SEQUENCE 451 AA; 51416 MW; 2EA8FA6A7B816A00 CRC64; MRVPPHNLEA EVAVLGSILI DPSVINDVLE ILSHEDFYLK KHQHIFRAME ELYDEGKPVD VVSVCDKLQS MGKLEEVGGD LEVAQLAEAV PSSAHALHYA EIVKEKSILR KLIEISRKIS ESAYMEEDVE ILLDNAEKMI FEISEMKTTK SYDHLRGIMH RVFENLENFR ERANLIEPGV LITGLPTGFK SLDKQTTGFH SSDLVIIAAR PSMGKTSFAL SIARNMAVNF EIPVGIFSLE MSKEQLAQRL LSMESGVDLY SIRTGYLDQE KWERLTIAAS KLYKAPIVVD DESLLDPRSL RAKARRMKKE YDVKAIFVDY LQLMHLKGRK ESRQQEISEI SRSLKLLARE LDIVVIALSQ LSRAVEQRED KRPRLSDLRE SGAIEQDADT VIFIYREEYY RSKKSKEESK LHEPHEAEII IGKQRNGPVG TITLIFDPRT VTFHEVDVVH S // ID Q9WXY3_THEMA Unreviewed; 358 AA. AC Q9WXY3; G4FH44; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase-related deacylase {ECO:0000313|EMBL:AGL49053.1}; DE SubName: Full=Carboxypeptidase G2, putative {ECO:0000313|EMBL:AAD35223.1}; GN OrderedLocusNames=TM_0129 {ECO:0000313|EMBL:AAD35223.1}; GN ORFNames=Tmari_0127 {ECO:0000313|EMBL:AGL49053.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35223.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35223.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35223.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49053.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49053.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35223.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49053.1; -; Genomic_DNA. DR PIR; A72416; A72416. DR RefSeq; NP_227945.1; NC_000853.1. DR RefSeq; WP_004082717.1; NZ_CP011107.1. DR STRING; 243274.TM0129; -. DR MEROPS; M20.001; -. DR EnsemblBacteria; AAD35223; AAD35223; TM_0129. DR EnsemblBacteria; AGL49053; AGL49053; Tmari_0127. DR GeneID; 896956; -. DR KEGG; tma:TM0129; -. DR KEGG; tmi:THEMA_04160; -. DR KEGG; tmm:Tmari_0127; -. DR KEGG; tmw:THMA_0125; -. DR PATRIC; 23935096; VBITheMar51294_0126. DR eggNOG; ENOG4106TC3; Bacteria. DR eggNOG; COG0624; LUCA. DR KO; K01295; -. DR OMA; HADTVWP; -. DR OrthoDB; EOG6KDKQ9; -. DR BioCyc; TMAR243274:GC6P-129-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.360; -; 1. DR InterPro; IPR017150; Pept_M20_glutamate_carboxypep. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF037238; Carboxypeptidase_G2; 1. DR SUPFAM; SSF55031; SSF55031; 1. PE 4: Predicted; KW Carboxypeptidase {ECO:0000313|EMBL:AAD35223.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD35223.1}; KW Protease {ECO:0000313|EMBL:AAD35223.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 160 254 M20_dimer. {ECO:0000259|Pfam:PF07687}. SQ SEQUENCE 358 AA; 39841 MW; 57B8E646C404A2EF CRC64; MKWIEIYEKL VNIDTGPDLP LEGKLRRTSF LTEILEDLGF RVEKREAAYV AFRGKPPYVT LIGHLDTVFP EGESKRRPFT IEGNIAKGPG VCDMKGGVVI LLESLKRFLQ QNDTDLCVVL NVDEELGSPL SGEVFKEVAG MSSHCLSFEP GRENGELISS RKGIISLWLF ARGKKGHASR LDEGANAIVE LAFKVVELTS LNGRFPNLTL NPTIVKGGAE SNVTPDKAEV YFDVRYYDDK EYEFLEETLK RLSAVHPEAN VSYTLKLRRL PMKEDPDFVN IVKMSAEEIG MTVSFVRATG GGDVAFFSQN GVPSIDGLGI PGGKMHSEDE YARLDQFEDR VNLVVHLLRK LGGEKNVR // ID Q9X060_THEMA Unreviewed; 251 AA. AC Q9X060; G4FF25; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=Circadian phase modifier / NCAIR mutase (PurE)-related protein {ECO:0000313|EMBL:AGL49892.1}; DE SubName: Full=Phosphoribosylaminoimidazole carboxylase-related protein {ECO:0000313|EMBL:AAD36044.1}; GN OrderedLocusNames=TM_0965 {ECO:0000313|EMBL:AAD36044.1}; GN ORFNames=Tmari_0967 {ECO:0000313|EMBL:AGL49892.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36044.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36044.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36044.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49892.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49892.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36044.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49892.1; -; Genomic_DNA. DR PIR; B72312; B72312. DR RefSeq; NP_228773.1; NC_000853.1. DR RefSeq; WP_004080597.1; NZ_CP011107.1. DR STRING; 243274.TM0965; -. DR EnsemblBacteria; AAD36044; AAD36044; TM_0965. DR EnsemblBacteria; AGL49892; AGL49892; Tmari_0967. DR GeneID; 898702; -. DR KEGG; tma:TM0965; -. DR KEGG; tmi:THEMA_09520; -. DR KEGG; tmm:Tmari_0967; -. DR KEGG; tmw:THMA_0988; -. DR PATRIC; 23936861; VBITheMar51294_0979. DR eggNOG; ENOG4105DTC; Bacteria. DR eggNOG; COG1691; LUCA. DR KO; K06898; -. DR OMA; PEVIWGP; -. DR OrthoDB; EOG66F05P; -. DR BioCyc; TMAR243274:GC6P-995-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.7700; -; 1. DR InterPro; IPR000031; PurE_dom. DR Pfam; PF00731; AIRC; 1. DR SMART; SM01001; AIRC; 1. DR SUPFAM; SSF52255; SSF52255; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 117 249 AIRC. {ECO:0000259|SMART:SM01001}. SQ SEQUENCE 251 AA; 27297 MW; 34E4F1D13DCEDAD4 CRC64; MFEDVLRSLA SGEITIQEAE EKILSKFFER TNELMLDMER DKRQGFPEIV FALGKTKEQT IAAVEKFLER KGIAFVSGLD EEKKRELKDR FFGYVIKEAG RLVVLKRENT TLEKLNGKVG VITAGTSDVP FAEETSLILE ELGVNVQKVY DAGVAGIHRS FYALSKTEDS DLLIVFAGME GILPSLIASL TDLPVIAVPT PVGYGFGGEG LGALSTMLQT CVPGLVVVNI GNTVGAAAAA VRILRRIRKD G // ID Q9WZ38_THEMA Unreviewed; 554 AA. AC Q9WZ38; G4FDQ2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=Peptidase M23B {ECO:0000313|EMBL:AGL49491.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35653.1}; GN OrderedLocusNames=TM_0568 {ECO:0000313|EMBL:AAD35653.1}; GN ORFNames=Tmari_0566 {ECO:0000313|EMBL:AGL49491.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35653.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35653.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35653.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49491.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49491.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35653.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49491.1; -; Genomic_DNA. DR PIR; G72361; G72361. DR RefSeq; NP_228378.1; NC_000853.1. DR RefSeq; WP_004081297.1; NZ_CP011107.1. DR STRING; 243274.TM0568; -. DR EnsemblBacteria; AAD35653; AAD35653; TM_0568. DR EnsemblBacteria; AGL49491; AGL49491; Tmari_0566. DR GeneID; 897632; -. DR KEGG; tma:TM0568; -. DR KEGG; tmi:THEMA_01830; -. DR KEGG; tmm:Tmari_0566; -. DR KEGG; tmw:THMA_0582; -. DR PATRIC; 23936045; VBITheMar51294_0577. DR eggNOG; ENOG4107QMT; Bacteria. DR eggNOG; COG3584; LUCA. DR OMA; PTFRIAR; -. DR OrthoDB; EOG6SJJMS; -. DR BioCyc; TMAR243274:GC6P-592-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro. DR Gene3D; 3.10.350.10; -; 1. DR InterPro; IPR010611; 3D_dom. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR018392; LysM_dom. DR InterPro; IPR016047; Peptidase_M23. DR Pfam; PF06725; 3D; 1. DR Pfam; PF01476; LysM; 1. DR Pfam; PF01551; Peptidase_M23; 1. DR SMART; SM00257; LysM; 1. DR SUPFAM; SSF51261; SSF51261; 1. DR SUPFAM; SSF54106; SSF54106; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 284 331 LysM. {ECO:0000259|SMART:SM00257}. FT COILED 22 87 {ECO:0000256|SAM:Coils}. FT COILED 205 239 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 554 AA; 62107 MW; 68C1CF27C49C1BED CRC64; MAGIKKILMF SLILIFLAAC VSPELEEKLN NLENQIRQLN TQIDSIEKKM LDLENKMKAQ ESSQEELEAL KRDVRYLKED LSSLQEEFSS KMSDLENSYY SISMKLPAVE KAASIFSEIE DMKSKISELE RKVSIVSLGS SPEVSEDLKH ILLDLEERVS TLEKNVSVVD RIEERLESTE KLLSKVALRV LSQGETEAKV VNVSNDELES RISDIEKKLS YLETNQKALE QIVQNLKDQK PSSYANIDVE SYSQQLKKYL DEFRRLVRSY EIARILGIEE GYVFVRVERG DTLAKISNAF NLGPDGVEKI MKLNGIDDPR KLIAGRIIKV PVTNLSTSFP VGEKPDPKVI VSGFGLKTDG TFSTGVEVES DGQKVKAALP GRVKSVSNGT VVIYHGNDVE TVYRNLAVVS VNAGDWVSAG DTIGYGGKNV VFELYVEGEP KDPMLLFFSN MGEFEISFYT EWEDGKLPEH PAFRLTKSGK IPEDWKTAAA DTTIFPLGSV LYIPELRDTP SGGVFVVEDI GGVIMGRKID IYLDSIREAL QNRKIVSRVF VWRD // ID Q9WZY7_THEMA Unreviewed; 185 AA. AC Q9WZY7; G4FCU0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35966.1}; GN OrderedLocusNames=TM_0885 {ECO:0000313|EMBL:AAD35966.1}; GN ORFNames=Tmari_0887 {ECO:0000313|EMBL:AGL49812.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35966.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35966.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35966.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49812.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49812.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35966.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49812.1; -; Genomic_DNA. DR PIR; F72320; F72320. DR RefSeq; NP_228693.1; NC_000853.1. DR RefSeq; WP_004080707.1; NZ_CP011107.1. DR STRING; 243274.TM0885; -. DR EnsemblBacteria; AAD35966; AAD35966; TM_0885. DR EnsemblBacteria; AGL49812; AGL49812; Tmari_0887. DR GeneID; 898559; -. DR KEGG; tma:TM0885; -. DR KEGG; tmi:THEMA_00210; -. DR KEGG; tmm:Tmari_0887; -. DR KEGG; tmw:THMA_0907; -. DR PATRIC; 23936701; VBITheMar51294_0899. DR eggNOG; ENOG4108UHP; Bacteria. DR eggNOG; COG1751; LUCA. DR KO; K09126; -. DR OMA; QGVKVCY; -. DR OrthoDB; EOG60CWPM; -. DR BioCyc; TMAR243274:GC6P-915-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.1380.30; -; 1. DR InterPro; IPR015074; DUF1867. DR InterPro; IPR023161; PK-like_domain. DR InterPro; IPR015795; Pyrv_Knase_C. DR Pfam; PF02887; PK_C; 1. DR PIRSF; PIRSF016138; UCP016138; 1. DR ProDom; PD022619; DUF1867; 1. DR SUPFAM; SSF52935; SSF52935; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 15 161 PK_C. {ECO:0000259|Pfam:PF02887}. SQ SEQUENCE 185 AA; 20109 MW; 2A0495EF6F92F876 CRC64; MVLFEKPGKE NTRKTLEIAI QKASELSSKK LLIASATGYS ARMALEMIPE DMKLVVVTHH AGFEEPDTQE FDEELRKLLK EKGHDVLTAT HALSAGERSL RRKFGGIYPL EIIANTLRMF SEGVKVGVEI TLMAADAGLV KTSELVVACG GTESGLDSAI VVKPANSPNL FDLKITEILC KPLIS // ID Q9WZT8_THEMA Unreviewed; 101 AA. AC Q9WZT8; G4FCZ2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35914.1}; GN OrderedLocusNames=TM_0832 {ECO:0000313|EMBL:AAD35914.1}; GN ORFNames=Tmari_0834 {ECO:0000313|EMBL:AGL49759.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35914.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35914.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35914.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49759.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49759.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35914.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49759.1; -; Genomic_DNA. DR PIR; D72328; D72328. DR RefSeq; NP_228641.1; NC_000853.1. DR RefSeq; WP_004080808.1; NZ_CP011107.1. DR STRING; 243274.TM0832; -. DR EnsemblBacteria; AAD35914; AAD35914; TM_0832. DR EnsemblBacteria; AGL49759; AGL49759; Tmari_0834. DR GeneID; 898502; -. DR KEGG; tma:TM0832; -. DR KEGG; tmi:THEMA_00480; -. DR KEGG; tmm:Tmari_0834; -. DR KEGG; tmw:THMA_0853; -. DR PATRIC; 23936590; VBITheMar51294_0845. DR eggNOG; ENOG410684A; Bacteria. DR eggNOG; ENOG410XVBM; LUCA. DR OMA; KDIRFRR; -. DR OrthoDB; EOG6VTK8F; -. DR BioCyc; TMAR243274:GC6P-861-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR007922; DUF721/UPF0232. DR Pfam; PF05258; DUF721; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 101 AA; 11946 MW; BE6E0B16BCBEE9F9 CRC64; MILLRQLLDE LSTKQPLFFE LKIKMLLSEW DKIVGPVIAR HTKVEKVENG TVYIVCDDSL WMTELTMQKD RLLKILNERS GKELFRDIKF RRGKVDGKVL R // ID Q9WZX4_THEMA Unreviewed; 583 AA. AC Q9WZX4; G4FCV4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 98. DE SubName: Full=Cell division protein FtsI [Peptidoglycan synthetase] {ECO:0000313|EMBL:AGL49797.1}; DE EC=2.4.1.129 {ECO:0000313|EMBL:AGL49797.1}; DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:AAD35952.1}; GN OrderedLocusNames=TM_0870 {ECO:0000313|EMBL:AAD35952.1}; GN ORFNames=Tmari_0872 {ECO:0000313|EMBL:AGL49797.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35952.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35952.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35952.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49797.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49797.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35952.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49797.1; -; Genomic_DNA. DR PIR; A72323; A72323. DR RefSeq; NP_228679.1; NC_000853.1. DR RefSeq; WP_004080731.1; NZ_CP011107.1. DR STRING; 243274.TM0870; -. DR DNASU; 898543; -. DR EnsemblBacteria; AAD35952; AAD35952; TM_0870. DR EnsemblBacteria; AGL49797; AGL49797; Tmari_0872. DR GeneID; 898543; -. DR KEGG; tma:TM0870; -. DR KEGG; tmi:THEMA_00285; -. DR KEGG; tmm:Tmari_0872; -. DR KEGG; tmw:THMA_0892; -. DR PATRIC; 23936668; VBITheMar51294_0883. DR eggNOG; ENOG4107TV0; Bacteria. DR eggNOG; COG0768; LUCA. DR KO; K03587; -. DR OMA; IVMESKT; -. DR OrthoDB; EOG6N0HHV; -. DR BioCyc; TMAR243274:GC6P-900-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008658; F:penicillin binding; IEA:InterPro. DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR005543; PASTA_dom. DR InterPro; IPR005311; PBP_dimer. DR InterPro; IPR001460; PCN-bd_Tpept. DR Pfam; PF03793; PASTA; 1. DR Pfam; PF00905; Transpeptidase; 1. DR SMART; SM00740; PASTA; 1. DR SUPFAM; SSF56519; SSF56519; 1. DR SUPFAM; SSF56601; SSF56601; 1. DR PROSITE; PS51178; PASTA; 1. PE 4: Predicted; KW Cell cycle {ECO:0000313|EMBL:AGL49797.1}; KW Cell division {ECO:0000313|EMBL:AGL49797.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000313|EMBL:AGL49797.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49797.1}. FT DOMAIN 522 581 PASTA. {ECO:0000259|PROSITE:PS51178}. SQ SEQUENCE 583 AA; 64834 MW; C633F9DD56DF951A CRC64; MEKRLWLLLA IFAIFLTVSF MNLFFFPLAG ERENWFVSIP PRRGSVLDVR GRKIVYDSPE YVAYLDVDFF KRQNGDIKAL EKTLQNCGIT KSAEEVMEYK FFKLTEGEDK VDVLKKIESE LLPFVNIELV YTRKKIQDYA TGILLGTVID GTGKGGIEGF FDDQLQGKRK GFLELRYRGA RLSPTLVNYS PPENGKDVWL SLDLDLQRRV YDIISKAVEG NSAEAGHVIV MESKTGRILS MVTTRNWNDL IGGYIEPGST IKPLVYAIAL ETHSASPDFT VECEGSIKPV EQLPVIIRDI EKHGLVDFSA GIVKSCNVMS VKVGELITEK TGVEGFYEWL RKVGFGEKTG IEMEGEIAGV LREPKKWSLI DPAEISIGQG IGVTPVQLIA SLNIFANDGY WVKPTILKDS PVKKRRVFSK ETTDVIRQAM VRVVEEGTGK LAQVKGIAIA GKTGTAQKAV GGEYRNLYHS LFVGFFPAED PKYTILVHLD SPSGAFYGGE VAAPVFREIV EILTEKEDGR IRIVKGLMPD LRGLPVRDAL LVLESLGVKD VEIKGKGWKV SEQTPPPNHP LEGPVILFLS DQK // ID Q9WYJ2_THEMA Unreviewed; 68 AA. AC Q9WYJ2; G4FHR9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35444.1}; GN OrderedLocusNames=TM_0357 {ECO:0000313|EMBL:AAD35444.1}; GN ORFNames=Tmari_0355 {ECO:0000313|EMBL:AGL49280.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35444.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35444.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35444.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49280.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49280.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35444.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49280.1; -; Genomic_DNA. DR PIR; E72386; E72386. DR RefSeq; NP_228168.1; NC_000853.1. DR RefSeq; WP_004083158.1; NZ_CP011107.1. DR STRING; 243274.TM0357; -. DR EnsemblBacteria; AAD35444; AAD35444; TM_0357. DR EnsemblBacteria; AGL49280; AGL49280; Tmari_0355. DR GeneID; 897315; -. DR KEGG; tma:TM0357; -. DR KEGG; tmi:THEMA_02930; -. DR KEGG; tmm:Tmari_0355; -. DR KEGG; tmw:THMA_0365; -. DR PATRIC; 23935595; VBITheMar51294_0362. DR OMA; IKKKQPR; -. DR OrthoDB; EOG6GN78B; -. DR BioCyc; TMAR243274:GC6P-371-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 65 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 68 AA; 7711 MW; 4E5C3179E3F97A16 CRC64; MRFVSDFLFF AGFGLLFIAI VFFDLGTRAI KKKQNQKKKF YDKKGWQFLS VSLGAFAVSI LLALIGRG // ID Q9WZ80_THEMA Unreviewed; 56 AA. AC Q9WZ80; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35696.1}; GN OrderedLocusNames=TM_0611 {ECO:0000313|EMBL:AAD35696.1}; GN ORFNames=Tmari_0611 {ECO:0000313|EMBL:AGL49536.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35696.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35696.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35696.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49536.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49536.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35696.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49536.1; -; Genomic_DNA. DR PIR; G72355; G72355. DR RefSeq; NP_228421.1; NC_000853.1. DR RefSeq; WP_010865161.1; NZ_CP011107.1. DR STRING; 243274.TM0611; -. DR DNASU; 897694; -. DR EnsemblBacteria; AAD35696; AAD35696; TM_0611. DR EnsemblBacteria; AGL49536; AGL49536; Tmari_0611. DR GeneID; 897694; -. DR KEGG; tma:TM0611; -. DR KEGG; tmi:THEMA_01610; -. DR KEGG; tmm:Tmari_0611; -. DR KEGG; tmw:THMA_0627; -. DR OrthoDB; EOG6R2H4S; -. DR BioCyc; TMAR243274:GC6P-636-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 56 AA; 6468 MW; 346F85EB61A078A0 CRC64; MITQTKKSRT TREKHPPVVS DTPESRQNPS KGLKGSHEKA LSMLWSESVR WSSKMW // ID Q9X2F1_THEMA Unreviewed; 402 AA. AC Q9X2F1; G4FGL7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Transposase, putative {ECO:0000313|EMBL:AAD36894.1}; GN OrderedLocusNames=TM_1831 {ECO:0000313|EMBL:AAD36894.1}; GN ORFNames=Tmari_1840 {ECO:0000313|EMBL:AGL50764.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36894.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36894.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36894.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50764.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50764.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36894.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50764.1; -; Genomic_DNA. DR PIR; C72205; C72205. DR RefSeq; NP_229628.1; NC_000853.1. DR RefSeq; WP_004082376.1; NZ_CP011107.1. DR STRING; 243274.TM1831; -. DR DNASU; 897819; -. DR EnsemblBacteria; AAD36894; AAD36894; TM_1831. DR EnsemblBacteria; AGL50764; AGL50764; Tmari_1840. DR GeneID; 897819; -. DR KEGG; tma:TM1831; -. DR KEGG; tmi:THEMA_05045; -. DR KEGG; tmm:Tmari_1840; -. DR KEGG; tmw:THMA_1875; -. DR PATRIC; 23938649; VBITheMar51294_1851. DR eggNOG; ENOG4108K3X; Bacteria. DR eggNOG; COG0675; LUCA. DR KO; K07496; -. DR OMA; DVRESDW; -. DR BioCyc; TMAR243274:GC6P-1882-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR024064; FdhE-like. DR InterPro; IPR001959; Transposase_2. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR Pfam; PF01385; OrfB_IS605; 1. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR SUPFAM; SSF144020; SSF144020; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 164 281 OrfB_IS605. {ECO:0000259|Pfam:PF01385}. FT DOMAIN 300 366 OrfB_Zn_ribbon. FT {ECO:0000259|Pfam:PF07282}. SQ SEQUENCE 402 AA; 46115 MW; 69B4583130E17E88 CRC64; MSRRVIRTYK LAVPGHLSQT CEELNRTAAR IYNKTMSLVR KIHQKKGFWL SWPTADKYIL RWAENIKIHV HSKQAFVQLY FQALKGYFKA TKKNPDAKPP YKKKRYLPFI WKESAVKLLP DGTLRLSLGK EREPFVVQTP LKPPLRIKQT RLVFEDGYYL HLAIEVEIEE KSANSGVMAV DPGVLRPITC FDGKEVISYH GGVLSSILRY RNKRLASFQS AIAECKKGSR RYNKLVRAKK RVLRRLRNQI NDIMHKITSS FIGLCLRKQI GTIVIGDVTG IRERADYSDN ANQKIHQWQF RKLIEMIRYK AEQFGIEVEL ISEANTSKTC PVCGAKNKPN GRRYHCKTCG FEYHRDGVGA INIWKRYPGT GQVVAGLAPV RGVRFHPHLC GHGASLAPWK VA // ID Q9WYP2_THEMA Unreviewed; 383 AA. AC Q9WYP2; G4FHX0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=Regulator of myo-inositol utilization InoR, ROK family {ECO:0000313|EMBL:AGL49333.1}; DE SubName: Full=Transcriptional regulator, XylR-related {ECO:0000313|EMBL:AAD35496.1}; GN OrderedLocusNames=TM_0411 {ECO:0000313|EMBL:AAD35496.1}; GN ORFNames=Tmari_0408 {ECO:0000313|EMBL:AGL49333.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35496.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35496.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35496.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49333.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49333.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35496.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49333.1; -; Genomic_DNA. DR PIR; A72381; A72381. DR RefSeq; NP_228221.1; NC_000853.1. DR RefSeq; WP_004083258.1; NZ_CP011107.1. DR STRING; 243274.TM0411; -. DR EnsemblBacteria; AAD35496; AAD35496; TM_0411. DR EnsemblBacteria; AGL49333; AGL49333; Tmari_0408. DR GeneID; 897411; -. DR KEGG; tma:TM0411; -. DR KEGG; tmi:THEMA_02670; -. DR KEGG; tmm:Tmari_0408; -. DR KEGG; tmw:THMA_0417; -. DR PATRIC; 23935705; VBITheMar51294_0416. DR eggNOG; ENOG4108QR2; Bacteria. DR eggNOG; COG1940; LUCA. DR OMA; DIEGSIM; -. DR OrthoDB; EOG6QK4PG; -. DR BioCyc; TMAR243274:GC6P-426-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR000600; ROK. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00480; ROK; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS01125; ROK; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 383 AA; 41965 MW; 298ADFF96F9938F7 CRC64; MLNEMEKTVL QMIMAGSDIS RVDISRALGI SKPVVSKAVN RLIELGFVKE AGRKESSSKG GRKPVLLSFV PESRYVIGVD IGGTKIDAVL TDLVGNVLNK EHILLPSNLD KRKLLELIKK VIHPFLVYER ILGIGIGIPG TVDEDHLVKR IPAFDVTDWD LKEELEKTFG YPVFVENNAN LDAFAEAKIG AGRGFRCVLL ISVGWGIGSG IVYDGKIFRG ARGKAGEFGH IVTDWSKEKE IVLEKGFGHL EEWFSGFSMS KRFGKSPEWV FEKRHNEIKK NLEHFGVAVA NAIVLFDPDV VIIKGGIGLH QFEKISAVVR SVVSKIVPED ILKDVEIRKG EIEEYGVAIG GALFVIENIL GLKGGGKYEG CQASREVGSK AGV // ID Q9X1M2_THEMA Unreviewed; 194 AA. AC Q9X1M2; G4FFS4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36603.1}; GN OrderedLocusNames=TM_1536 {ECO:0000313|EMBL:AAD36603.1}; GN ORFNames=Tmari_1544 {ECO:0000313|EMBL:AGL50468.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36603.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36603.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36603.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50468.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50468.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36603.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50468.1; -; Genomic_DNA. DR PIR; D72242; D72242. DR RefSeq; NP_229336.1; NC_000853.1. DR RefSeq; WP_004081917.1; NZ_CP011107.1. DR STRING; 243274.TM1536; -. DR EnsemblBacteria; AAD36603; AAD36603; TM_1536. DR EnsemblBacteria; AGL50468; AGL50468; Tmari_1544. DR GeneID; 897978; -. DR KEGG; tma:TM1536; -. DR KEGG; tmi:THEMA_06605; -. DR KEGG; tmm:Tmari_1544; -. DR KEGG; tmw:THMA_1570; -. DR PATRIC; 23938032; VBITheMar51294_1554. DR eggNOG; ENOG410664W; Bacteria. DR eggNOG; COG3374; LUCA. DR KO; K08980; -. DR OMA; SSYNLIF; -. DR OrthoDB; EOG6G4VV1; -. DR BioCyc; TMAR243274:GC6P-1576-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR009324; DUF981. DR Pfam; PF06168; DUF981; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 61 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 91 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 118 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 124 144 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 151 172 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 194 AA; 20710 MW; 7946E3D72BFF4976 CRC64; MFVDYLTVFM ADVVAGLGVL IAFVLKGLND SEKAKSFAPA FAAVGLLAIA TGLHMVLTWP LPGSHNIAFG EPFLLYGFVF LAAAIAVAKG WDLMPTTIFA LFAGIYAIIV GGSIMGYGMT KHPFTSGLGF IAAGLVGVLS PVVWKLRENK VIRFLGVVLL ALTLLLWFIT MYGSVTGHIN PQGSFGKWTP IPMR // ID Q9WZU6_THEMA Unreviewed; 253 AA. AC Q9WZU6; G4FCY2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 108. DE SubName: Full=Response regulator {ECO:0000313|EMBL:AAD35924.1}; GN OrderedLocusNames=TM_0842 {ECO:0000313|EMBL:AAD35924.1}; GN ORFNames=Tmari_0844 {ECO:0000313|EMBL:AGL49769.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35924.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35924.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35924.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49769.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49769.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains GGDEF domain. CC {ECO:0000256|SAAS:SAAS00496774}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35924.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49769.1; -; Genomic_DNA. DR PIR; C72326; C72326. DR RefSeq; NP_228651.1; NC_000853.1. DR RefSeq; WP_004080787.1; NZ_CP011107.1. DR PDB; 2QXY; X-ray; 1.95 A; A/B=2-132. DR PDBsum; 2QXY; -. DR STRING; 243274.TM0842; -. DR DNASU; 898513; -. DR EnsemblBacteria; AAD35924; AAD35924; TM_0842. DR EnsemblBacteria; AGL49769; AGL49769; Tmari_0844. DR GeneID; 898513; -. DR KEGG; tma:TM0842; -. DR KEGG; tmi:THEMA_00430; -. DR KEGG; tmm:Tmari_0844; -. DR KEGG; tmw:THMA_0863; -. DR PATRIC; 23936610; VBITheMar51294_0855. DR eggNOG; ENOG410859Y; Bacteria. DR eggNOG; COG0784; LUCA. DR KO; K02485; -. DR OMA; PVMILTK; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-871-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR Pfam; PF00072; Response_reg; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR SUPFAM; SSF55073; SSF55073; 1. DR PROSITE; PS50887; GGDEF; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2QXY}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 117 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT DOMAIN 156 253 GGDEF. {ECO:0000259|PROSITE:PS50887}. FT REGION 43 44 Sulfate binding. {ECO:0000213|PDB:2QXY}. SQ SEQUENCE 253 AA; 29679 MW; 95D6712C14DCF7ED CRC64; MTPTVMVVDE SRITFLAVKN ALEKDGFNVI WAKNEQEAFT FLRREKIDLV FVDVFEGEES LNLIRRIREE FPDTKVAVLS AYVDKDLIIN SVKAGAVDYI LKPFRLDYLL ERVKKIISST PRVTVSLRKN IEDLEITLKF EDIVRKEIKR SNRTGSRFCV MYVKFEDIMR DYETIKKFFR ETDYVLPISA SEYLFVLTLT GKHGIEAVTR RMKEKLSERF SYTYVCYPDD GKTYEEIILT LKDRMAKPRG NES // ID Q9WZD6_THEMA Unreviewed; 377 AA. AC Q9WZD6; G4FDF6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Pleiotropic regulatory protein {ECO:0000313|EMBL:AAD35750.1}; GN OrderedLocusNames=TM_0668 {ECO:0000313|EMBL:AAD35750.1}; GN ORFNames=Tmari_0668 {ECO:0000313|EMBL:AGL49593.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35750.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35750.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35750.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49593.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49593.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. CC {ECO:0000256|RuleBase:RU004508}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35750.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49593.1; -; Genomic_DNA. DR PIR; A72350; A72350. DR RefSeq; NP_228477.1; NC_000853.1. DR RefSeq; WP_004081105.1; NZ_CP011107.1. DR STRING; 243274.TM0668; -. DR EnsemblBacteria; AAD35750; AAD35750; TM_0668. DR EnsemblBacteria; AGL49593; AGL49593; Tmari_0668. DR GeneID; 897783; -. DR KEGG; tma:TM0668; -. DR KEGG; tmi:THEMA_01325; -. DR KEGG; tmm:Tmari_0668; -. DR KEGG; tmw:THMA_0683; -. DR PATRIC; 23936250; VBITheMar51294_0678. DR eggNOG; ENOG4105CF4; Bacteria. DR eggNOG; COG0399; LUCA. DR OMA; FHEKVGY; -. DR OrthoDB; EOG6TXQZ2; -. DR BioCyc; TMAR243274:GC6P-693-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000653; DegT/StrS_aminotransferase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF01041; DegT_DnrJ_EryC1; 1. DR PIRSF; PIRSF000390; PLP_StrS; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-1, KW ECO:0000256|RuleBase:RU004508, ECO:0000256|SAAS:SAAS00486653}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT MOD_RES 191 191 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR000390-1}. SQ SEQUENCE 377 AA; 43084 MW; 04B90A9A74CC0733 CRC64; MIPLFDLTRQ YERIRGEILN AIDKLISSGN VILGENVRRL EEEIASFTGV KHGVGVASGS DALLIALRAM GVEKGDTVVT TPYTFFATAS APYRLGARVI FVDVDESTFN MDLNQLEHVL KKEKVKAIIP VHLFGRTVDL EALSFLREKY GVMILEDCAQ SMGSEWKFSS GEIRKSGSVG DAAIFSFFPT KNLGTYGDGG MIVTNSDEIA EESRILRVHG ARKKYFHEKV GYNSRLDEIH AAILRVKLRY LERWTEERTR VARTYQKLFE EKKLPVVYPR VEEKGFRYHV FHQYVVLFEN EEVRERVREG LKERGIQTAI YYPLPLHLQK CFRDLGYQEG DFPVAESLSK RSLALPMFPE LRDDEIKEVV DTIALFL // ID Q9X254_THEMA Unreviewed; 98 AA. AC Q9X254; G4FGB8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Integral membrane protein YggT, involved in response to extracytoplasmic stress (Osmotic shock) {ECO:0000313|EMBL:AGL50664.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36797.1}; GN OrderedLocusNames=TM_1732 {ECO:0000313|EMBL:AAD36797.1}; GN ORFNames=Tmari_1740 {ECO:0000313|EMBL:AGL50664.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36797.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36797.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36797.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50664.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50664.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36797.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50664.1; -; Genomic_DNA. DR PIR; C72217; C72217. DR RefSeq; NP_229530.1; NC_000853.1. DR RefSeq; WP_004082248.1; NZ_CP011107.1. DR STRING; 243274.TM1732; -. DR EnsemblBacteria; AAD36797; AAD36797; TM_1732. DR EnsemblBacteria; AGL50664; AGL50664; Tmari_1740. DR GeneID; 897239; -. DR KEGG; tma:TM1732; -. DR KEGG; tmi:THEMA_05575; -. DR KEGG; tmm:Tmari_1740; -. DR KEGG; tmw:THMA_1774; -. DR PATRIC; 23938440; VBITheMar51294_1750. DR eggNOG; ENOG4105WB4; Bacteria. DR eggNOG; COG0762; LUCA. DR KO; K02221; -. DR OMA; PIGYIDI; -. DR OrthoDB; EOG6RZB7H; -. DR BioCyc; TMAR243274:GC6P-1780-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003425; CCB3/YggT. DR Pfam; PF02325; YGGT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 95 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 98 AA; 11166 MW; 29C057BD4160EB2F CRC64; MFVIANLLRS IAVVLRTFIY VEIVSIVVSA IFSWTTPYYY HPVRRFFDAL SSIVLNPIRR VVPPIGSVDI SPMIAIFILM FLDGFLVQTL FDLAVRLS // ID Q9X1T6_THEMA Unreviewed; 260 AA. AC Q9X1T6; G4FFY8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36667.1}; GN OrderedLocusNames=TM_1600 {ECO:0000313|EMBL:AAD36667.1}; GN ORFNames=Tmari_1608 {ECO:0000313|EMBL:AGL50532.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36667.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36667.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36667.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50532.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50532.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36667.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50532.1; -; Genomic_DNA. DR PIR; D72234; D72234. DR RefSeq; NP_229400.1; NC_000853.1. DR RefSeq; WP_004082047.1; NZ_CP011107.1. DR STRING; 243274.TM1600; -. DR EnsemblBacteria; AAD36667; AAD36667; TM_1600. DR EnsemblBacteria; AGL50532; AGL50532; Tmari_1608. DR GeneID; 897941; -. DR KEGG; tma:TM1600; -. DR KEGG; tmi:THEMA_06250; -. DR KEGG; tmm:Tmari_1608; -. DR KEGG; tmw:THMA_1640; -. DR PATRIC; 23938174; VBITheMar51294_1619. DR eggNOG; ENOG41069PX; Bacteria. DR eggNOG; ENOG410Y290; LUCA. DR OMA; EIERNYM; -. DR OrthoDB; EOG6B8XK6; -. DR BioCyc; TMAR243274:GC6P-1646-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 260 AA; 29786 MW; BC22156F50F85051 CRC64; MDGDSVKKYV LVVLFFLAAT IFALPEIVEK WMYANYYAKR IMVEIGLKSR FRYEEVYKWG ADKMVLVHEP VSVNWVRLGQ SCYMGSGTTL KRSPMLILDL EDLAFKEILQ GRDLKIEETN EGYEIYIHDT GEYRVLLSSD GFPKEIERNY MDTKSKLIYE EVKPLSADKN EILKDYTLVD SGVEFPKELV DILSNFRFLI IREGTSGLEI EGIYKNGQKV EIFIGNDLPK GGLQVNINGL KIAIVADEKT LEEIKVILGQ // ID Q9WZG7_THEMA Unreviewed; 236 AA. AC Q9WZG7; G4FDB6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Lipoate-protein ligase A {ECO:0000313|EMBL:AGL49633.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35790.1}; GN OrderedLocusNames=TM_0708 {ECO:0000313|EMBL:AAD35790.1}; GN ORFNames=Tmari_0708 {ECO:0000313|EMBL:AGL49633.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35790.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35790.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35790.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49633.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49633.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains BPL/LPL catalytic domain. CC {ECO:0000256|SAAS:SAAS00514708}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35790.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49633.1; -; Genomic_DNA. DR PIR; C72343; C72343. DR RefSeq; NP_228517.1; NC_000853.1. DR RefSeq; WP_004081031.1; NZ_CP011107.1. DR STRING; 243274.TM0708; -. DR DNASU; 898375; -. DR EnsemblBacteria; AAD35790; AAD35790; TM_0708. DR EnsemblBacteria; AGL49633; AGL49633; Tmari_0708. DR GeneID; 898375; -. DR KEGG; tma:TM0708; -. DR KEGG; tmi:THEMA_01125; -. DR KEGG; tmm:Tmari_0708; -. DR KEGG; tmw:THMA_0723; -. DR PATRIC; 23936334; VBITheMar51294_0720. DR eggNOG; ENOG4107S5Z; Bacteria. DR eggNOG; COG0095; LUCA. DR KO; K03800; -. DR OMA; VLQHGSM; -. DR OrthoDB; EOG61KBFV; -. DR BioCyc; TMAR243274:GC6P-734-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro. DR InterPro; IPR004143; BPL_LPL_catalytic. DR Pfam; PF03099; BPL_LplA_LipB; 1. DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Ligase {ECO:0000313|EMBL:AGL49633.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 25 212 BPL/LPL catalytic. FT {ECO:0000259|PROSITE:PS51733}. SQ SEQUENCE 236 AA; 26719 MW; A12C774C0824F7C9 CRC64; MIEKGVFPGA LNMAIDSLMA EWSANMNSVL FRFYGWKRPT VSLGRFQKED GINVPDWIDV VRRPSGGRAL LHHREITYCL AVPKKINFGK LSVLEFHRLV HSLIRDALVE AGLHAELSSK RRGNTALCFD APSRYEIVIN GVKVVGSAQF RTAESIVEHG SIVLKQDIDL LKTIFGEDVP PLKGILDLYD VDVKALEERI LAQFEKVFGT SRKIQLDSSM LKEARERSPL YEVRRR // ID Q9X0S4_THEMA Unreviewed; 291 AA. AC Q9X0S4; G4FEE9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 90. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD36272.1}; DE SubName: Full=Xylobiose ABC transport system, permease protein 2 {ECO:0000313|EMBL:AGL50128.1}; GN OrderedLocusNames=TM_1197 {ECO:0000313|EMBL:AAD36272.1}; GN ORFNames=Tmari_1204 {ECO:0000313|EMBL:AGL50128.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36272.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36272.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36272.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50128.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50128.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36272.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50128.1; -; Genomic_DNA. DR PIR; B72284; B72284. DR RefSeq; NP_229002.1; NC_000853.1. DR RefSeq; WP_004080130.1; NZ_CP011107.1. DR STRING; 243274.TM1197; -. DR TCDB; 3.A.1.5.31; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36272; AAD36272; TM_1197. DR EnsemblBacteria; AGL50128; AGL50128; Tmari_1204. DR GeneID; 898287; -. DR KEGG; tma:TM1197; -. DR KEGG; tmi:THEMA_08345; -. DR KEGG; tmm:Tmari_1204; -. DR KEGG; tmw:THMA_1223; -. DR PATRIC; 23937336; VBITheMar51294_1215. DR eggNOG; ENOG4106NQH; Bacteria. DR eggNOG; ENOG4111MNR; LUCA. DR KO; K02034; -. DR OMA; ILKDWAR; -. DR OrthoDB; EOG6WX4NQ; -. DR BioCyc; TMAR243274:GC6P-1227-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 80 103 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 115 135 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 199 223 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 244 270 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 76 271 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 291 AA; 32875 MW; 8085463F10DB84D0 CRC64; MKQIVRVFRD LFRDYRFTVA FIALLFLLVL SLLSYVSPYD PVSIYQVPRG LPPSFEHPFG TNWLGQDVFW RLTFAVRNSL LIAVITAFFS RIIAIIVGIV SGYKGGALDQ VLMTIGDTTM VLPILIVLIV ISMILKDWAR SFVNLGLLLA FFSWAWDARV IRSQVLSVRE RDFVRVAVLS GMSTMKIVGK QLLPHVLPVI FTTFINNMSW AIGMEITLAY LGLGIDPTVP TLGTMLQRAI TRQALFLGLW WWLAAPIVTA ILLFIALYWL SVSISEYLDP RARFQRVGVG K // ID Q9WXS7_THEMA Unreviewed; 335 AA. AC Q9WXS7; G4FGY7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35166.1}; DE SubName: Full=Xylobiose ABC transport system, permease protein 1 {ECO:0000313|EMBL:AGL48995.1}; GN OrderedLocusNames=TM_0072 {ECO:0000313|EMBL:AAD35166.1}; GN ORFNames=Tmari_0069 {ECO:0000313|EMBL:AGL48995.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35166.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35166.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35166.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48995.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48995.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35166.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48995.1; -; Genomic_DNA. DR PIR; H72420; H72420. DR RefSeq; NP_227888.1; NC_000853.1. DR RefSeq; WP_004082581.1; NZ_CP011107.1. DR STRING; 243274.TM0072; -. DR TCDB; 3.A.1.5.13; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35166; AAD35166; TM_0072. DR EnsemblBacteria; AGL48995; AGL48995; Tmari_0069. DR GeneID; 896897; -. DR KEGG; tma:TM0072; -. DR KEGG; tmi:THEMA_04445; -. DR KEGG; tmm:Tmari_0069; -. DR KEGG; tmw:THMA_0068; -. DR PATRIC; 23934984; VBITheMar51294_0070. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR KO; K02033; -. DR OMA; YIARNAM; -. DR OrthoDB; EOG66F098; -. DR BioCyc; TMAR243274:GC6P-72-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 33 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 111 137 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 158 184 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 196 218 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 256 282 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 302 325 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 109 325 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 335 AA; 38223 MW; 653D1AA484DC9FF3 CRC64; MSFVRRYLLP RLITYFLVVF VGLTIVFFLP RFLPSDPIQA YIDRLITQGG NLNPEYFNKL VETIKELYGL QGSLWNQYVN FWKRLLKGDF GPSYFQFPTP VMKLIRQSLP WTAWLLFVTT VISWIIGNIL GGLAGYFSDK KWVKILDGIA MVIRPMPYYI LALGLLILLA YIFPIFPIGG GFAIGMKFTF SWENLLILLK HAFLPALSLV LIGVFSWFQA MKLVVQSVKT EDYVKYAKMG GVEERRIVRR YVIRNAMLPQ ITGLALSLGQ IFGGALITEI VFSYPGIGSL LYNAIFTGDY NLLMGISTLS ILLVTTSILV IDLLYPLFDP RVRYR // ID Q9WYN6_THEMA Unreviewed; 266 AA. AC Q9WYN6; G4FHW4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=2-oxoglutarate oxidoreductase, beta subunit {ECO:0000313|EMBL:AGL49327.1}; DE EC=1.2.7.3 {ECO:0000313|EMBL:AGL49327.1}; DE SubName: Full=Keto/oxoacid ferredoxin oxidoreductase, beta subunit, putative {ECO:0000313|EMBL:AAD35490.1}; GN OrderedLocusNames=TM_0405 {ECO:0000313|EMBL:AAD35490.1}; GN ORFNames=Tmari_0402 {ECO:0000313|EMBL:AGL49327.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35490.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35490.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35490.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49327.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49327.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35490.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49327.1; -; Genomic_DNA. DR PIR; C72380; C72380. DR RefSeq; NP_228215.1; NC_000853.1. DR RefSeq; WP_004083245.1; NZ_CP011107.1. DR STRING; 243274.TM0405; -. DR EnsemblBacteria; AAD35490; AAD35490; TM_0405. DR EnsemblBacteria; AGL49327; AGL49327; Tmari_0402. DR GeneID; 897404; -. DR KEGG; tma:TM0405; -. DR KEGG; tmi:THEMA_02700; -. DR KEGG; tmm:Tmari_0402; -. DR KEGG; tmw:THMA_0411; -. DR PATRIC; 23935693; VBITheMar51294_0410. DR eggNOG; ENOG4105DQU; Bacteria. DR eggNOG; COG1013; LUCA. DR KO; K00175; -. DR OMA; FNNNIYG; -. DR OrthoDB; EOG647TWJ; -. DR BioCyc; TMAR243274:GC6P-420-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR SUPFAM; SSF52518; SSF52518; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49327.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 52 199 TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}. SQ SEQUENCE 266 AA; 29679 MW; FD0CF88F57E39909 CRC64; MKTERLISYL RPGRWPSVWC PGCGNGIVLK AFLEAVDDLA LPKEKVAVVS GIGCSSRATG YLDFNTLHTL HGRAIAFATG VKLAKPDFEV VVMGGDGDIL SIGGNHFIHA CRRNIDITVV IFNNMIYGMT GGQVSSTTPQ YYQTSTTPLG AFEKPFDAVE IALSAGATFV ARSTVYHYDH LVRVLKKALQ HRGISVVDVL TNCHTYFGRY NGMPEPHQMM EYFKNNTCFL ERPEEGKIKI GIFREEEKED FLTVYRRLTR KEGAME // ID Q9X2C2_THEMA Unreviewed; 546 AA. AC Q9X2C2; G4FGJ0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=CRISPR-associated protein, family {ECO:0000313|EMBL:AGL50736.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36865.1}; GN OrderedLocusNames=TM_1802 {ECO:0000313|EMBL:AAD36865.1}; GN ORFNames=Tmari_1812 {ECO:0000313|EMBL:AGL50736.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36865.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36865.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36865.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50736.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50736.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36865.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50736.1; -; Genomic_DNA. DR PIR; G72210; G72210. DR RefSeq; NP_229599.1; NC_000853.1. DR RefSeq; WP_004082349.1; NZ_CP011107.1. DR STRING; 243274.TM1802; -. DR EnsemblBacteria; AAD36865; AAD36865; TM_1802. DR EnsemblBacteria; AGL50736; AGL50736; Tmari_1812. DR GeneID; 897657; -. DR KEGG; tma:TM1802; -. DR KEGG; tmi:THEMA_05180; -. DR KEGG; tmm:Tmari_1812; -. DR KEGG; tmw:THMA_1848; -. DR PATRIC; 23938593; VBITheMar51294_1823. DR eggNOG; ENOG4107X1C; Bacteria. DR eggNOG; ENOG410ZW5I; LUCA. DR KO; K19114; -. DR OMA; RILWIIP; -. DR OrthoDB; EOG690M9Z; -. DR BioCyc; TMAR243274:GC6P-1853-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR013420; CRISPR-assoc_prot_Csh1_C. DR InterPro; IPR013389; CRISPR-assoc_prot_TM1802. DR Pfam; PF09484; Cas_TM1802; 1. DR TIGRFAMs; TIGR02591; cas_Csh1; 1. DR TIGRFAMs; TIGR02556; cas_TM1802; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 546 AA; 62704 MW; 02D0A08B66046F1B CRC64; MLEKIYNLGK IGGDSFSNFA EEVPSDEGIA IFLESNSEGL VFKDVVSIEK KPGGKNSKIF LYRKQRGNFS SSVSPTMKFL DKSSGSRDPL ERTFDVFLGF FDHPKISHIK DVLERNKEEI IDKLRNYDVK NRFLTISIDG KFPAEVPEIL QAFEDKVTQK KTKGEAKCFL CGKEANSRLS DVFKFATFDK PGFTPFLSKK HPIQICDDCR SVLEKARRAI DEKLSFSFFS NNRILWIIPS VPDQDILESV IEKIYEIKDT DKNSKFRSFA RLEEEIEKVL SENERAVYDF VLIEKEQQAE RIVLHVEEVS PTRVRRILEE SKKIESQLKE DGFKVSVNFS VIHKFFEDLD RYFNSLFSAV FSEGTFDKKL LLTLFLSKIR SDFFGNDTLL SAREAFATYV YLRRLNVLKG GASVLKGEDF FSRYPEFFDE PWKKAVFLEG VLANYLLYLQ YVKRNSKAFT KKLKGLRLTK RDVEGLLPEI RAKIEAYGGM SESVAELFRE TAEAFLEAGN WSASPDEISF VFVSGLSLGK TFFREVGVDE SSEEQE // ID Q9WZ40_THEMA Unreviewed; 294 AA. AC Q9WZ40; G4FDQ0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 117. DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000256|HAMAP-Rule:MF_00920}; DE Short=SRP receptor {ECO:0000256|HAMAP-Rule:MF_00920}; GN Name=ftsY {ECO:0000256|HAMAP-Rule:MF_00920}; GN OrderedLocusNames=TM_0570 {ECO:0000313|EMBL:AAD35655.1}; GN ORFNames=Tmari_0568 {ECO:0000313|EMBL:AGL49493.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35655.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35655.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35655.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49493.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49493.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Acts as a receptor for the CC complex formed by the signal recognition particle (SRP) and the CC ribosome-nascent chain (RNC). {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. CC {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00920}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00920}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_00920}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00920}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35655.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49493.1; -; Genomic_DNA. DR PIR; A72362; A72362. DR RefSeq; NP_228380.1; NC_000853.1. DR RefSeq; WP_004081293.1; NZ_CP011107.1. DR PDB; 1VMA; X-ray; 1.60 A; A/B=1-294. DR PDBsum; 1VMA; -. DR STRING; 243274.TM0570; -. DR EnsemblBacteria; AAD35655; AAD35655; TM_0570. DR EnsemblBacteria; AGL49493; AGL49493; Tmari_0568. DR GeneID; 897634; -. DR KEGG; tma:TM0570; -. DR KEGG; tmi:THEMA_01820; -. DR KEGG; tmm:Tmari_0568; -. DR KEGG; tmw:THMA_0584; -. DR PATRIC; 23936049; VBITheMar51294_0579. DR eggNOG; ENOG4105CCP; Bacteria. DR eggNOG; COG0552; LUCA. DR KO; K03110; -. DR OMA; GCDIIKH; -. DR OrthoDB; EOG62K1ZH; -. DR BioCyc; TMAR243274:GC6P-594-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00920; FtsY; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004390; SR_rcpt_FtsY. DR InterPro; IPR000897; SRP54_GTPase_dom. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SMART; SM00963; SRP54_N; 1. DR SUPFAM; SSF47364; SSF47364; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00064; ftsY; 1. DR PROSITE; PS00300; SRP54; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VMA}; KW Cell cycle {ECO:0000313|EMBL:AAD35655.1}; KW Cell division {ECO:0000313|EMBL:AAD35655.1}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00920}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00920}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00920}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00920}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00920}; KW Receptor {ECO:0000256|HAMAP-Rule:MF_00920, KW ECO:0000313|EMBL:AGL49493.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 266 279 SRP54. {ECO:0000259|PROSITE:PS00300}. FT NP_BIND 99 106 GTP. {ECO:0000256|HAMAP-Rule:MF_00920}. FT NP_BIND 181 185 GTP. {ECO:0000256|HAMAP-Rule:MF_00920}. FT NP_BIND 245 248 GTP. {ECO:0000256|HAMAP-Rule:MF_00920}. SQ SEQUENCE 294 AA; 32046 MW; 54D54E0B1F18A833 CRC64; MGLFDFLKKG LQKTKETFFG RVVKLLKGKK LDDETREELE ELLIQADVGV ETTEYILERL EEKDGDALES LKEIILEILN FDTKLNVPPE PPFVIMVVGV NGTGKTTSCG KLAKMFVDEG KSVVLAAADT FRAAAIEQLK IWGERVGATV ISHSEGADPA AVAFDAVAHA LARNKDVVII DTAGRLHTKK NLMEELRKVH RVVKKKIPDA PHETLLVIDA TTGQNGLVQA KIFKEAVNVT GIILTKLDGT AKGGITLAIA RELGIPIKFI GVGEKAEDLR PFDPEAFVEV LLSE // ID Q9X0J8_THEMA Unreviewed; 225 AA. AC Q9X0J8; G4FEN4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36190.1}; GN OrderedLocusNames=TM_1114 {ECO:0000313|EMBL:AAD36190.1}; GN ORFNames=Tmari_1120 {ECO:0000313|EMBL:AGL50044.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36190.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36190.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36190.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50044.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50044.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36190.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50044.1; -; Genomic_DNA. DR PIR; G72291; G72291. DR RefSeq; NP_228920.1; NC_000853.1. DR RefSeq; WP_004080310.1; NZ_CP011107.1. DR STRING; 243274.TM1114; -. DR EnsemblBacteria; AAD36190; AAD36190; TM_1114. DR EnsemblBacteria; AGL50044; AGL50044; Tmari_1120. DR GeneID; 898651; -. DR KEGG; tma:TM1114; -. DR KEGG; tmi:THEMA_08775; -. DR KEGG; tmm:Tmari_1120; -. DR KEGG; tmw:THMA_1137; -. DR PATRIC; 23937161; VBITheMar51294_1129. DR eggNOG; ENOG4108E4K; Bacteria. DR eggNOG; ENOG41103JB; LUCA. DR OMA; DYYANSV; -. DR OrthoDB; EOG6G20KD; -. DR BioCyc; TMAR243274:GC6P-1143-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 225 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972327. SQ SEQUENCE 225 AA; 25643 MW; 0149960FD4C778A1 CRC64; MRKLLWLVLM GALFTFALAQ SALEVWKYEN GQYISLPATN DLARAFSAFP ADGSCNKPEW QIEFTTEVQV AQWLEWSLSA TKWTWFVRKP GDYYANSVTG TIASNGDVIV SFSGFDDPTY TGTSSVNPEI EAYYTVMTTE GMPDQNSWVR APDVNNLSYT LVDSEALHNG MLFYLWNRIK VVNCNSASTY RNTGYIYLTL QNQKPWIDEE GNYVEDLENY VTSER // ID Q9X2B8_THEMA Unreviewed; 159 AA. AC Q9X2B8; G4FGI6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=CRISPR-associated RecB family exonuclease Cas4a {ECO:0000313|EMBL:AGL50732.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36861.1}; GN OrderedLocusNames=TM_1798 {ECO:0000313|EMBL:AAD36861.1}; GN ORFNames=Tmari_1808 {ECO:0000313|EMBL:AGL50732.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36861.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36861.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36861.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50732.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50732.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36861.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50732.1; -; Genomic_DNA. DR PIR; C72210; C72210. DR RefSeq; NP_229595.1; NC_000853.1. DR RefSeq; WP_004082345.1; NZ_CP011107.1. DR STRING; 243274.TM1798; -. DR EnsemblBacteria; AAD36861; AAD36861; TM_1798. DR EnsemblBacteria; AGL50732; AGL50732; Tmari_1808. DR GeneID; 897368; -. DR KEGG; tma:TM1798; -. DR KEGG; tmi:THEMA_05200; -. DR KEGG; tmm:Tmari_1808; -. DR KEGG; tmw:THMA_1844; -. DR PATRIC; 23938585; VBITheMar51294_1819. DR eggNOG; ENOG4108ZIK; Bacteria. DR eggNOG; COG1468; LUCA. DR KO; K07464; -. DR OMA; AYREYCF; -. DR OrthoDB; EOG6D5G6Z; -. DR BioCyc; TMAR243274:GC6P-1849-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. DR InterPro; IPR013343; CRISPR-assoc_prot_Cas4. DR InterPro; IPR022765; Dna2/Cas4_DUF83. DR Pfam; PF01930; Cas_Cas4; 1. DR TIGRFAMs; TIGR00372; cas4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Exonuclease {ECO:0000313|EMBL:AGL50732.1}; KW Hydrolase {ECO:0000313|EMBL:AGL50732.1}; KW Nuclease {ECO:0000313|EMBL:AGL50732.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 158 Cas_Cas4. {ECO:0000259|Pfam:PF01930}. SQ SEQUENCE 159 AA; 18285 MW; B3F414EFEB79D53B CRC64; MMISGSVVLS YINCKREAWL MAHGVLPDQG NMHIEIGRFI HEDYSDSVML PGMKIDTMFE REGVRVVGEV KKSSASKRGA EYQLLYYLYR LEEKGVKARG EIIVPKENKR IPVELTEENR EKIKKVLEEV SSLLEEETPP PPKRKGICRK CGYELFCFS // ID Q9X1F0_THEMA Unreviewed; 176 AA. AC Q9X1F0; G4FFH1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Glycerol uptake operon antiterminator regulatory protein {ECO:0000313|EMBL:AGL50366.1}; DE SubName: Full=Glycerol uptake operon antiterminator-related protein {ECO:0000313|EMBL:AAD36506.1}; GN OrderedLocusNames=TM_1436 {ECO:0000313|EMBL:AAD36506.1}; GN ORFNames=Tmari_1442 {ECO:0000313|EMBL:AGL50366.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36506.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36506.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36506.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50366.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50366.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36506.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50366.1; -; Genomic_DNA. DR PIR; A72255; A72255. DR RefSeq; NP_229236.1; NC_000853.1. DR RefSeq; WP_004081703.1; NZ_CP011107.1. DR PDB; 1VKF; X-ray; 1.65 A; A/B/C/D=1-176. DR PDBsum; 1VKF; -. DR STRING; 243274.TM1436; -. DR EnsemblBacteria; AAD36506; AAD36506; TM_1436. DR EnsemblBacteria; AGL50366; AGL50366; Tmari_1442. DR GeneID; 898039; -. DR KEGG; tma:TM1436; -. DR KEGG; tmi:THEMA_07135; -. DR KEGG; tmm:Tmari_1442; -. DR KEGG; tmw:THMA_1466; -. DR PATRIC; 23937820; VBITheMar51294_1448. DR eggNOG; ENOG41083UR; Bacteria. DR eggNOG; COG1954; LUCA. DR KO; K02443; -. DR OMA; FLHVEKI; -. DR OrthoDB; EOG62G5N8; -. DR BioCyc; TMAR243274:GC6P-1474-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR GO; GO:0009607; P:response to biotic stimulus; IEA:InterPro. DR Gene3D; 3.20.20.400; -; 1. DR InterPro; IPR006699; G3P_antiterm. DR Pfam; PF04309; G3P_antiterm; 1. DR PIRSF; PIRSF016897; GlpP; 1. DR SUPFAM; SSF110391; SSF110391; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VKF}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT REGION 163 165 Citrate binding. {ECO:0000213|PDB:1VKF}. FT BINDING 10 10 Citrate. {ECO:0000213|PDB:1VKF}. FT BINDING 96 96 Citrate. {ECO:0000213|PDB:1VKF}. FT BINDING 145 145 Citrate; via amide nitrogen. FT {ECO:0000213|PDB:1VKF}. SQ SEQUENCE 176 AA; 19297 MW; 4BA55EBF2D3E224A CRC64; MFKGIIAALW DMDSIGEIEP DVVFLLKSDI LNLKFHLKIL KDRGKTVFVD MDFVNGLGEG EEAILFVKKA GADGIITIKP KNYVVAKKNG IPAVLRFFAL DSKAVERGIE QIETLGVDVV EVLPGAVAPK VARKIPGRTV IAAGLVETEE EAREILKHVS AISTSSRILW KMKFLP // ID Q9X1E8_THEMA Unreviewed; 138 AA. AC Q9X1E8; G4FFG9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36504.1}; GN OrderedLocusNames=TM_1434 {ECO:0000313|EMBL:AAD36504.1}; GN ORFNames=Tmari_1440 {ECO:0000313|EMBL:AGL50364.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36504.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36504.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36504.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50364.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50364.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36504.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50364.1; -; Genomic_DNA. DR PIR; G72254; G72254. DR RefSeq; NP_229234.1; NC_000853.1. DR RefSeq; WP_004081696.1; NZ_CP011107.1. DR STRING; 243274.TM1434; -. DR EnsemblBacteria; AAD36504; AAD36504; TM_1434. DR EnsemblBacteria; AGL50364; AGL50364; Tmari_1440. DR GeneID; 898041; -. DR KEGG; tma:TM1434; -. DR KEGG; tmi:THEMA_07145; -. DR KEGG; tmm:Tmari_1440; -. DR KEGG; tmw:THMA_1464; -. DR PATRIC; 23937816; VBITheMar51294_1446. DR eggNOG; ENOG4105K4S; Bacteria. DR eggNOG; COG3862; LUCA. DR OMA; FTCIVCP; -. DR OrthoDB; EOG6CGCG2; -. DR BioCyc; TMAR243274:GC6P-1472-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.10.530.10; -; 1. DR InterPro; IPR012460; DUF1667. DR Pfam; PF07892; DUF1667; 1. DR SUPFAM; SSF160148; SSF160148; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 138 AA; 15281 MW; 1F2C8BA233E35E56 CRC64; MFKNVVCVQC PIGCKIKVEL TEDGHIKSIT GNRCPRGVEY AKDEIKDPKR VVPTSIRVLN GELPLASVKT DKPIPKRFIP ELMKIVREIK VEAPVKAGDV VLRDLFGTGA NLVVTRTVRR LENGSKEIQK DSTGWSDG // ID Q9WY78_THEMA Unreviewed; 426 AA. AC Q9WY78; G4FHF0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 117. DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}; DE EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}; DE AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_02019}; GN Name=murF {ECO:0000256|HAMAP-Rule:MF_02019}; GN OrderedLocusNames=TM_0236 {ECO:0000313|EMBL:AAD35327.1}; GN ORFNames=Tmari_0234 {ECO:0000313|EMBL:AGL49160.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35327.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35327.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35327.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49160.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49160.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Involved in cell wall formation. Catalyzes the final CC step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the CC precursor of murein. {ECO:0000256|HAMAP-Rule:MF_02019, CC ECO:0000256|RuleBase:RU004136}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D- CC glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N- CC acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D- CC alanine. {ECO:0000256|HAMAP-Rule:MF_02019, CC ECO:0000256|RuleBase:RU004136}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019, CC ECO:0000256|RuleBase:RU004136}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily. CC {ECO:0000256|HAMAP-Rule:MF_02019}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35327.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49160.1; -; Genomic_DNA. DR PIR; F72402; F72402. DR RefSeq; NP_228050.1; NC_000853.1. DR RefSeq; WP_004082934.1; NZ_CP011107.1. DR PDB; 3ZL8; X-ray; 1.65 A; A=1-426. DR PDBsum; 3ZL8; -. DR STRING; 243274.TM0236; -. DR DNASU; 897136; -. DR EnsemblBacteria; AAD35327; AAD35327; TM_0236. DR EnsemblBacteria; AGL49160; AGL49160; Tmari_0234. DR GeneID; 897136; -. DR KEGG; tma:TM0236; -. DR KEGG; tmi:THEMA_03545; -. DR KEGG; tmm:Tmari_0234; -. DR KEGG; tmw:THMA_0243; -. DR PATRIC; 23935347; VBITheMar51294_0239. DR eggNOG; ENOG4107EES; Bacteria. DR eggNOG; COG0770; LUCA. DR KO; K01929; -. DR OMA; KVQHFDT; -. DR OrthoDB; EOG6PKFCR; -. DR BioCyc; TMAR243274:GC6P-249-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.1390.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_02019; MurF; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR005863; UDP-N-AcMur_synth. DR PANTHER; PTHR23135:SF3; PTHR23135:SF3; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR SUPFAM; SSF63418; SSF63418; 1. DR TIGRFAMs; TIGR01143; murF; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3ZL8}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU003630}; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU003630, ECO:0000313|EMBL:AAD35327.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU003630}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU004136}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 11 53 Mur_ligase. {ECO:0000259|Pfam:PF01225}. FT DOMAIN 87 271 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 290 367 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. FT NP_BIND 89 95 ATP. {ECO:0000256|HAMAP-Rule:MF_02019}. FT NP_BIND 91 95 ADP. {ECO:0000213|PDB:3ZL8}. FT NP_BIND 258 260 ADP. {ECO:0000213|PDB:3ZL8}. FT NP_BIND 307 310 ADP. {ECO:0000213|PDB:3ZL8}. FT BINDING 264 264 ADP. {ECO:0000213|PDB:3ZL8}. FT BINDING 293 293 ADP. {ECO:0000213|PDB:3ZL8}. FT BINDING 405 405 ADP. {ECO:0000213|PDB:3ZL8}. SQ SEQUENCE 426 AA; 47897 MW; BDF0E2EFEF6326A9 CRC64; MKDLLTRRFV LNSKEVREGD VFVAVKGKRF DGHDFIDEAL RNGAYAIIAE RKTVNSDRIF LVESSVDTLA KLAREKLGNF SGTVVGVTGS SGKTTTKEIL YNLLKNKRSV FKTPGNMNTE YGLPLSILND YKGEEILVLE MAASRPGDIA HLCKIAPPDV AVLLNVGSAH LEFFGTRERI METKMEIIKH SKENAIAVTL FDDPDLRKEV PRYRNTLFFG KEGGDSVLKD WWYYEGSTIA EFEAFDSLFT VKLSGYWNGG QLLNIAASLC VMRTLGETVD IFDLASLKTV PGRFNVREKK GVLIVDDTYN ASPEAFQTSI EALLRFPGKK FAVVGAMKEL GERSKEFHEE LGERLNVLDG VYVFLSEPEA EWIKSKKIIL KSDDPEKIAK DLATRVKKGD VVLFKASRAV RIERVLEMFE KELEKR // ID Q9WXX4_THEMA Unreviewed; 184 AA. AC Q9WXX4; G4FH35; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Oxidoreductase, putative {ECO:0000313|EMBL:AAD35214.1}; GN OrderedLocusNames=TM_0120 {ECO:0000313|EMBL:AAD35214.1}; GN ORFNames=Tmari_0118 {ECO:0000313|EMBL:AGL49044.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35214.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35214.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35214.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49044.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49044.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35214.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49044.1; -; Genomic_DNA. DR PIR; H72414; H72414. DR RefSeq; NP_227936.1; NC_000853.1. DR RefSeq; WP_004082703.1; NZ_CP011107.1. DR STRING; 243274.TM0120; -. DR EnsemblBacteria; AAD35214; AAD35214; TM_0120. DR EnsemblBacteria; AGL49044; AGL49044; Tmari_0118. DR GeneID; 896947; -. DR KEGG; tma:TM0120; -. DR KEGG; tmm:Tmari_0118; -. DR KEGG; tmw:THMA_0116; -. DR PATRIC; 23935080; VBITheMar51294_0118. DR eggNOG; ENOG4108ZWN; Bacteria. DR eggNOG; COG0778; LUCA. DR OMA; DNERPYM; -. DR OrthoDB; EOG6423FV; -. DR BioCyc; TMAR243274:GC6P-120-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.109.10; -; 1. DR InterPro; IPR029479; Nitroreductase. DR InterPro; IPR000415; Nitroreductase-like. DR Pfam; PF00881; Nitroreductase; 1. DR SUPFAM; SSF55469; SSF55469; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 164 Nitroreductase. FT {ECO:0000259|Pfam:PF00881}. SQ SEQUENCE 184 AA; 21651 MW; CAFE01387556EA5B CRC64; MLYDLAKQRK TVRKFKEEKP SIEKLMYCLK VANEAPSGMN AQPWRFLVVK DEETKRQIRE TCEKAEKDFY ENVRGKLKEW LNENSFNWKK PFLEEAPYLL LVFSKKDAPY SRESVWLAIG YLLLALEEQG LGTVPYTPPN PNELTKIVNT PSDLRFEVIL PVGYPDDPKP KYPREEMKVS FNHF // ID Q9X0A9_THEMA Unreviewed; 293 AA. AC Q9X0A9; G4FEY0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Permease of the drug/metabolite transporter (DMT) superfamily {ECO:0000313|EMBL:AGL49944.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36094.1}; GN OrderedLocusNames=TM_1017 {ECO:0000313|EMBL:AAD36094.1}; GN ORFNames=Tmari_1020 {ECO:0000313|EMBL:AGL49944.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36094.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36094.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36094.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49944.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49944.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36094.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49944.1; -; Genomic_DNA. DR PIR; A72306; A72306. DR RefSeq; NP_228823.1; NC_000853.1. DR RefSeq; WP_004080516.1; NZ_CP011107.1. DR STRING; 243274.TM1017; -. DR EnsemblBacteria; AAD36094; AAD36094; TM_1017. DR EnsemblBacteria; AGL49944; AGL49944; Tmari_1020. DR GeneID; 897206; -. DR KEGG; tma:TM1017; -. DR KEGG; tmi:THEMA_09270; -. DR KEGG; tmm:Tmari_1020; -. DR KEGG; tmw:THMA_1039; -. DR PATRIC; 23936963; VBITheMar51294_1030. DR eggNOG; ENOG4105SX7; Bacteria. DR eggNOG; COG0697; LUCA. DR OMA; TYFMLAS; -. DR OrthoDB; EOG68H8B8; -. DR BioCyc; TMAR243274:GC6P-1046-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 5 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 29 51 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 138 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 163 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 175 194 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 206 228 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 235 255 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 261 280 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 6 135 EamA. {ECO:0000259|Pfam:PF00892}. FT DOMAIN 146 279 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 293 AA; 32619 MW; 11EE3D692B180D71 CRC64; MDLRVLLSGL AYSTIFGLSF LFTKNALDYV TPLTFLSFRF IVAFLSYLLL LITGAVKLGK KPYWKLWKLV LFQPVLYFLF ETYGLQRVNS SEAGMIIALI PIVVNLLAPF ILKEKGDLLH YLLVGMGFLG VSLIVGFNIT PGNIVGKVFM LLAVLSGAMY SVFSRKFSKE FTPTEITFFM MMTGAVFFTL LSLSTGDFRP VFNVDVVIGA LYLGVLSSTV AFFLLNYAIR KLSPIFTTLF SNFTTVVSVI AGVVFRNETV GIQQIAGMGL IISSLIIMSL RRSYKRLSRA QKL // ID Q9WZJ6_THEMA Unreviewed; 395 AA. AC Q9WZJ6; G4FD86; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35818.1}; GN OrderedLocusNames=TM_0737 {ECO:0000313|EMBL:AAD35818.1}; GN ORFNames=Tmari_0738 {ECO:0000313|EMBL:AGL49663.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35818.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35818.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35818.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49663.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49663.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35818.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49663.1; -; Genomic_DNA. DR PIR; D72339; D72339. DR RefSeq; NP_228546.1; NC_000853.1. DR RefSeq; WP_004080989.1; NZ_CP011107.1. DR STRING; 243274.TM0737; -. DR EnsemblBacteria; AAD35818; AAD35818; TM_0737. DR EnsemblBacteria; AGL49663; AGL49663; Tmari_0738. DR GeneID; 898404; -. DR KEGG; tma:TM0737; -. DR KEGG; tmi:THEMA_00970; -. DR KEGG; tmm:Tmari_0738; -. DR KEGG; tmw:THMA_0755; -. DR PATRIC; 23936394; VBITheMar51294_0750. DR eggNOG; ENOG4108KCY; Bacteria. DR eggNOG; COG2908; LUCA. DR OMA; NHDYYIL; -. DR OrthoDB; EOG6K13PJ; -. DR BioCyc; TMAR243274:GC6P-763-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.60.21.10; -; 3. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR Pfam; PF00149; Metallophos; 1. DR SUPFAM; SSF56300; SSF56300; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 157 Metallophos. {ECO:0000259|Pfam:PF00149}. SQ SEQUENCE 395 AA; 46554 MW; BEBAB469806FC708 CRC64; MFISDLHIGD GSAKDDFFFD KELVNFIEDM SQTEDVELFV VGDGFEILES RTVKEIGLVS FEEVVETLDE TVIDEIEKKH SEVFETLKKF SRRHRVYYVV GNHDYHILKN KKLQNALKNR FEKFEILPYY YDPHSKLLVL HGNQFDVINR FTVDRKTKKV IPPLGDYIAR YMMINFDSQV VNFAPEDVIR DYDNVRPLLD VFHWFDYVTE IYDLSVDLVE LWLKSFLSML KTREARKWMK NNFPRTHWLS KVFVNRFGGV ELGKVLVRSI YTLRKLRRVD YLQKWAKSIL KGNLRWKEFM TGYSGDLHEV EEVDILVMGH VHHFAYRIVP TTQGKKLYVN CGSWRPVLEK LGIRKRHGFH RKAELPKIIM DFSGKNVEVK ASITNVLGKI QGGDL // ID Q9X104_THEMA Unreviewed; 664 AA. AC Q9X104; G4FE71; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Cell division protein FtsA {ECO:0000313|EMBL:AGL50206.1}; DE SubName: Full=Cell division protein FtsA, putative {ECO:0000313|EMBL:AAD36352.1}; GN OrderedLocusNames=TM_1277 {ECO:0000313|EMBL:AAD36352.1}; GN ORFNames=Tmari_1282 {ECO:0000313|EMBL:AGL50206.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36352.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36352.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36352.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50206.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50206.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36352.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50206.1; -; Genomic_DNA. DR PIR; A72273; A72273. DR RefSeq; NP_229082.1; NC_000853.1. DR RefSeq; WP_004079959.1; NZ_CP011107.1. DR STRING; 243274.TM1277; -. DR EnsemblBacteria; AAD36352; AAD36352; TM_1277. DR EnsemblBacteria; AGL50206; AGL50206; Tmari_1282. DR GeneID; 898206; -. DR KEGG; tma:TM1277; -. DR KEGG; tmi:THEMA_07950; -. DR KEGG; tmm:Tmari_1282; -. DR KEGG; tmw:THMA_1302; -. DR PATRIC; 23937492; VBITheMar51294_1292. DR eggNOG; ENOG4107RK5; Bacteria. DR eggNOG; COG0849; LUCA. DR OMA; MVPMAGD; -. DR OrthoDB; EOG6TR0B6; -. DR BioCyc; TMAR243274:GC6P-1308-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0007049; P:cell cycle; IEA:InterPro. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR InterPro; IPR003494; SHS2_FtsA. DR SMART; SM00842; FtsA; 1. PE 4: Predicted; KW Cell cycle {ECO:0000313|EMBL:AAD36352.1}; KW Cell division {ECO:0000313|EMBL:AAD36352.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 192 FtsA. {ECO:0000259|SMART:SM00842}. SQ SEQUENCE 664 AA; 73610 MW; EE5D03AEF7CAC1F6 CRC64; MIFALDVGTR KIAGLIAVEE KGTIRIVDSE LIEHKTRTMF DGQVHDVLGV AETVKEVKER LESRNEIELK EVAVALAGRF LKTQVGEAEL DFSKVGHITR EDVMKLEIEA VTKAQESVEE DFFCVGYSVV EYRLDGMWMK KLEGHRGGKA YVKVVSAFLP VHVVDSLMRV LETVGLTPVH VTLEPIAAMD LTVPEDLRYL NISLVDVGAG TSDIAISKEG TVVAYGMIPM AGDEITEAIG KKFLLDFQTA EHVKRTVFSE ERVKVKNILD REIELNVREV SEAIKPVVDQ ITTEISTVVT ELNGGAPSVV MVVGGGAKVP GFVESLARKL DLPLDRVSLK SVESTGLVED LTGKVKGSEY ITPVGIAYSA MRNRGSVFSQ VFVNGVPVKL MGGVGRYSVM QVLIQAGYRF SSLVGGEMIS FELNGKTLLR PKRRTSVKIF VNGEEANLSS RVKHGDRIDI QTEEEETPLR IKDLVKPVKV KLPDGGVEEV FPEIVKNGTP VPPDADVEEG DVVSFPEKIK ISEIKSKISY GKTRIVVNGE EKWISLVNFD LLKGEVPLKD DEEVPLGEEI DLVEKGRKTL EEALEVPHIT VSFNGELKKI PLKILHRIDE ERVELKDFKP MVIDLLKDLK LDGLKDYELL KNGRRAMFTE LLEDGDVIEF RIKK // ID Q9X0B8_THEMA Unreviewed; 293 AA. AC Q9X0B8; G4FEX0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 109. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36105.1}; GN OrderedLocusNames=TM_1028 {ECO:0000313|EMBL:AAD36105.1}; GN ORFNames=Tmari_1032 {ECO:0000313|EMBL:AGL49956.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36105.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36105.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36105.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49956.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49956.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36105.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49956.1; -; Genomic_DNA. DR PIR; C72303; C72303. DR RefSeq; NP_228834.1; NC_000853.1. DR RefSeq; WP_004080497.1; NZ_CP011107.1. DR STRING; 243274.TM1028; -. DR EnsemblBacteria; AAD36105; AAD36105; TM_1028. DR EnsemblBacteria; AGL49956; AGL49956; Tmari_1032. DR GeneID; 897095; -. DR KEGG; tma:TM1028; -. DR KEGG; tmi:THEMA_09220; -. DR KEGG; tmm:Tmari_1032; -. DR KEGG; tmw:THMA_1050; -. DR PATRIC; 23936985; VBITheMar51294_1041. DR eggNOG; ENOG4105CIG; Bacteria. DR eggNOG; COG1131; LUCA. DR KO; K01990; -. DR OMA; STTIRIM; -. DR OrthoDB; EOG65J54C; -. DR BioCyc; TMAR243274:GC6P-1057-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD36105.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD36105.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 229 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 293 AA; 33580 MW; E4A069F6248FB0AF CRC64; MSVVEVRDLT KYYGKSRGVE GVTFSVEEGE IFGFIGPNGA GKTTTIRLLL GLIFPDSGLA EIFGKDVLKE GKEIRKNVGY IPGEVSFYPE VTVEEFLRYS ASFYEKVDWD YVKELCGVFS LDTKKRIKEL SMGNKKKVAI VQALMHRPKL LILDEPTNGL DPIVQNTFFE ILKNEKEKGT TVFFSSHILS EVERLCDRVA MIKDGRIIRV EKVENLKGER YKVVRVKGEN LEKLKDLAEV NRLKFENGTA EFLFSGNVER LLEILRSLKL SDFWVEEPSL EEIFMSYYRE GEE // ID Q9WXX3_THEMA Unreviewed; 285 AA. AC Q9WXX3; G4FH34; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Acetamidase, putative {ECO:0000313|EMBL:AAD35213.1}; GN OrderedLocusNames=TM_0119 {ECO:0000313|EMBL:AAD35213.1}; GN ORFNames=Tmari_0117 {ECO:0000313|EMBL:AGL49043.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35213.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35213.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35213.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49043.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49043.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35213.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49043.1; -; Genomic_DNA. DR PIR; G72414; G72414. DR RefSeq; NP_227935.1; NC_000853.1. DR RefSeq; WP_004082702.1; NZ_CP011107.1. DR PDB; 2F4L; X-ray; 2.50 A; A/B/C/D=1-285. DR PDBsum; 2F4L; -. DR STRING; 243274.TM0119; -. DR DNASU; 896946; -. DR EnsemblBacteria; AAD35213; AAD35213; TM_0119. DR EnsemblBacteria; AGL49043; AGL49043; Tmari_0117. DR GeneID; 896946; -. DR KEGG; tma:TM0119; -. DR KEGG; tmi:THEMA_04210; -. DR KEGG; tmm:Tmari_0117; -. DR KEGG; tmw:THMA_0115; -. DR PATRIC; 23935078; VBITheMar51294_0117. DR eggNOG; ENOG4105D9J; Bacteria. DR eggNOG; COG2421; LUCA. DR KO; K01426; -. DR OMA; PYKPHIG; -. DR OrthoDB; EOG6QP0ZJ; -. DR BioCyc; TMAR243274:GC6P-119-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR004304; FmdA_AmdA. DR Pfam; PF03069; FmdA_AmdA; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2F4L}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000213|PDB:2F4L}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000213|PDB:2F4L}. FT METAL 146 146 Zinc 1. {ECO:0000213|PDB:2F4L}. FT METAL 148 148 Zinc 1. {ECO:0000213|PDB:2F4L}. FT METAL 173 173 Zinc 1. {ECO:0000213|PDB:2F4L}. FT METAL 173 173 Zinc 2. {ECO:0000213|PDB:2F4L}. FT METAL 175 175 Zinc 2; via tele nitrogen. FT {ECO:0000213|PDB:2F4L}. FT METAL 189 189 Zinc 2. {ECO:0000213|PDB:2F4L}. SQ SEQUENCE 285 AA; 31196 MW; 131E9167BD6DDDBE CRC64; MKVVPAQRCV YSFSANMAPV EEVYPGEQVV FETLDALGGS YDKIDFSKVN PATGPVFVNG VKPGDTLKVR IKRIELPRRG MIVTGKGFGV LGDEVEGFHT KELEIEKWAV LFDGVRIPIH PMVGVIGVAP QEGEYPTGTA HRHGGNMDTK EITENVTVHL PVFQEGALLA LGDVHATMGD GEVCVSACEV PAKVVVEIDV SKEEIKWPVV ETNDAYYIIV SLPDIEEALK EVTRETVWFI QRRKTIPFTD AYMLASLSVD VGISQLVNPA KTAKARIPKY IFTGV // ID Q9X0B7_THEMA Unreviewed; 111 AA. AC Q9X0B7; G4FEX1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36104.1}; GN OrderedLocusNames=TM_1027 {ECO:0000313|EMBL:AAD36104.1}; GN ORFNames=Tmari_1031 {ECO:0000313|EMBL:AGL49955.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36104.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36104.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36104.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49955.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49955.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36104.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49955.1; -; Genomic_DNA. DR PIR; B72303; B72303. DR RefSeq; NP_228833.1; NC_000853.1. DR RefSeq; WP_004080499.1; NZ_CP011107.1. DR STRING; 243274.TM1027; -. DR EnsemblBacteria; AAD36104; AAD36104; TM_1027. DR EnsemblBacteria; AGL49955; AGL49955; Tmari_1031. DR GeneID; 897056; -. DR KEGG; tma:TM1027; -. DR KEGG; tmi:THEMA_09225; -. DR KEGG; tmm:Tmari_1031; -. DR KEGG; tmw:THMA_1049; -. DR PATRIC; 23936983; VBITheMar51294_1040. DR eggNOG; ENOG4105V8J; Bacteria. DR eggNOG; ENOG4112105; LUCA. DR OrthoDB; EOG6HQSPK; -. DR BioCyc; TMAR243274:GC6P-1056-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 111 AA; 12259 MW; D1229EF20A92CF33 CRC64; MSSEFLGVQG NIARYSATYS MGTVFPQKAE LIGFPSIGPF YIHPDLLKKD VVLEIPDIGF VWQNEPGSYG VDSVIYFNGQ ECYRASCYEN GLAAEIKTVQ TGLVIVQQLV E // ID Q9X157_THEMA Unreviewed; 642 AA. AC Q9X157; G4FF74; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36407.1}; GN OrderedLocusNames=TM_1335 {ECO:0000313|EMBL:AAD36407.1}; GN ORFNames=Tmari_1343 {ECO:0000313|EMBL:AGL50267.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36407.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36407.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36407.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50267.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50267.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36407.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50267.1; -; Genomic_DNA. DR PIR; G72265; G72265. DR RefSeq; NP_229137.1; NC_000853.1. DR RefSeq; WP_004081534.1; NZ_CP011107.1. DR STRING; 243274.TM1335; -. DR EnsemblBacteria; AAD36407; AAD36407; TM_1335. DR EnsemblBacteria; AGL50267; AGL50267; Tmari_1343. DR GeneID; 898147; -. DR KEGG; tma:TM1335; -. DR KEGG; tmi:THEMA_07670; -. DR KEGG; tmm:Tmari_1343; -. DR KEGG; tmw:THMA_1359; -. DR PATRIC; 23937603; VBITheMar51294_1347. DR OMA; STERSEY; -. DR OrthoDB; EOG6DJXWQ; -. DR BioCyc; TMAR243274:GC6P-1366-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 642 AA; 75711 MW; 76C852484CC2F37D CRC64; MLEIVAFRGD EYGLSARILA DFLDEFRIHE MSPDNFNGKE EIENDFIIVC NPKLLTENFL RQAYEYSRDR GIYFGVISAL SIDLLREKLA NYQEQISLDP QQYLIILRKE NKSIKHRLNA EVFTRYESTV DNFDRVKHKK LCLSMVIDGN RRHLHLSDGK ICGINRDIPL EEIYRYFPDC QNCEYERVYA QDVQAECIFM DSCSSTLIST SEKGEYINVG MNFLKNAKVL ISSYRPKQGY NSEALLFHHL ISHGFEAGEV LYILNTNSYN HCSDYLPYIL YGFPNAKVTI PEKLEVDRLR MGKSEIVLEI DRIAGMRLLE IHAGEDILNE VLKRQFYVFS SDEIRKDVFY SVIPYPLKNS IKLFLYSWEE VNGPLRIVFG VGKRLREDVY SKRYFNMRKL ELLGFRHKKI QNQVHDYFSK INEQTEVLDE ANRNLKNFDL HRLSKNLSAV EERIYNLLAD HLLSQNPKFF IEVYGENMTV RCAEEDLHKT IRCPYCGNYL SIKESENTLV PMKRYSGFCS NCHNVFDTES VHPPKYPEIV LVHEQPDRKI FYVKVWNENA HTTNNLVCFN LWCENRSEME NIYLSRDFQV FTLEPGGEEK FEVEVALKRT DQRINKTYCL YVYWFEDFNL SVSTYTFRLK NV // ID Q9X0G1_THEMA Unreviewed; 236 AA. AC Q9X0G1; G4FES6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Rhamnulose-1-phosphate aldolase {ECO:0000313|EMBL:AGL50000.1}; DE EC=4.1.2.19 {ECO:0000313|EMBL:AGL50000.1}; DE SubName: Full=Sugar-phosphate aldolase {ECO:0000313|EMBL:AAD36149.1}; GN OrderedLocusNames=TM_1072 {ECO:0000313|EMBL:AAD36149.1}; GN ORFNames=Tmari_1076 {ECO:0000313|EMBL:AGL50000.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36149.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36149.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36149.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50000.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50000.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36149.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50000.1; -; Genomic_DNA. DR PIR; B72299; B72299. DR RefSeq; NP_228878.1; NC_000853.1. DR RefSeq; WP_004080415.1; NZ_CP011107.1. DR PDB; 1PVT; X-ray; 2.50 A; A=1-236. DR PDBsum; 1PVT; -. DR STRING; 243274.TM1072; -. DR DNASU; 897053; -. DR EnsemblBacteria; AAD36149; AAD36149; TM_1072. DR EnsemblBacteria; AGL50000; AGL50000; Tmari_1076. DR GeneID; 897053; -. DR KEGG; tma:TM1072; -. DR KEGG; tmi:THEMA_09000; -. DR KEGG; tmm:Tmari_1076; -. DR KEGG; tmw:THMA_1094; -. DR PATRIC; 23937073; VBITheMar51294_1085. DR eggNOG; ENOG4105C9J; Bacteria. DR eggNOG; COG0235; LUCA. DR KO; K01629; -. DR OMA; THLMIHA; -. DR OrthoDB; EOG61GGBF; -. DR BioCyc; TMAR243274:GC6P-1101-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central. DR GO; GO:0008994; F:rhamnulose-1-phosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. DR Gene3D; 3.40.225.10; -; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; SSF53639; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1PVT}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000313|EMBL:AGL50000.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 6 219 Aldolase_II. {ECO:0000259|SMART:SM01007}. SQ SEQUENCE 236 AA; 26753 MW; D9B974E41D65B687 CRC64; MRETIREIQK VAYWLAIKGL SEANAGNISV RLDERPEGYE VKSVNEYGFD YDGPEMYLLI TATGSRMREV YEDDSKICLL HVLPGKHYEI LHGNGKPTSE FPTHLMIHAK FKEMNPEKKA IVHTHPLNLL TLMNLEEFQE LLPKMMKIHP EVLIFFPQGI SVVEFEKPGS VELGLKTVEK SEGKDAVLWD KHGVVAFGKD VAEAYDRVEI LEKAAEILLR VLSLGRNPTG VPEGWL // ID Q9X076_THEMA Unreviewed; 118 AA. AC Q9X076; G4FF14; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Putative ACR involved in intracellular sulfur reduction {ECO:0000313|EMBL:AGL49909.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36060.1}; GN OrderedLocusNames=TM_0981 {ECO:0000313|EMBL:AAD36060.1}; GN ORFNames=Tmari_0984 {ECO:0000313|EMBL:AGL49909.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36060.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36060.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36060.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49909.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49909.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36060.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49909.1; -; Genomic_DNA. DR PIR; B72310; B72310. DR RefSeq; NP_228789.1; NC_000853.1. DR RefSeq; WP_004080583.1; NZ_CP011107.1. DR STRING; 243274.TM0981; -. DR EnsemblBacteria; AAD36060; AAD36060; TM_0981. DR EnsemblBacteria; AGL49909; AGL49909; Tmari_0984. DR GeneID; 898727; -. DR KEGG; tma:TM0981; -. DR KEGG; tmi:THEMA_09445; -. DR KEGG; tmm:Tmari_0984; -. DR KEGG; tmw:THMA_1003; -. DR PATRIC; 23936891; VBITheMar51294_0994. DR eggNOG; ENOG4105K2M; Bacteria. DR eggNOG; COG1553; LUCA. DR KO; K07235; -. DR OMA; ACIAASK; -. DR OrthoDB; EOG61VZ8Q; -. DR BioCyc; TMAR243274:GC6P-1011-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.1260.10; -; 1. DR InterPro; IPR027396; DsrEFH-like. DR InterPro; IPR003787; Sulphur_relay_DrsE/F-like. DR Pfam; PF02635; DrsE; 1. DR SUPFAM; SSF75169; SSF75169; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 115 DrsE. {ECO:0000259|Pfam:PF02635}. SQ SEQUENCE 118 AA; 13175 MW; E516B9F1A2420F1E CRC64; MKIGIQVMVP PYTYEDLDTA IKIAEAAMEK GHEVTLFLFA DSVICTNKNI KPIKIDRNIP QKLVELMQKG NFEVHICGIC MDYRGITTDM IIEGSKPSGL PELANLIATC DRFINLMA // ID Q9X088_THEMA Unreviewed; 101 AA. AC Q9X088; G4FF02; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36072.1}; GN OrderedLocusNames=TM_0993 {ECO:0000313|EMBL:AAD36072.1}; GN ORFNames=Tmari_0997 {ECO:0000313|EMBL:AGL49922.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36072.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36072.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36072.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49922.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49922.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36072.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49922.1; -; Genomic_DNA. DR PIR; G72308; G72308. DR RefSeq; NP_228801.1; NC_000853.1. DR RefSeq; WP_004080564.1; NZ_CP011107.1. DR STRING; 243274.TM0993; -. DR EnsemblBacteria; AAD36072; AAD36072; TM_0993. DR EnsemblBacteria; AGL49922; AGL49922; Tmari_0997. DR GeneID; 897076; -. DR KEGG; tma:TM0993; -. DR KEGG; tmi:THEMA_09385; -. DR KEGG; tmm:Tmari_0997; -. DR KEGG; tmw:THMA_1015; -. DR PATRIC; 23936917; VBITheMar51294_1007. DR eggNOG; ENOG4108E51; Bacteria. DR eggNOG; ENOG41103IX; LUCA. DR OrthoDB; EOG6PW269; -. DR BioCyc; TMAR243274:GC6P-1023-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 101 AA; 11413 MW; FD69D1F94849C1D8 CRC64; MGYDFTFPST ITSCSLVSVS ELETTKAIPW SLSNKPDFVE NVYALTVEGI TQDGTKTFFS LPMIEVSGEL YFWTIYIYSY EQKDVVPTPA TEVRMYPTPS L // ID Q9X1A2_THEMA Unreviewed; 199 AA. AC Q9X1A2; G4FFB8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE SubName: Full=NUDIX hydrolase domain-containing protein {ECO:0000313|EMBL:AGL50313.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36452.1}; GN OrderedLocusNames=TM_1382 {ECO:0000313|EMBL:AAD36452.1}; GN ORFNames=Tmari_1389 {ECO:0000313|EMBL:AGL50313.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36452.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36452.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36452.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50313.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50313.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36452.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50313.1; -; Genomic_DNA. DR PIR; G72261; G72261. DR RefSeq; NP_229183.1; NC_000853.1. DR RefSeq; WP_004081580.1; NZ_CP011107.1. DR PDB; 3E57; X-ray; 1.89 A; A/B=1-199. DR PDBsum; 3E57; -. DR STRING; 243274.TM1382; -. DR DNASU; 898096; -. DR EnsemblBacteria; AAD36452; AAD36452; TM_1382. DR EnsemblBacteria; AGL50313; AGL50313; Tmari_1389. DR GeneID; 898096; -. DR KEGG; tma:TM1382; -. DR KEGG; tmi:THEMA_07415; -. DR KEGG; tmm:Tmari_1389; -. DR KEGG; tmw:THMA_1409; -. DR PATRIC; 23937706; VBITheMar51294_1394. DR eggNOG; ENOG4108ZPF; Bacteria. DR eggNOG; COG4112; LUCA. DR OMA; RQVIPYI; -. DR OrthoDB; EOG6XM7CX; -. DR BioCyc; TMAR243274:GC6P-1417-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00293; NUDIX; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3E57}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50313.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 54 192 Nudix hydrolase. FT {ECO:0000259|PROSITE:PS51462}. SQ SEQUENCE 199 AA; 23077 MW; B42B4394D4CCA3B2 CRC64; MKSERILVVK TEDFLKEFGE FEGFMRVNFE DFLNFLDQYG FFRERDEAEY DETTKQVIPY VVIMDGDRVL ITKRTTKQSE KRLHNLYSLG IGGHVREGDG ATPREAFLKG LEREVNEEVD VSLRELEFLG LINSSTTEVS RVHLGALFLG RGKFFSVKEK DLFEWELIKL EELEKFSGVM EGWSKISAAV LLNLFLTQN // ID Q9WYK1_THEMA Unreviewed; 225 AA. AC Q9WYK1; G4FHS9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=DUF124 domain-containing protein {ECO:0000313|EMBL:AGL49290.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35454.1}; GN OrderedLocusNames=TM_0367 {ECO:0000313|EMBL:AAD35454.1}; GN ORFNames=Tmari_0365 {ECO:0000313|EMBL:AGL49290.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35454.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35454.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35454.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49290.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49290.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35454.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49290.1; -; Genomic_DNA. DR PIR; G72387; G72387. DR RefSeq; NP_228178.1; NC_000853.1. DR RefSeq; WP_004083177.1; NZ_CP011107.1. DR STRING; 243274.TM0367; -. DR EnsemblBacteria; AAD35454; AAD35454; TM_0367. DR EnsemblBacteria; AGL49290; AGL49290; Tmari_0365. DR GeneID; 897326; -. DR KEGG; tma:TM0367; -. DR KEGG; tmi:THEMA_02880; -. DR KEGG; tmm:Tmari_0365; -. DR KEGG; tmw:THMA_0375; -. DR PATRIC; 23935615; VBITheMar51294_0372. DR eggNOG; ENOG4105ECD; Bacteria. DR eggNOG; COG2013; LUCA. DR OMA; EPGAMVY; -. DR OrthoDB; EOG6GJBSD; -. DR BioCyc; TMAR243274:GC6P-381-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.60.160.10; -; 1. DR InterPro; IPR002838; AIM24. DR InterPro; IPR016031; Trp_RNA-bd_attenuator-like_dom. DR Pfam; PF01987; AIM24; 1. DR SUPFAM; SSF51219; SSF51219; 1. DR TIGRFAMs; TIGR00266; TIGR00266; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 225 AA; 24300 MW; 96BC7BD410B5358D CRC64; MKYEIVLKGS YALLKVFLST GESVVVEPGA MVYMKGPIEV KTSATGGVWK ALKRAILGGE NFFMNTYISR GESEIGLAPQ LPGDIDVIPL KDILYVQSTS FLACDPSVEM DVSFGGLKSF FSGEGIFLLK FIGHGDVAVS SFGGIKSVEL QPGEEFTVDT GHVVAFDGTV KWNVRTFGGL KSTLFGGEGL VCTFTGPGRV YIQTRNYPAF VEWIKSLVPR QTGSR // ID Q9X0E5_THEMA Unreviewed; 171 AA. AC Q9X0E5; G4FEU3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36132.1}; GN OrderedLocusNames=TM_1055 {ECO:0000313|EMBL:AAD36132.1}; GN ORFNames=Tmari_1059 {ECO:0000313|EMBL:AGL49983.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36132.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36132.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36132.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49983.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49983.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36132.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49983.1; -; Genomic_DNA. DR PIR; A72302; A72302. DR RefSeq; NP_228861.1; NC_000853.1. DR RefSeq; WP_004080450.1; NZ_CP011107.1. DR PDB; 1RCU; X-ray; 2.50 A; A/B/C/D=1-171. DR PDBsum; 1RCU; -. DR STRING; 243274.TM1055; -. DR EnsemblBacteria; AAD36132; AAD36132; TM_1055. DR EnsemblBacteria; AGL49983; AGL49983; Tmari_1059. DR GeneID; 896979; -. DR KEGG; tma:TM1055; -. DR KEGG; tmi:THEMA_09085; -. DR KEGG; tmm:Tmari_1059; -. DR KEGG; tmw:THMA_1077; -. DR PATRIC; 23937039; VBITheMar51294_1068. DR eggNOG; ENOG4107ZNN; Bacteria. DR eggNOG; COG1611; LUCA. DR KO; K06966; -. DR OMA; QMRSFIL; -. DR OrthoDB; EOG6QRWB5; -. DR BioCyc; TMAR243274:GC6P-1084-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IBA:GO_Central. DR GO; GO:0009691; P:cytokinin biosynthetic process; IBA:GO_Central. DR InterPro; IPR005268; CHP00725. DR InterPro; IPR031100; LOG_fam. DR Pfam; PF03641; Lysine_decarbox; 1. DR TIGRFAMs; TIGR00725; TIGR00725; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1RCU}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 171 AA; 18435 MW; B56AB696EA8FC4AD CRC64; MKKVVVVGYS GPVNKSPVSE LRDICLELGR TLAKKGYLVF NGGRDGVMEL VSQGVREAGG TVVGILPDEE AGNPYLSVAV KTGLDFQMRS FVLLRNADVV VSIGGEIGTA IEILGAYALG KPVILLRGTG GWTDRISQVL IDGKYLDNRR IVEIHQAWTV EEAVQIIEQI L // ID Q9WZJ8_THEMA Unreviewed; 279 AA. AC Q9WZJ8; G4FD84; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Two-component response regulator {ECO:0000313|EMBL:AGL49665.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35820.1}; GN OrderedLocusNames=TM_0739 {ECO:0000313|EMBL:AAD35820.1}; GN ORFNames=Tmari_0740 {ECO:0000313|EMBL:AGL49665.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35820.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35820.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35820.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49665.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49665.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35820.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49665.1; -; Genomic_DNA. DR PIR; F72339; F72339. DR RefSeq; NP_228548.1; NC_000853.1. DR RefSeq; WP_004080985.1; NZ_CP011107.1. DR STRING; 243274.TM0739; -. DR EnsemblBacteria; AAD35820; AAD35820; TM_0739. DR EnsemblBacteria; AGL49665; AGL49665; Tmari_0740. DR GeneID; 898406; -. DR KEGG; tma:TM0739; -. DR KEGG; tmi:THEMA_00960; -. DR KEGG; tmm:Tmari_0740; -. DR KEGG; tmw:THMA_0757; -. DR PATRIC; 23936398; VBITheMar51294_0752. DR eggNOG; ENOG4108W7Q; Bacteria. DR eggNOG; COG2206; LUCA. DR OMA; VERDRIH; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-765-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR006675; HDIG_dom. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00277; HDIG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 106 240 HDc. {ECO:0000259|SMART:SM00471}. SQ SEQUENCE 279 AA; 32035 MW; B1C6494321C85B3B CRC64; MKCFFESEEF EKAVEKIDRL YEKVDSIEEA EIAFLREKKP FQGVAVVKEE TYTIYKTGEK LVELEDPEKA ASIAYILAGE KLLSGGWVRR MVSGLLQAMI VLMEIEDENG WSHSQRVARL AERVGKKLGL SEEKLSLLRE YAMLHDVGKI GIEQLMLYTP TRIRIFEQYP QDHTIMGSVF LASLEVLWDV VPIVRHHHEN WDGTGYPDGL KGEEIPLEAR IISVCDYYDV LTNFVSSEWE GRTKTHEEAL EIIKKEAGKK FDPKVVEAFL EIFSDEAVE // ID Q9X274_THEMA Unreviewed; 329 AA. AC Q9X274; G4FGD8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 101. DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:AAD36817.1}; DE SubName: Full=Endoglucanase C307 (Endo-1,4-beta-glucanase C307) (Cellulase C307) {ECO:0000313|EMBL:AGL50684.1}; DE EC=3.2.1.4 {ECO:0000313|EMBL:AGL50684.1}; GN OrderedLocusNames=TM_1752 {ECO:0000313|EMBL:AAD36817.1}; GN ORFNames=Tmari_1760 {ECO:0000313|EMBL:AGL50684.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36817.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36817.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36817.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50684.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50684.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) CC family. {ECO:0000256|RuleBase:RU361153}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36817.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50684.1; -; Genomic_DNA. DR PIR; C72216; C72216. DR RefSeq; NP_229550.1; NC_000853.1. DR RefSeq; WP_004082285.1; NZ_CP011107.1. DR PDB; 1VJZ; X-ray; 2.05 A; A=1-329. DR PDBsum; 1VJZ; -. DR STRING; 243274.TM1752; -. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR DNASU; 897117; -. DR EnsemblBacteria; AAD36817; AAD36817; TM_1752. DR EnsemblBacteria; AGL50684; AGL50684; Tmari_1760. DR GeneID; 897117; -. DR KEGG; tma:TM1752; -. DR KEGG; tmm:Tmari_1760; -. DR KEGG; tmw:THMA_1794; -. DR PATRIC; 23938480; VBITheMar51294_1770. DR eggNOG; ENOG4105CTM; Bacteria. DR eggNOG; COG2730; LUCA. DR KO; K01179; -. DR OMA; HRAPGYC; -. DR OrthoDB; EOG6F2949; -. DR BioCyc; TMAR243274:GC6P-1800-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0006073; P:cellular glucan metabolic process; IBA:GO_Central. DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF00150; Cellulase; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VJZ}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361153, KW ECO:0000313|EMBL:AGL50684.1}; KW Hydrolase {ECO:0000256|RuleBase:RU361153, KW ECO:0000313|EMBL:AGL50684.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 26 294 Cellulase. {ECO:0000259|Pfam:PF00150}. SQ SEQUENCE 329 AA; 39301 MW; 7BA353E02AC65979 CRC64; MNNTIPRWRG FNLLEAFSIK STGNFKEEDF LWMAQWDFNF VRIPMCHLLW SDRGNPFIIR EDFFEKIDRV IFWGEKYGIH ICISLHRAPG YSVNKEVEEK TNLWKDETAQ EAFIHHWSFI ARRYKGISST HLSFNLINEP PFPDPQIMSV EDHNSLIKRT ITEIRKIDPE RLIIIDGLGY GNIPVDDLTI ENTVQSCRGY IPFSVTHYKA EWVDSKDFPV PEWPNGWHFG EYWNREKLLE HYLTWIKLRQ KGIEVFCGEM GAYNKTPHDV VLKWLEDLLE IFKTLNIGFA LWNFRGPFGI LDSERKDVEY EEWYGHKLDR KMLELLRKY // ID Q9X1Z7_THEMA Unreviewed; 34 AA. AC Q9X1Z7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36736.1}; GN OrderedLocusNames=TM_1669 {ECO:0000313|EMBL:AAD36736.1}; GN ORFNames=Tmari_1678 {ECO:0000313|EMBL:AGL50602.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36736.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36736.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36736.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50602.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50602.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36736.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50602.1; -; Genomic_DNA. DR PIR; C72225; C72225. DR RefSeq; NP_229469.1; NC_000853.1. DR RefSeq; WP_010865379.1; NZ_CP011107.1. DR EnsemblBacteria; AAD36736; AAD36736; TM_1669. DR EnsemblBacteria; AGL50602; AGL50602; Tmari_1678. DR GeneID; 897905; -. DR KEGG; tma:TM1669; -. DR KEGG; tmm:Tmari_1678; -. DR KEGG; tmw:THMA_1710; -. DR OrthoDB; EOG632DDT; -. DR BioCyc; TMAR243274:GC6P-1715-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 34 AA; 3920 MW; EA49D2EED5C10A3D CRC64; MISVDGKYYS FSLDIVQKDE GTEVRLYPKP QSIL // ID Q9X0H6_THEMA Unreviewed; 173 AA. AC Q9X0H6; G4FEQ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36167.1}; GN OrderedLocusNames=TM_1091 {ECO:0000313|EMBL:AAD36167.1}; GN ORFNames=Tmari_1096 {ECO:0000313|EMBL:AGL50020.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36167.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36167.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36167.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50020.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50020.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36167.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50020.1; -; Genomic_DNA. DR PIR; B72298; B72298. DR RefSeq; NP_228897.1; NC_000853.1. DR RefSeq; WP_004080370.1; NZ_CP011107.1. DR STRING; 243274.TM1091; -. DR EnsemblBacteria; AAD36167; AAD36167; TM_1091. DR EnsemblBacteria; AGL50020; AGL50020; Tmari_1096. DR GeneID; 898675; -. DR KEGG; tma:TM1091; -. DR KEGG; tmi:THEMA_08895; -. DR KEGG; tmm:Tmari_1096; -. DR KEGG; tmw:THMA_1114; -. DR PATRIC; 23937113; VBITheMar51294_1105. DR eggNOG; ENOG4108E52; Bacteria. DR eggNOG; ENOG41103IW; LUCA. DR OMA; VSWLDVI; -. DR OrthoDB; EOG6S52M3; -. DR BioCyc; TMAR243274:GC6P-1120-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 173 AA; 19456 MW; 46DCDD966C1BF44C CRC64; MKILVGSPVS LEEFETIDLF ISWLDVIPDN ARFSIVGTSK FFIIGKNGRE WKKGYEFGIV DADINIFVVG GDLALYPEVF YIAKENGAKL VVGFCEIQNF IDFNFVKAKF WAHTQETSLA SIVLLNFLGK VHNNIYFPLE KTKNQTGVVA EGVAPVFLEL KKNFFSSEEA EDV // ID Q9WZ69_THEMA Unreviewed; 447 AA. AC Q9WZ69; G4FDL9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=NAD(FAD)-utilizing dehydrogenase {ECO:0000313|EMBL:AGL49524.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35685.1}; GN OrderedLocusNames=TM_0600 {ECO:0000313|EMBL:AAD35685.1}; GN ORFNames=Tmari_0599 {ECO:0000313|EMBL:AGL49524.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35685.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35685.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35685.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49524.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49524.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35685.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49524.1; -; Genomic_DNA. DR PIR; A72358; A72358. DR RefSeq; NP_228410.1; NC_000853.1. DR RefSeq; WP_004081235.1; NZ_CP011107.1. DR STRING; 243274.TM0600; -. DR DNASU; 897678; -. DR EnsemblBacteria; AAD35685; AAD35685; TM_0600. DR EnsemblBacteria; AGL49524; AGL49524; Tmari_0599. DR GeneID; 897678; -. DR KEGG; tma:TM0600; -. DR KEGG; tmi:THEMA_01665; -. DR KEGG; tmm:Tmari_0599; -. DR KEGG; tmw:THMA_0616; -. DR PATRIC; 23936115; VBITheMar51294_0611. DR eggNOG; ENOG4107QYN; Bacteria. DR eggNOG; COG2509; LUCA. DR KO; K07137; -. DR OMA; GQNFREQ; -. DR OrthoDB; EOG67X1P7; -. DR BioCyc; TMAR243274:GC6P-625-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR SUPFAM; SSF51905; SSF51905; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 447 AA; 51344 MW; 62D88EEA22BBC1D4 CRC64; MLKRLGIVGF GASAIGFING LIESGKVKDY RITVLERGKD YSHNTISGVR MDGKIFISHG MGGEIYIPLE IQAKTVEFYL KFSGYTPTVD KRVGIVNYLK SFERDGRKIE FGESFSDEEI YKRFYHHGFE PVKSYFFHLG TDILKETNKN IYEYFSSFEN IEFLFGTTVE DVEFGPPHRV HTNRGDFEFD ELVIAVGRSG HRLMERLKEK YPQLVRPNQF VDIGVRYELP NHVMDPFSDM YEVKVRYRTK TGYICRIFCQ NPAGKVTLEK YEDFTTVNGY SDSLHKTENT NFAILVTTRF TEPFKDPTGY GVNLAKLANI LAGDKEKVIL QTYGDFKEFR RTKRLGRVHP TLDSESYILG DANLVFPSKI RESLVDFVEN LEKVIPGASY FDNLLYAVEV KFYTNKFLND IVEGLHVVGD CSGWTRSIQY ATSMGYMRAV GMKIQSL // ID Q9WYT1_THEMA Unreviewed; 100 AA. AC Q9WYT1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35533.1}; GN OrderedLocusNames=TM_0450 {ECO:0000313|EMBL:AAD35533.1}; GN ORFNames=Tmari_0447 {ECO:0000313|EMBL:AGL49372.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35533.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35533.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35533.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49372.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49372.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35533.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49372.1; -; Genomic_DNA. DR PIR; C72375; C72375. DR RefSeq; NP_228260.1; NC_000853.1. DR RefSeq; WP_010865123.1; NC_000853.1. DR STRING; 243274.TM0450; -. DR EnsemblBacteria; AAD35533; AAD35533; TM_0450. DR EnsemblBacteria; AGL49372; AGL49372; Tmari_0447. DR GeneID; 897469; -. DR KEGG; tma:TM0450; -. DR KEGG; tmm:Tmari_0447; -. DR PATRIC; 23935785; VBITheMar51294_0456. DR OrthoDB; EOG6MSS8R; -. DR BioCyc; TMAR243274:GC6P-465-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 100 AA; 11588 MW; B2EA70599060294C CRC64; MLSFRNWWAR EDSNPRPPGY EPGALPTELR AHTAIRLYSN KTPLSRSVIS MKKDPIKEML VKYPRILVIK AALKILKDGN KIDRERIEKT IVKIMTKKEG // ID Q9X0T4_THEMA Unreviewed; 107 AA. AC Q9X0T4; G4FED9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Na(+) H(+) antiporter subunit G {ECO:0000313|EMBL:AGL50138.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36282.1}; GN OrderedLocusNames=TM_1207 {ECO:0000313|EMBL:AAD36282.1}; GN ORFNames=Tmari_1214 {ECO:0000313|EMBL:AGL50138.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36282.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36282.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36282.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50138.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50138.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36282.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50138.1; -; Genomic_DNA. DR PIR; E72280; E72280. DR RefSeq; NP_229012.1; NC_000853.1. DR RefSeq; WP_004080104.1; NZ_CP011107.1. DR STRING; 243274.TM1207; -. DR EnsemblBacteria; AAD36282; AAD36282; TM_1207. DR EnsemblBacteria; AGL50138; AGL50138; Tmari_1214. DR GeneID; 898277; -. DR KEGG; tma:TM1207; -. DR KEGG; tmi:THEMA_08295; -. DR KEGG; tmm:Tmari_1214; -. DR KEGG; tmw:THMA_1233; -. DR PATRIC; 23937356; VBITheMar51294_1225. DR eggNOG; ENOG410845S; Bacteria. DR eggNOG; COG1320; LUCA. DR KO; K05571; -. DR OMA; FVGVPLW; -. DR OrthoDB; EOG6VF36X; -. DR BioCyc; TMAR243274:GC6P-1237-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005451; F:monovalent cation:proton antiporter activity; IEA:InterPro. DR InterPro; IPR005133; PhaG_MnhG_YufB. DR Pfam; PF03334; PhaG_MnhG_YufB; 1. DR TIGRFAMs; TIGR01300; CPA3_mnhG_phaG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 82 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 107 AA; 11278 MW; 5DAF092FD5026395 CRC64; MNEVIGEVLI AIGAFFYFLG GLGVFRMPDV YNRLQAGTKA TTLGTFSTVL GIGIAKPEFL LKAIVIIAFI ALTNPVGSSV LARASYLSGV KPCECTVIDE YKGGDEG // ID Q9WYB2_THEMA Unreviewed; 340 AA. AC Q9WYB2; G4FHI9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 100. DE SubName: Full=Transcriptional regulator, GntR family {ECO:0000313|EMBL:AAD35364.1}; DE SubName: Full=Transcriptional repressor of the arabinose operon {ECO:0000313|EMBL:AGL49199.1}; GN OrderedLocusNames=TM_0275 {ECO:0000313|EMBL:AAD35364.1}; GN ORFNames=Tmari_0273 {ECO:0000313|EMBL:AGL49199.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35364.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35364.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35364.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49199.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49199.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 HTH gntR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000706}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35364.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49199.1; -; Genomic_DNA. DR PIR; A72398; A72398. DR RefSeq; NP_228088.1; NC_000853.1. DR RefSeq; WP_004082979.1; NZ_CP011107.1. DR STRING; 243274.TM0275; -. DR EnsemblBacteria; AAD35364; AAD35364; TM_0275. DR EnsemblBacteria; AGL49199; AGL49199; Tmari_0273. DR GeneID; 897190; -. DR KEGG; tma:TM0275; -. DR KEGG; tmi:THEMA_03350; -. DR KEGG; tmm:Tmari_0273; -. DR KEGG; tmw:THMA_0282; -. DR PATRIC; 23935427; VBITheMar51294_0279. DR eggNOG; ENOG4105CMD; Bacteria. DR eggNOG; COG1609; LUCA. DR KO; K02103; -. DR KO; K03710; -. DR OMA; EDMAKKG; -. DR OrthoDB; EOG64BQ72; -. DR BioCyc; TMAR243274:GC6P-288-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00392; GntR; 1. DR PRINTS; PR00035; HTHGNTR. DR SMART; SM00345; HTH_GNTR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF53822; SSF53822; 1. DR PROSITE; PS50949; HTH_GNTR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000706}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU000706}; KW Transcription regulation {ECO:0000256|RuleBase:RU000706}. FT DOMAIN 1 59 HTH gntR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50949}. SQ SEQUENCE 340 AA; 38650 MW; 10AE4A95C344F9E3 CRC64; MIDEIKSGKY KHGDKLPTEK ELMERFNASR ETVRKALERL VVKNLVIRKP GLGTFVNIEK KNKVVGILVQ QITSYIFPYI ALGAEEVLFA NGYKMLLGNA SEDPHKERQI INEWLEVGVD GLIIDPVYSA TKRSNRDLIE DMAKKGTKVV LVHTNWDIEG VGSVVLDDWY GGEKAAEIFY QYGHRNVAVL YKTIHLPSVV RAQAFLKRGR ELGFEKVHEK SFHVSEFTGI VMQSAFELLS LPKDQRPTAV FCYNDATALQ FFLAAKRMGL KIPEDVSVIG FDDAPIGDFR EILTTFEHPK EEVGKKAVEI LLKMIDGEKP EKYVFKPKLI MRESVTYPKK // ID Q9WYR2_THEMA Unreviewed; 286 AA. AC Q9WYR2; G4FHZ0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 91. DE SubName: Full=Multiple sugar ABC transporter, membrane-spanning permease protein MsmF {ECO:0000313|EMBL:AGL49353.1}; DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35516.1}; GN OrderedLocusNames=TM_0431 {ECO:0000313|EMBL:AAD35516.1}; GN ORFNames=Tmari_0428 {ECO:0000313|EMBL:AGL49353.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35516.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35516.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35516.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49353.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49353.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35516.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49353.1; -; Genomic_DNA. DR PIR; G72379; G72379. DR RefSeq; NP_228241.1; NC_000853.1. DR RefSeq; WP_004083320.1; NZ_CP011107.1. DR STRING; 243274.TM0431; -. DR DNASU; 897444; -. DR EnsemblBacteria; AAD35516; AAD35516; TM_0431. DR EnsemblBacteria; AGL49353; AGL49353; Tmari_0428. DR GeneID; 897444; -. DR KEGG; tma:TM0431; -. DR KEGG; tmi:THEMA_02570; -. DR KEGG; tmm:Tmari_0428; -. DR KEGG; tmw:THMA_0437; -. DR PATRIC; 23935747; VBITheMar51294_0437. DR eggNOG; ENOG4105D5X; Bacteria. DR eggNOG; COG1175; LUCA. DR KO; K17242; -. DR OMA; ATMWKWM; -. DR OrthoDB; EOG69SKBS; -. DR BioCyc; TMAR243274:GC6P-446-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 37 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 66 92 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 104 123 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 152 176 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 197 219 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 225 247 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 259 279 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 62 278 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 286 AA; 32742 MW; CB3D14E86D47C5E2 CRC64; MIRSLVRSRF IFVLPGLVFL VLFVAVPVIS VFIMGFFKWN LLSPPRFVGL ENFKMLLKDK WFWNSVWVSI KLLLLAVPMQ FFVSLGLALC LYEETTASKI LRAFFYWPYM MPAVAGTTMW KWLLSYDIGL LNHILRTLGL PPVPWLIKPF PALFSIALLR TWGMTGLLMV MFITGLQNVP QDYIEAAMID GANRWQRFWY VVFPAMSNTN LLVLMTAIAH TLRSFAGVYV LTTGGPGYAT TIIPLYIYQT AFTQFRIGYS YAASVIYFLI AFAIAMITLK LRESRS // ID Q9X1D4_THEMA Unreviewed; 318 AA. AC Q9X1D4; G4FFF1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Iron-sulfur cluster assembly protein SufB {ECO:0000313|EMBL:AGL50346.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36487.1}; GN OrderedLocusNames=TM_1416 {ECO:0000313|EMBL:AAD36487.1}; GN ORFNames=Tmari_1422 {ECO:0000313|EMBL:AGL50346.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36487.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36487.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36487.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50346.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50346.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36487.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50346.1; -; Genomic_DNA. DR PIR; F72255; F72255. DR RefSeq; NP_229217.1; NC_000853.1. DR RefSeq; WP_004081655.1; NZ_CP011107.1. DR STRING; 243274.TM1416; -. DR EnsemblBacteria; AAD36487; AAD36487; TM_1416. DR EnsemblBacteria; AGL50346; AGL50346; Tmari_1422. DR GeneID; 898059; -. DR KEGG; tma:TM1416; -. DR KEGG; tmi:THEMA_07235; -. DR KEGG; tmm:Tmari_1422; -. DR KEGG; tmw:THMA_1446; -. DR PATRIC; 23937778; VBITheMar51294_1427. DR eggNOG; ENOG4107WVB; Bacteria. DR eggNOG; COG0719; LUCA. DR KO; K07033; -. DR OMA; PVHLCFG; -. DR OrthoDB; EOG6QZMP4; -. DR BioCyc; TMAR243274:GC6P-1454-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR InterPro; IPR000825; SUF_FeS_clus_asmbl_SufBD. DR Pfam; PF01458; UPF0051; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 318 AA; 35341 MW; 77C50CC49D50EC7E CRC64; MIVKDYRREF EALAKAYEKA GGDVSKFLDR RIASIIISGD KVIGLNGVEG VELTPYRIEN GVQVDMRIKE GVVVEYPVHV CTGYLEKKGL QRVVFNIRLE KNAKAIFVAH CVFPWTEDFT HDALMNVELE EGAWMEYHDE HTHSETGSIN LITRSIARVG ERAVYRNTFT LVKTRIGTLR VFMDASLEKD AVGELYTKVK AVEDDDVEVK EILRLNGMGA RGLAKTNAVA IDRAKVSVVN EVYGNAPHTR GHVECLEIAK GDGVDVRALP VLVVKNDSSE LTHEASIGRV NAKQLETLMA KGLTEEEATE MIIKGILT // ID Q9WYY8_THEMA Unreviewed; 64 AA. AC Q9WYY8; G4FDV3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35603.1}; GN OrderedLocusNames=TM_0518 {ECO:0000313|EMBL:AAD35603.1}; GN ORFNames=Tmari_0514 {ECO:0000313|EMBL:AGL49439.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35603.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35603.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35603.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49439.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49439.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35603.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49439.1; -; Genomic_DNA. DR PIR; D72365; D72365. DR RefSeq; NP_228328.1; NC_000853.1. DR RefSeq; WP_004081411.1; NZ_CP011107.1. DR STRING; 243274.TM0518; -. DR EnsemblBacteria; AAD35603; AAD35603; TM_0518. DR EnsemblBacteria; AGL49439; AGL49439; Tmari_0514. DR GeneID; 897565; -. DR KEGG; tma:TM0518; -. DR KEGG; tmi:THEMA_02085; -. DR KEGG; tmm:Tmari_0514; -. DR KEGG; tmw:THMA_0530; -. DR PATRIC; 23935941; VBITheMar51294_0525. DR eggNOG; ENOG4105Z7Q; Bacteria. DR eggNOG; ENOG41123SF; LUCA. DR OMA; GICCECL; -. DR OrthoDB; EOG6DC6QF; -. DR BioCyc; TMAR243274:GC6P-542-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 64 AA; 7553 MW; 1C5CD1B7ABC1F773 CRC64; MKACPNKERN LSYCNCSYPG CPRKGICCEC MHYHRQHGEL PACYFPNDAE KTWDRSIEHF KRVV // ID Q9WY27_THEMA Unreviewed; 267 AA. AC Q9WY27; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Nitrilase/cyanide hydratase and apolipoprotein N-acyltransferase {ECO:0000313|EMBL:AGL49107.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35276.1}; GN OrderedLocusNames=TM_0183 {ECO:0000313|EMBL:AAD35276.1}; GN ORFNames=Tmari_0181 {ECO:0000313|EMBL:AGL49107.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35276.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35276.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35276.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49107.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49107.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35276.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49107.1; -; Genomic_DNA. DR PIR; B72408; B72408. DR RefSeq; NP_227998.1; NC_000853.1. DR RefSeq; WP_010865067.1; NZ_CP011107.1. DR STRING; 243274.TM0183; -. DR EnsemblBacteria; AAD35276; AAD35276; TM_0183. DR EnsemblBacteria; AGL49107; AGL49107; Tmari_0181. DR GeneID; 897031; -. DR KEGG; tma:TM0183; -. DR KEGG; tmi:THEMA_03860; -. DR KEGG; tmm:Tmari_0181; -. DR KEGG; tmw:THMA_0184; -. DR PATRIC; 23935222; VBITheMar51294_0184. DR eggNOG; ENOG4105CQP; Bacteria. DR eggNOG; COG0388; LUCA. DR OMA; YRICAAP; -. DR OrthoDB; EOG6CVV93; -. DR BioCyc; TMAR243274:GC6P-189-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR Gene3D; 3.60.110.10; -; 1. DR InterPro; IPR003010; C-N_Hydrolase. DR Pfam; PF00795; CN_hydrolase; 1. DR SUPFAM; SSF56317; SSF56317; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000313|EMBL:AGL49107.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lipoprotein {ECO:0000313|EMBL:AGL49107.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49107.1}. FT DOMAIN 1 261 CN hydrolase. FT {ECO:0000259|PROSITE:PS50263}. SQ SEQUENCE 267 AA; 30068 MW; 2BC9B9D0707FD81D CRC64; MRVAAVQMLP AIGDFEGNLE RIEQFIEMAV SEGAEVVVFP ELTISGYTWD EAILKRGALF FSEVAKKKLL KLSREGQILI AVGTPRVVLG KLRNSLVIFK KKKELLFYDK THLFRGEKNV FEPGEYFLVF SYRGVVFGTL ICYEIGFPEI SRILTFKGSK VILSAFAFGK ARGHTYDVAT RSRAVENGVF LVASSMCGEG FVEFVGRTRI VGPNGKVMNE IESGEGLICE DLDLDAVYHY RYDEEGDSHA YLRNYISHLY TLQKGRL // ID Q9WZB1_THEMA Unreviewed; 468 AA. AC Q9WZB1; G4FDI1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Clostripain-related protein {ECO:0000313|EMBL:AAD35727.1}; GN OrderedLocusNames=TM_0643 {ECO:0000313|EMBL:AAD35727.1}; GN ORFNames=Tmari_0643 {ECO:0000313|EMBL:AGL49568.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35727.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35727.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35727.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49568.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49568.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35727.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49568.1; -; Genomic_DNA. DR PIR; B72351; B72351. DR RefSeq; NP_228452.1; NC_000853.1. DR RefSeq; WP_004081155.1; NZ_CP011107.1. DR STRING; 243274.TM0643; -. DR DNASU; 897747; -. DR EnsemblBacteria; AAD35727; AAD35727; TM_0643. DR EnsemblBacteria; AGL49568; AGL49568; Tmari_0643. DR GeneID; 897747; -. DR KEGG; tma:TM0643; -. DR KEGG; tmi:THEMA_01450; -. DR KEGG; tmm:Tmari_0643; -. DR KEGG; tmw:THMA_0658; -. DR PATRIC; 23936200; VBITheMar51294_0653. DR eggNOG; ENOG4108X2E; Bacteria. DR eggNOG; ENOG4111KB4; LUCA. DR OMA; DHGSAWI; -. DR OrthoDB; EOG6PGK59; -. DR BioCyc; TMAR243274:GC6P-668-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.60.40.920; -; 1. DR InterPro; IPR003344; Big_1_dom. DR InterPro; IPR008964; Invasin/intimin_cell_adhesion. DR InterPro; IPR005077; Peptidase_C11. DR Pfam; PF03415; Peptidase_C11; 1. DR SMART; SM00634; BID_1; 1. DR SUPFAM; SSF49373; SSF49373; 1. DR PROSITE; PS51127; BIG1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 21 113 Big-1 (bacterial Ig-like domain 1). FT {ECO:0000259|PROSITE:PS51127}. SQ SEQUENCE 468 AA; 52060 MW; 3C626AB04DBE3FCA CRC64; MRWFLLIVVS ALFLSGCMPE IYTHASTPST IIADNETHIA GRYAFVDVQV LDEYGLPVSG EDVSFYVDGA FLGEATTDTS GVARIGFFSP SEKTYTFTAV AGGVSRSFDV SFTKPKWLFI VWMAADNNLY YYSEDDLSEM RNASGSVSVV VVYDGIGIGD GMLVLDESGN FQAVVGTMGI DFNSGSYTNL EAWLEMILNQ FDADHYALVI WDHGSAWIGD SYYISTKVIG YDDFQGTAIA VSNLRKALEN ALSGDKLDIL GFDACLMGSL EVIYELRNTA DYIVASSFNE PAEGWDYSFL GEIAPDSTPL DVARMIVDSY REYYSSDTYQ NELSLAVYDT SQVEVFVSDL NLFISDLKAD LSKVDAVYSD VVKSYIDDYN QTVLVDLGDF IDRWVSSSRI TTAPDLSSVV VYSYGEIAGK TLSFPISIFM PESMSCYQDY QTDYQTLSFP YDTQWDEFLE YWLNQKGG // ID Q9WZQ1_THEMA Unreviewed; 488 AA. AC Q9WZQ1; G4FD30; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35876.1}; GN OrderedLocusNames=TM_0794 {ECO:0000313|EMBL:AAD35876.1}; GN ORFNames=Tmari_0795 {ECO:0000313|EMBL:AGL49720.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35876.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35876.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35876.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49720.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49720.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35876.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49720.1; -; Genomic_DNA. DR PIR; C72334; C72334. DR RefSeq; NP_228603.1; NC_000853.1. DR RefSeq; WP_004080878.1; NZ_CP011107.1. DR STRING; 243274.TM0794; -. DR EnsemblBacteria; AAD35876; AAD35876; TM_0794. DR EnsemblBacteria; AGL49720; AGL49720; Tmari_0795. DR GeneID; 898462; -. DR KEGG; tma:TM0794; -. DR KEGG; tmi:THEMA_00680; -. DR KEGG; tmm:Tmari_0795; -. DR KEGG; tmw:THMA_0813; -. DR PATRIC; 23936508; VBITheMar51294_0806. DR eggNOG; ENOG410615P; Bacteria. DR eggNOG; ENOG4111VM7; LUCA. DR KO; K01992; -. DR OMA; SEVMISK; -. DR OrthoDB; EOG6FRCV8; -. DR BioCyc; TMAR243274:GC6P-821-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 117 141 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 153 174 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 234 258 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 295 312 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 318 337 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 358 382 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 388 410 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 431 449 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 455 476 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 488 AA; 54906 MW; 443575A903A88A5D CRC64; MSASSQSSEG DGSPQTISMR KLSVLLRYAP ARGRKGLYSV LISVLMTGFL FYSLMGNNFK AILEEFGEEA FSASLSFSTT MFSVMFLLGV SFYLSNSLVL EGEIEFLLTL PVERSTIVIY QLLISLFYQS FILIMMVLNF FMYSLLMNNW MPFVTGVFHT VFLLLGGAIL SVLFGRLLRT SLSRKLYSLI QLLAVFLFLI LVNLPDFSVS FGRWFISNWN VFAYAVFSRE NPIFLLYEIL ICLGTFLVFR VISTTVMFEP VLRKERMPVE KPTRFPGKGF FKKDLITLLR EERSLYLLLY PIGFGVLMTF VGSPDFGLIF AIGIAALYNA TMSAMLWRKE MEVWPLPKVL PVKTSEVMIS KILVSSLLNS AVVSAFVIFL AIYQKQVFYI FFAPAGLSLF LFISALGLLL SKWEKTGSLT NPAKVFSGPE ILLLQLVAIG VVGVLGYALS TGSHLMFFSI LLATVVGSVF GFIWAFKRIV FRAERLEE // ID Q9WXZ0_THEMA Unreviewed; 450 AA. AC Q9WXZ0; G4FH57; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 110. DE SubName: Full=Response regulator {ECO:0000313|EMBL:AAD35236.1}; GN OrderedLocusNames=TM_0143 {ECO:0000313|EMBL:AAD35236.1}; GN ORFNames=Tmari_0141 {ECO:0000313|EMBL:AGL49067.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35236.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35236.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35236.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49067.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49067.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains GGDEF domain. CC {ECO:0000256|SAAS:SAAS00496774}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35236.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49067.1; -; Genomic_DNA. DR PIR; E72414; E72414. DR RefSeq; NP_227958.1; NC_000853.1. DR RefSeq; WP_004082745.1; NZ_CP011107.1. DR STRING; 243274.TM0143; -. DR EnsemblBacteria; AAD35236; AAD35236; TM_0143. DR EnsemblBacteria; AGL49067; AGL49067; Tmari_0141. DR GeneID; 896973; -. DR KEGG; tma:TM0143; -. DR KEGG; tmi:THEMA_04090; -. DR KEGG; tmm:Tmari_0141; -. DR KEGG; tmw:THMA_0138; -. DR PATRIC; 23935128; VBITheMar51294_0142. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR KO; K02488; -. DR OMA; FEKPTIP; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-143-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR Pfam; PF00990; GGDEF; 1. DR Pfam; PF00072; Response_reg; 1. DR SMART; SM00267; GGDEF; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR SUPFAM; SSF55073; SSF55073; 1. DR TIGRFAMs; TIGR00254; GGDEF; 1. DR PROSITE; PS50887; GGDEF; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 121 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT DOMAIN 321 450 GGDEF. {ECO:0000259|PROSITE:PS50887}. SQ SEQUENCE 450 AA; 51253 MW; C6E7CE545299DF1E CRC64; MKKVLIVDDS KFWRLVVSDI VKNIKKDVEI LLAEGGMDGL QKALNHRPDY FIIDYNMPDF SGLYLSVVLR EMKAFKDSGI VILTASSDTI NSFWAKKSGA NLFINKGKKE EIEKELQVFL NTPYESLKNC ESSESGNVFH IVEKRLKREI LEKEILSYLK YSRDERYVIS LLVMLFRNFS MFGSFRALLI STSEGRIYSF GKPVDKEVLR KFLISKLEKP TSPSFWSFHG AFGEGSISDD NISAVVKDDG TELGVVLFED VENPFLLRSA LEDSLSSLMV LFRNLNDFRD YVIASETDGL TGLFNKRAIM RFLEEVLRSE KNIAVAMMDI DDFKKINDTF GHPVGDEVLR VVANILRETV KIGKVGRYGG EEFMVVFETG ERDAVVKTMD NIMENIRNFD WQKIFGSEKK VTLSGGVAFS KKESSPVELI EEADKKLYTA KRSGKDRYVI // ID Q9X041_THEMA Unreviewed; 342 AA. AC Q9X041; G4FF46; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36025.1}; GN OrderedLocusNames=TM_0944 {ECO:0000313|EMBL:AAD36025.1}; GN ORFNames=Tmari_0946 {ECO:0000313|EMBL:AGL49871.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36025.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36025.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36025.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49871.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49871.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36025.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49871.1; -; Genomic_DNA. DR PIR; C72313; C72313. DR RefSeq; NP_228752.1; NC_000853.1. DR RefSeq; WP_004080618.1; NZ_CP011107.1. DR STRING; 243274.TM0944; -. DR EnsemblBacteria; AAD36025; AAD36025; TM_0944. DR EnsemblBacteria; AGL49871; AGL49871; Tmari_0946. DR GeneID; 898681; -. DR KEGG; tma:TM0944; -. DR KEGG; tmi:THEMA_09625; -. DR KEGG; tmm:Tmari_0946; -. DR KEGG; tmw:THMA_0967; -. DR PATRIC; 23936819; VBITheMar51294_0958. DR eggNOG; ENOG4106VXF; Bacteria. DR eggNOG; ENOG410YQGV; LUCA. DR OMA; IAYLCYW; -. DR OrthoDB; EOG6N0HG9; -. DR BioCyc; TMAR243274:GC6P-974-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR SUPFAM; SSF50998; SSF50998; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 342 AA; 38557 MW; 0AB09C8A70BD245A CRC64; MEGIQHLRYK LGTAALLVSL IVSVFAGILE TERIDLNVNP LRGTINEGVI TLVDSLKREV VAVNALSKRV TARFTGFSYP VWGMYLKGNF YVTDMFEGKF VELTPSGKRK REILLGGDPT VFLYHNGVFY ISLFSQGTLV GVDLRSFKVV ERYRTGVSST YFVPTSKGIA YLCYWRDEDD PDVIYLRYGS MTSVRLGLSR PLRYVEGSSG DYVLDYRNGW LVKLVNGKVV WKKNLPDFAY GISFYGPDIA VASLVSPVIS VVDRNGSVKQ INVPHPVLYL EEIENYLVAL SVEAEEIYLI KNDRVVQTVK TGKYPLKIFK ISEKEFAVLC TDSGELIFYT VY // ID Q9WY21_THEMA Unreviewed; 283 AA. AC Q9WY21; G4FH91; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=DUF370 and DUF2179 domains-containing protein {ECO:0000313|EMBL:AGL49101.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35270.1}; GN OrderedLocusNames=TM_0177 {ECO:0000313|EMBL:AAD35270.1}; GN ORFNames=Tmari_0175 {ECO:0000313|EMBL:AGL49101.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35270.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35270.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35270.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49101.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49101.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35270.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49101.1; -; Genomic_DNA. DR PIR; G72409; G72409. DR RefSeq; NP_227992.1; NC_000853.1. DR RefSeq; WP_004082812.1; NZ_CP011107.1. DR STRING; 243274.TM0177; -. DR EnsemblBacteria; AAD35270; AAD35270; TM_0177. DR EnsemblBacteria; AGL49101; AGL49101; Tmari_0175. DR GeneID; 897017; -. DR KEGG; tma:TM0177; -. DR KEGG; tmi:THEMA_03915; -. DR KEGG; tmm:Tmari_0175; -. DR KEGG; tmw:THMA_0173; -. DR PATRIC; 23935202; VBITheMar51294_0178. DR eggNOG; ENOG4108JYZ; Bacteria. DR eggNOG; COG1284; LUCA. DR OMA; IAYYIAM; -. DR OrthoDB; EOG6GXTV2; -. DR BioCyc; TMAR243274:GC6P-178-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR019264; DUF2179. DR InterPro; IPR003740; YitT. DR Pfam; PF10035; DUF2179; 1. DR Pfam; PF02588; YitT_membrane; 1. DR PIRSF; PIRSF006483; Membrane_protein_YitT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 106 125 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 145 168 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 220 274 DUF2179. {ECO:0000259|Pfam:PF10035}. SQ SEQUENCE 283 AA; 31202 MW; 30BC74CE64D6C74C CRC64; MIEKIKEYVL STLGTLITAV GLVVFLIPND IAAGGVSGLS IILHSFVPIP VGVWMYILNG LLFLIAFLTI GFDFSAKTIY CTFVFNFFVD LFDRIIPLPK YTGDDLFLAV FFGTILTASG LAITFSQNAS TGGTDILARI LNKYFWISMG TGLLMVDVAI AVLAGLVFSA RTGMYALLGV ILNGIMVDFM MRGIEQSSEV IIISEKCDDI KDFVLNVLQR GATYIPAKGA YTGKERKILL VVVRRRELNE LIRFIKKADP KAFVIIKEVR QALGEGFKEL EEL // ID Q9WY66_THEMA Unreviewed; 77 AA. AC Q9WY66; G4FHD7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 like protein) {ECO:0000313|EMBL:AGL49147.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35315.1}; GN OrderedLocusNames=TM_0223 {ECO:0000313|EMBL:AAD35315.1}; GN ORFNames=Tmari_0221 {ECO:0000313|EMBL:AGL49147.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35315.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35315.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35315.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49147.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49147.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35315.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49147.1; -; Genomic_DNA. DR PIR; B72401; B72401. DR RefSeq; NP_228038.1; NC_000853.1. DR RefSeq; WP_004082908.1; NZ_CP011107.1. DR STRING; 243274.TM0223; -. DR EnsemblBacteria; AAD35315; AAD35315; TM_0223. DR EnsemblBacteria; AGL49147; AGL49147; Tmari_0221. DR GeneID; 897120; -. DR KEGG; tma:TM0223; -. DR KEGG; tmi:THEMA_03610; -. DR KEGG; tmm:Tmari_0221; -. DR KEGG; tmw:THMA_0230; -. DR PATRIC; 23935318; VBITheMar51294_0225. DR eggNOG; COG1188; LUCA. DR OMA; VTDDMKY; -. DR OrthoDB; EOG64NB4B; -. DR BioCyc; TMAR243274:GC6P-236-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR025490; RNAbp_HP1423. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF01479; S4; 1. DR PIRSF; PIRSF038881; RNAbp_HP1423; 1. DR SMART; SM00363; S4; 1. DR PROSITE; PS50889; S4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Stress response {ECO:0000313|EMBL:AGL49147.1}. FT DOMAIN 1 60 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 77 AA; 8725 MW; 4D3C4364462DD18C CRC64; MRLDLFLKIS VVKRRTIAQK LLKGQRVLVN GRPAKASYEV KDGDIVEVFL PTKKIILRVV GNGGYEILSE ERVSKPF // ID Q9WYH9_THEMA Unreviewed; 253 AA. AC Q9WYH9; G4FHQ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:AAD35430.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL49267.1}; GN OrderedLocusNames=TM_0344 {ECO:0000313|EMBL:AAD35430.1}; GN ORFNames=Tmari_0342 {ECO:0000313|EMBL:AGL49267.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35430.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35430.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35430.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49267.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49267.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35430.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49267.1; -; Genomic_DNA. DR PIR; F72388; F72388. DR RefSeq; NP_228155.1; NC_000853.1. DR RefSeq; WP_004083127.1; NZ_CP011107.1. DR STRING; 243274.TM0344; -. DR EnsemblBacteria; AAD35430; AAD35430; TM_0344. DR EnsemblBacteria; AGL49267; AGL49267; Tmari_0342. DR GeneID; 897300; -. DR KEGG; tma:TM0344; -. DR KEGG; tmi:THEMA_02995; -. DR KEGG; tmm:Tmari_0342; -. DR KEGG; tmw:THMA_0352; -. DR PATRIC; 23935569; VBITheMar51294_0349. DR eggNOG; ENOG4108B6Y; Bacteria. DR eggNOG; COG0287; LUCA. DR KO; K04517; -. DR OMA; WHALESA; -. DR OrthoDB; EOG6B8XMB; -. DR BioCyc; TMAR243274:GC6P-358-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central. DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IBA:GO_Central. DR GO; GO:0008977; F:prephenate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR GO; GO:0006571; P:tyrosine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR003099; Prephen_DH. DR Pfam; PF02153; PDH; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS51176; PDH_ADH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49267.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 253 Prephenate/arogenate dehydrogenase. FT {ECO:0000259|PROSITE:PS51176}. SQ SEQUENCE 253 AA; 28780 MW; 063FD8F2B8900317 CRC64; MKISVLGAGC IGGSIALKLK EKHHVTAFDR DEETMKALEE NGIETVSKES DLYDTDLLVL ALPMSVEERF LKETDFSGKI LDVASVKTPF MEIARERGLN FTGGHPMAGN ERKGKSGWDR EMFDGKIFFL CSLDGKEDGM IENIVKDLGA RPLWIDYRIH DEIVAAVSHV QYLISLSARY VGKPFEEYAG PGYLSNTRLS KQNMEMALDM IRYNKENILK YLENARNFLN VLYHLTEKED FENLKKVIRE VIS // ID Q9WXQ7_THEMA Unreviewed; 154 AA. AC Q9WXQ7; G4FGW5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Ferrous iron transport protein A {ECO:0000313|EMBL:AGL48973.1}; DE SubName: Full=Iron(II) transport protein A {ECO:0000313|EMBL:AAD35144.1}; GN OrderedLocusNames=TM_0050 {ECO:0000313|EMBL:AAD35144.1}; GN ORFNames=Tmari_0047 {ECO:0000313|EMBL:AGL48973.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35144.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35144.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35144.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48973.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48973.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35144.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48973.1; -; Genomic_DNA. DR PIR; C72423; C72423. DR RefSeq; NP_227866.1; NC_000853.1. DR RefSeq; WP_004082532.1; NZ_CP011107.1. DR STRING; 243274.TM0050; -. DR EnsemblBacteria; AAD35144; AAD35144; TM_0050. DR EnsemblBacteria; AGL48973; AGL48973; Tmari_0047. DR GeneID; 896874; -. DR KEGG; tma:TM0050; -. DR KEGG; tmi:THEMA_04555; -. DR KEGG; tmm:Tmari_0047; -. DR KEGG; tmw:THMA_0046; -. DR PATRIC; 23934940; VBITheMar51294_0048. DR eggNOG; ENOG41084Q7; Bacteria. DR eggNOG; COG1918; LUCA. DR KO; K04758; -. DR OMA; AYRIYVR; -. DR OrthoDB; EOG6J48SS; -. DR BioCyc; TMAR243274:GC6P-50-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR InterPro; IPR007167; Fe-transptr_FeoA. DR InterPro; IPR008988; Transcriptional_repressor_C. DR Pfam; PF04023; FeoA; 2. DR SMART; SM00899; FeoA; 2. DR SUPFAM; SSF50037; SSF50037; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 73 FeoA. {ECO:0000259|SMART:SM00899}. FT DOMAIN 78 142 FeoA. {ECO:0000259|SMART:SM00899}. SQ SEQUENCE 154 AA; 17179 MW; BA9076E7D0309A78 CRC64; MKLSRLVPGV PARIKRLEVS GELHEKLVGM GFVPGEEIEI VQVAPLGDPI VCKIGNRNIT LRKREADLIE VEVVGGELPL ILADDGTYEI TKLNGGRRFL FRMKNLGIES GKKIQVSGRR YYIEGREIDL GYGEATKIWV RRVSDAGEES HPQK // ID Q9WZD9_THEMA Unreviewed; 304 AA. AC Q9WZD9; G4FDF3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=M-related protein {ECO:0000313|EMBL:AAD35755.1}; GN OrderedLocusNames=TM_0671 {ECO:0000313|EMBL:AAD35755.1}; GN ORFNames=Tmari_0671 {ECO:0000313|EMBL:AGL49596.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35755.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35755.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35755.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49596.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49596.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35755.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49596.1; -; Genomic_DNA. DR PIR; F72346; F72346. DR RefSeq; NP_228480.1; NC_000853.1. DR RefSeq; WP_004081101.1; NZ_CP011107.1. DR STRING; 243274.TM0671; -. DR DNASU; 897786; -. DR EnsemblBacteria; AAD35755; AAD35755; TM_0671. DR EnsemblBacteria; AGL49596; AGL49596; Tmari_0671. DR GeneID; 897786; -. DR KEGG; tma:TM0671; -. DR KEGG; tmi:THEMA_01310; -. DR KEGG; tmm:Tmari_0671; -. DR KEGG; tmw:THMA_0686; -. DR PATRIC; 23936256; VBITheMar51294_0681. DR eggNOG; ENOG4106FZD; Bacteria. DR eggNOG; ENOG410Y38C; LUCA. DR OMA; YISFEIN; -. DR OrthoDB; EOG63RGRK; -. DR BioCyc; TMAR243274:GC6P-696-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.10.220.30; -; 1. DR InterPro; IPR011002; FliG_a-hlx. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 28 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 86 151 {ECO:0000256|SAM:Coils}. FT COILED 206 240 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 304 AA; 35304 MW; 28495B4BCD024D43 CRC64; MPGKRRGFFV VFLITFLILV ILFMYGYISF EINRLYGGRV SPFEDWKSYI AFLASKVPFL KDRISYQPLK AESPAEYYSR IYQRYIEIYN QKIDELISKE KELEEQAKVL EAQRNVVEKM IEEIQSLKNQ LLEEKNRLES YKKQVDELVN VLLNTDPRNL ASALNEVDDE TLAVIFKRTD PEYAGEFLEA LSGVNPQKAA RVMELMVGVE STIERLETLV KQAQEAVKQI TEKESQLFQK EAYLKAVADA LNNITPEVAV DFLRREKVDP ETLRTVLSMM DREHASVLVQ YIVQNAPDLL EERK // ID Q9WZ70_THEMA Unreviewed; 120 AA. AC Q9WZ70; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35686.1}; GN OrderedLocusNames=TM_0601 {ECO:0000313|EMBL:AAD35686.1}; GN ORFNames=Tmari_0600 {ECO:0000313|EMBL:AGL49525.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35686.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35686.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35686.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49525.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49525.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35686.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49525.1; -; Genomic_DNA. DR PIR; B72358; B72358. DR RefSeq; NP_228411.1; NC_000853.1. DR RefSeq; WP_010865158.1; NZ_CP011107.1. DR STRING; 243274.TM0601; -. DR EnsemblBacteria; AAD35686; AAD35686; TM_0601. DR EnsemblBacteria; AGL49525; AGL49525; Tmari_0600. DR GeneID; 897679; -. DR KEGG; tma:TM0601; -. DR KEGG; tmi:THEMA_01660; -. DR KEGG; tmm:Tmari_0600; -. DR KEGG; tmw:THMA_0617; -. DR OMA; LICTREY; -. DR OrthoDB; EOG6D8BCQ; -. DR BioCyc; TMAR243274:GC6P-626-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 120 AA; 13759 MW; 4B4CBF1A63A68538 CRC64; MRQDSKEPPL DEKNGEKDDK TLPESEPVHV EDVKKQNGGY GTGNKTVREA LFHERTDSRV SEESGKDDSK KLSKRNIEHV EDGKKNEHTE KYQNHSKESQ VHPSLICTRE YSTTLKPVLE // ID Q9X2D1_THEMA Unreviewed; 717 AA. AC Q9X2D1; G4FGJ9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=CRISPR-associated protein, Csm1 family {ECO:0000313|EMBL:AGL50746.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36874.1}; GN OrderedLocusNames=TM_1811 {ECO:0000313|EMBL:AAD36874.1}; GN ORFNames=Tmari_1822 {ECO:0000313|EMBL:AGL50746.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36874.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36874.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36874.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50746.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50746.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36874.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50746.1; -; Genomic_DNA. DR PIR; H72208; H72208. DR RefSeq; NP_229608.1; NC_000853.1. DR RefSeq; WP_004082358.1; NZ_CP011107.1. DR STRING; 243274.TM1811; -. DR EnsemblBacteria; AAD36874; AAD36874; TM_1811. DR EnsemblBacteria; AGL50746; AGL50746; Tmari_1822. DR GeneID; 897829; -. DR KEGG; tma:TM1811; -. DR KEGG; tmi:THEMA_05135; -. DR KEGG; tmm:Tmari_1822; -. DR KEGG; tmw:THMA_1857; -. DR PATRIC; 23938611; VBITheMar51294_1832. DR eggNOG; ENOG410695F; Bacteria. DR eggNOG; COG1353; LUCA. DR KO; K07016; -. DR OMA; YIEAREN; -. DR OrthoDB; EOG632CZD; -. DR BioCyc; TMAR243274:GC6P-1862-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR013408; CRISPR-assoc_prot_Csm1. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR006674; HD_domain. DR Pfam; PF01966; HD; 1. DR TIGRFAMs; TIGR02578; cas_TM1811_Csm1; 1. DR PROSITE; PS50887; GGDEF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 489 622 GGDEF. {ECO:0000259|PROSITE:PS50887}. SQ SEQUENCE 717 AA; 83829 MW; FBEF3F39E03FA5F8 CRC64; MKDREELVVG ALLHDIGKVV RRAGDDRRHQ IAGYDFTNKV KKFAVIQDYI HYHHEKDLLK KSLENEKVWY VCFADNLSSK ERMTEDQKFE ELRRMVNLLS KIPEGESSRN VTYFPAKPAN EVVEAVKDMK EDQKTYEDLY RRFVEDAQKI SPTPDDVNFL TYKYFSFIPQ ETRVEGDMDI SLYDHLKVTA MLALSLYDYA KENDLKFESY QEMKSHFENS NVKPFLLVGG DVSGIQNFIA NVSSKGALRS YRGRSFFIEI LQEVVVDEIL DKTGFYRTNV HFIGGGHFYL VLSNTEKVKK ALEEIRNELN EWFRNRGLSL HLVIESVEFS VKDVEDMSKV FKKIGEKLNE RKYRMYTEKD LEAIFPDDLN LIQEKGNHTC KICGNRVDKL FSIREGEEEI ACDFCKEMYE LGRELLEESH VYLAERKNGK FEIFKRKFDF SREPGEGFSY KLRRIYEFSE KEKNVRRIQV VTYFKEQEFE KIAEKAPGKK IASLLVDVDN LGKIFLKGLK KKTLSRYSTL SRLMSFFFKE RVESIVEGKN VMVIYSGGDD LYLVGGWNDV LDVAKELREA FGRFTTNDFM TFSAGYVITD EKTSMSLIRE MSERAESAAK KSGKNSIAFS NRNYYAVKWN TFFEMYNFYQ ELKEIADKVD RSVIRKALNL TREESPLNKA FLAYIEAREN KDEDKRVANL MRENIDHLGE NALNVILQFV DLLSRKS // ID Q9X0Z5_THEMA Unreviewed; 81 AA. AC Q9X0Z5; G4FE80; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36343.1}; GN OrderedLocusNames=TM_1268 {ECO:0000313|EMBL:AAD36343.1}; GN ORFNames=Tmari_1273 {ECO:0000313|EMBL:AGL50197.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36343.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36343.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36343.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50197.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50197.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36343.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50197.1; -; Genomic_DNA. DR PIR; C72274; C72274. DR RefSeq; NP_229073.1; NC_000853.1. DR RefSeq; WP_004079977.1; NZ_CP011107.1. DR STRING; 243274.TM1268; -. DR EnsemblBacteria; AAD36343; AAD36343; TM_1268. DR EnsemblBacteria; AGL50197; AGL50197; Tmari_1273. DR GeneID; 898215; -. DR KEGG; tma:TM1268; -. DR KEGG; tmi:THEMA_07995; -. DR KEGG; tmm:Tmari_1273; -. DR KEGG; tmw:THMA_1293; -. DR PATRIC; 23937476; VBITheMar51294_1284. DR eggNOG; ENOG4106F5B; Bacteria. DR eggNOG; ENOG410Y7YP; LUCA. DR OMA; DCKIWIS; -. DR OrthoDB; EOG6F81WH; -. DR BioCyc; TMAR243274:GC6P-1299-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 81 AA; 9766 MW; 944B4597BD45D06B CRC64; MSDFKRILEE IAEKYNCKIW ISEKIGKRWS FYRDLKAGRE KFLPAELLVE NERFGVFAED FPEDKRDEVI PLLQKILDEL E // ID Q9X0I2_THEMA Unreviewed; 250 AA. AC Q9X0I2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36174.1}; GN OrderedLocusNames=TM_1098 {ECO:0000313|EMBL:AAD36174.1}; GN ORFNames=Tmari_1104 {ECO:0000313|EMBL:AGL50028.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36174.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36174.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36174.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50028.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50028.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36174.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50028.1; -; Genomic_DNA. DR PIR; D72294; D72294. DR RefSeq; NP_228904.1; NC_000853.1. DR RefSeq; WP_010865262.1; NC_000853.1. DR STRING; 243274.TM1098; -. DR MEROPS; M79.A04; -. DR EnsemblBacteria; AAD36174; AAD36174; TM_1098. DR EnsemblBacteria; AGL50028; AGL50028; Tmari_1104. DR GeneID; 898667; -. DR KEGG; tma:TM1098; -. DR KEGG; tmm:Tmari_1104; -. DR eggNOG; ENOG4108E53; Bacteria. DR eggNOG; COG1266; LUCA. DR KO; K07052; -. DR OMA; FILMTRR; -. DR OrthoDB; EOG6K9QK6; -. DR BioCyc; TMAR243274:GC6P-1127-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003675; CAAX_protease. DR Pfam; PF02517; Abi; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 53 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 84 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 109 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 121 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 152 174 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 250 AA; 28399 MW; B7EEF9562906B551 CRC64; MSVLYSIIAL ALYLAFMFSI NLFRIRRFEK AIFYQSLLGL AGAVTVCVAF RYVPSFRVSF VDLHWFLILL FVNVFFLGGS EVRFPPFMNR FIVMVSVVFL SPFSEELFFR GVFLKLNGND IWTNALVFSF LHLFNVIVGF ERFSFANLVY RFVVALIFAH SAAVSGSLFP AVLYHTTNNL VAFILMTRRG RNVHNVRGNR RIREEHTDPT SGSIPGEERK ESDLEERAGR NGDGGEDQKD SSGGRSDSQS // ID Q9X1P8_THEMA Unreviewed; 266 AA. AC Q9X1P8; G4FFV0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36628.1}; GN OrderedLocusNames=TM_1562 {ECO:0000313|EMBL:AAD36628.1}; GN ORFNames=Tmari_1570 {ECO:0000313|EMBL:AGL50494.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36628.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36628.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36628.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50494.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50494.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36628.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50494.1; -; Genomic_DNA. DR PIR; E72240; E72240. DR RefSeq; NP_229362.1; NC_000853.1. DR RefSeq; WP_004081971.1; NZ_CP011107.1. DR STRING; 243274.TM1562; -. DR EnsemblBacteria; AAD36628; AAD36628; TM_1562. DR EnsemblBacteria; AGL50494; AGL50494; Tmari_1570. DR GeneID; 897965; -. DR KEGG; tma:TM1562; -. DR KEGG; tmi:THEMA_06470; -. DR KEGG; tmm:Tmari_1570; -. DR KEGG; tmw:THMA_1597; -. DR PATRIC; 23938086; VBITheMar51294_1580. DR OMA; AIGSEQK; -. DR OrthoDB; EOG64N9V6; -. DR BioCyc; TMAR243274:GC6P-1603-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972335. SQ SEQUENCE 266 AA; 29400 MW; 79755E577AFB7F24 CRC64; MKKVFLLILV ISTLAVASQL EIFSSSGEWA FFENPARLLS MNKQGVMGSY QVFSGEGESL GTFLVGLFQT PAPNIAGVLY LKRSTLTESS YRTTIEYDAA FSPEESLNVG AGVSFTMDQE ERKEIDLHGG VSGYLFKDVG FGVSVRDFTL WSQKGTYMGG TYLLKLFYDS SRKNRFSYSL VFDQEVLENR IDFTIGSEQK AGLGVSVLSN TKTKENTVKI SLGFYATVNN VSVGFGTFII SSPVSSDPFS EYYYTQGTGI KFAVRW // ID Q9X1L4_THEMA Unreviewed; 289 AA. AC Q9X1L4; G4FFR6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE RecName: Full=1,4-dihydroxy-2-naphthoate octaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01937}; DE Short=DHNA-octaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01937}; DE EC=2.5.1.74 {ECO:0000256|HAMAP-Rule:MF_01937}; GN Name=menA {ECO:0000256|HAMAP-Rule:MF_01937}; GN OrderedLocusNames=TM_1528 {ECO:0000313|EMBL:AAD36595.1}; GN ORFNames=Tmari_1536 {ECO:0000313|EMBL:AGL50460.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36595.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36595.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36595.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50460.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50460.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to CC demethylmenaquinone (DMK). {ECO:0000256|HAMAP-Rule:MF_01937}. CC -!- CATALYTIC ACTIVITY: An all-trans-polyprenyl diphosphate + 1,4- CC dihydroxy-2-naphthoate = a demethylmenaquinol + diphosphate + CC CO(2). {ECO:0000256|HAMAP-Rule:MF_01937}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis; CC menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2. CC {ECO:0000256|HAMAP-Rule:MF_01937}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01937}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01937}. CC -!- SIMILARITY: Belongs to the MenA family. Type 1 subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01937}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36595.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50460.1; -; Genomic_DNA. DR PIR; D72241; D72241. DR RefSeq; NP_229328.1; NC_000853.1. DR RefSeq; WP_004081897.1; NZ_CP011107.1. DR STRING; 243274.TM1528; -. DR EnsemblBacteria; AAD36595; AAD36595; TM_1528. DR EnsemblBacteria; AGL50460; AGL50460; Tmari_1536. DR GeneID; 897982; -. DR KEGG; tma:TM1528; -. DR KEGG; tmi:THEMA_06650; -. DR KEGG; tmm:Tmari_1536; -. DR KEGG; tmw:THMA_1562; -. DR PATRIC; 23938016; VBITheMar51294_1546. DR eggNOG; ENOG4107R8E; Bacteria. DR eggNOG; COG1575; LUCA. DR KO; K02548; -. DR OMA; FIGIYIC; -. DR OrthoDB; EOG6W7220; -. DR BioCyc; TMAR243274:GC6P-1568-MONOMER; -. DR UniPathway; UPA00079; UER00168. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0046428; F:1,4-dihydroxy-2-naphthoate octaprenyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01937; MenA_1; 1. DR InterPro; IPR004657; MenA. DR InterPro; IPR000537; UbiA_prenyltransferase. DR InterPro; IPR026046; UBIAD1. DR Pfam; PF01040; UbiA; 1. DR PIRSF; PIRSF005355; UBIAD1; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01937}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01937}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01937}; KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01937}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01937, KW ECO:0000313|EMBL:AAD36595.1}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01937}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01937}. FT TRANSMEM 12 32 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 35 55 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 84 104 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 108 128 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 135 155 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 160 180 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 206 226 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 229 249 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 268 288 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01937}. SQ SEQUENCE 289 AA; 31677 MW; 0BFB85E898AFFF6B CRC64; MKYFVAVRPF SFVASAFPVT VGAMLAEEFS LIRYILSLIA SIFLHAGVNT TNDYFDYKKG VDTKDSLGSS GLLVSGKITP REELLLSVFC YAVSVVLGLV LIKISGPALL WLGLTGLVLG YAYTGHPFYL KYKSLGMFLV FILMGPLMVL GAYYVQTGRF SLEALLVSIP VGIATDLILL ANEIRDSEFD RRSGIKTLPI LIGDRAASFL YAVLTGLIYV FIVILVSTGV FRVISLVSLV SLPLYIRVIK QLFQKSAGRK NAREIADVDK MSALAEMILF VSMILGLLR // ID Q9X1E5_THEMA Unreviewed; 195 AA. AC Q9X1E5; G4FFG6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Glycerol uptake operon antiterminator {ECO:0000313|EMBL:AAD36501.1}; DE SubName: Full=Glycerol uptake operon antiterminator regulatory protein {ECO:0000313|EMBL:AGL50361.1}; GN OrderedLocusNames=TM_1431 {ECO:0000313|EMBL:AAD36501.1}; GN ORFNames=Tmari_1437 {ECO:0000313|EMBL:AGL50361.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36501.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36501.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36501.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50361.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50361.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36501.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50361.1; -; Genomic_DNA. DR PIR; D72254; D72254. DR RefSeq; NP_229231.1; NC_000853.1. DR RefSeq; WP_004081688.1; NZ_CP011107.1. DR STRING; 243274.TM1431; -. DR EnsemblBacteria; AAD36501; AAD36501; TM_1431. DR EnsemblBacteria; AGL50361; AGL50361; Tmari_1437. DR GeneID; 898044; -. DR KEGG; tma:TM1431; -. DR KEGG; tmm:Tmari_1437; -. DR KEGG; tmw:THMA_1461; -. DR PATRIC; 23937810; VBITheMar51294_1443. DR eggNOG; ENOG4108ZIA; Bacteria. DR eggNOG; COG1954; LUCA. DR KO; K02443; -. DR OMA; GIKHDEY; -. DR OrthoDB; EOG62G5N8; -. DR BioCyc; TMAR243274:GC6P-1469-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR GO; GO:0009607; P:response to biotic stimulus; IEA:InterPro. DR Gene3D; 3.20.20.400; -; 1. DR InterPro; IPR006699; G3P_antiterm. DR Pfam; PF04309; G3P_antiterm; 1. DR PIRSF; PIRSF016897; GlpP; 1. DR SUPFAM; SSF110391; SSF110391; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 195 AA; 21657 MW; E83EDCD24FC22789 CRC64; MKRGSVEIPR MGKTMNLYPV IPAVRAEKDI EEALESPSEV IFLLTGTVMN IEEIVYKLKN GKKEVFVHVD LVKGLSLDRC SLEFLREIVG VDGIISTHIH LLKIARKLGM RIIQRVFLVD SGALESGLAQ AEDLEPDFLE ILPGIVPEFI KEITKRYSGD IIAGGLIRKK EQVFAALEAG AKAISTSCKD LWKII // ID Q9WZJ7_THEMA Unreviewed; 161 AA. AC Q9WZJ7; G4FD85; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35819.1}; GN OrderedLocusNames=TM_0738 {ECO:0000313|EMBL:AAD35819.1}; GN ORFNames=Tmari_0739 {ECO:0000313|EMBL:AGL49664.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35819.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35819.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35819.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49664.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49664.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35819.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49664.1; -; Genomic_DNA. DR PIR; E72339; E72339. DR RefSeq; NP_228547.1; NC_000853.1. DR RefSeq; WP_004080988.1; NZ_CP011107.1. DR STRING; 243274.TM0738; -. DR EnsemblBacteria; AAD35819; AAD35819; TM_0738. DR EnsemblBacteria; AGL49664; AGL49664; Tmari_0739. DR GeneID; 898405; -. DR KEGG; tma:TM0738; -. DR KEGG; tmi:THEMA_00965; -. DR KEGG; tmm:Tmari_0739; -. DR KEGG; tmw:THMA_0756; -. DR PATRIC; 23936396; VBITheMar51294_0751. DR eggNOG; ENOG4105FWR; Bacteria. DR eggNOG; ENOG4111RDP; LUCA. DR OMA; NALMFGM; -. DR OrthoDB; EOG6CGCG5; -. DR BioCyc; TMAR243274:GC6P-764-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 95 118 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 161 AA; 18092 MW; 211EDF096BBA6222 CRC64; MISNPILGYK LDPGEPGIPH SAPASRSIMR VLSQEISNLI YFKKEALREG GTIIYSNIAL DLRKRGSFLA AVAGRTQVFI YTPGTKSSER THSLGSELQD KQQEIERKIL ELERQLKTET DPLERERLRE DLERLKLALN ILKASLRAPE LLVGVLLDSL V // ID Q9X0F6_THEMA Unreviewed; 327 AA. AC Q9X0F6; G4FET2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD36141.1}; DE SubName: Full=Putative rhamnose ABC transporter, permease component 1 {ECO:0000313|EMBL:AGL49994.1}; GN OrderedLocusNames=TM_1066 {ECO:0000313|EMBL:AAD36141.1}; GN ORFNames=Tmari_1070 {ECO:0000313|EMBL:AGL49994.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36141.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36141.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36141.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49994.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49994.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36141.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49994.1; -; Genomic_DNA. DR PIR; E72300; E72300. DR RefSeq; NP_228872.1; NC_000853.1. DR RefSeq; WP_004080421.1; NZ_CP011107.1. DR STRING; 243274.TM1066; -. DR TCDB; 3.A.1.5.12; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36141; AAD36141; TM_1066. DR EnsemblBacteria; AGL49994; AGL49994; Tmari_1070. DR GeneID; 897769; -. DR KEGG; tma:TM1066; -. DR KEGG; tmi:THEMA_09030; -. DR KEGG; tmm:Tmari_1070; -. DR KEGG; tmw:THMA_1088; -. DR PATRIC; 23937061; VBITheMar51294_1079. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR KO; K02033; -. DR OMA; LRANMLD; -. DR OrthoDB; EOG66F098; -. DR BioCyc; TMAR243274:GC6P-1095-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 9 29 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 101 128 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 140 162 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 194 213 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 247 274 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 294 320 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 101 317 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 327 AA; 36733 MW; 690CA91191D3CDCD CRC64; MVAYILRRLI TAFITLWIIS IISFVIIQLP PGDFLTSYIA QLKVSGEDVD IATIEALKKQ YGLDKPIYVQ YLKWLWGILH GDFGYSFSWK KPVNELLWNR LGVTVLVATL SLIFSWIFGF IIGMYSAVHP YSIGDYLATI LGYIGLAVPN FLLALILMWG IYSLTGINLS GLHSVKYLNT PMTIDKFLDI LNHLWIPVLV LGTSGMAGLI RTLRANLLDE LHKPYVEAAL SKGLPENKVF WKYPLRIAMI PFISTVGWSL PWIFSGATIT AIVLNLPSVG PLLLNALKNQ DMYLAGSLVM FLSFFTVIGT LISDILLAWV DPRIRFE // ID Q9WZC5_THEMA Unreviewed; 170 AA. AC Q9WZC5; G4FDG7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 105. DE SubName: Full=Rubrerythrin {ECO:0000313|EMBL:AAD35741.1}; GN OrderedLocusNames=TM_0657 {ECO:0000313|EMBL:AAD35741.1}; GN ORFNames=Tmari_0657 {ECO:0000313|EMBL:AGL49582.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35741.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35741.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35741.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49582.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49582.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC {ECO:0000256|RuleBase:RU003668}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35741.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49582.1; -; Genomic_DNA. DR PIR; F72348; F72348. DR RefSeq; NP_228466.1; NC_000853.1. DR RefSeq; WP_004081119.1; NZ_CP011107.1. DR SMR; Q9WZC5; 2-168. DR STRING; 243274.TM0657; -. DR DNASU; 897767; -. DR EnsemblBacteria; AAD35741; AAD35741; TM_0657. DR EnsemblBacteria; AGL49582; AGL49582; Tmari_0657. DR GeneID; 897767; -. DR KEGG; tma:TM0657; -. DR KEGG; tmi:THEMA_01380; -. DR KEGG; tmm:Tmari_0657; -. DR KEGG; tmw:THMA_0672; -. DR PATRIC; 23936228; VBITheMar51294_0667. DR eggNOG; ENOG4108RAC; Bacteria. DR eggNOG; COG1592; LUCA. DR OMA; CQVCGNT; -. DR OrthoDB; EOG69SKK0; -. DR BioCyc; TMAR243274:GC6P-682-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR Gene3D; 2.20.28.10; -; 1. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR024934; Rubredoxin-like_dom. DR InterPro; IPR004039; Rubredoxin-type_fold. DR InterPro; IPR003251; Rubrerythrin. DR Pfam; PF02915; Rubrerythrin; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 130 Ferritin-like diiron. FT {ECO:0000259|PROSITE:PS50905}. FT DOMAIN 135 168 Rubredoxin-like. FT {ECO:0000259|PROSITE:PS50903}. SQ SEQUENCE 170 AA; 19674 MW; 0692EC363B579FD8 CRC64; MREMTKKFLE DAFAGESMAH MKYLIFADEA EQRGLKKLAN LFRAIAYAEY VHARNHYREL GKIYKEMAEN VQQCIDGETF EIDEMYPVYN TVAQFQEEKG AERSTKFAWE AEKIHAEMYK KAKELVEKGE DYTAEKIYIC PVCGHTVEGE PPEKCPVCGA PKSAYREFSI // ID Q9X2D8_THEMA Unreviewed; 166 AA. AC Q9X2D8; G4FGK5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Chromate transport protein, putative {ECO:0000313|EMBL:AAD36881.1}; GN OrderedLocusNames=TM_1818 {ECO:0000313|EMBL:AAD36881.1}; GN ORFNames=Tmari_1828 {ECO:0000313|EMBL:AGL50752.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36881.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36881.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36881.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50752.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50752.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36881.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50752.1; -; Genomic_DNA. DR PIR; E72206; E72206. DR RefSeq; NP_229615.1; NC_000853.1. DR RefSeq; WP_004082364.1; NZ_CP011107.1. DR STRING; 243274.TM1818; -. DR EnsemblBacteria; AAD36881; AAD36881; TM_1818. DR EnsemblBacteria; AGL50752; AGL50752; Tmari_1828. DR GeneID; 897364; -. DR KEGG; tma:TM1818; -. DR KEGG; tmi:THEMA_05105; -. DR KEGG; tmm:Tmari_1828; -. DR KEGG; tmw:THMA_1863; -. DR PATRIC; 23938623; VBITheMar51294_1838. DR eggNOG; ENOG4107XFU; Bacteria. DR eggNOG; COG2059; LUCA. DR KO; K07240; -. DR OMA; ADINQQA; -. DR OrthoDB; EOG6M0T6H; -. DR BioCyc; TMAR243274:GC6P-1869-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015109; F:chromate transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003370; Chromate_transpt. DR Pfam; PF02417; Chromate_transp; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 67 94 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 115 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 148 165 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 166 AA; 17718 MW; E12A360ED47BB7CB CRC64; MLKLAFIFLK IGFLSFGGGW AIVGILKNEL VTGGFLSPEE FSQAVSIAQM TPGPVAINLA TYTGYKFFGL IGAVLNTLAF LGAPILVITT AIFLRKYVKL QRVRLMKALE GATTTLLIVT LLSLLSSVQN PVLILLSAAA FVCSFFKVHP LFIIFGCGVI GAILGF // ID Q9X0K4_THEMA Unreviewed; 436 AA. AC Q9X0K4; G4FEM8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Glycerol-3-phosphate ABC transporter, periplasmic glycerol-3-phosphate-binding protein {ECO:0000313|EMBL:AAD36196.1}; GN OrderedLocusNames=TM_1120 {ECO:0000313|EMBL:AAD36196.1}; GN ORFNames=Tmari_1126 {ECO:0000313|EMBL:AGL50050.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36196.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36196.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36196.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50050.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50050.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36196.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50050.1; -; Genomic_DNA. DR PIR; E72292; E72292. DR RefSeq; NP_228926.1; NC_000853.1. DR RefSeq; WP_004080298.1; NZ_CP011107.1. DR STRING; 243274.TM1120; -. DR EnsemblBacteria; AAD36196; AAD36196; TM_1120. DR EnsemblBacteria; AGL50050; AGL50050; Tmari_1126. DR GeneID; 898644; -. DR KEGG; tma:TM1120; -. DR KEGG; tmi:THEMA_08745; -. DR KEGG; tmm:Tmari_1126; -. DR KEGG; tmw:THMA_1143; -. DR PATRIC; 23937175; VBITheMar51294_1136. DR eggNOG; ENOG4105BZ7; Bacteria. DR eggNOG; COG1653; LUCA. DR KO; K05813; -. DR OMA; EMKAYLQ; -. DR OrthoDB; EOG69D38D; -. DR BioCyc; TMAR243274:GC6P-1149-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 436 AA; 49444 MW; 631E45E80B55382C CRC64; MKKFFVLLMI LLVVTSLAKV KIQFWHAMGG WRIELLQNMA EDFMKTHPDI EVEVQYTGSY RDTLNKLVAA VQGGTPPHVV QIYEIGTQFM IDSGIAVPIG DLIEKDPSFD VGKFLPQVLD YYRVKGKLYS MPFNSSNPIL YYNKTLFKEV GLDPNKPPRT FNELIEYCKK LTVKDEKGNI VRAGITWPLH SWFFEQFVAL QNAPLVDNEN GRAGRATKAV FNHEGALRFL KLWDTLTKEG LMINTTKEDW TGARQLFISQ KVAMLISSTS DVKLMMDAAK ENGFELGTAF LPKPEGVELG GTPIGGGSLW IIGGHPEEEI KAAWEFVKWM AEPEQQIRWH LGTGYFPVRK DAVETLLYQG YYSEYPHHLT ALLQLLLSVQ TPNTRGAVIG PFPEVRDIIE TAIEKMINGE MTPEEALAWA EKEATRAIRE YNELYE // ID Q9X1W0_THEMA Unreviewed; 133 AA. AC Q9X1W0; G4FG14; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36692.1}; DE SubName: Full=UvrB/UvrC protein {ECO:0000313|EMBL:AGL50558.1}; GN OrderedLocusNames=TM_1625 {ECO:0000313|EMBL:AAD36692.1}; GN ORFNames=Tmari_1634 {ECO:0000313|EMBL:AGL50558.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36692.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36692.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36692.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50558.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50558.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36692.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50558.1; -; Genomic_DNA. DR PIR; A72229; A72229. DR RefSeq; NP_229425.1; NC_000853.1. DR RefSeq; WP_004082098.1; NZ_CP011107.1. DR STRING; 243274.TM1625; -. DR EnsemblBacteria; AAD36692; AAD36692; TM_1625. DR EnsemblBacteria; AGL50558; AGL50558; Tmari_1634. DR GeneID; 897682; -. DR KEGG; tma:TM1625; -. DR KEGG; tmi:THEMA_06120; -. DR KEGG; tmm:Tmari_1634; -. DR KEGG; tmw:THMA_1666; -. DR PATRIC; 23938224; VBITheMar51294_1644. DR OMA; QKCLMDV; -. DR OrthoDB; EOG6RZB83; -. DR BioCyc; TMAR243274:GC6P-1671-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR001943; UVR_dom. DR Pfam; PF02151; UVR; 1. DR PROSITE; PS50151; UVR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 95 130 UVR. {ECO:0000259|PROSITE:PS50151}. SQ SEQUENCE 133 AA; 15763 MW; 3D65EEB9C609D56B CRC64; MKCLRCGHET SKSYKVDFDG VEKEIAYCQK CLMDVLKESV PLKNTPSPSE DSMEKKRHLS FDGEMVIFVE TPLRILEEMF GKLWSDQEKE NFENERKITF LERKLKEAIK NEDYRKANRL KQLILQIKNK TVK // ID Q9WXY4_THEMA Unreviewed; 384 AA. AC Q9WXY4; G4FH45; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=Permease of the major facilitator superfamily {ECO:0000313|EMBL:AGL49054.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35224.1}; GN OrderedLocusNames=TM_0130 {ECO:0000313|EMBL:AAD35224.1}; GN ORFNames=Tmari_0128 {ECO:0000313|EMBL:AGL49054.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35224.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35224.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35224.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49054.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49054.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35224.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49054.1; -; Genomic_DNA. DR PIR; A72413; A72413. DR RefSeq; NP_227946.1; NC_000853.1. DR RefSeq; WP_004082719.1; NZ_CP011107.1. DR STRING; 243274.TM0130; -. DR EnsemblBacteria; AAD35224; AAD35224; TM_0130. DR EnsemblBacteria; AGL49054; AGL49054; Tmari_0128. DR GeneID; 896957; -. DR KEGG; tma:TM0130; -. DR KEGG; tmi:THEMA_04155; -. DR KEGG; tmm:Tmari_0128; -. DR KEGG; tmw:THMA_0126; -. DR PATRIC; 23935098; VBITheMar51294_0127. DR eggNOG; ENOG4108JU2; Bacteria. DR eggNOG; COG0477; LUCA. DR OMA; TESKIVQ; -. DR OrthoDB; EOG6JHRM6; -. DR BioCyc; TMAR243274:GC6P-130-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 52 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 94 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 209 231 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 243 264 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 296 318 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 330 353 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 359 377 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 7 381 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 384 AA; 42557 MW; C18C02FD215A0855 CRC64; MSRKKAFLFI VLLGLVSLFA DVTYEGARSI IGPFMKTLGA SAAALGFAVG LGELTGYAFR LISGILSDKT RKYWLFTILG YAINLFAVPA LAFAGNWQTA LVLIIAERFG KALRTPARDV LLSFASEEVG MGKGFGIHEA LDQIGAILGP LALTFALAFE KSYRFCFFIL LIPALVAMVL LLTARITFPA LQEMKKKKDS PVDRNLGKTY WFYLAIVSMV AFAFADFPII AYHMKSFEVA KDFFVPATYS LAMAVDAVAA LVFGHLFDKK GFVALAYAVL LSSFFPVLSF SNSFPLIFAG VILWGIGMGA QESIMRAVVA KIVPAEKRGF AYGMFFTVYG VFWFFGSWIM GTLYDINRFY LILFSFVIQF AAALLLLRMK RYEW // ID Q9X1X8_THEMA Unreviewed; 273 AA. AC Q9X1X8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE SubName: Full=Nicotinate-nucleotide pyrophosphorylase {ECO:0000313|EMBL:AAD36712.1}; DE SubName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000313|EMBL:AGL50578.1}; DE EC=2.4.2.19 {ECO:0000313|EMBL:AGL50578.1}; GN OrderedLocusNames=TM_1645 {ECO:0000313|EMBL:AAD36712.1}; GN ORFNames=Tmari_1654 {ECO:0000313|EMBL:AGL50578.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36712.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36712.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36712.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50578.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50578.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the NadC/ModD family. CC {ECO:0000256|PIRNR:PIRNR006250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36712.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50578.1; -; Genomic_DNA. DR PIR; B72227; B72227. DR RefSeq; NP_229445.1; NC_000853.1. DR RefSeq; WP_008194698.1; NZ_CP011107.1. DR PDB; 1O4U; X-ray; 2.50 A; A/B=1-273. DR PDBsum; 1O4U; -. DR STRING; 243274.TM1645; -. DR EnsemblBacteria; AAD36712; AAD36712; TM_1645. DR EnsemblBacteria; AGL50578; AGL50578; Tmari_1654. DR GeneID; 896858; -. DR KEGG; tma:TM1645; -. DR KEGG; tmm:Tmari_1654; -. DR KEGG; tmw:THMA_1686; -. DR PATRIC; 23938264; VBITheMar51294_1664. DR eggNOG; ENOG4105D18; Bacteria. DR eggNOG; COG0157; LUCA. DR KO; K00767; -. DR OMA; FEPVKHV; -. DR OrthoDB; EOG6KT2XH; -. DR BioCyc; TMAR243274:GC6P-1691-MONOMER; -. DR BRENDA; 2.4.2.19; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.1170.20; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004393; NadC. DR InterPro; IPR027277; NadC/ModD. DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C. DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N. DR Pfam; PF01729; QRPTase_C; 1. DR Pfam; PF02749; QRPTase_N; 1. DR PIRSF; PIRSF006250; NadC_ModD; 1. DR SUPFAM; SSF51690; SSF51690; 1. DR TIGRFAMs; TIGR00078; nadC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O4U}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000256|PIRNR:PIRNR006250, KW ECO:0000313|EMBL:AGL50578.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|PIRNR:PIRNR006250, KW ECO:0000313|EMBL:AGL50578.1}. FT DOMAIN 18 101 QRPTase_N. {ECO:0000259|Pfam:PF02749}. FT DOMAIN 104 270 QRPTase_C. {ECO:0000259|Pfam:PF01729}. SQ SEQUENCE 273 AA; 30181 MW; 5890A19DE7A9087E CRC64; MEKILDLLMS FVKEDEGKLD LASFPLRNTT AGAHLLLKTE NVVASGIEVS RMFLEKMGLL SKFNVEDGEY LEGTGVIGEI EGNTYKLLVA ERTLLNVLSV MFSVATTTRR FAEKLKHAKI AATRKILPGL GVLQKIAVVH GGGDPHRLDL SGCVMIKDNH LKMYGSAERA VQEVRKIIPF TTKIEVEVEN LEDALRAVEA GADIVMLDNL SPEEVKDISR RIKDINPNVI VEVSGGITEE NVSLYDFETV DVISSSRLTL QEVFVDLSLE IQR // ID Q9X1K4_THEMA Unreviewed; 357 AA. AC Q9X1K4; G4FFQ3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Hydrolase, ama/hipO/hyuC family {ECO:0000313|EMBL:AAD36583.1}; DE SubName: Full=N-acetyl-L,L-diaminopimelate deacetylase {ECO:0000313|EMBL:AGL50448.1}; DE EC=3.5.1.47 {ECO:0000313|EMBL:AGL50448.1}; GN OrderedLocusNames=TM_1516 {ECO:0000313|EMBL:AAD36583.1}; GN ORFNames=Tmari_1524 {ECO:0000313|EMBL:AGL50448.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36583.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36583.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36583.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50448.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50448.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36583.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50448.1; -; Genomic_DNA. DR PIR; E72245; E72245. DR RefSeq; NP_229316.1; NC_000853.1. DR RefSeq; WP_004081868.1; NZ_CP011107.1. DR STRING; 243274.TM1516; -. DR MEROPS; M20.A27; -. DR EnsemblBacteria; AAD36583; AAD36583; TM_1516. DR EnsemblBacteria; AGL50448; AGL50448; Tmari_1524. DR GeneID; 897988; -. DR KEGG; tma:TM1516; -. DR KEGG; tmi:THEMA_06720; -. DR KEGG; tmm:Tmari_1524; -. DR KEGG; tmw:THMA_1548; -. DR PATRIC; 23937990; VBITheMar51294_1533. DR eggNOG; ENOG4105CH2; Bacteria. DR eggNOG; COG1473; LUCA. DR KO; K05823; -. DR OMA; TQRYILD; -. DR OrthoDB; EOG6B09WM; -. DR BioCyc; TMAR243274:GC6P-1556-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0050118; F:N-acetyldiaminopimelate deacetylase activity; IEA:UniProtKB-EC. DR Gene3D; 3.30.70.360; -; 1. DR InterPro; IPR017439; Amidohydrolase. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1. DR SUPFAM; SSF55031; SSF55031; 1. DR TIGRFAMs; TIGR01891; amidohydrolases; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD36583.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 167 258 M20_dimer. {ECO:0000259|Pfam:PF07687}. SQ SEQUENCE 357 AA; 40407 MW; BDBCAAD985AB5971 CRC64; MDEIELRHIL HMNPELSFKE YRTKETLRKA VIEIGYEKII EVAGTGLVIE KKETEDPYVV LRADMDALPI KEETGWEFAS RNEYMHACGH DFHMSALYGA MKRLRNVKKN FLFVFQPAEE TGGGAKEVVD FLKDKYEIKA AVGFHVTDEY DAGTVASRPG VLFASATEFD VYFKGVPAHV AFAEKGKDAL KAAVSFLGWL YNKKWNALVG VGKISGGRAR NIVPDEIKLE GTIRSEALRI TEEVISNMVK QLGELKEEMG VDFAVERGSV YPEVKVDQNL FETLRETCQR LGFSFVECDM KWTGEDFGYF SQVFPSLLFW FGVGEGERFG LHHPRFLPND RYIPMAADLL AELAMVI // ID Q9WZ71_THEMA Unreviewed; 151 AA. AC Q9WZ71; G4FDL7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Iron-dependent transcriptional repressor, putative {ECO:0000313|EMBL:AAD35687.1}; GN OrderedLocusNames=TM_0602 {ECO:0000313|EMBL:AAD35687.1}; GN ORFNames=Tmari_0602 {ECO:0000313|EMBL:AGL49527.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35687.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35687.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35687.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49527.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49527.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35687.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49527.1; -; Genomic_DNA. DR PIR; C72358; C72358. DR RefSeq; NP_228412.1; NC_000853.1. DR RefSeq; WP_004081231.1; NZ_CP011107.1. DR STRING; 243274.TM0602; -. DR EnsemblBacteria; AAD35687; AAD35687; TM_0602. DR EnsemblBacteria; AGL49527; AGL49527; Tmari_0602. DR GeneID; 897681; -. DR KEGG; tma:TM0602; -. DR KEGG; tmi:THEMA_01655; -. DR KEGG; tmm:Tmari_0602; -. DR KEGG; tmw:THMA_0618; -. DR PATRIC; 23936119; VBITheMar51294_0613. DR eggNOG; ENOG41062HE; Bacteria. DR eggNOG; COG1321; LUCA. DR OMA; KMPSAKQ; -. DR OrthoDB; EOG6M9F3P; -. DR BioCyc; TMAR243274:GC6P-627-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.10.60.10; -; 1. DR InterPro; IPR001367; Fe_dep_repressor. DR InterPro; IPR022689; Iron_dep_repressor. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02742; Fe_dep_repr_C; 1. DR SMART; SM00529; HTH_DTXR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF47979; SSF47979; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 62 130 Fe_dep_repr_C. FT {ECO:0000259|Pfam:PF02742}. SQ SEQUENCE 151 AA; 17628 MW; 23BFF56927B5BB38 CRC64; MLSPTEKRYL LAVLLTTEEG STRLKRVSDF LKVKMPSAKQ ILEDLASKKL INYVRRGPIS LTKKGTELAQ KELERFNNLK EFLKKILFLD EEEAEKGAWE IFFNLEESIA DRVVDFMNFL THCPHITPIC IKGFKEYLET GEFPTLCRLR R // ID Q9X1S9_THEMA Unreviewed; 247 AA. AC Q9X1S9; G4FFY1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040}; GN OrderedLocusNames=TM_1593 {ECO:0000313|EMBL:AAD36660.1}; GN ORFNames=Tmari_1601 {ECO:0000313|EMBL:AGL50525.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36660.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36660.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36660.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50525.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50525.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to CC target apoproteins. Can hydrolyze ATP. {ECO:0000256|HAMAP- CC Rule:MF_02040}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02040}. CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. CC {ECO:0000256|HAMAP-Rule:MF_02040}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36660.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50525.1; -; Genomic_DNA. DR PIR; E72233; E72233. DR RefSeq; NP_229393.1; NC_000853.1. DR RefSeq; WP_004082033.1; NZ_CP011107.1. DR STRING; 243274.TM1593; -. DR DNASU; 897412; -. DR EnsemblBacteria; AAD36660; AAD36660; TM_1593. DR EnsemblBacteria; AGL50525; AGL50525; Tmari_1601. DR GeneID; 897412; -. DR KEGG; tma:TM1593; -. DR KEGG; tmi:THEMA_06290; -. DR KEGG; tmm:Tmari_1601; -. DR KEGG; tmw:THMA_1633; -. DR PATRIC; 23938160; VBITheMar51294_1612. DR eggNOG; ENOG4105D1F; Bacteria. DR eggNOG; COG0489; LUCA. DR KO; K03593; -. DR OMA; ELPDCTT; -. DR OrthoDB; EOG64XXQJ; -. DR BioCyc; TMAR243274:GC6P-1639-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_02040; Mrp_NBP35; 1. DR InterPro; IPR019591; Mrp/NBP35_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23264; PTHR23264; 1. DR Pfam; PF10609; ParA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02040, KW ECO:0000313|EMBL:AGL50525.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02040}; KW Iron {ECO:0000256|HAMAP-Rule:MF_02040}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02040}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02040}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02040, KW ECO:0000313|EMBL:AGL50525.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT NP_BIND 12 19 ATP. {ECO:0000256|HAMAP-Rule:MF_02040}. SQ SEQUENCE 247 AA; 26769 MW; 7A7C8EDA5692A638 CRC64; MEKTKKIAVM SGKGGVGKTT VAVNLAVALA AEGYQVGLLD LDLHGPNVQR MLGVSLPPSE GEKIVPAKYG DSLKVFSLAM ILQEGAPVIW RGPLKHKAIE QLTRDVEWGD LDYLICDLPP GTGDEALSTF QIIKPDAVIV VSTPQKVAGD DVRRAINFVK RLSGKILGLV ENMSYLVCPN CGEKIYVFGK GETEKLAEEF GIPLIARIPM DPEVVSLSDE GRPAVVYKRG TVIEEEFKKI VEKVLSL // ID Q9X0T0_THEMA Unreviewed; 577 AA. AC Q9X0T0; G4FEE3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE SubName: Full=Maltose ABC transporter, permease protein {ECO:0000313|EMBL:AAD36278.1}; DE SubName: Full=Maltose/maltodextrin ABC transporter, permease protein MalF {ECO:0000313|EMBL:AGL50134.1}; GN OrderedLocusNames=TM_1203 {ECO:0000313|EMBL:AAD36278.1}; GN ORFNames=Tmari_1210 {ECO:0000313|EMBL:AGL50134.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36278.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36278.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36278.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50134.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50134.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36278.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50134.1; -; Genomic_DNA. DR PIR; A72283; A72283. DR RefSeq; NP_229008.1; NC_000853.1. DR RefSeq; WP_004080110.1; NZ_CP011107.1. DR STRING; 243274.TM1203; -. DR TCDB; 3.A.1.1.22; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36278; AAD36278; TM_1203. DR EnsemblBacteria; AGL50134; AGL50134; Tmari_1210. DR GeneID; 898281; -. DR KEGG; tma:TM1203; -. DR KEGG; tmi:THEMA_08315; -. DR KEGG; tmm:Tmari_1210; -. DR KEGG; tmw:THMA_1229; -. DR PATRIC; 23937348; VBITheMar51294_1221. DR eggNOG; ENOG4105D56; Bacteria. DR eggNOG; COG1175; LUCA. DR KO; K10109; -. DR OMA; WAIPVFI; -. DR OrthoDB; EOG6VMTK6; -. DR BioCyc; TMAR243274:GC6P-1233-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR032605; DUF4896. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR032550; TM_PBP2_N. DR Pfam; PF00528; BPD_transp_1; 1. DR Pfam; PF16237; DUF4896; 1. DR Pfam; PF16296; TM_PBP2_N; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 7 26 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 32 51 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 58 77 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 338 362 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 374 394 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 426 445 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 479 507 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 544 568 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 339 565 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 577 AA; 65769 MW; FD2FB68A6FA6820C CRC64; MKNIVKLFLW FLLAILNIAL FWAGVFLFQN EYYELSIVLF SLLVLIDFFI INPRGYPYRY TIPALILLFV LVLYPIYFTF KVAFTNYGTG HFMSRQEAIE RLLYDPNFSY VVDSTPVSYK VFVVYDGLSP TDDFLILFKT GDTIFLGERP KPVVARGQEV LLSQFNLVPI TGETISLNGD TFRIVPWPAD LSEINLVVRG EKTYKSFYSP DDEILRLNAP YFKSRIAQGY LVNAEYVLPD GKKLALRIAP DGEWRFMYVE RLYRLAYKEI YDGVKMKITT TVVNNLTGRE VVEREGAFYD VDENGNETFL VGFIDFVGWK NFLRIVKDPK VSGPFFRIFL WTFVWAVLSV VLSLAVGLPF ALVLNNPRLK GRNLYRTLLI IPWAIPVFIS ALVWRNGLLN ESYGVINKFL LPLFGLEPIK WFNDPFWARV GVLLVNVWLT FPYMMTISLG ALQSIPPELY EVAAIDGAGR FRRFVHITFP LLMTIIAPLL VSSFAFSFNN FTIIYLITGG GPPIPNSTTP TGYTDILISY VYKLAFEGGQ GQDFGFASAI SILIFFLVGG ISFVNFKLSG AFEEVSR // ID Q9X089_THEMA Unreviewed; 37 AA. AC Q9X089; G4FF01; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36073.1}; GN OrderedLocusNames=TM_0994 {ECO:0000313|EMBL:AAD36073.1}; GN ORFNames=Tmari_0998 {ECO:0000313|EMBL:AGL49923.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36073.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36073.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36073.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49923.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49923.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36073.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49923.1; -; Genomic_DNA. DR PIR; H72308; H72308. DR RefSeq; NP_228802.1; NC_000853.1. DR RefSeq; WP_004080563.1; NZ_CP011107.1. DR STRING; 243274.TM0994; -. DR EnsemblBacteria; AAD36073; AAD36073; TM_0994. DR EnsemblBacteria; AGL49923; AGL49923; Tmari_0998. DR GeneID; 896821; -. DR KEGG; tma:TM0994; -. DR KEGG; tmi:THEMA_09380; -. DR KEGG; tmm:Tmari_0998; -. DR KEGG; tmw:THMA_1016; -. DR PATRIC; 23936919; VBITheMar51294_1008. DR OrthoDB; EOG6F821G; -. DR BioCyc; TMAR243274:GC6P-1024-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 37 AA; 4067 MW; 0744A5073D4BE441 CRC64; MSRKMLLVLL SFLVVLAGCT AVVGIIAEEG IKQRHRN // ID Q9X147_THEMA Unreviewed; 442 AA. AC Q9X147; G4FHZ9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=AstB/chuR-related protein {ECO:0000313|EMBL:AAD36396.1}; GN OrderedLocusNames=TM_1324 {ECO:0000313|EMBL:AAD36396.1}; GN ORFNames=Tmari_1330 {ECO:0000313|EMBL:AGL50254.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36396.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36396.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36396.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50254.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50254.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36396.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50254.1; -; Genomic_DNA. DR PIR; H72266; H72266. DR RefSeq; NP_229126.1; NC_000853.1. DR RefSeq; WP_004083337.1; NZ_CP011107.1. DR STRING; 243274.TM1324; -. DR EnsemblBacteria; AAD36396; AAD36396; TM_1324. DR EnsemblBacteria; AGL50254; AGL50254; Tmari_1330. DR GeneID; 898158; -. DR KEGG; tma:TM1324; -. DR KEGG; tmi:THEMA_07725; -. DR KEGG; tmm:Tmari_1330; -. DR KEGG; tmw:THMA_1348; -. DR PATRIC; 23937583; VBITheMar51294_1337. DR eggNOG; ENOG4105J4D; Bacteria. DR eggNOG; COG0641; LUCA. DR KO; K06871; -. DR OMA; CERVSES; -. DR OrthoDB; EOG60PH7N; -. DR BioCyc; TMAR243274:GC6P-1355-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00421379}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|SAAS:SAAS00421379}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00421379}; KW Metal-binding {ECO:0000256|SAAS:SAAS00421379}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00421341}. FT DOMAIN 91 301 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 442 AA; 52021 MW; 11B502F42CDC01EA CRC64; MFKPSRYNVI FRDGDYVVFV NFLTRAIARL EKSKAEIAEK ILKDPDEEIP EEWLSIKKDL IYGGYIVDED FDEIEHLKLM NRMTRYDSSS VMVTIIPTLA CNFDCIYCYE SKTGPSMTAK TAERIVEYLK RLIRTRRSIS VGWFGGEPLL CFDVVKFVNS SLIEACRENN VDFHSSMSTN GYLLDKEKAE WFDRLEIRNV QITIDGPEDV HNKYRPLKGG KGTFDTIVEN LENLFRVTEK LQVTFRMNVG PDNFHRVEEF LNVLERFPKD RTRVYFRWIF GSNSREFFFR KVYEIRDRES LNILNFYESA AKRGFNVFLP VLVQNRYCEY DCVSSVVIGP QGELYPCTVR VGKGMEIGRL TNRGLEYDRK KYLRWHSFDA FESEECMRCK LLPVCMGGCR SARFDGKTGC PEEKKDPEKF AREWYRIKLL ERQVEKLEAF KI // ID Q9X030_THEMA Unreviewed; 152 AA. AC Q9X030; G4FF58; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36013.1}; GN OrderedLocusNames=TM_0932 {ECO:0000313|EMBL:AAD36013.1}; GN ORFNames=Tmari_0934 {ECO:0000313|EMBL:AGL49859.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36013.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36013.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36013.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49859.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49859.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36013.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49859.1; -; Genomic_DNA. DR PIR; D72315; D72315. DR RefSeq; NP_228740.1; NC_000853.1. DR RefSeq; WP_004080630.1; NZ_CP011107.1. DR STRING; 243274.TM0932; -. DR EnsemblBacteria; AAD36013; AAD36013; TM_0932. DR EnsemblBacteria; AGL49859; AGL49859; Tmari_0934. DR GeneID; 898606; -. DR KEGG; tma:TM0932; -. DR KEGG; tmi:THEMA_09690; -. DR KEGG; tmm:Tmari_0934; -. DR KEGG; tmw:THMA_0954; -. DR PATRIC; 23936795; VBITheMar51294_0946. DR eggNOG; ENOG4108B68; Bacteria. DR eggNOG; COG1787; LUCA. DR KO; K07449; -. DR OMA; KNPYRFE; -. DR OrthoDB; EOG66TG77; -. DR BioCyc; TMAR243274:GC6P-962-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro. DR Gene3D; 3.40.1350.10; -; 1. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR007560; Restrct_endonuc_IV_Mrr. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR Pfam; PF04471; Mrr_cat; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 39 132 Mrr_cat. {ECO:0000259|Pfam:PF04471}. SQ SEQUENCE 152 AA; 17550 MW; 9E17B036285A85E7 CRC64; MIYIILSLLS FSLLVLFLQW GKKRRKQDLR NLLEAGLKNP YRFEEFAREY LKEHGFRSVR TTRKSKDFGA DIVAKRRGST VVFQVKRRNS TVEKEVVKEL VAAAYIYGAT EVGIFTNGEL STGLKKELEE LKRSGGFIKR VHVVKNINPE EL // ID Q9WYA6_THEMA Unreviewed; 202 AA. AC Q9WYA6; G4FHI3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Methionine synthase activation domain protein {ECO:0000313|EMBL:AGL49193.1}; DE EC=2.1.1.13 {ECO:0000313|EMBL:AGL49193.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35358.1}; GN OrderedLocusNames=TM_0269 {ECO:0000313|EMBL:AAD35358.1}; GN ORFNames=Tmari_0267 {ECO:0000313|EMBL:AGL49193.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35358.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35358.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35358.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49193.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49193.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35358.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49193.1; -; Genomic_DNA. DR PIR; C72397; C72397. DR RefSeq; NP_228082.1; NC_000853.1. DR RefSeq; WP_004082973.1; NZ_CP011107.1. DR PDB; 1J6R; X-ray; 2.30 A; A/B=1-202. DR PDBsum; 1J6R; -. DR STRING; 243274.TM0269; -. DR EnsemblBacteria; AAD35358; AAD35358; TM_0269. DR EnsemblBacteria; AGL49193; AGL49193; Tmari_0267. DR GeneID; 897183; -. DR KEGG; tma:TM0269; -. DR KEGG; tmi:THEMA_03380; -. DR KEGG; tmm:Tmari_0267; -. DR KEGG; tmw:THMA_0276; -. DR PATRIC; 23935415; VBITheMar51294_0273. DR eggNOG; ENOG41081B6; Bacteria. DR eggNOG; ENOG410ZWPM; LUCA. DR OMA; RISPGYG; -. DR OrthoDB; EOG610423; -. DR BioCyc; TMAR243274:GC6P-282-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC. DR InterPro; IPR017342; S-AdoMet-dep_Met_synth_prd. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR PIRSF; PIRSF037984; Met_synth_TM0269_prd; 1. DR SUPFAM; SSF56507; SSF56507; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1J6R}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Methyltransferase {ECO:0000313|EMBL:AGL49193.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL49193.1}. SQ SEQUENCE 202 AA; 22890 MW; AE241A1C2DE73C27 CRC64; MPKVEIAPSE IKIPDNVLKA KLGFGGAEEI PEEFRKTVNR AYEELLDAAK PVVLWRDFEV DGSLSFDDMR LTGELATKHL SGSKIITVFL ATLGKKVDEK IEEYFRKGED LLAFFIDGIA SEMVEYALRK VDAELRMKRS NLEGSFRISP GYGDLPLSLN KKIAEIFKEE VDVNVIEDSY VLVPRKTITA FVGWREKNEK QT // ID Q9X1X2_THEMA Unreviewed; 206 AA. AC Q9X1X2; G4FG26; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36704.1}; GN OrderedLocusNames=TM_1637 {ECO:0000313|EMBL:AAD36704.1}; GN ORFNames=Tmari_1646 {ECO:0000313|EMBL:AGL50570.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36704.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36704.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36704.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50570.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50570.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36704.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50570.1; -; Genomic_DNA. DR PIR; E72230; E72230. DR RefSeq; NP_229437.1; NC_000853.1. DR RefSeq; WP_004082118.1; NZ_CP011107.1. DR STRING; 243274.TM1637; -. DR EnsemblBacteria; AAD36704; AAD36704; TM_1637. DR EnsemblBacteria; AGL50570; AGL50570; Tmari_1646. DR GeneID; 897366; -. DR KEGG; tma:TM1637; -. DR KEGG; tmi:THEMA_06060; -. DR KEGG; tmm:Tmari_1646; -. DR KEGG; tmw:THMA_1678; -. DR PATRIC; 23938248; VBITheMar51294_1656. DR eggNOG; ENOG4105P78; Bacteria. DR eggNOG; ENOG4111Z2M; LUCA. DR OMA; YKEILIT; -. DR OrthoDB; EOG654P5W; -. DR BioCyc; TMAR243274:GC6P-1683-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.25.10.10; -; 2. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR SUPFAM; SSF48371; SSF48371; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 206 AA; 24564 MW; 80BE89246520DB09 CRC64; MSDEKRKKEE LIERIVSEKG EEAFPKLLEL LEDEDPEVKE IVSEVFYRLG DRAREFLFNE IQKRRERGFE KNDITNLYII DILGDLGEKR MKNVLYELME KYDSEEALLI IYEALAKIGE GEVFLPELEY LMFEDAYRKE LCEQVAMVLA NIPTERSLRI LLKALKSKEF SEDQKEFFRR AVEMILYRKP ELSKYVTDEE RKELGL // ID Q9WZX1_THEMA Unreviewed; 160 AA. AC Q9WZX1; G4FCV7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35949.1}; GN OrderedLocusNames=TM_0867 {ECO:0000313|EMBL:AAD35949.1}; GN ORFNames=Tmari_0869 {ECO:0000313|EMBL:AGL49794.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35949.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35949.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35949.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49794.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49794.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35949.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49794.1; -; Genomic_DNA. DR PIR; F72322; F72322. DR RefSeq; NP_228676.1; NC_000853.1. DR RefSeq; WP_004080737.1; NZ_CP011107.1. DR STRING; 243274.TM0867; -. DR EnsemblBacteria; AAD35949; AAD35949; TM_0867. DR EnsemblBacteria; AGL49794; AGL49794; Tmari_0869. DR GeneID; 898540; -. DR KEGG; tma:TM0867; -. DR KEGG; tmi:THEMA_00300; -. DR KEGG; tmm:Tmari_0869; -. DR KEGG; tmw:THMA_0889; -. DR PATRIC; 23936662; VBITheMar51294_0880. DR OMA; FSLYQIR; -. DR OrthoDB; EOG68DD2R; -. DR BioCyc; TMAR243274:GC6P-897-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 74 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 115 132 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 156 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 160 AA; 18792 MW; D5F475DC953EB1E0 CRC64; MIWFLEGLSF SVVGFFVSVF FSYLYLKRRE RIDLSALKIF NEFTTLGLIY LFSWMLNSLF FYLIVVVLAV LFFLGKSVRF LMSINEQYRI MFLSFGYNDK EFSLYQIRKK LFKSFVRPAL KFFGLYIVFS SADLKNPFVI SILLVLGVTI GLLNGVDKFD // ID Q9WZ02_THEMA Unreviewed; 321 AA. AC Q9WZ02; G4FDT9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 90. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35617.1}; DE SubName: Full=Oligopeptide transport system permease protein OppB {ECO:0000313|EMBL:AGL49454.1}; GN OrderedLocusNames=TM_0532 {ECO:0000313|EMBL:AAD35617.1}; GN ORFNames=Tmari_0529 {ECO:0000313|EMBL:AGL49454.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35617.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35617.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35617.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49454.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49454.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35617.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49454.1; -; Genomic_DNA. DR PIR; B72367; B72367. DR RefSeq; NP_228342.1; NC_000853.1. DR RefSeq; WP_004081376.1; NZ_CP011107.1. DR STRING; 243274.TM0532; -. DR EnsemblBacteria; AAD35617; AAD35617; TM_0532. DR EnsemblBacteria; AGL49454; AGL49454; Tmari_0529. DR GeneID; 897584; -. DR KEGG; tma:TM0532; -. DR KEGG; tmi:THEMA_02015; -. DR KEGG; tmm:Tmari_0529; -. DR KEGG; tmw:THMA_0545; -. DR PATRIC; 23935971; VBITheMar51294_0540. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR KO; K02033; -. DR OMA; AIPVMGV; -. DR OrthoDB; EOG66F098; -. DR BioCyc; TMAR243274:GC6P-556-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 9 27 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 96 120 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 132 157 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 184 203 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 246 268 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 288 314 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 96 307 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 321 AA; 36200 MW; 4D3F19C06C1425F4 CRC64; MLKYIARRLI IMIPELIIIS FIVFIIMEAA PGDFLDMYRL DPSVSQQFLE KMEKELGLDK PWIVQYGIWL KNVLKGDFGY SFYYRRPVST LIWERVFATV ILSVSSLAFE WLLGIIVGVF SALKKYSIWD KILTVVAFSG IALPGFFLAI LLLYMAAKTG WFPIAGMVSV NHNQMTTWEK FKDIASHLVL PTIALGFGGF ASLMRYMRGS LLDVLNEDYV EFARAKGMPE RVVIYKHALR NAINPMITFL GFSISNVLGG AVIIENIFAW PGMGRLIYQA LLQQDIYIVM ASAVISAIML VIGNLVADVL LAAVDPRVRF E // ID Q9X178_THEMA Unreviewed; 474 AA. AC Q9X178; G4FF93; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 79. DE RecName: Full=RNA-splicing ligase RtcB {ECO:0000256|RuleBase:RU371113}; DE EC=6.5.1.- {ECO:0000256|RuleBase:RU371113}; GN Name=rtcB {ECO:0000256|RuleBase:RU371113}; GN OrderedLocusNames=TM_1357 {ECO:0000313|EMBL:AAD36428.1}; GN ORFNames=Tmari_1364 {ECO:0000313|EMBL:AGL50288.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36428.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36428.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36428.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50288.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50288.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|RuleBase:RU371113}; CC Note=Binds 2 manganese ions per subunit. CC {ECO:0000256|RuleBase:RU371113}; CC -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU371113}. CC -!- SIMILARITY: Belongs to the RtcB family. CC {ECO:0000256|RuleBase:RU371113}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36428.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50288.1; -; Genomic_DNA. DR PIR; E72265; E72265. DR RefSeq; NP_229158.1; NC_000853.1. DR RefSeq; WP_004081553.1; NZ_CP011107.1. DR SMR; Q9X178; 1-474. DR STRING; 243274.TM1357; -. DR EnsemblBacteria; AAD36428; AAD36428; TM_1357. DR EnsemblBacteria; AGL50288; AGL50288; Tmari_1364. DR GeneID; 898123; -. DR KEGG; tma:TM1357; -. DR KEGG; tmi:THEMA_07555; -. DR KEGG; tmm:Tmari_1364; -. DR KEGG; tmw:THMA_1382; -. DR PATRIC; 23937652; VBITheMar51294_1369. DR eggNOG; ENOG4105E0Y; Bacteria. DR eggNOG; COG1690; LUCA. DR KO; K14415; -. DR OMA; YDVAHNV; -. DR OrthoDB; EOG6F81M0; -. DR BioCyc; TMAR243274:GC6P-1390-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008452; F:RNA ligase activity; IEA:InterPro. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR InterPro; IPR001233; RtcB. DR PANTHER; PTHR11118; PTHR11118; 1. DR Pfam; PF01139; RtcB; 1. DR SUPFAM; SSF103365; SSF103365; 1. DR PROSITE; PS01288; UPF0027; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Ligase {ECO:0000256|RuleBase:RU371113}; KW Manganese {ECO:0000256|RuleBase:RU371113}; KW Metal-binding {ECO:0000256|RuleBase:RU371113}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 474 AA; 52531 MW; E9AA7B3B8008349A CRC64; MKIERLDKYI WKIPKEGDMK VDAIIFTDAE SVNDPQFREA MKQLMNVATL PGIVKYALAM PDIHWGYGFP IGGVAAFDVK EGIISPGGVG FDINCGVRLM KTDLTYEDVK DRMRSLVEAI YEFVPAGVGS TGDIVLGKKG LRKVLVEGAE WAVKSGYGLE EDLERIEDGG KIHPADPSYV SEEAFERGSD ELGTLGAGNH FVEVQMVQEI YDEELAEFFG LEIGTITVMI HSGSRGFGHQ VATDYIRLMR DNLKEHNKNL PDKQLINAPF EHPLGQAYYS AMNCAANYAF ANREILGHLV RKAFWKVFGR DTRVDLIYDV AHNIAKVEEY EVDGKRRKLV VHRKGATRSL GPGSEKVPSI YREVGQPVII PGDMGTASYL LVGTKKAEEK TFGSTAHGAG RVLGRSAALK KLDYREVLDE LAEKNIVVMS KSKKTLVEEA PEVYKDVDRV VQIVHEIGIS RKVARMIPLG VVKG // ID Q9WXQ9_THEMA Unreviewed; 110 AA. AC Q9WXQ9; G4FGW7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35146.1}; GN OrderedLocusNames=TM_0052 {ECO:0000313|EMBL:AAD35146.1}; GN ORFNames=Tmari_0049 {ECO:0000313|EMBL:AGL48975.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35146.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35146.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35146.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48975.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48975.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35146.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48975.1; -; Genomic_DNA. DR PIR; E72423; E72423. DR RefSeq; NP_227868.1; NC_000853.1. DR RefSeq; WP_004082537.1; NZ_CP011107.1. DR STRING; 243274.TM0052; -. DR EnsemblBacteria; AAD35146; AAD35146; TM_0052. DR EnsemblBacteria; AGL48975; AGL48975; Tmari_0049. DR GeneID; 896876; -. DR KEGG; tma:TM0052; -. DR KEGG; tmi:THEMA_04545; -. DR KEGG; tmm:Tmari_0049; -. DR KEGG; tmw:THMA_0048; -. DR PATRIC; 23934944; VBITheMar51294_0050. DR OMA; VFLYGTF; -. DR OrthoDB; EOG6HF61X; -. DR BioCyc; TMAR243274:GC6P-52-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 48 66 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 86 103 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 110 AA; 12518 MW; 817FD24E83769F15 CRC64; MNILMFILTL ISGILYMKID LLFGIFLGVV SLVFLAGQFE ISKEKYHAHM FVGSIIVLFF AGMSLLEYLT GFLRPILGEE RITLSAGHYT LFLTGLVALF MIFKKRMRSE // ID Q9X1C8_THEMA Unreviewed; 458 AA. AC Q9X1C8; G4FFE4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36479.1}; GN OrderedLocusNames=TM_1408 {ECO:0000313|EMBL:AAD36479.1}; GN ORFNames=Tmari_1415 {ECO:0000313|EMBL:AGL50339.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36479.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36479.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36479.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50339.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50339.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36479.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50339.1; -; Genomic_DNA. DR PIR; A72258; A72258. DR RefSeq; NP_229209.1; NC_000853.1. DR RefSeq; WP_004081639.1; NZ_CP011107.1. DR STRING; 243274.TM1408; -. DR EnsemblBacteria; AAD36479; AAD36479; TM_1408. DR EnsemblBacteria; AGL50339; AGL50339; Tmari_1415. DR GeneID; 898068; -. DR KEGG; tma:TM1408; -. DR KEGG; tmi:THEMA_07275; -. DR KEGG; tmm:Tmari_1415; -. DR KEGG; tmw:THMA_1437; -. DR PATRIC; 23937762; VBITheMar51294_1420. DR eggNOG; ENOG4105U0N; Bacteria. DR eggNOG; COG4267; LUCA. DR OMA; GFELRKM; -. DR OrthoDB; EOG66QKTH; -. DR BioCyc; TMAR243274:GC6P-1445-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR031617; PelG. DR Pfam; PF16933; PelG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 41 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 53 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 95 116 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 122 141 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 153 172 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 184 203 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 223 244 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 264 285 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 319 338 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 354 373 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 380 402 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 408 424 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 458 AA; 52718 MW; B353F4DB00B77B10 CRC64; MAGKSFDLLF SRNNLFSDVL AFFYSTFVYF APWLVVLFYI IWSSRWFSPS PFFLSVLSYS LIFSMIIAGG MSFLISRFLA NCIYSRDQRK IYESYIGAVL LVFSVSLVIG LIFFAVNNQY SLVQKILACY TFVGFSLVWI LMQFASVTEK ESLAVLAFAG GIVVSVLLAR FWDISMEEKL LLTLDIGIGL IIFMLNFLIL SYLRSSIRIG FDFLLLTRKH PQLLFIGYFY YLSIWIDNFI AWKVKGIEIA PGFFMSPEYD IPKFMASLFF IPSLVVFNLS METVFQRNYK GLMQSIVSDK PMRVISENLK KLSLSLRHAF SNMFALNMVA MISCFLLRDS LRLWFNLSES FNRIFVWDVV GVSMNIAFMS LLVASLHFEY YGIALEGTAL VLTSNMILSV FFIENIPGLS FAVAFSGGFL YLLLRFKSKD FLYEVYTKQP LGLEKVKKTS WKPKEMIR // ID Q9X193_THEMA Unreviewed; 328 AA. AC Q9X193; G4FFA9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Protease inhibitor I4 {ECO:0000313|EMBL:AGL50304.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36443.1}; GN OrderedLocusNames=TM_1373 {ECO:0000313|EMBL:AAD36443.1}; GN ORFNames=Tmari_1380 {ECO:0000313|EMBL:AGL50304.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36443.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36443.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36443.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50304.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50304.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36443.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50304.1; -; Genomic_DNA. DR PIR; F72260; F72260. DR RefSeq; NP_229174.1; NC_000853.1. DR RefSeq; WP_004081570.1; NZ_CP011107.1. DR STRING; 243274.TM1373; -. DR EnsemblBacteria; AAD36443; AAD36443; TM_1373. DR EnsemblBacteria; AGL50304; AGL50304; Tmari_1380. DR GeneID; 898106; -. DR KEGG; tma:TM1373; -. DR KEGG; tmi:THEMA_07470; -. DR KEGG; tmm:Tmari_1380; -. DR KEGG; tmw:THMA_1399; -. DR PATRIC; 23937686; VBITheMar51294_1385. DR eggNOG; ENOG4108WA9; Bacteria. DR eggNOG; ENOG4111KJX; LUCA. DR OMA; ITIITRY; -. DR OrthoDB; EOG6S267S; -. DR BioCyc; TMAR243274:GC6P-1407-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.575.10; -; 1. DR InterPro; IPR008947; PLipase_C/P1_nuclease. DR SUPFAM; SSF48537; SSF48537; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50304.1}; KW Protease {ECO:0000313|EMBL:AGL50304.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 328 AA; 38220 MW; 6CC9E8247C1AF288 CRC64; MRKLSIVFLI VVSALVFSWS GHEGLTYYIV KDIVPDEMVT ITPYNYQENR VYNLSKLVLE DVCGQDTISA WEGAILPPNP SPEDGKVPAW QILTVYSSEP DWGMDQGLDL SPYQFLIGNS QGVRHMKYRI LGLEFFEADK SFYYFHDMAK EAFRKGDRYW GYRFLARALH YIEDLSQPYH NTPGEVGEIF QALFDRSIMK MLMNAHYVYD DYLAYLIYSG DEETIKTIEE ATPVFLKSEW HLVQEVRKLA LSYFPKVHRE IKKVFGEKLK ERTSDLESFT VISVEEFREA DQRGDLVLLK RYTLELIGKV SSYLKGYLID FLKAVKSF // ID Q9WYS0_THEMA Unreviewed; 214 AA. AC Q9WYS0; G4FE31; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 110. DE SubName: Full=Putative regulator for galacturonate utilization {ECO:0000313|EMBL:AGL49361.1}; DE SubName: Full=Transcriptional regulator, GntR family {ECO:0000313|EMBL:AAD35524.1}; GN OrderedLocusNames=TM_0439 {ECO:0000313|EMBL:AAD35524.1}; GN ORFNames=Tmari_0436 {ECO:0000313|EMBL:AGL49361.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35524.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35524.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35524.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:3FMS} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 6-214. RX PubMed=19307717; DOI=10.1107/S0907444909004727; RA Zheng M., Cooper D.R., Grossoehme N.E., Yu M., Hung L.W., Cieslik M., RA Derewenda U., Lesley S.A., Wilson I.A., Giedroc D.P., Derewenda Z.S.; RT "Structure of Thermotoga maritima TM0439: implications for the RT mechanism of bacterial GntR transcription regulators with Zn2+-binding RT FCD domains."; RL Acta Crystallogr. D 65:356-365(2009). RN [3] {ECO:0000213|PDB:3SXM, ECO:0000213|PDB:3SXZ} RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 75-211. RA Czelakowski G.P., Derewenda Z.S.; RT "Metal-free FCD domain of TM0439 a putative transcriptional RT regulator."; RL Submitted (JUL-2011) to the PDB data bank. RN [4] {ECO:0000213|PDB:3SXY} RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS). RA Czelakowski G.P., Derewenda Z.S.; RT "Metal-free full-length structure of Tm0439, a metal-binding FCD RT family transcriptional regulator."; RL Submitted (JUL-2011) to the PDB data bank. RN [5] {ECO:0000213|PDB:3SXK} RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 75-211 IN COMPLEX WITH ZINC. RA Czelakowski G.P., Derewenda Z.S.; RT "Zn2+-bound FCD domain of TM0439, a putative transcriptional RT regulator."; RL Submitted (JUL-2011) to the PDB data bank. RN [6] {ECO:0000313|EMBL:AGL49361.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49361.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains HTH gntR-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00452141}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35524.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49361.1; -; Genomic_DNA. DR PIR; B72377; B72377. DR RefSeq; NP_228249.1; NC_000853.1. DR RefSeq; WP_004081527.1; NZ_CP011107.1. DR PDB; 3FMS; X-ray; 2.20 A; A=6-214. DR PDB; 3SXK; X-ray; 1.63 A; A/B=75-211. DR PDB; 3SXM; X-ray; 1.55 A; A/B=75-211. DR PDB; 3SXY; X-ray; 1.65 A; A/B=1-214. DR PDB; 3SXZ; X-ray; 2.32 A; A/B=75-211. DR PDBsum; 3FMS; -. DR PDBsum; 3SXK; -. DR PDBsum; 3SXM; -. DR PDBsum; 3SXY; -. DR PDBsum; 3SXZ; -. DR STRING; 243274.TM0439; -. DR EnsemblBacteria; AAD35524; AAD35524; TM_0439. DR EnsemblBacteria; AGL49361; AGL49361; Tmari_0436. DR GeneID; 897454; -. DR KEGG; tma:TM0439; -. DR KEGG; tmi:THEMA_02530; -. DR KEGG; tmm:Tmari_0436; -. DR KEGG; tmw:THMA_0445; -. DR PATRIC; 23935763; VBITheMar51294_0445. DR eggNOG; ENOG4105DRR; Bacteria. DR eggNOG; COG1802; LUCA. DR OMA; EANITEH; -. DR OrthoDB; EOG6677QH; -. DR BioCyc; TMAR243274:GC6P-454-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.20.120.530; -; 1. DR InterPro; IPR011711; GntR_C. DR InterPro; IPR008920; TF_FadR/GntR_C. DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF07729; FCD; 1. DR Pfam; PF00392; GntR; 1. DR SMART; SM00895; FCD; 1. DR SMART; SM00345; HTH_GNTR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF48008; SSF48008; 1. DR PROSITE; PS50949; HTH_GNTR; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3FMS, ECO:0000213|PDB:3SXK, KW ECO:0000213|PDB:3SXM, ECO:0000213|PDB:3SXY}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00452277}; KW Metal-binding {ECO:0000213|PDB:3SXK}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00452220}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00452220}; KW Zinc {ECO:0000213|PDB:3SXK}. FT DOMAIN 7 74 HTH gntR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50949}. FT METAL 130 130 Zinc. {ECO:0000213|PDB:3SXK}. FT METAL 134 134 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:3SXK}. FT METAL 174 174 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:3SXK}. FT METAL 196 196 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:3SXK}. SQ SEQUENCE 214 AA; 25138 MW; 84ECC9A008DF031C CRC64; MKKIEVDLVR TKVYNLLKEM ILNHELKLGE KLNVRELSEK LGISFTPVRD ALLQLATEGL VKVVPRVGFF VTDVDEKFIR ETIETRIMME VFCLENYFDK IAGSEELLEI KGEIDDVEKS AKREIFDDSD ERLHKLFIRA SGNELIISLY EKIWDRIDLV RHLNERYVVS NREHKELIER IISGDKEGAI EKLKEHLKNV EAETIKNLYT YERS // ID Q9WZ39_THEMA Unreviewed; 218 AA. AC Q9WZ39; G4FDQ1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=DUF2225 domain-containing protein {ECO:0000313|EMBL:AGL49492.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35654.1}; GN OrderedLocusNames=TM_0569 {ECO:0000313|EMBL:AAD35654.1}; GN ORFNames=Tmari_0567 {ECO:0000313|EMBL:AGL49492.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35654.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35654.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35654.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49492.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49492.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35654.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49492.1; -; Genomic_DNA. DR PIR; H72361; H72361. DR RefSeq; NP_228379.1; NC_000853.1. DR RefSeq; WP_004081295.1; NZ_CP011107.1. DR STRING; 243274.TM0569; -. DR EnsemblBacteria; AAD35654; AAD35654; TM_0569. DR EnsemblBacteria; AGL49492; AGL49492; Tmari_0567. DR GeneID; 897633; -. DR KEGG; tma:TM0569; -. DR KEGG; tmi:THEMA_01825; -. DR KEGG; tmm:Tmari_0567; -. DR KEGG; tmw:THMA_0583; -. DR PATRIC; 23936047; VBITheMar51294_0578. DR eggNOG; ENOG4105GFC; Bacteria. DR eggNOG; COG1655; LUCA. DR KO; K09766; -. DR OMA; VMYLIGE; -. DR OrthoDB; EOG6ZSP7K; -. DR BioCyc; TMAR243274:GC6P-593-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR018708; DUF2225. DR InterPro; IPR011990; TPR-like_helical_dom. DR Pfam; PF09986; DUF2225; 1. DR SUPFAM; SSF48452; SSF48452; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 73 97 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 218 AA; 26273 MW; 69649881EF12943D CRC64; MSKFWEKEFT CPFCGTKFKK KMVFFDSIKI KARDIDLKPV FEDVNPMFYE VVTCPNCYFS AFDKDFETIT IKGEETERKL KKLLEEAKKK VELKNVENHV EAIKRYALSG MVYSVLNQRK KVAISYLKIA WLFRELGKSE EEKRYLERAL KEFESHYKYD YYEESDEPMI LFYLGVLNQI LGNRKEAARW YELLLRKYDG KSLYAKVGRE RWQELRRS // ID Q9X174_THEMA Unreviewed; 103 AA. AC Q9X174; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=TonB-dependent receptor {ECO:0000313|EMBL:AGL50284.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36424.1}; GN OrderedLocusNames=TM_1353 {ECO:0000313|EMBL:AAD36424.1}; GN ORFNames=Tmari_1360 {ECO:0000313|EMBL:AGL50284.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36424.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36424.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36424.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50284.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50284.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36424.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50284.1; -; Genomic_DNA. DR PIR; A72265; A72265. DR RefSeq; NP_229154.1; NC_000853.1. DR RefSeq; WP_010865326.1; NC_000853.1. DR STRING; 243274.TM1353; -. DR EnsemblBacteria; AAD36424; AAD36424; TM_1353. DR EnsemblBacteria; AGL50284; AGL50284; Tmari_1360. DR GeneID; 898127; -. DR KEGG; tma:TM1353; -. DR KEGG; tmm:Tmari_1360; -. DR PATRIC; 23937644; VBITheMar51294_1365. DR eggNOG; ENOG4105YRP; Bacteria. DR eggNOG; ENOG4112531; LUCA. DR OMA; ICEGEKL; -. DR OrthoDB; EOG6ND0N1; -. DR BioCyc; TMAR243274:GC6P-1386-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.1390.20; -; 1. DR InterPro; IPR028979; Ser_kin/Pase_Hpr_N-like. DR SUPFAM; SSF75138; SSF75138; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Receptor {ECO:0000313|EMBL:AGL50284.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 103 AA; 11223 MW; E1AC069D432D1A37 CRC64; MEKLGLEHVC GDLNTEVEHG FTCDLLSEVL GKAQPSTLWI TVQSHVNIIA VATVVGIKGI VLCDGHEYEK DTVKKAEENG VVLLKSQENS FIVSGKVYEL GLR // ID Q9WYV3_THEMA Unreviewed; 235 AA. AC Q9WYV3; G4FDY7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 115. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35568.1}; DE SubName: Full=Hydroxymethylpyrimidine ABC transporter, ATPase component {ECO:0000313|EMBL:AGL49405.1}; GN OrderedLocusNames=TM_0483 {ECO:0000313|EMBL:AAD35568.1}; GN ORFNames=Tmari_0480 {ECO:0000313|EMBL:AGL49405.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35568.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35568.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35568.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49405.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49405.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35568.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49405.1; -; Genomic_DNA. DR PIR; B72369; B72369. DR RefSeq; NP_228293.1; NC_000853.1. DR RefSeq; WP_004081483.1; NZ_CP011107.1. DR STRING; 243274.TM0483; -. DR EnsemblBacteria; AAD35568; AAD35568; TM_0483. DR EnsemblBacteria; AGL49405; AGL49405; Tmari_0480. DR GeneID; 897522; -. DR KEGG; tma:TM0483; -. DR KEGG; tmi:THEMA_02255; -. DR KEGG; tmm:Tmari_0480; -. DR KEGG; tmw:THMA_0496; -. DR PATRIC; 23935871; VBITheMar51294_0490. DR eggNOG; ENOG4105D7T; Bacteria. DR eggNOG; COG1116; LUCA. DR KO; K02049; -. DR OMA; CLVISAS; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-507-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35568.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35568.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 218 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 235 AA; 26811 MW; DB09FBFEB343FAD5 CRC64; MIKVSQLTVR YGELKAVEDL SLEVQRGEIL SLVGPSGCGK TTVVKAILGL IPYEGKIEIF TSRLGYCPQK DVLFDWMTVY ENAVLPLVLR KEQPPSNIKE LFERFGLSGF EEKRPYQLSG GMRQKLSLLR AVLSGEELLV LDEPFSSVDA YTRKKLQIWL SEIVHRMKST VVLITHDVEE AVFLSDRILI LSDRPARILK EIRVPFSKPR TIKTFSDPRF SEIEEEVLET LMNQP // ID Q9WZI2_THEMA Unreviewed; 139 AA. AC Q9WZI2; G4FDA0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35805.1}; GN OrderedLocusNames=TM_0723 {ECO:0000313|EMBL:AAD35805.1}; GN ORFNames=Tmari_0724 {ECO:0000313|EMBL:AGL49649.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35805.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35805.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35805.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49649.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49649.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35805.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49649.1; -; Genomic_DNA. DR PIR; A72342; A72342. DR RefSeq; NP_228532.1; NC_000853.1. DR RefSeq; WP_004081009.1; NZ_CP011107.1. DR PDB; 1VMJ; X-ray; 1.52 A; A=1-139. DR PDBsum; 1VMJ; -. DR STRING; 243274.TM0723; -. DR EnsemblBacteria; AAD35805; AAD35805; TM_0723. DR EnsemblBacteria; AGL49649; AGL49649; Tmari_0724. DR GeneID; 898390; -. DR KEGG; tma:TM0723; -. DR KEGG; tmi:THEMA_01045; -. DR KEGG; tmm:Tmari_0724; -. DR KEGG; tmw:THMA_0739; -. DR PATRIC; 23936366; VBITheMar51294_0736. DR eggNOG; ENOG4108RN8; Bacteria. DR eggNOG; COG0432; LUCA. DR OMA; CLVNAMH; -. DR OrthoDB; EOG6065B2; -. DR BioCyc; TMAR243274:GC6P-749-MONOMER; -. DR BRENDA; 2.5.1.3; 6331. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.60.120.460; -; 1. DR InterPro; IPR001602; UPF0047. DR Pfam; PF01894; UPF0047; 1. DR PIRSF; PIRSF004681; UCP004681; 1. DR SUPFAM; SSF111038; SSF111038; 1. DR TIGRFAMs; TIGR00149; TIGR00149_YjbQ; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VMJ}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT METAL 81 81 Sodium; via tele nitrogen. FT {ECO:0000213|PDB:1VMJ}. FT METAL 88 88 Sodium. {ECO:0000213|PDB:1VMJ}. FT METAL 92 92 Sodium; via tele nitrogen. FT {ECO:0000213|PDB:1VMJ}. SQ SEQUENCE 139 AA; 16329 MW; E3660BCA45A78C88 CRC64; MKSYRKELWF HTKRRREFIN ITPLLEECVR ESGIKEGLLL CNAMHITASV FINDDEPGLH HDFEVWLEKL APEKPYSQYK HNDTGEDNAD AHLKRTIMGR EVVIAITDRK MDLGPWEQVF YGEFDGMRPK RVLVKIIGE // ID Q9X068_THEMA Unreviewed; 40 AA. AC Q9X068; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Methyl-accepting chemoreceptor-related protein {ECO:0000313|EMBL:AAD36052.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL49901.1}; GN OrderedLocusNames=TM_0973 {ECO:0000313|EMBL:AAD36052.1}; GN ORFNames=Tmari_0976 {ECO:0000313|EMBL:AGL49901.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36052.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36052.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36052.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49901.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49901.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36052.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49901.1; -; Genomic_DNA. DR PIR; B72309; B72309. DR RefSeq; NP_228781.1; NC_000853.1. DR RefSeq; WP_010865230.1; NZ_CP011107.1. DR DNASU; 898719; -. DR EnsemblBacteria; AAD36052; AAD36052; TM_0973. DR EnsemblBacteria; AGL49901; AGL49901; Tmari_0976. DR GeneID; 898719; -. DR KEGG; tma:TM0973; -. DR KEGG; tmi:THEMA_09480; -. DR KEGG; tmm:Tmari_0976; -. DR KEGG; tmw:THMA_0996; -. DR PATRIC; 23936875; VBITheMar51294_0986. DR OrthoDB; EOG6G20X5; -. DR BioCyc; TMAR243274:GC6P-1003-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Receptor {ECO:0000313|EMBL:AAD36052.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 40 AA; 4503 MW; C018ADB98EA52FAB CRC64; MVADEIRKLA EESRSSSSKI AEYLSTINTG IRRYRISSPS // ID Q9WXN3_THEMA Unreviewed; 68 AA. AC Q9WXN3; G4FGU3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35120.1}; GN OrderedLocusNames=TM_0026 {ECO:0000313|EMBL:AAD35120.1}; GN ORFNames=Tmari_0023 {ECO:0000313|EMBL:AGL48949.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35120.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35120.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35120.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48949.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48949.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35120.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48949.1; -; Genomic_DNA. DR PIR; D72428; D72428. DR RefSeq; NP_227842.1; NC_000853.1. DR RefSeq; WP_004082479.1; NZ_CP011107.1. DR STRING; 243274.TM0026; -. DR EnsemblBacteria; AAD35120; AAD35120; TM_0026. DR EnsemblBacteria; AGL48949; AGL48949; Tmari_0023. DR GeneID; 896844; -. DR KEGG; tma:TM0026; -. DR KEGG; tmi:THEMA_04670; -. DR KEGG; tmm:Tmari_0023; -. DR KEGG; tmw:THMA_0022; -. DR PATRIC; 23934892; VBITheMar51294_0024. DR OMA; TIFAWAF; -. DR OrthoDB; EOG65N1G7; -. DR BioCyc; TMAR243274:GC6P-26-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 53 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 68 AA; 8122 MW; B27E993610EFE698 CRC64; MFTKAVLSIF SWALVLELIV LFYYLWRGLR PVEFYLNLGL LGLTVPFLVF LVVREKKKRR EEDDGKDR // ID Q9WYC2_THEMA Unreviewed; 150 AA. AC Q9WYC2; G4FHK0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Transcriptional regulator, PadR family {ECO:0000313|EMBL:AGL49210.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35374.1}; GN OrderedLocusNames=TM_0286 {ECO:0000313|EMBL:AAD35374.1}; GN ORFNames=Tmari_0284 {ECO:0000313|EMBL:AGL49210.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35374.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35374.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35374.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49210.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49210.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35374.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49210.1; -; Genomic_DNA. DR PIR; D72396; D72396. DR RefSeq; NP_228098.1; NC_000853.1. DR RefSeq; WP_004082997.1; NZ_CP011107.1. DR STRING; 243274.TM0286; -. DR EnsemblBacteria; AAD35374; AAD35374; TM_0286. DR EnsemblBacteria; AGL49210; AGL49210; Tmari_0284. DR GeneID; 897205; -. DR KEGG; tma:TM0286; -. DR KEGG; tmi:THEMA_03295; -. DR KEGG; tmm:Tmari_0284; -. DR KEGG; tmw:THMA_0293; -. DR PATRIC; 23935451; VBITheMar51294_0291. DR eggNOG; ENOG4105NT9; Bacteria. DR eggNOG; COG1695; LUCA. DR OMA; CAKDIRY; -. DR OrthoDB; EOG6P338B; -. DR BioCyc; TMAR243274:GC6P-299-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005149; Tscrpt_reg_PadR_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF03551; PadR; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 12 80 PadR. {ECO:0000259|Pfam:PF03551}. SQ SEQUENCE 150 AA; 17531 MW; E1979B6D2685338B CRC64; MRDTKGHLKF LVLHIISQQP SHGYYIMKKI SQIIGAEPPS PGALYPILSS LRKQKYIETY NEGKRKVYRL TDKGRKYLEE HKEEIKKALD FAERFRVFSE ICGLSLRNVV DVIFKNAKDL TPEQKKKLKH ATEDFERNVY NIIYGGKNSK // ID Q9X0J1_THEMA Unreviewed; 80 AA. AC Q9X0J1; G4FEP1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36183.1}; GN OrderedLocusNames=TM_1107 {ECO:0000313|EMBL:AAD36183.1}; GN ORFNames=Tmari_1113 {ECO:0000313|EMBL:AGL50037.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36183.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36183.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36183.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50037.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50037.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36183.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50037.1; -; Genomic_DNA. DR PIR; E72295; E72295. DR RefSeq; NP_228913.1; NC_000853.1. DR RefSeq; WP_004080321.1; NZ_CP011107.1. DR STRING; 243274.TM1107; -. DR EnsemblBacteria; AAD36183; AAD36183; TM_1107. DR EnsemblBacteria; AGL50037; AGL50037; Tmari_1113. DR GeneID; 898658; -. DR KEGG; tma:TM1107; -. DR KEGG; tmi:THEMA_08810; -. DR KEGG; tmm:Tmari_1113; -. DR KEGG; tmw:THMA_1130; -. DR PATRIC; 23937147; VBITheMar51294_1122. DR KO; K05570; -. DR OMA; MIWILTV; -. DR OrthoDB; EOG693GW3; -. DR BioCyc; TMAR243274:GC6P-1136-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 75 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 80 AA; 8884 MW; D82FF9A2D0CCE062 CRC64; MKWLLVSPLI LSVLQVLLGK NQWEKLLGIS SLSTKVGVLI YALSYLVPGL SQARDVAVFY LLAGGSGVIL FSYFLRRNRE // ID Q9X1M4_THEMA Unreviewed; 89 AA. AC Q9X1M4; G4FFS6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36605.1}; GN OrderedLocusNames=TM_1538 {ECO:0000313|EMBL:AAD36605.1}; GN ORFNames=Tmari_1546 {ECO:0000313|EMBL:AGL50470.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36605.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36605.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36605.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50470.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50470.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36605.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50470.1; -; Genomic_DNA. DR PIR; F72242; F72242. DR RefSeq; NP_229338.1; NC_000853.1. DR RefSeq; WP_004081921.1; NZ_CP011107.1. DR STRING; 243274.TM1538; -. DR EnsemblBacteria; AAD36605; AAD36605; TM_1538. DR EnsemblBacteria; AGL50470; AGL50470; Tmari_1546. DR GeneID; 897977; -. DR KEGG; tma:TM1538; -. DR KEGG; tmi:THEMA_06595; -. DR KEGG; tmm:Tmari_1546; -. DR KEGG; tmw:THMA_1572; -. DR PATRIC; 23938036; VBITheMar51294_1556. DR eggNOG; ENOG410680E; Bacteria. DR eggNOG; ENOG410XUGZ; LUCA. DR OMA; ESFGEKW; -. DR OrthoDB; EOG6V4GHS; -. DR BioCyc; TMAR243274:GC6P-1578-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR019301; Flagellar_prot_FlgJ_N. DR Pfam; PF10135; Rod-binding; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 30 75 Rod-binding. {ECO:0000259|Pfam:PF10135}. SQ SEQUENCE 89 AA; 10360 MW; 0EDDB87C51F5CEDB CRC64; MFVYGVSSNI KNLRDASIEF VSDLFYRIFK EMYESIPKYD LVPETTAEKW FKEMLLQEYS KHAAEQSPLA DMVMKSLGGK KISSLPQRK // ID Q9X1N3_THEMA Unreviewed; 470 AA. AC Q9X1N3; G4FFT5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 100. DE SubName: Full=Deoxyguanosinetriphosphate triphosphohydrolase {ECO:0000313|EMBL:AGL50479.1}; DE EC=3.1.5.1 {ECO:0000313|EMBL:AGL50479.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36614.1}; GN OrderedLocusNames=TM_1547 {ECO:0000313|EMBL:AAD36614.1}; GN ORFNames=Tmari_1555 {ECO:0000313|EMBL:AGL50479.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36614.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36614.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36614.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50479.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50479.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36614.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50479.1; -; Genomic_DNA. DR PIR; F72238; F72238. DR RefSeq; NP_229347.1; NC_000853.1. DR RefSeq; WP_004081938.1; NZ_CP011107.1. DR STRING; 243274.TM1547; -. DR DNASU; 897606; -. DR EnsemblBacteria; AAD36614; AAD36614; TM_1547. DR EnsemblBacteria; AGL50479; AGL50479; Tmari_1555. DR GeneID; 897606; -. DR KEGG; tma:TM1547; -. DR KEGG; tmi:THEMA_06545; -. DR KEGG; tmm:Tmari_1555; -. DR KEGG; tmw:THMA_1582; -. DR PATRIC; 23938056; VBITheMar51294_1565. DR eggNOG; ENOG4105DCI; Bacteria. DR eggNOG; COG1078; LUCA. DR KO; K06885; -. DR OMA; KLYFPKD; -. DR OrthoDB; EOG6WX4K7; -. DR BioCyc; TMAR243274:GC6P-1588-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008832; F:dGTPase activity; IBA:GO_Central. DR GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central. DR Gene3D; 1.10.3210.10; -; 2. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL50479.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 48 205 HDc. {ECO:0000259|SMART:SM00471}. SQ SEQUENCE 470 AA; 55015 MW; B1E18FC7A34FFACD CRC64; MFKKVSRDPV HSEIYLYPLE ILATDTKVVQ RLRFLSQLAG ATVVYPGATH TRFAHSLGTM HVAGLYARNL FKESDRIRIV RLAALLHDVG HGPFSHQFDD VVFKRYGYED GHDEFRNRLI TEKLPEEMMR VFNSYNERLK QAVIEDIRES VGEVSLEDAF QEIAKRVVEV YRGEETGSVD FNIIQGPLGA DRLDFLLRDS YYSGVGHFAP MNVDRVLRNS LVKEVDGKEI LCYHVKVVDN IYSILFSRFM MYKNVYFHKT SRAADLMIQE ILLRACEILD LEERLKDLDE FLELTDYSIL RELELKGDSE TKKLVERFKN RDLWKMVVER PFSAEGFDPS ELSLSAARNL IDKIVENIDR VLSSVNVEDS DKSILEEIRD NKEKFFRIDT PYKLTIFHPD EFLQNNVFLY DPKHDEILTV DEYVKKYPAY RLMVSNMIQI VRVYVTEDVR EVLFKYGVIP EDGRRVITRW // ID Q9WYG4_THEMA Unreviewed; 224 AA. AC Q9WYG4; G4FHP2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35416.1}; GN OrderedLocusNames=TM_0329 {ECO:0000313|EMBL:AAD35416.1}; GN ORFNames=Tmari_0327 {ECO:0000313|EMBL:AGL49252.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35416.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35416.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35416.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49252.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49252.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35416.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49252.1; -; Genomic_DNA. DR PIR; C72390; C72390. DR RefSeq; NP_228140.1; NC_000853.1. DR RefSeq; WP_004083091.1; NZ_CP011107.1. DR STRING; 243274.TM0329; -. DR REBASE; 1812; TmaI. DR EnsemblBacteria; AAD35416; AAD35416; TM_0329. DR EnsemblBacteria; AGL49252; AGL49252; Tmari_0327. DR GeneID; 897280; -. DR KEGG; tma:TM0329; -. DR KEGG; tmi:THEMA_03075; -. DR KEGG; tmm:Tmari_0327; -. DR KEGG; tmw:THMA_0337; -. DR PATRIC; 23935539; VBITheMar51294_0334. DR eggNOG; ENOG410YPJ7; LUCA. DR OMA; PPMEREW; -. DR OrthoDB; EOG6FFS4K; -. DR BioCyc; TMAR243274:GC6P-343-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 134 157 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 224 AA; 26776 MW; 9F40DF99904C6B1F CRC64; MRKTDPLIDI FKKNKERIDI LGKAWDIFYF EGRAPDVGKR RENFIVEMIR KELSHFIKSV NQAPDTERNW DIEITFQDDS TKRYSIKTTE GFSDVKIAWD GFPTKDRILT FNFQADIFYI ARNKDKIILC VIDLEKLRDL QREVEKNESK LEEYYSLPSS NTNPRGFGLK SSTVKRLIEL SKKEENYLEI DYKPFPVELI LKAKEEYFKG WYDLIKELIE KYQQ // ID Q9WZR5_THEMA Unreviewed; 355 AA. AC Q9WZR5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=Regulator of chitobiose utilization ChiR, ROK family {ECO:0000313|EMBL:AGL49734.1}; DE SubName: Full=Transcriptional regulator, XylR-related {ECO:0000313|EMBL:AAD35890.1}; GN OrderedLocusNames=TM_0808 {ECO:0000313|EMBL:AAD35890.1}; GN ORFNames=Tmari_0809 {ECO:0000313|EMBL:AGL49734.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35890.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35890.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35890.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49734.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49734.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35890.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49734.1; -; Genomic_DNA. DR PIR; A72331; A72331. DR RefSeq; NP_228617.1; NC_000853.1. DR RefSeq; WP_010865207.1; NC_000853.1. DR STRING; 243274.TM0808; -. DR EnsemblBacteria; AAD35890; AAD35890; TM_0808. DR EnsemblBacteria; AGL49734; AGL49734; Tmari_0809. DR GeneID; 898476; -. DR KEGG; tma:TM0808; -. DR KEGG; tmi:THEMA_00610; -. DR KEGG; tmm:Tmari_0809; -. DR PATRIC; 23936536; VBITheMar51294_0820. DR eggNOG; ENOG4105UW8; Bacteria. DR eggNOG; COG1940; LUCA. DR OMA; KISMREI; -. DR OrthoDB; EOG6V1M2D; -. DR BioCyc; TMAR243274:GC6P-835-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR000600; ROK. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00480; ROK; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 355 AA; 38961 MW; 25528D8B89EBE68C CRC64; MGGTLLNISP TQHKILKLLI ENEKISMREI SEKLSVNMST VSRNFRSLLE SGFALKVEEA SPGSSGGRKT ALYTANPNKF FILGIGVEQN RLIGVVIDAK GNEVEKSEIH RSFRGDEIVN ALVDCVEPFK EKYPNTVGIS IGMPGIIKEN KVIFSSALGI EDLDLGRILS KEFGTEIFVL NDANAAVVGY GFQKKNVVYF LISVPYYLNQ PVGVGAGLWL EGSLYQGSNG AAGEFEIDIL PSILSGPATL DEVDLKNLSS DSFLKLLSKL SEVASFVSYL LDPETVIFGG DITLFSPEFH SGLAKNVRDH LEKRHISDVE VLFDERGLWT VAFGAAKAFW KRILEDYEFA GKILK // ID Q9WZZ9_THEMA Unreviewed; 91 AA. AC Q9WZZ9; G4FCS8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=SpoVS-related protein {ECO:0000313|EMBL:AAD35978.1}; DE SubName: Full=SpoVS-related protein, type 3 {ECO:0000313|EMBL:AGL49824.1}; GN OrderedLocusNames=TM_0897 {ECO:0000313|EMBL:AAD35978.1}; GN ORFNames=Tmari_0899 {ECO:0000313|EMBL:AGL49824.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35978.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35978.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35978.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49824.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49824.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35978.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49824.1; -; Genomic_DNA. DR PIR; H72317; H72317. DR RefSeq; NP_228705.1; NC_000853.1. DR RefSeq; WP_004080683.1; NZ_CP011107.1. DR STRING; 243274.TM0897; -. DR EnsemblBacteria; AAD35978; AAD35978; TM_0897. DR EnsemblBacteria; AGL49824; AGL49824; Tmari_0899. DR GeneID; 898571; -. DR KEGG; tma:TM0897; -. DR KEGG; tmi:THEMA_00150; -. DR KEGG; tmm:Tmari_0899; -. DR KEGG; tmw:THMA_0919; -. DR PATRIC; 23936725; VBITheMar51294_0911. DR eggNOG; ENOG4105T9I; Bacteria. DR eggNOG; COG2359; LUCA. DR OMA; PAFIEIQ; -. DR OrthoDB; EOG6ND0PF; -. DR BioCyc; TMAR243274:GC6P-927-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR007347; SpoVS. DR Pfam; PF04232; SpoVS; 1. DR ProDom; PD061837; SpoVS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 91 AA; 9689 MW; F4D9D1DF50571293 CRC64; MEILKVSSNS NPNKVAGAIA GSLTKSEKVE IQAIGAGAVN QAVKALAVAR RFLEESGKDL FVVPGFIEIK IGDDVRTGIS FKVFLENNKN E // ID Q9X203_THEMA Unreviewed; 168 AA. AC Q9X203; G4FG62; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36742.1}; GN OrderedLocusNames=TM_1675 {ECO:0000313|EMBL:AAD36742.1}; GN ORFNames=Tmari_1683 {ECO:0000313|EMBL:AGL50607.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36742.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36742.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36742.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50607.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50607.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36742.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50607.1; -; Genomic_DNA. DR PIR; A72226; A72226. DR RefSeq; NP_229475.1; NC_000853.1. DR RefSeq; WP_004082191.1; NZ_CP011107.1. DR STRING; 243274.TM1675; -. DR EnsemblBacteria; AAD36742; AAD36742; TM_1675. DR EnsemblBacteria; AGL50607; AGL50607; Tmari_1683. DR GeneID; 897902; -. DR KEGG; tma:TM1675; -. DR KEGG; tmi:THEMA_05865; -. DR KEGG; tmm:Tmari_1683; -. DR KEGG; tmw:THMA_1717; -. DR PATRIC; 23938324; VBITheMar51294_1692. DR eggNOG; ENOG41066IS; Bacteria. DR eggNOG; COG2245; LUCA. DR OMA; IIGAFEL; -. DR OrthoDB; EOG6DG2V4; -. DR BioCyc; TMAR243274:GC6P-1723-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010397; DUF996. DR Pfam; PF06195; DUF996; 1. DR PIRSF; PIRSF019678; UCP019678; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 44 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 109 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 160 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 168 AA; 17934 MW; 9A1978D870DB4DA5 CRC64; MNLSTAKTLA GVGMILKLFG AVPVVGWIFS LVGLILFLIG IYNISQQVGE RRIFNYLLIP AVLLLIVSVI FSVSLVASLF AGGLFAGGVT LAGFVTIVVL GIIALVYKVK AYRMIAESLK ISVFNTAASF YKWGAILLVV FGMGFILMFV GDILTIVGFF SKPSEEAA // ID Q9X1B5_THEMA Unreviewed; 350 AA. AC Q9X1B5; G4FFD1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36466.1}; GN OrderedLocusNames=TM_1395 {ECO:0000313|EMBL:AAD36466.1}; GN ORFNames=Tmari_1402 {ECO:0000313|EMBL:AGL50326.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36466.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36466.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36466.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50326.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50326.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36466.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50326.1; -; Genomic_DNA. DR PIR; D72259; D72259. DR RefSeq; NP_229196.1; NC_000853.1. DR RefSeq; WP_004081606.1; NZ_CP011107.1. DR STRING; 243274.TM1395; -. DR EnsemblBacteria; AAD36466; AAD36466; TM_1395. DR EnsemblBacteria; AGL50326; AGL50326; Tmari_1402. DR GeneID; 898081; -. DR KEGG; tma:TM1395; -. DR KEGG; tmi:THEMA_07340; -. DR KEGG; tmm:Tmari_1402; -. DR KEGG; tmw:THMA_1424; -. DR PATRIC; 23937736; VBITheMar51294_1407. DR eggNOG; ENOG4105WYY; Bacteria. DR eggNOG; ENOG41127PQ; LUCA. DR OMA; NLDEGEF; -. DR OrthoDB; EOG6B3618; -. DR BioCyc; TMAR243274:GC6P-1432-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 224 251 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 350 AA; 40091 MW; 7BF5C10633655992 CRC64; MELVVDAHEL KEWVYLLDKL VGTTEPTARF LSFFYRDGLW VSASDNCAKV EIFLGEIPRF EGSRIVSLDL VKYFLSDVKV SDVRITVLQE RLVLKAGNEV LDVRCKTGEI PPGDGEEEFL CTLTKREFEG ALNFASSNLD EGEFLILLFE EKDVLMFGAS AGIMTLAQIS TIPKKPFSTK IPYVTVRHIF KAFQRLDVQT LDFYEKSGKL VVKYPHFVME VCGDEVSEEE IKKLKSLLEE KTAERIEARR QVLAKLVRKA AVLSRGDYAT ISRRGENLKV QVKRKNLSYT AELFVESGRD FVVVFPSKKL RSALARMDTE RIFLEITERF LKISNFSGTR VIYLELEEFF // ID Q9WY97_THEMA Unreviewed; 130 AA. AC Q9WY97; G4FHH0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35345.1}; GN OrderedLocusNames=TM_0256 {ECO:0000313|EMBL:AAD35345.1}; GN ORFNames=Tmari_0254 {ECO:0000313|EMBL:AGL49180.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35345.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35345.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35345.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49180.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49180.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35345.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49180.1; -; Genomic_DNA. DR PIR; H72399; H72399. DR RefSeq; NP_228070.1; NC_000853.1. DR RefSeq; WP_004082960.1; NZ_CP011107.1. DR STRING; 243274.TM0256; -. DR EnsemblBacteria; AAD35345; AAD35345; TM_0256. DR EnsemblBacteria; AGL49180; AGL49180; Tmari_0254. DR GeneID; 897164; -. DR KEGG; tma:TM0256; -. DR KEGG; tmi:THEMA_03445; -. DR KEGG; tmm:Tmari_0254; -. DR KEGG; tmw:THMA_0263; -. DR PATRIC; 23935387; VBITheMar51294_0259. DR OMA; SGCFEAR; -. DR OrthoDB; EOG64R667; -. DR BioCyc; TMAR243274:GC6P-269-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 58 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 130 AA; 15613 MW; 4B7E7C228E1CABB7 CRC64; MAVIRFRVPF WYKFIMILLW VVSFDLTIFL FYKPLHSVLR YSILILDIIF GVWVFSLFKK EIVIDVEKSR LILGKESFDL SSIERVERYG MSIVFYLSDG TRRVFSHPIE DFELLRKLID EKGSGWFETR // ID Q9WZY2_THEMA Unreviewed; 384 AA. AC Q9WZY2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Oxaloacetate decarboxylase, beta subunit {ECO:0000313|EMBL:AAD35961.1}; DE SubName: Full=Sodium ion-translocating decarboxylase, beta subunit {ECO:0000313|EMBL:AGL49807.1}; DE EC=4.1.1.70 {ECO:0000313|EMBL:AGL49807.1}; GN OrderedLocusNames=TM_0880 {ECO:0000313|EMBL:AAD35961.1}; GN ORFNames=Tmari_0882 {ECO:0000313|EMBL:AGL49807.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35961.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35961.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35961.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49807.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49807.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35961.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49807.1; -; Genomic_DNA. DR PIR; B72324; B72324. DR RefSeq; NP_228688.1; NC_000853.1. DR RefSeq; WP_010865216.1; NC_000853.1. DR STRING; 243274.TM0880; -. DR EnsemblBacteria; AAD35961; AAD35961; TM_0880. DR EnsemblBacteria; AGL49807; AGL49807; Tmari_0882. DR GeneID; 898554; -. DR KEGG; tma:TM0880; -. DR KEGG; tmm:Tmari_0882; -. DR PATRIC; 23936691; VBITheMar51294_0894. DR eggNOG; ENOG4105D9Q; Bacteria. DR eggNOG; COG1883; LUCA. DR KO; K01572; -. DR OMA; PMIADPK; -. DR OrthoDB; EOG6VTK44; -. DR BioCyc; TMAR243274:GC6P-910-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0018801; F:glutaconyl-CoA decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR InterPro; IPR005661; OadB_MmdB. DR Pfam; PF03977; OAD_beta; 1. DR PIRSF; PIRSF015658; MmdB_OadB; 1. DR TIGRFAMs; TIGR01109; Na_pump_decarbB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000313|EMBL:AGL49807.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 29 48 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 71 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 113 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 139 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 171 198 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 219 245 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 282 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 294 314 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 362 383 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 384 AA; 41116 MW; 115FEDDF4F2B6876 CRC64; MILNTKGVEK LSIISALANF FAQTAFPHLT FGNIAMFAVA IALLYVAIVK HSEPLLLIPI AFGIILANIP VETTGILNEG GFLYYIKKGL DLGIYPPLIF LGIGALTDFS FMLSYPITIF LGAAAQMGIF FTFFVAKVLG FSLKQAASIA IIGGADGPTA IYITNTLSPE LIAPIAISAY SYIALIPILQ PVVSRILVSK EERKIRMKPP RKVSRFERLS FPIVITIVTA LLIPKSLPLV GSLMFGNLLR EAGIVKRLVE AASRYILDTV TILLMLSVGA SARADVFLTP QSLMIFFLGA AAFIVSMSSG ILFAKLMNLF LKDKINPLIG AAGVSAVPDS ARVAQKLAQE EDPRNHILMH AMGPNVAGVI GSATVAGVFL MFLS // ID Q9X176_THEMA Unreviewed; 116 AA. AC Q9X176; G4FF91; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=DRTGG domain-containing protein {ECO:0000313|EMBL:AGL50286.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36426.1}; GN OrderedLocusNames=TM_1355 {ECO:0000313|EMBL:AAD36426.1}; GN ORFNames=Tmari_1362 {ECO:0000313|EMBL:AGL50286.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36426.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36426.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36426.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50286.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50286.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36426.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50286.1; -; Genomic_DNA. DR PIR; C72265; C72265. DR RefSeq; NP_229156.1; NC_000853.1. DR RefSeq; WP_004081551.1; NZ_CP011107.1. DR STRING; 243274.TM1355; -. DR DNASU; 898125; -. DR EnsemblBacteria; AAD36426; AAD36426; TM_1355. DR EnsemblBacteria; AGL50286; AGL50286; Tmari_1362. DR GeneID; 898125; -. DR KEGG; tma:TM1355; -. DR KEGG; tmi:THEMA_07565; -. DR KEGG; tmm:Tmari_1362; -. DR KEGG; tmw:THMA_1380; -. DR PATRIC; 23937648; VBITheMar51294_1367. DR eggNOG; ENOG4105M07; Bacteria. DR eggNOG; ENOG4111UPR; LUCA. DR OMA; IIFVRGK; -. DR OrthoDB; EOG6WT8KD; -. DR BioCyc; TMAR243274:GC6P-1388-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.40.1390.20; -; 1. DR InterPro; IPR010766; DRTGG. DR InterPro; IPR028979; Ser_kin/Pase_Hpr_N-like. DR Pfam; PF07085; DRTGG; 1. DR SUPFAM; SSF75138; SSF75138; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 103 DRTGG. {ECO:0000259|Pfam:PF07085}. SQ SEQUENCE 116 AA; 12785 MW; 691979A9ED8B5608 CRC64; MTIEEIARIV EGEILCGNKD LNIERAVATD LMSDVLAFAE PNVLLITGLH SPQAVRTAMV VGIPAVLFVR KRDIPETIVN FAKECNITVL ATNLSMFETC GRLYMNGLKP VRRAIE // ID Q9WY67_THEMA Unreviewed; 231 AA. AC Q9WY67; G4FHD8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 92. DE SubName: Full=Biotin--(Acetyl-CoA carboxylase) synthetase {ECO:0000313|EMBL:AAD35316.1}; DE SubName: Full=Biotin-protein ligase {ECO:0000313|EMBL:AGL49148.1}; DE EC=6.3.4.15 {ECO:0000313|EMBL:AGL49148.1}; GN OrderedLocusNames=TM_0224 {ECO:0000313|EMBL:AAD35316.1}; GN ORFNames=Tmari_0222 {ECO:0000313|EMBL:AGL49148.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35316.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35316.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35316.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49148.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49148.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains BPL/LPL catalytic domain. CC {ECO:0000256|SAAS:SAAS00514708}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35316.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49148.1; -; Genomic_DNA. DR PIR; C72401; C72401. DR RefSeq; NP_228039.1; NC_000853.1. DR RefSeq; WP_004082910.1; NZ_CP011107.1. DR STRING; 243274.TM0224; -. DR EnsemblBacteria; AAD35316; AAD35316; TM_0224. DR EnsemblBacteria; AGL49148; AGL49148; Tmari_0222. DR GeneID; 897121; -. DR KEGG; tma:TM0224; -. DR KEGG; tmi:THEMA_03605; -. DR KEGG; tmm:Tmari_0222; -. DR KEGG; tmw:THMA_0231; -. DR PATRIC; 23935320; VBITheMar51294_0226. DR eggNOG; ENOG410805E; Bacteria. DR eggNOG; COG0340; LUCA. DR KO; K03524; -. DR OMA; INESDYP; -. DR OrthoDB; EOG6DNTBX; -. DR BioCyc; TMAR243274:GC6P-237-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro. DR InterPro; IPR004408; Biotin_CoA_COase_ligase. DR InterPro; IPR004143; BPL_LPL_catalytic. DR PANTHER; PTHR12835; PTHR12835; 1. DR Pfam; PF03099; BPL_LplA_LipB; 1. DR TIGRFAMs; TIGR00121; birA_ligase; 1. DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Ligase {ECO:0000313|EMBL:AGL49148.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 175 BPL/LPL catalytic. FT {ECO:0000259|PROSITE:PS51733}. SQ SEQUENCE 231 AA; 26274 MW; 5C0A3C00DDDCFC05 CRC64; MIGEKIISFE SIDSTNRFLK ENYRFYPDGT VVVALEQTSG YGRSGRHWHS PKGGLWFSVL FKPRKPLELS FYTRVFSVAV VKTLENMKIH ANIKWPNDVY INGRKLAGVL SEGIFEGAKP LAVVVGVGMN VNNEIPAELK TRAISLKEIM GKEISIVKLM ESMLKNARVI FRKYSRKKEA LTRIWKRYLL QKEGDLISLE GKKGKIVKIN PDSLLIDFDG EIKKVYSLSP H // ID Q9WYK3_THEMA Unreviewed; 147 AA. AC Q9WYK3; G4FHT1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35456.1}; GN OrderedLocusNames=TM_0369 {ECO:0000313|EMBL:AAD35456.1}; GN ORFNames=Tmari_0367 {ECO:0000313|EMBL:AGL49292.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35456.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35456.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35456.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49292.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49292.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35456.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49292.1; -; Genomic_DNA. DR PIR; G72384; G72384. DR RefSeq; NP_228180.1; NC_000853.1. DR RefSeq; WP_004083181.1; NZ_CP011107.1. DR STRING; 243274.TM0369; -. DR EnsemblBacteria; AAD35456; AAD35456; TM_0369. DR EnsemblBacteria; AGL49292; AGL49292; Tmari_0367. DR GeneID; 897328; -. DR KEGG; tma:TM0369; -. DR KEGG; tmi:THEMA_02870; -. DR KEGG; tmm:Tmari_0367; -. DR KEGG; tmw:THMA_0377; -. DR PATRIC; 23935619; VBITheMar51294_0374. DR eggNOG; COG1318; LUCA. DR KO; K07745; -. DR OMA; RVTWVDS; -. DR OrthoDB; EOG651SZ7; -. DR BioCyc; TMAR243274:GC6P-383-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR022285; CHP03879_regulat_dom_put. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR TIGRFAMs; TIGR03879; near_KaiC_dom; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 119 147 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 147 AA; 16215 MW; EE4ADE750B3B0135 CRC64; MKLNFNPVTK EEIHQLETAL LVGTLFRKEV LEEIRNSAER LTWVDSLAVA AGALARAKAG MTASEIAEEL GRTEATIREH VKGETKAGKL VNETYELLKE GKLSVEGLIG EGIKVVTTTT GSDEKLQEVK KELEEIKQKL ESVIQKL // ID Q9WYW7_THEMA Unreviewed; 284 AA. AC Q9WYW7; G4FDX3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 92. DE SubName: Full=Nodulin 21-related protein {ECO:0000313|EMBL:AGL49419.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35582.1}; GN OrderedLocusNames=TM_0497 {ECO:0000313|EMBL:AAD35582.1}; GN ORFNames=Tmari_0494 {ECO:0000313|EMBL:AGL49419.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35582.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35582.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35582.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49419.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49419.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35582.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49419.1; -; Genomic_DNA. DR PIR; H72370; H72370. DR RefSeq; NP_228307.1; NC_000853.1. DR RefSeq; WP_004081450.1; NZ_CP011107.1. DR STRING; 243274.TM0497; -. DR DNASU; 897538; -. DR EnsemblBacteria; AAD35582; AAD35582; TM_0497. DR EnsemblBacteria; AGL49419; AGL49419; Tmari_0494. DR GeneID; 897538; -. DR KEGG; tma:TM0497; -. DR KEGG; tmi:THEMA_02185; -. DR KEGG; tmm:Tmari_0494; -. DR KEGG; tmw:THMA_0510; -. DR PATRIC; 23935899; VBITheMar51294_0504. DR eggNOG; ENOG4105R5J; Bacteria. DR eggNOG; COG1814; LUCA. DR OMA; NYYISVA; -. DR OrthoDB; EOG6Z6FQQ; -. DR BioCyc; TMAR243274:GC6P-521-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005623; C:cell; IBA:GOC. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0030026; P:cellular manganese ion homeostasis; IBA:GO_Central. DR GO; GO:0071281; P:cellular response to iron ion; IBA:GO_Central. DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central. DR GO; GO:0034755; P:iron ion transmembrane transport; IBA:GOC. DR GO; GO:0071421; P:manganese ion transmembrane transport; IBA:GO_Central. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR008217; Ccc1_fam. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF01988; VIT1; 1. DR SUPFAM; SSF103473; SSF103473; 2. DR SUPFAM; SSF47240; SSF47240; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 62 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 196 218 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 225 246 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 258 276 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 284 AA; 32050 MW; C175A2A03594D272 CRC64; MKEILDFQKN EITEYHVYRK LSKRTNKKNA EILLAIAEDE KSHYEKLKNI TGKDVKPSYI RIFWYSLLSV LFGLTFTLKL MENNEKKAER AYERLEKEYP EVVHILKDEE KHEEELLNML DEERLNYVSS MVLGLNDALV ELTGALAGLT FAFQNTKIVG LSGLITGIAA AFSMAASEYL SQRAEEGSGE SKPLKAAIYT GIAYIITVAV LVAPFLILKN PFLSLVLTLT GAVLIVLLFT FFVSVVKEKD FAKYFLEMFL LSFGVAGFSF LVGILARKIF GIEI // ID Q9WYQ0_THEMA Unreviewed; 294 AA. AC Q9WYQ0; G4FHX8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE SubName: Full=Myo-inositol ABC transporter, permease protein InoF {ECO:0000313|EMBL:AGL49341.1}; DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35504.1}; GN OrderedLocusNames=TM_0419 {ECO:0000313|EMBL:AAD35504.1}; GN ORFNames=Tmari_0416 {ECO:0000313|EMBL:AGL49341.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35504.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35504.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35504.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49341.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49341.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35504.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49341.1; -; Genomic_DNA. DR PIR; C72378; C72378. DR RefSeq; NP_228229.1; NC_000853.1. DR RefSeq; WP_004083273.1; NZ_CP011107.1. DR STRING; 243274.TM0419; -. DR TCDB; 3.A.1.1.38; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35504; AAD35504; TM_0419. DR EnsemblBacteria; AGL49341; AGL49341; Tmari_0416. DR GeneID; 897421; -. DR KEGG; tma:TM0419; -. DR KEGG; tmi:THEMA_02630; -. DR KEGG; tmm:Tmari_0416; -. DR KEGG; tmw:THMA_0425; -. DR PATRIC; 23935721; VBITheMar51294_0424. DR eggNOG; ENOG4105EW7; Bacteria. DR eggNOG; COG1175; LUCA. DR HOGENOM; HOG000220409; -. DR KO; K17238; -. DR OMA; LMQIIAT; -. DR OrthoDB; EOG6FRCV4; -. DR BioCyc; TMAR243274:GC6P-434-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 7 33 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 67 90 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 102 122 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 151 174 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 206 228 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 255 276 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 63 276 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 294 AA; 33822 MW; BCB6368711A56359 CRC64; MKKLKPWLLL SPLLIFVIIF FVIPVILTVV IAFTDMDYSF TWNFVGFQNF KDISTDFIIP RVIANTFIYT FGTLGLFNLG TALLLSLLTT SISDRWGNFF RTLWMLPRLT PSVVYGLLWL WMFDPTEYGL VNFIRGLFGL PPQDWLHSAP MWMIIFANGF IGASMGMLVF TAAIKSIPED YYRAARIDGA SWFMIVRKIT LPLIKWHLLF VTAYQTLSLL ASFEYILIIT DGGPVYRTEV WALYTYHNAF SHFRFGYGAA LSIILVIIGV ISAFVYMKFF GFESLMEKPK VEVE // ID Q9X2I9_THEMA Unreviewed; 254 AA. AC Q9X2I9; G4FGR8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 93. DE RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039}; DE EC=3.1.4.- {ECO:0000256|RuleBase:RU362039}; GN OrderedLocusNames=TM_1876 {ECO:0000313|EMBL:AAD36938.1}; GN ORFNames=Tmari_1891 {ECO:0000313|EMBL:AGL50815.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36938.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36938.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36938.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50815.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50815.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|RuleBase:RU362039}; CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CC YfcE family. {ECO:0000256|RuleBase:RU362039}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36938.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50815.1; -; Genomic_DNA. DR PIR; G72200; G72200. DR RefSeq; NP_229672.1; NC_000853.1. DR RefSeq; WP_004082427.1; NZ_CP011107.1. DR STRING; 243274.TM1876; -. DR DNASU; 897400; -. DR EnsemblBacteria; AAD36938; AAD36938; TM_1876. DR EnsemblBacteria; AGL50815; AGL50815; Tmari_1891. DR GeneID; 897400; -. DR KEGG; tma:TM1876; -. DR KEGG; tmi:THEMA_04790; -. DR KEGG; tmm:Tmari_1891; -. DR KEGG; tmw:THMA_1926; -. DR PATRIC; 23938741; VBITheMar51294_1897. DR eggNOG; ENOG4108VPS; Bacteria. DR eggNOG; COG0639; LUCA. DR OMA; HELSEYT; -. DR OrthoDB; EOG6RJV4B; -. DR BioCyc; TMAR243274:GC6P-1927-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR011152; Pesterase_MJ0912. DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29. DR PANTHER; PTHR11124; PTHR11124; 2. DR Pfam; PF12850; Metallophos_2; 1. DR PIRSF; PIRSF000883; Pesterase_MJ0912; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00040; yfcE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000256|RuleBase:RU362039}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 201 Metallophos_2. FT {ECO:0000259|Pfam:PF12850}. SQ SEQUENCE 254 AA; 28079 MW; 2E56D0D5F4C30451 CRC64; MRLAFFGDVH GNFEALKAVL EDMENKGVDE VFCLGDLVGY GPDPEAVVQT IMEKNIKTIM GNYDDAVGYS KESCGCSYAP GRETEVGDIS LKWSIENTSE KTREFLRNLP KKLSFEVEGV RFLLVHGSPL NELLEYVKPN TPPDRLKKIV ESVEENVVVN GHTHLPMVKW VMGKLVLNPG SAGRPKDGDP RASYMIVDVE NGTVSFEIVR VRYDVKTTVE KIARNGLPVE LATVLALGQT FDMGPGKVTF TLGR // ID Q9X2G4_THEMA Unreviewed; 308 AA. AC Q9X2G4; G4FGP1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36911.1}; GN OrderedLocusNames=TM_1849 {ECO:0000313|EMBL:AAD36911.1}; GN ORFNames=Tmari_1864 {ECO:0000313|EMBL:AGL50788.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36911.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36911.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36911.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50788.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50788.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36911.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50788.1; -; Genomic_DNA. DR PIR; B72203; B72203. DR RefSeq; NP_229645.1; NC_000853.1. DR RefSeq; WP_004082400.1; NZ_CP011107.1. DR EnsemblBacteria; AAD36911; AAD36911; TM_1849. DR EnsemblBacteria; AGL50788; AGL50788; Tmari_1864. DR GeneID; 897810; -. DR KEGG; tma:TM1849; -. DR KEGG; tmi:THEMA_04925; -. DR KEGG; tmm:Tmari_1864; -. DR KEGG; tmw:THMA_1899; -. DR PATRIC; 23938687; VBITheMar51294_1870. DR eggNOG; ENOG4105ZFG; Bacteria. DR eggNOG; ENOG41127WZ; LUCA. DR OMA; FFEMELP; -. DR OrthoDB; EOG6Q5NR8; -. DR BioCyc; TMAR243274:GC6P-1900-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR025491; DUF4382. DR Pfam; PF14321; DUF4382; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 28 162 DUF4382. {ECO:0000259|Pfam:PF14321}. FT COILED 250 277 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 308 AA; 34502 MW; 7396FFA1D67B95E9 CRC64; MKYVLWAILI LSLLAGCVLF TTGTNTVKVP VYLTDNPTFN IEKLLVKISN AEYHYSLDGE EYTATAALLE NEFDLLSLAG TKVQFFEMEL PEGANLEWIR LYIDAATAVT NDSTETVRVP SRKIKIIKPV IVQGGDSIVL DFDVARSLKI ATTGNGEYLL RPVIVPYHHR ERNEYGPGEG EEHRYEVEGK LKETLSGTPC LVALFEGETC PGTLVNLEIT DDDFNFEELK EATYTVCVYT DFELPEENEV ANTDEELEVD EDDMENANNE ISTILADLSP FASETFYLND STITYIFDSN LIKLTLGD // ID Q9WXM0_THEMA Unreviewed; 650 AA. AC Q9WXM0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=DNA helicase, putative {ECO:0000313|EMBL:AAD35099.1}; DE SubName: Full=Putative ATP-dependent helicase {ECO:0000313|EMBL:AGL48928.1}; GN OrderedLocusNames=TM_0005 {ECO:0000313|EMBL:AAD35099.1}; GN ORFNames=Tmari_0002 {ECO:0000313|EMBL:AGL48928.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35099.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35099.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35099.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48928.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48928.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35099.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48928.1; -; Genomic_DNA. DR PIR; G72429; G72429. DR RefSeq; NP_227821.1; NC_000853.1. DR RefSeq; WP_010865024.1; NZ_CP011107.1. DR STRING; 243274.TM0005; -. DR EnsemblBacteria; AAD35099; AAD35099; TM_0005. DR EnsemblBacteria; AGL48928; AGL48928; Tmari_0002. DR GeneID; 896813; -. DR KEGG; tma:TM0005; -. DR KEGG; tmi:THEMA_04775; -. DR KEGG; tmm:Tmari_0002; -. DR KEGG; tmw:THMA_0001; -. DR PATRIC; 23934850; VBITheMar51294_0003. DR eggNOG; ENOG4105DKE; Bacteria. DR eggNOG; COG1112; LUCA. DR OMA; DFFLIHG; -. DR OrthoDB; EOG6JQGXM; -. DR BioCyc; TMAR243274:GC6P-5-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004483; SMUBP-2/Hcs1-like. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00376; TIGR00376; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD35099.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Helicase {ECO:0000313|EMBL:AAD35099.1}; KW Hydrolase {ECO:0000313|EMBL:AAD35099.1}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD35099.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 650 AA; 74242 MW; 9378FED72603B2DF CRC64; MTVQQFIKKL VRLVELERNA EINAMLDEMK RLSGEEREKK GRAVLGLTGK FIGEELGYFL VRFGRRKKID TEIGVGDLVL ISKGNPLKSD YTGTVVEKGE RFITVAVDRL PSWKLKNVRI DLFASDITFR RQIENLMTLS SEGKKALEFL LGKRKPEESF EEEFTPFDEG LNESQREAVS LALGSSDFFL IHGPFGTGKT RTLVEYIRQE VARGKKILVT AESNLAVDNL VERLWGKVSL VRIGHPSRVS SHLKESTLAH QIETSSEYEK VKKMKEELAK LIKKRDSFTK PSPQWRRGLS DKKILEYAEK NWSARGVSKE KIKEMAEWIK LNSQIQDIRD LIERKEEIIA SRIVREAQVV LSTNSSAALE ILSGIVFDVV VVDEASQATI PSILIPISKG KKFVLAGDHK QLPPTILSED AKDLSRTLFE ELITRYPEKS SLLDTQYRMN ELLMEFPSEE FYDGKLKAAE KVRNITLFDL GVEIPNFGKF WDVVLSPKNV LVFIDTKNRS DRFERQRKDS PSRENPLEAQ IVKEVVEKLL SMGVKEDWIG IITPYDDQVN LIRELIEAKV EVHSVDGFQG REKEVIIISF VRSNKNGEIG FLEDLRRLNV SLTRAKRKLI ATGDSSTLSV HPTYRRFVEF VKKKGTYVIF // ID Q9X253_THEMA Unreviewed; 229 AA. AC Q9X253; G4FGB7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36796.1}; GN OrderedLocusNames=TM_1731 {ECO:0000313|EMBL:AAD36796.1}; GN ORFNames=Tmari_1739 {ECO:0000313|EMBL:AGL50663.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36796.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36796.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36796.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50663.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50663.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|PIRSR:PIRSR004848-1}; CC -!- SIMILARITY: Belongs to the UPF0001 family. CC {ECO:0000256|RuleBase:RU004514}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36796.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50663.1; -; Genomic_DNA. DR PIR; B72217; B72217. DR RefSeq; NP_229529.1; NC_000853.1. DR RefSeq; WP_004082246.1; NZ_CP011107.1. DR STRING; 243274.TM1731; -. DR EnsemblBacteria; AAD36796; AAD36796; TM_1731. DR EnsemblBacteria; AGL50663; AGL50663; Tmari_1739. DR GeneID; 897873; -. DR KEGG; tma:TM1731; -. DR KEGG; tmi:THEMA_05580; -. DR KEGG; tmm:Tmari_1739; -. DR KEGG; tmw:THMA_1773; -. DR PATRIC; 23938438; VBITheMar51294_1749. DR eggNOG; ENOG4105DFA; Bacteria. DR eggNOG; COG0325; LUCA. DR KO; K06997; -. DR OMA; HGSTMVR; -. DR OrthoDB; EOG6G7R84; -. DR BioCyc; TMAR243274:GC6P-1779-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR Gene3D; 3.20.20.10; -; 1. DR InterPro; IPR001608; Ala_racemase_N. DR InterPro; IPR029066; PLP-binding_barrel. DR InterPro; IPR011078; UPF0001. DR PANTHER; PTHR10146; PTHR10146; 1. DR Pfam; PF01168; Ala_racemase_N; 1. DR PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1. DR SUPFAM; SSF51419; SSF51419; 1. DR TIGRFAMs; TIGR00044; TIGR00044; 1. DR PROSITE; PS01211; UPF0001; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR004848-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 12 225 Ala_racemase_N. FT {ECO:0000259|Pfam:PF01168}. FT MOD_RES 35 35 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR004848-1}. SQ SEQUENCE 229 AA; 26420 MW; DAD7A23C6DF5CCB1 CRC64; MGLKENLERV LNRMKNAALR ANRDPSEVRL VVASKYASVQ QMEELVFLGI REFGENRAQD LVKKSEYFKG KPIIWHFIGR IQTNKVKYIV PRCELIHSVW REEELKEIEK RAEKLGKIQK ILLEVNVFKE ETKAGLLVEE VEGFLKLCQE FPHVEVLGFM TMAPYVGDPE EVRWGFRTLR ELRDELASRF NGNVKLKELS MGMSNDFEVA IEEGATMVRI GSAIFEGGK // ID Q9X0L8_THEMA Unreviewed; 418 AA. AC Q9X0L8; G4FEL4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36210.1}; GN OrderedLocusNames=TM_1134 {ECO:0000313|EMBL:AAD36210.1}; GN ORFNames=Tmari_1140 {ECO:0000313|EMBL:AGL50064.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36210.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36210.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36210.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50064.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50064.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36210.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50064.1; -; Genomic_DNA. DR PIR; B72290; B72290. DR RefSeq; NP_228940.1; NC_000853.1. DR RefSeq; WP_004080273.1; NZ_CP011107.1. DR STRING; 243274.TM1134; -. DR EnsemblBacteria; AAD36210; AAD36210; TM_1134. DR EnsemblBacteria; AGL50064; AGL50064; Tmari_1140. DR GeneID; 898630; -. DR KEGG; tma:TM1134; -. DR KEGG; tmi:THEMA_08675; -. DR KEGG; tmm:Tmari_1140; -. DR KEGG; tmw:THMA_1157; -. DR PATRIC; 23937203; VBITheMar51294_1150. DR OMA; ERNPSWN; -. DR OrthoDB; EOG6FZ4HF; -. DR BioCyc; TMAR243274:GC6P-1163-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 57 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 118 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 180 201 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 213 236 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 279 301 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 418 AA; 48081 MW; 8E29C3AC3E424E87 CRC64; MFHDVLFGSA LLLVLMKDIN LYSLLLLSGS AVTAILKRIS RAYLIVLPVS GILLWILSKE KDLVFASLIV TFFLVFSDFE NERSKVYSLA FFFVLSLIFE KNPSSFLFVS GAMALFFLHE KKFLYASVIP LLAFVPEFRL PFLLPETHQP ESGESVQQMV KNVVVVIEKF TQSGSLAMKL LWEVIFWVAV AGVVLLVVVF FKEFRMNLKV SHYVFAALGV FVVSFYLFVL FVNMVVQNVN LDVGIPELTP VGQMLSSTSS ASVTVVEIER NPSWNSVRWV LTAVSLFVVV LFFHTTLKLF LRTLKTSSEE IETEESREEE KEDIEEKEHH TERRVIHTLE DAYLFLRWKY FPGKEHLTPY ELISGKKFRH FRDLTELYVE SKYAGKGIKL PEKEIAKIFS ESEKELKKTN INLQKNLH // ID Q9WYL4_THEMA Unreviewed; 166 AA. AC Q9WYL4; G4FHU4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=NADH oxidoreductase, putative {ECO:0000313|EMBL:AAD35468.1}; DE SubName: Full=Putative NADH dehydrogenase/NAD(P)H nitroreductase {ECO:0000313|EMBL:AGL49306.1}; DE EC=1.-.-.- {ECO:0000313|EMBL:AGL49306.1}; GN OrderedLocusNames=TM_0383 {ECO:0000313|EMBL:AAD35468.1}; GN ORFNames=Tmari_0381 {ECO:0000313|EMBL:AGL49306.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35468.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35468.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35468.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49306.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49306.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35468.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49306.1; -; Genomic_DNA. DR PIR; G72383; G72383. DR RefSeq; NP_228193.1; NC_000853.1. DR RefSeq; WP_004083201.1; NZ_CP011107.1. DR STRING; 243274.TM0383; -. DR EnsemblBacteria; AAD35468; AAD35468; TM_0383. DR EnsemblBacteria; AGL49306; AGL49306; Tmari_0381. DR GeneID; 897360; -. DR KEGG; tma:TM0383; -. DR KEGG; tmi:THEMA_02805; -. DR KEGG; tmm:Tmari_0381; -. DR KEGG; tmw:THMA_0390; -. DR PATRIC; 23935649; VBITheMar51294_0389. DR eggNOG; ENOG4108ZWN; Bacteria. DR eggNOG; COG0778; LUCA. DR OMA; AMCREAP; -. DR OrthoDB; EOG64JFVW; -. DR BioCyc; TMAR243274:GC6P-397-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.109.10; -; 1. DR InterPro; IPR029479; Nitroreductase. DR InterPro; IPR000415; Nitroreductase-like. DR Pfam; PF00881; Nitroreductase; 2. DR SUPFAM; SSF55469; SSF55469; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL49306.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 59 Nitroreductase. FT {ECO:0000259|Pfam:PF00881}. FT DOMAIN 67 145 Nitroreductase. FT {ECO:0000259|Pfam:PF00881}. SQ SEQUENCE 166 AA; 19119 MW; EEA9CE7718C33A47 CRC64; MSIIYRRRSI RKYQKKDVPD ELVKEIIRAA MHAPSACNQQ PWHFVVIRNE ETKKKIAEIH PHAQMSAEAP VVILVCGDPT LEKCKGYWIQ DCSAAVENLL LRATELGLGA VWCGVYPREE RVKAFRELLG IPEHVVPFAL VPVGYPAEHP VQVDRFKPER IHYEKW // ID Q9WZ07_THEMA Unreviewed; 758 AA. AC Q9WZ07; G4FDT4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=P-loop containing nucleoside triphosphate hydrolase {ECO:0000313|EMBL:AGL49459.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35622.1}; GN OrderedLocusNames=TM_0537 {ECO:0000313|EMBL:AAD35622.1}; GN ORFNames=Tmari_0534 {ECO:0000313|EMBL:AGL49459.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35622.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35622.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35622.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49459.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49459.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35622.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49459.1; -; Genomic_DNA. DR PIR; F72363; F72363. DR RefSeq; NP_228347.1; NC_000853.1. DR RefSeq; WP_004081368.1; NZ_CP011107.1. DR STRING; 243274.TM0537; -. DR EnsemblBacteria; AAD35622; AAD35622; TM_0537. DR EnsemblBacteria; AGL49459; AGL49459; Tmari_0534. DR GeneID; 897589; -. DR KEGG; tma:TM0537; -. DR KEGG; tmi:THEMA_01990; -. DR KEGG; tmm:Tmari_0534; -. DR KEGG; tmw:THMA_0550; -. DR PATRIC; 23935981; VBITheMar51294_0545. DR eggNOG; ENOG410828B; Bacteria. DR eggNOG; ENOG410ZWZ3; LUCA. DR OMA; ANFIRYC; -. DR OrthoDB; EOG6QP0X3; -. DR BioCyc; TMAR243274:GC6P-561-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AGL49459.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 351 372 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 378 397 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 133 227 {ECO:0000256|SAM:Coils}. FT COILED 238 279 {ECO:0000256|SAM:Coils}. FT COILED 285 312 {ECO:0000256|SAM:Coils}. FT COILED 473 521 {ECO:0000256|SAM:Coils}. FT COILED 533 593 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 758 AA; 89186 MW; C045DAA40A869E7E CRC64; MKIERVHVEG FGKFENFSFP LKSGLNIIFG GNAAGKTTLA NFIRYCLTGE LPELENYRPW FSNRFGGYLE TSEGRVEFGQ GRLDPELFSF TSFISEGVDN TLNGSKKVAS FLMESYRNRP EAVELERILN EDFSVLMKKT KELEAEISNL KERVEAWKEK RRSLLLVLKR KKELSRDLQE KRRLLEEEID RFESEKSERL SSIEARINEV KAELLRVEKE LEEIERETAV PEEKVREAIE LAQKLDYLRE RGEELKREIE SLEEKSKDTE ERLKTIMKDF SVSSLEELKL KLENMKLQIE LVENEQKAKL NEIIGHLREP LREIDEKLEE IQAKIENTGD HMKRFDKTLS IFRVFVAVFL TFALVSIIFA FLKPGYLFFY LTLAGTGASV ISMWNYYRLR KKLFELESEF MNLSTQKRSL IERKNQIVSK LKETAGVDNI EELEKFLRDQ IVKKVFERIP FLSKYGSEPR KAVENVEEQM RELLILKSSV EASLSDKKKN LEELQEYSRE QEEVLKNTLK EIGVDSEDKL KVLRDLLERR ANLRKTRDSL EKEIANLMKE KEEIESSRSN ARIEELKREV EQIESELEKL VVSPLEEPFD VLEALFRKKV ELEILERAIG YIPEFKDRIK KEHEELLRGY TRDLAVELTD VYRRFFKENQ VFKVSPDLMV TINVPEEKKV VDVLNTSALK LLSFQMKRFI SRVLEIESPF VVDNTFVDLD DEKIDLLWQE LKEVSKTRQV VLFTSDRRLL KEEPVLKL // ID Q9X2I4_THEMA Unreviewed; 91 AA. AC Q9X2I4; G4FGR3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36933.1}; GN OrderedLocusNames=TM_1871 {ECO:0000313|EMBL:AAD36933.1}; GN ORFNames=Tmari_1886 {ECO:0000313|EMBL:AGL50810.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36933.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36933.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36933.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50810.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50810.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36933.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50810.1; -; Genomic_DNA. DR PIR; B72200; B72200. DR RefSeq; NP_229667.1; NC_000853.1. DR RefSeq; WP_004082422.1; NZ_CP011107.1. DR STRING; 243274.TM1871; -. DR EnsemblBacteria; AAD36933; AAD36933; TM_1871. DR EnsemblBacteria; AGL50810; AGL50810; Tmari_1886. DR GeneID; 897798; -. DR KEGG; tma:TM1871; -. DR KEGG; tmi:THEMA_04815; -. DR KEGG; tmm:Tmari_1886; -. DR KEGG; tmw:THMA_1921; -. DR PATRIC; 23938731; VBITheMar51294_1892. DR eggNOG; ENOG4106DQA; Bacteria. DR eggNOG; ENOG410Y5SX; LUCA. DR OMA; MWIIDIF; -. DR OrthoDB; EOG61S349; -. DR BioCyc; TMAR243274:GC6P-1922-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 91 AA; 10926 MW; 439D52D2A380BFC9 CRC64; MKFLFWEFGK KNKSRETAKK RLEQIVGTTK RRQMNITEII PKEILDKNSD KIKERIASWL SETFNVEKEK IKIDLEEREG HVVIITNVFF K // ID Q9WZP1_THEMA Unreviewed; 171 AA. AC Q9WZP1; G4FD40; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35866.1}; GN OrderedLocusNames=TM_0784 {ECO:0000313|EMBL:AAD35866.1}; GN ORFNames=Tmari_0785 {ECO:0000313|EMBL:AGL49710.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35866.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35866.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35866.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49710.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49710.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35866.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49710.1; -; Genomic_DNA. DR PIR; A72333; A72333. DR RefSeq; NP_228593.1; NC_000853.1. DR RefSeq; WP_004080901.1; NZ_CP011107.1. DR STRING; 243274.TM0784; -. DR EnsemblBacteria; AAD35866; AAD35866; TM_0784. DR EnsemblBacteria; AGL49710; AGL49710; Tmari_0785. DR GeneID; 898452; -. DR KEGG; tma:TM0784; -. DR KEGG; tmi:THEMA_00730; -. DR KEGG; tmm:Tmari_0785; -. DR KEGG; tmw:THMA_0803; -. DR PATRIC; 23936488; VBITheMar51294_0796. DR OMA; CDRVIDS; -. DR OrthoDB; EOG6J48N2; -. DR BioCyc; TMAR243274:GC6P-811-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 171 AA; 18491 MW; 4B89D681EE06FEE6 CRC64; MRVAAGAPVL ASGRFKRVGL KNGYTLLVDR SAVLPEELSL NGSPLEKNGA ILVDALKESD FALERDGKFF LKISQPIVVH FFEGISVKIF PELTPSVCVT GVFTGEKGIL VLGKEEAICD RVIDSFENSV RNSYDIPKFL RDVRENSGIL GIVAIAGKVV GTWAKGKLDV L // ID Q9X205_THEMA Unreviewed; 402 AA. AC Q9X205; G4FG64; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Transposase, putative {ECO:0000313|EMBL:AAD36744.1}; GN OrderedLocusNames=TM_1677 {ECO:0000313|EMBL:AAD36744.1}; GN ORFNames=Tmari_1685 {ECO:0000313|EMBL:AGL50609.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36744.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36744.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36744.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50609.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50609.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36744.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50609.1; -; Genomic_DNA. DR PIR; C72226; C72226. DR RefSeq; NP_229477.1; NC_000853.1. DR RefSeq; WP_004082193.1; NZ_CP011107.1. DR STRING; 243274.TM1677; -. DR EnsemblBacteria; AAD36744; AAD36744; TM_1677. DR EnsemblBacteria; AGL50609; AGL50609; Tmari_1685. DR GeneID; 897901; -. DR KEGG; tma:TM1677; -. DR KEGG; tmi:THEMA_05855; -. DR KEGG; tmm:Tmari_1685; -. DR KEGG; tmw:THMA_1719; -. DR PATRIC; 23938328; VBITheMar51294_1694. DR eggNOG; ENOG4108K3X; Bacteria. DR eggNOG; COG0675; LUCA. DR KO; K07496; -. DR OMA; SCCGQIR; -. DR OrthoDB; EOG6DRPD6; -. DR BioCyc; TMAR243274:GC6P-1725-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR024064; FdhE-like. DR InterPro; IPR001959; Transposase_2. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR Pfam; PF01385; OrfB_IS605; 1. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR SUPFAM; SSF144020; SSF144020; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 164 281 OrfB_IS605. {ECO:0000259|Pfam:PF01385}. FT DOMAIN 300 366 OrfB_Zn_ribbon. FT {ECO:0000259|Pfam:PF07282}. SQ SEQUENCE 402 AA; 46019 MW; 6CF9574A1BD48623 CRC64; MPGRVIRTYK LAVPGHLSQT CEELNRTAAR IYNKTMSIVR KIHRKKGFWL SWPTADKYIL RWAENIKIHV HSKQAFVQLY FQALKGYFKA AKKNQDAKPP HKKKRYLPFI WKESAVKLLP DGTLRLSLGK ERESFVVQTP LKPPLRIKQT RLVFEDGYYL HLAIEVEIEE KNAGSGVMAA DLGVLRPITC FDGKEVISYH GGVLSSTLRY RNKRLASFQS AIAECKKGSR RYNKLVRAKK RVLRRLRNQI NDIMHKITSS FIGLCLRKQI RTIVIGDVTG IRERADYSDN ANQKIHQWQF RKLIEMIRYK AEQFGIEVKL ISEANTSKTC PVCGAKNNPN GRRYHCKACG FEYHRDGVGA INIWKRYPGT GQVVAGLAPV RGVRFHPHLC GHGASLAPWK VA // ID Q9X201_THEMA Unreviewed; 385 AA. AC Q9X201; G4FG60; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36740.1}; GN OrderedLocusNames=TM_1673 {ECO:0000313|EMBL:AAD36740.1}; GN ORFNames=Tmari_1681 {ECO:0000313|EMBL:AGL50605.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36740.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36740.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36740.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50605.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50605.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36740.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50605.1; -; Genomic_DNA. DR PIR; G72225; G72225. DR RefSeq; NP_229473.1; NC_000853.1. DR RefSeq; WP_004082189.1; NZ_CP011107.1. DR STRING; 243274.TM1673; -. DR EnsemblBacteria; AAD36740; AAD36740; TM_1673. DR EnsemblBacteria; AGL50605; AGL50605; Tmari_1681. DR GeneID; 897903; -. DR KEGG; tma:TM1673; -. DR KEGG; tmi:THEMA_05875; -. DR KEGG; tmm:Tmari_1681; -. DR KEGG; tmw:THMA_1715; -. DR PATRIC; 23938320; VBITheMar51294_1690. DR OMA; HFDEELS; -. DR OrthoDB; EOG657J7S; -. DR BioCyc; TMAR243274:GC6P-1721-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 385 AA; 45202 MW; 5332AC2A1226BB87 CRC64; MDVWKVLGRY SNVLVLSKKN SILILEINGK APKPGESVRV WNNRVMTGKE LKAKLLAHFD EELSLKVLKV PGLLEFLHDI SRGFDKKYVH FVKLFVKHLV PSRFLKMNNE EKKIIMKSFP EVFESGPSSV RIRFSVKSFF EYVQKNFPIN RNINEEALRR TVTLKRPILS TEEYDVYQMN EPLSKGFAGK NYMALPLSGK YLIVVFRRRN FPFVEFKLKE EPDLTFFEDF VNDKVAVEKR ENGWVLIWKD REMMEFELPD KELLPRPEKL VDDDLLDAVF LLNSLLEENV RFASMPSFGV QEMWWEKDNN RVILVVNTVR FGRVVADVIL EGRSLSVRFY AEKNSEELSA HSEELQKEFE RLGLIAHVFF LRKDPMNWEG FNAYG // ID Q9X2G0_THEMA Unreviewed; 674 AA. AC Q9X2G0; G4FGM9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE SubName: Full=Maltodextrin glucosidase {ECO:0000313|EMBL:AGL50776.1}; DE EC=3.2.1.20 {ECO:0000313|EMBL:AGL50776.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36906.1}; GN OrderedLocusNames=TM_1844 {ECO:0000313|EMBL:AAD36906.1}; GN ORFNames=Tmari_1852 {ECO:0000313|EMBL:AGL50776.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36906.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36906.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36906.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50776.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50776.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36906.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50776.1; -; Genomic_DNA. DR PIR; G72204; G72204. DR RefSeq; NP_229640.1; NC_000853.1. DR RefSeq; WP_004082388.1; NZ_CP011107.1. DR STRING; 243274.TM1844; -. DR EnsemblBacteria; AAD36906; AAD36906; TM_1844. DR EnsemblBacteria; AGL50776; AGL50776; Tmari_1852. DR GeneID; 897620; -. DR KEGG; tma:TM1844; -. DR KEGG; tmi:THEMA_04985; -. DR KEGG; tmm:Tmari_1852; -. DR KEGG; tmw:THMA_1887; -. DR PATRIC; 23938677; VBITheMar51294_1865. DR eggNOG; ENOG410846P; Bacteria. DR eggNOG; ENOG410ZXBU; LUCA. DR OMA; EDTIFVE; -. DR OrthoDB; EOG6M3PMN; -. DR BioCyc; TMAR243274:GC6P-1895-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:2001070; F:starch binding; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 3. DR InterPro; IPR032640; AMPK1_CBM. DR InterPro; IPR002044; CBM_fam20. DR InterPro; IPR004193; Glyco_hydro_13_N. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR Pfam; PF16561; AMPK1_CBM; 2. DR Pfam; PF02922; CBM_48; 1. DR SMART; SM01065; CBM_2; 3. DR SUPFAM; SSF81296; SSF81296; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000313|EMBL:AGL50776.1}; KW Hydrolase {ECO:0000313|EMBL:AGL50776.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 24 105 CBM20 (carbohydrate binding type-20). FT {ECO:0000259|SMART:SM01065}. FT DOMAIN 143 224 CBM20 (carbohydrate binding type-20). FT {ECO:0000259|SMART:SM01065}. FT DOMAIN 283 364 CBM20 (carbohydrate binding type-20). FT {ECO:0000259|SMART:SM01065}. SQ SEQUENCE 674 AA; 75946 MW; 27922ECBF73081F8 CRC64; MKKLLILSVL LLSAFVFSDV FVENGKVIFT FEWEGAKVVY LAGTFNNWNP TALPMEEVEP GLWRAELELE PGTYQYKYVI DGTTWKEDPN APGYVDDGFG GYNGIFTLVE KDGELFIVGP QKKEESKKYE PNPDREDTIF VEDGIVVLKY YNPEAEFVTI AGSFNNWNAE EIEMYPLGDG WWEGVLELGP GVYEYKFVVN GEEWVTDPNA FAFADDGFGG KNGVFEVYEE NGELKVKSPI EETVQEETSE EAPEVAQQET AEAEPEEVEK SELKEGLSVE DGFVVFAVRK PEASEAYVAG SFNNWSTTAN PMEKEGNLWV ARIKLNPGTY QYKYVFTIAG NQVWQEDPNA PSYVPDGFGG KNGAFMLSEE DGKLVIKPLE QKSESETPFF GKYSIDLTYK YATDTFLKSL ESSHELTLGV KTDFLKATLN FKPEGSFLDS ANIKVEKDGF EVFGHYNVAS LVEGKPYEEW FAETGFGLGI SFLSYKFTAD VAFDTNAEKE RFLIGVSGEN FGTYFGSNYL LGIEKIDLAG FLSFDLLGAK TTVWTGLIFA KPVLYFVNLE VDSDNFDVNY LYYEKTSSED KGFLKASIDL FNLELYGDYN FNNKTYTVSA GYVFDDTYVL GLAYRYGDYD NFENDPDKIT VFGELRNEFA SAKLGVTYDA YKNIYLDFQG EVNF // ID Q9X1C9_THEMA Unreviewed; 716 AA. AC Q9X1C9; G4FFE5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Putative membrane protein {ECO:0000313|EMBL:AGL50340.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36480.1}; GN OrderedLocusNames=TM_1409 {ECO:0000313|EMBL:AAD36480.1}; GN ORFNames=Tmari_1416 {ECO:0000313|EMBL:AGL50340.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36480.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36480.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36480.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50340.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50340.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36480.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50340.1; -; Genomic_DNA. DR PIR; B72258; B72258. DR RefSeq; NP_229210.1; NC_000853.1. DR RefSeq; WP_004081642.1; NZ_CP011107.1. DR STRING; 243274.TM1409; -. DR EnsemblBacteria; AAD36480; AAD36480; TM_1409. DR EnsemblBacteria; AGL50340; AGL50340; Tmari_1416. DR GeneID; 898067; -. DR KEGG; tma:TM1409; -. DR KEGG; tmi:THEMA_07270; -. DR KEGG; tmm:Tmari_1416; -. DR KEGG; tmw:THMA_1438; -. DR PATRIC; 23937764; VBITheMar51294_1421. DR eggNOG; ENOG4108HW0; Bacteria. DR eggNOG; COG4878; LUCA. DR OMA; FYYKIWW; -. DR OrthoDB; EOG6X6R94; -. DR BioCyc; TMAR243274:GC6P-1446-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR018695; DUF2194. DR Pfam; PF09960; DUF2194; 1. DR SUPFAM; SSF52317; SSF52317; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 716 AA; 82403 MW; 6786DFFF5CD24D01 CRC64; MRKFLLLILV LLAFPFFSKT LLLYKGSEGG YGYNILSWLA PEPEVLGEDY EFVDVEKSLP DFEDYDFVIT CYYSSSMPGA KKYLKKLVDF LLNGGKLFII NNLGAFEDSS GDNPSLSDIN TLLNLLGVSF RYGWRQETVF SYEIEDGYLI KLPSFPVKKA FDGFEVFSSN VKIVSYAVTK KGKHPVIFYG PFGGMALFDH AFNENGEPVV DLRKIVMDIV GGYRENKVLM LDENHHIRKM FEYALFEVDS SRSGVLQKYR AIVIPDVSFL EEKEIKSYLE NGGVVILVGS GTHYIQGEVV LEKENLYIPQ DITVGERKVG YIPAPENAKA FITISGTPVS WMEKREKGAF VFFPEDLLEK WSRGILFNEF LEASDFVISP MVNAFSVFLD DFPLPAYGIE YDILGTTDEI FYYKIWWRDM KELCEDFSIK PITALVTSYE QKTDYNGFFE FLEKDSSLKV LKNLIEDERV DTGIHGYNHV PPKSENWDLE ELGKAYKSLR IFLSQLSSSY EPVAFVAPNN EIDQAGIEVL KSVFPTIKVI GTAYSLKDST GEFTLLDDAL ILPRTTSGCY PLQRLLMETV STLLNLGTYH HFSHPDDVIS LDRNPERYSW NEMFDQLRSF FRIMKENYPW LRNMDSKELY NTFKDYFENK PRILYHDKKI VIVLPRTAEL PRYFFLKAKG DVNVHGGVIL FRDKDLCVVE MREYKMEISE VIEDGR // ID Q9WZD8_THEMA Unreviewed; 156 AA. AC Q9WZD8; G4FDF4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35752.1}; GN OrderedLocusNames=TM_0670 {ECO:0000313|EMBL:AAD35752.1}; GN ORFNames=Tmari_0670 {ECO:0000313|EMBL:AGL49595.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35752.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35752.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35752.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49595.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49595.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35752.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49595.1; -; Genomic_DNA. DR PIR; C72350; C72350. DR RefSeq; NP_228479.1; NC_000853.1. DR RefSeq; WP_004081103.1; NZ_CP011107.1. DR STRING; 243274.TM0670; -. DR EnsemblBacteria; AAD35752; AAD35752; TM_0670. DR EnsemblBacteria; AGL49595; AGL49595; Tmari_0670. DR GeneID; 897785; -. DR KEGG; tma:TM0670; -. DR KEGG; tmi:THEMA_01315; -. DR KEGG; tmm:Tmari_0670; -. DR KEGG; tmw:THMA_0685; -. DR PATRIC; 23936254; VBITheMar51294_0680. DR OMA; RAFHKYD; -. DR OrthoDB; EOG6091CJ; -. DR BioCyc; TMAR243274:GC6P-695-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 156 AA; 17729 MW; 634FE23407979E6D CRC64; MDRIPVIKRS GEVLYIDRKS IKSYVDRFLS SQSDEQYFYV SDLKISSSGK RYRVEIVLKD PHGKIFSGES EGPRTSRNLL KLIGEAATEA FNRAFHKYDE VSVDDIKEVA LAGRRFVFAH LTFLKNGKES WRIGAAPLEK DLLQSVVFAV IDALVK // ID Q9X0S6_THEMA Unreviewed; 633 AA. AC Q9X0S6; G4FEE7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein {ECO:0000313|EMBL:AAD36274.1}; DE SubName: Full=Xyloglucan ABC transport system, sugar-binding protein {ECO:0000313|EMBL:AGL50130.1}; GN OrderedLocusNames=TM_1199 {ECO:0000313|EMBL:AAD36274.1}; GN ORFNames=Tmari_1206 {ECO:0000313|EMBL:AGL50130.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36274.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36274.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36274.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50130.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50130.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36274.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50130.1; -; Genomic_DNA. DR PIR; D72284; D72284. DR RefSeq; NP_229004.1; NC_000853.1. DR RefSeq; WP_004080126.1; NZ_CP011107.1. DR STRING; 243274.TM1199; -. DR TCDB; 3.A.1.5.31; the atp-binding cassette (abc) superfamily. DR DNASU; 898285; -. DR EnsemblBacteria; AAD36274; AAD36274; TM_1199. DR EnsemblBacteria; AGL50130; AGL50130; Tmari_1206. DR GeneID; 898285; -. DR KEGG; tma:TM1199; -. DR KEGG; tmi:THEMA_08335; -. DR KEGG; tmm:Tmari_1206; -. DR KEGG; tmw:THMA_1225; -. DR PATRIC; 23937340; VBITheMar51294_1217. DR eggNOG; ENOG4106MXS; Bacteria. DR eggNOG; ENOG410ZJTT; LUCA. DR KO; K02035; -. DR OMA; PTDMANI; -. DR OrthoDB; EOG63JR4Z; -. DR BioCyc; TMAR243274:GC6P-1229-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GOC. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 633 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006753495. FT DOMAIN 82 522 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. SQ SEQUENCE 633 AA; 73081 MW; AD902479D3999970 CRC64; MKKVLVFVFL ALIAVSAVMA QMLPPGIPRE KTLILPFLFA PLPAPGNWNL WAGWRAQNCG LHQFVTEPLW TINPNPEEGG IINALAAEPP IYNEDFTKLT IKLRKGIYWS DGVEFTADDV VFTIKTVKDT SGLDYHGPMQ DVKDVYALDK YTVVVELKRP NSRFHAYFVE RWGALRPMPK HIFEKVEDVV SFDFNPPVSL GPYVLKDYDP AGYWVLWEKR KDWQRTVTGQ LFGEPVPEYV LFINYGTPEK NTMAMLRHEL DVLQGSAEQL ITLLRMSKTT RSYRKTWPYI DPRDISTRGP GFNHMVYPYN IKDVRWALAL SIDIVKLAIS TYDGMVAMTP GLPLVVNKNF YEWYFKRLEP WLEELTLDLG NGETFKPWDP KAPWRLLEWA KKMYKVDIDP NSEEEVRLTL GYGWWKYAPD AAEKLLKKHG FYRDENGKWH LPNGDLWKIT ILRGPDPTDM ANIIIEGIAE QWKEFGIEVV FNVSSAASTL AGEGRFEVVN TAHGGFAGEP WGFHPDLYRC FNAFRSEFVK PIGELTLGSA LRWSDPRMDK IIEELEKTDW NDYEKVIELG VEGLKLEIEE MVAIPVFNCP ITIVFDEYYW TNFPSPENDY ARCDNFTTWP QLKYLLHMVK PAK // ID Q9X2G9_THEMA Unreviewed; 290 AA. AC Q9X2G9; G4FGP6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 95. DE SubName: Full=Multiple sugar ABC transporter, membrane-spanning permease protein MsmF {ECO:0000313|EMBL:AGL50793.1}; DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD36916.1}; GN OrderedLocusNames=TM_1854 {ECO:0000313|EMBL:AAD36916.1}; GN ORFNames=Tmari_1869 {ECO:0000313|EMBL:AGL50793.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36916.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36916.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36916.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50793.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50793.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36916.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50793.1; -; Genomic_DNA. DR PIR; G72203; G72203. DR RefSeq; NP_229650.1; NC_000853.1. DR RefSeq; WP_004082405.1; NZ_CP011107.1. DR STRING; 243274.TM1854; -. DR EnsemblBacteria; AAD36916; AAD36916; TM_1854. DR EnsemblBacteria; AGL50793; AGL50793; Tmari_1869. DR GeneID; 897807; -. DR KEGG; tma:TM1854; -. DR KEGG; tmi:THEMA_04900; -. DR KEGG; tmm:Tmari_1869; -. DR KEGG; tmw:THMA_1904; -. DR PATRIC; 23938697; VBITheMar51294_1875. DR eggNOG; ENOG4106IWW; Bacteria. DR eggNOG; COG1175; LUCA. DR KO; K02025; -. DR OMA; WNANAPG; -. DR OrthoDB; EOG69SKBS; -. DR BioCyc; TMAR243274:GC6P-1905-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 38 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 74 93 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 105 126 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 152 174 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 206 226 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 260 279 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 68 279 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 290 AA; 33482 MW; 822FEFDA9DBD7DED CRC64; MSLKRREARL GWGLVSIYLL YTAIFWGYPF VWMLILAFSR WKFVGSPKFV GLQNFFRIFE DKIFWRVFLN TMNFLSYFIP MVFIASILFA IALNRMKYFK TFVTLSFLVA YVSSGVAYSI MFQRIFSETG PINRFLYNAF GITIPWFTDP QLAMLTIAIM VTWKFVGYYG LILYSGLQAI PKSIFEAAEL DGATSWVKFW KITLPLLNPA IVTVLILAVN LSFGIFTEPY MITGGGPMNR TLTFMLYMYN TAFQRINPSY ATTIAIMTAL INFSIVIFIR KVIEKEVTVV // ID Q9WY61_THEMA Unreviewed; 438 AA. AC Q9WY61; G4FHD2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 119. DE SubName: Full=Flagellum-specific ATP synthase {ECO:0000313|EMBL:AAD35310.1}; DE SubName: Full=Flagellum-specific ATP synthase FliI {ECO:0000313|EMBL:AGL49142.1}; GN OrderedLocusNames=TM_0218 {ECO:0000313|EMBL:AAD35310.1}; GN ORFNames=Tmari_0216 {ECO:0000313|EMBL:AGL49142.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35310.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35310.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35310.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49142.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49142.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35310.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49142.1; -; Genomic_DNA. DR PIR; D72404; D72404. DR RefSeq; NP_228033.1; NC_000853.1. DR RefSeq; WP_004082899.1; NZ_CP011107.1. DR SMR; Q9WY61; 92-432. DR STRING; 243274.TM0218; -. DR EnsemblBacteria; AAD35310; AAD35310; TM_0218. DR EnsemblBacteria; AGL49142; AGL49142; Tmari_0216. DR GeneID; 897105; -. DR KEGG; tma:TM0218; -. DR KEGG; tmi:THEMA_03635; -. DR KEGG; tmm:Tmari_0216; -. DR KEGG; tmw:THMA_0225; -. DR PATRIC; 23935308; VBITheMar51294_0220. DR eggNOG; ENOG4108JIR; Bacteria. DR eggNOG; COG1157; LUCA. DR KO; K02412; -. DR OMA; FHGKVTQ; -. DR OrthoDB; EOG6W9X53; -. DR BioCyc; TMAR243274:GC6P-231-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0030257; C:type III protein secretion system complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro. DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro. DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro. DR GO; GO:0015992; P:proton transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR004100; ATPase_F1_a/bsu_N. DR InterPro; IPR032463; ATPase_T3SS_FliI. DR InterPro; IPR005714; ATPase_T3SS_FliI/YscN. DR InterPro; IPR022425; FliI_clade2. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR15184:SF9; PTHR15184:SF9; 1. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03497; FliI_clade2; 1. DR TIGRFAMs; TIGR01026; fliI_yscN; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 156 337 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 438 AA; 48326 MW; 77B56D4850F98FDB CRC64; MKDILKELKK KLSEEDFNKF NGRVTRVVGL TVESKGPDAF LGEMCKISLQ NGKNALAEVV GFREESVILM PYEDVSGLKM GCEVIRTNKV LEVGVSRKMI GRVFDGLGRP IDGKPFVPED RYPLINNPPN PLKRRRIKDP LPVGIRSIDG FITIGKGQRI GIFAGSGVGK STLLGMIARN TTADINVLAL IGERGREVRE FIERDLGEEG LKRSILVVST SDQPALARVK SLLTATSIAE FFRDLGYDVL LMVDSLTRWA MAQREVGLAV GEPPTTRGYP PSVFAGLPKI LERAGNSDKG SITAIYTVLV EADDFNEPIS DTVRSIVDGH IILSRRLAES NHYPAVDVLA SVSRLMNDIV TEEHREAANR LRSLMSAYES AKDLIEIGAY KSGTNPLVDK AVEMKDEIDS FLKQGVFEKA SFEETLQKLL DLYLRSLD // ID Q9WY37_THEMA Unreviewed; 206 AA. AC Q9WY37; G4FHA8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 124. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35286.1}; DE SubName: Full=YbbL ABC transporter ATP-binding protein {ECO:0000313|EMBL:AGL49118.1}; GN OrderedLocusNames=TM_0194 {ECO:0000313|EMBL:AAD35286.1}; GN ORFNames=Tmari_0192 {ECO:0000313|EMBL:AGL49118.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35286.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35286.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35286.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49118.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49118.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35286.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49118.1; -; Genomic_DNA. DR PIR; B72407; B72407. DR RefSeq; NP_228009.1; NC_000853.1. DR RefSeq; WP_004082842.1; NZ_CP011107.1. DR STRING; 243274.TM0194; -. DR EnsemblBacteria; AAD35286; AAD35286; TM_0194. DR EnsemblBacteria; AGL49118; AGL49118; Tmari_0192. DR GeneID; 897054; -. DR KEGG; tma:TM0194; -. DR KEGG; tmm:Tmari_0192; -. DR KEGG; tmw:THMA_0200; -. DR PATRIC; 23935256; VBITheMar51294_0196. DR eggNOG; ENOG4108UWC; Bacteria. DR eggNOG; COG1136; LUCA. DR KO; K02068; -. DR OMA; LEMRGHH; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; TMAR243274:GC6P-205-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35286.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35286.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 206 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 206 AA; 23278 MW; 449B6961FD392FCA CRC64; MFVLKNVKYK DILNIEELHI PARKITVITG KSGTGKTTLL KMLNKLISPD SGEIFFKGTP LTEIDSVELR RKVVMLPQFP VVFPGNVKEN LLMGLKFSGK KIPHDEELRK ILKFVMLEKD LNDDPEKFSG GEKQRLALAR VLLMDPEVLL LDEPTSSLDE KTGIEIIKKV SNFAKSRGKT LVMVTHNPEL RKFADVLIEL KNGRVL // ID Q9WYS1_THEMA Unreviewed; 481 AA. AC Q9WYS1; G4FE30; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Epimerase in galacturonate pathway {ECO:0000313|EMBL:AGL49362.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35525.1}; GN OrderedLocusNames=TM_0440 {ECO:0000313|EMBL:AAD35525.1}; GN ORFNames=Tmari_0437 {ECO:0000313|EMBL:AGL49362.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35525.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35525.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35525.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49362.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49362.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35525.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49362.1; -; Genomic_DNA. DR PIR; C72377; C72377. DR RefSeq; NP_228250.1; NC_000853.1. DR RefSeq; WP_004081526.1; NZ_CP011107.1. DR STRING; 243274.TM0440; -. DR EnsemblBacteria; AAD35525; AAD35525; TM_0440. DR EnsemblBacteria; AGL49362; AGL49362; Tmari_0437. DR GeneID; 897455; -. DR KEGG; tma:TM0440; -. DR KEGG; tmi:THEMA_02525; -. DR KEGG; tmm:Tmari_0437; -. DR KEGG; tmw:THMA_0446; -. DR PATRIC; 23935765; VBITheMar51294_0446. DR eggNOG; ENOG4108M8Z; Bacteria. DR eggNOG; ENOG410XR1Z; LUCA. DR OMA; DADHIKD; -. DR OrthoDB; EOG6JX7HT; -. DR BioCyc; MetaCyc:MONOMER-17952; -. DR BioCyc; TMAR243274:GC6P-455-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR032586; UxaE. DR Pfam; PF16257; UxaE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 481 AA; 55626 MW; FDA35A5CEF6EDC27 CRC64; MVLKVFKDHF GRGYEVYEKS YREKDSLSFF LTKEEEGKIL VVAGEKAPEG LSFFKKQRAE GVSFFFCERN HENLEVLRKY FPDLKPVRAG LRASFGTGDR LGITTPAHVR ALKDSGLFPI FAQQSVRENE RTGRTWRDVL DDATWGVFQE GYSEGFGADA DHVKRPEDLV SAAREGFTMF TIDPSDHVRN LSKLTEKERN EKFEEILRKE RIDRIYLGKK YSVLGEKIEF DEKNLRDAAL VYYDAIAHVD MMYQILKDET PDFDFEVSVD ETETPTSPLF HIFVVEELRR RGVEFTNLAL RFIGEWEKGI DYKGDLAQFE REIKMHAEIA RMFEGYKISL HSGSDKFSVY PAFASATGGL FHVKTAGTSY LEAVKVISMV NPELFREIYR CTLDHFEEDR KSYHISADLS KVPEVEKVKD EDLPGLFEDI NVRQLIHVTY GSVLKDASLK ERLFKTLEQN EELFYETVAK HIKRHVDLLE G // ID Q9WYN3_THEMA Unreviewed; 435 AA. AC Q9WYN3; G4FHW1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE RecName: Full=Ammonium transporter {ECO:0000256|RuleBase:RU362002}; GN OrderedLocusNames=TM_0402 {ECO:0000313|EMBL:AAD35487.1}; GN ORFNames=Tmari_0399 {ECO:0000313|EMBL:AGL49324.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35487.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35487.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35487.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49324.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49324.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362002}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362002}. CC -!- SIMILARITY: Belongs to the ammonia transporter channel CC (TC 1.A.11.2) family. {ECO:0000256|RuleBase:RU362002}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|RuleBase:RU362002}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35487.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49324.1; -; Genomic_DNA. DR PIR; H72379; H72379. DR RefSeq; NP_228212.1; NC_000853.1. DR RefSeq; WP_004083240.1; NZ_CP011107.1. DR STRING; 243274.TM0402; -. DR EnsemblBacteria; AAD35487; AAD35487; TM_0402. DR EnsemblBacteria; AGL49324; AGL49324; Tmari_0399. DR GeneID; 897397; -. DR KEGG; tma:TM0402; -. DR KEGG; tmi:THEMA_02715; -. DR KEGG; tmm:Tmari_0399; -. DR KEGG; tmw:THMA_0408; -. DR PATRIC; 23935687; VBITheMar51294_0407. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR KO; K03320; -. DR OMA; GSWEWNG; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; TMAR243274:GC6P-417-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0072488; P:ammonium transmembrane transport; IBA:GO_Central. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central. DR GO; GO:0019740; P:nitrogen utilization; IBA:GO_Central. DR GO; GO:0015695; P:organic cation transport; IBA:GO_Central. DR Gene3D; 1.10.3430.10; -; 1. DR InterPro; IPR029020; Ammonium/urea_transptr. DR InterPro; IPR001905; Ammonium_transpt. DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom. DR PANTHER; PTHR11730; PTHR11730; 1. DR Pfam; PF00909; Ammonium_transp; 1. DR SUPFAM; SSF111352; SSF111352; 1. DR TIGRFAMs; TIGR00836; amt; 1. PE 3: Inferred from homology; KW Ammonia transport {ECO:0000256|RuleBase:RU362002}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU362002}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU362002}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362002}; KW Transport {ECO:0000256|RuleBase:RU362002}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 435 Ammonium transporter. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006753472. FT TRANSMEM 30 50 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 71 89 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 109 130 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 137 159 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 171 192 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 213 230 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 242 269 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 281 314 Helical. {ECO:0000256|RuleBase:RU362002}. FT TRANSMEM 374 399 Helical. {ECO:0000256|RuleBase:RU362002}. FT DOMAIN 34 426 Ammonium_transp. FT {ECO:0000259|Pfam:PF00909}. SQ SEQUENCE 435 AA; 46427 MW; 27CE4C42EC47D4B3 CRC64; MRKRVFSLLL VLAFLSVGFA QDGVTDVGWS LDMVWILISA ALVFFMQAGF AMVESGFTRA KNTVNVLMKN LMDFAIGSVV FFIFGYWIMF GKHPLTFDPS TKEGLWDFAM WMFQMAFAGT AATIVSGAMA ERTKFPAYLA YTGFITGIIY SVVGRWIWGG GWLAQKGFID FAGSTVVHSV GGWAAMIGAS LLGPRFGKYD SQGNPKPIPG HNIPLAALGT FILWFGWFGF NGGSTLAGTN GAIGMIILNT NLAAATGALA AMVTVWAKYG KPDASMTMNG ALAGLVAITA PCAVVSPVSS LIIGAIGGVI VVFAVEFFDK VLKIDDPVGA ISVHGVNGAW GTLAVGLFAE SKYALASGMG DVNGLFFGGG VHQLGVQFLG VVSVFAWTVV TSFLVFWFIK KTIGLRVDRD IELKGLDIEE HGMEGYADFE IFTTR // ID Q9X0P1_THEMA Unreviewed; 265 AA. AC Q9X0P1; G4FEJ0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36233.1}; GN OrderedLocusNames=TM_1157 {ECO:0000313|EMBL:AAD36233.1}; GN ORFNames=Tmari_1164 {ECO:0000313|EMBL:AGL50088.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36233.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36233.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36233.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50088.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50088.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36233.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50088.1; -; Genomic_DNA. DR PIR; C72287; C72287. DR RefSeq; NP_228963.1; NC_000853.1. DR RefSeq; WP_004080223.1; NZ_CP011107.1. DR STRING; 243274.TM1157; -. DR DNASU; 898329; -. DR EnsemblBacteria; AAD36233; AAD36233; TM_1157. DR EnsemblBacteria; AGL50088; AGL50088; Tmari_1164. DR GeneID; 898329; -. DR KEGG; tma:TM1157; -. DR KEGG; tmi:THEMA_08555; -. DR KEGG; tmm:Tmari_1164; -. DR KEGG; tmw:THMA_1181; -. DR PATRIC; 23937251; VBITheMar51294_1174. DR eggNOG; ENOG4106BW1; Bacteria. DR eggNOG; ENOG410Y2XE; LUCA. DR OMA; FEAEDCV; -. DR OrthoDB; EOG64N9VH; -. DR BioCyc; TMAR243274:GC6P-1186-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 82 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 265 AA; 30475 MW; 9F894F8A5026A280 CRC64; MKIIFGIFLI FIGTLLLTTI FLDVFSLSFL TRIFHNLGLF WPLILITFGV YFIYLSVRKR WLYFLSVGVF SAFLILLLVW PYESVSTPGK YQVFTGVKRI SLKSGGFTVR FIEGEELRVY ASSGIEVSKL GSDLIVKGSL WRKLGPKIVE IELPRDTFEL SFENGAFTVK GEFEENRFTR IETKDSVLNI RFNFQKMNVP LYFEAEDCVL EVLFRLPTGV SYFIDKKDGL LLKTIEGNIV ESDFNPDLFF KLKDGVFRVH LEGGI // ID Q9X2E3_THEMA Unreviewed; 283 AA. AC Q9X2E3; G4FGL0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651}; GN OrderedLocusNames=TM_1823 {ECO:0000313|EMBL:AAD36886.1}; GN ORFNames=Tmari_1833 {ECO:0000313|EMBL:AGL50757.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36886.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36886.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36886.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50757.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50757.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: HflC and HflK could regulate a protease. CC {ECO:0000256|PIRNR:PIRNR005651}. CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflC subfamily. CC {ECO:0000256|PIRNR:PIRNR005651}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36886.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50757.1; -; Genomic_DNA. DR PIR; B72207; B72207. DR RefSeq; NP_229620.1; NC_000853.1. DR RefSeq; WP_004082369.1; NZ_CP011107.1. DR STRING; 243274.TM1823; -. DR MEROPS; I87.001; -. DR EnsemblBacteria; AAD36886; AAD36886; TM_1823. DR EnsemblBacteria; AGL50757; AGL50757; Tmari_1833. DR GeneID; 897823; -. DR KEGG; tma:TM1823; -. DR KEGG; tmi:THEMA_05080; -. DR KEGG; tmm:Tmari_1833; -. DR KEGG; tmw:THMA_1868; -. DR PATRIC; 23938633; VBITheMar51294_1843. DR eggNOG; ENOG4105EPW; Bacteria. DR eggNOG; COG0330; LUCA. DR KO; K04087; -. DR OMA; TRVDYVE; -. DR OrthoDB; EOG6B8XHM; -. DR BioCyc; TMAR243274:GC6P-1874-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0052547; P:regulation of peptidase activity; IEA:InterPro. DR InterPro; IPR001107; Band_7. DR InterPro; IPR010200; HflC. DR InterPro; IPR001972; Stomatin_fam. DR PANTHER; PTHR10264; PTHR10264; 1. DR Pfam; PF01145; Band_7; 1. DR PIRSF; PIRSF005651; HflC; 1. DR PRINTS; PR00721; STOMATIN. DR SMART; SM00244; PHB; 1. DR SUPFAM; SSF117892; SSF117892; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD36886.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000313|EMBL:AAD36886.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 27 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 22 184 PHB. {ECO:0000259|SMART:SM00244}. SQ SEQUENCE 283 AA; 32490 MW; 7551352621CE024A CRC64; MKIWMISLLI ILIVVGAILL FSSFYVLDQT QQAVVLRFGK IVAVETEPGL HFKQPFVDNV VRFDKRILLY DIEPEKIIAA DKKTLVIDTY VLWRIKDAEA FIKSLKSVKL ALPRIDDVVY SHVRNIFAKA NFDEIISEKR EDLLREVTAL SREDLKDFGI EVVDVRVKHA DLPAENEKAV YERMKAERYS IAAQIRAEGE KEARKIRAEA DKTAKVLIAE AQSKAEQIKG TGEASAVKIY AEVFSKDKDF YEFWRTMEVY RSIEKGILII GDELDALKYL KTK // ID Q9WZD3_THEMA Unreviewed; 291 AA. AC Q9WZD3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 110. DE RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985}; DE EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985}; GN OrderedLocusNames=TM_0665 {ECO:0000313|EMBL:AAD35748.1}; GN ORFNames=Tmari_0665 {ECO:0000313|EMBL:AGL49590.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35748.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35748.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35748.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49590.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49590.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: O-acetyl-L-serine + hydrogen sulfide = L- CC cysteine + acetate. {ECO:0000256|RuleBase:RU003985}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU003985}; CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- CC synthase family. {ECO:0000256|RuleBase:RU003985}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35748.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49590.1; -; Genomic_DNA. DR PIR; F72349; F72349. DR RefSeq; NP_228474.1; NC_000853.1. DR RefSeq; WP_010865179.1; NZ_CP011107.1. DR PDB; 1O58; X-ray; 1.80 A; A/B/C/D=1-291. DR PDBsum; 1O58; -. DR STRING; 243274.TM0665; -. DR EnsemblBacteria; AAD35748; AAD35748; TM_0665. DR EnsemblBacteria; AGL49590; AGL49590; Tmari_0665. DR GeneID; 897780; -. DR KEGG; tma:TM0665; -. DR KEGG; tmi:THEMA_01340; -. DR KEGG; tmm:Tmari_0665; -. DR KEGG; tmw:THMA_0680; -. DR PATRIC; 23936244; VBITheMar51294_0675. DR eggNOG; ENOG4105C6T; Bacteria. DR eggNOG; COG0031; LUCA. DR KO; K01738; -. DR OMA; VKCRIGS; -. DR OrthoDB; EOG6Q2SP8; -. DR BioCyc; TMAR243274:GC6P-690-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central. DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central. DR InterPro; IPR005856; Cys_synth. DR InterPro; IPR005859; CysK. DR InterPro; IPR001216; P-phosphate_BS. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF00291; PALP; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR01139; cysK; 1. DR TIGRFAMs; TIGR01136; cysKM; 1. DR PROSITE; PS00901; CYS_SYNTHASE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O58}; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cysteine biosynthesis {ECO:0000256|RuleBase:RU003985}; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU003985}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU003985, KW ECO:0000313|EMBL:AGL49590.1}. FT DOMAIN 4 281 PALP. {ECO:0000259|Pfam:PF00291}. SQ SEQUENCE 291 AA; 31130 MW; 2089B88B573411EE CRC64; MMERLIGSTP IVRLDSIDSR IFLKLEKNNP GGSVKDRPAL FMILDAEKRG LLKNGIVEPT SGNMGIAIAM IGAKRGHRVI LTMPETMSVE RRKVLKMLGA ELVLTPGELG MKGAVEKALE ISRETGAHML NQFENPYNVY SHQFTTGPEI LKQMDYQIDA FVAGVGTGGT ISGVGRVLKG FFGNGVKIVA VEPAKSPVLS GGQPGKHAIQ GIGAGFVPKI LDRSVIDEVI TVEDEEAYEM ARYLAKKEGL LVGISSGANV AAALKVAQKL GPDARVVTVA PDHAERYLSI L // ID Q9X1N6_THEMA Unreviewed; 296 AA. AC Q9X1N6; G4FFT8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36616.1}; GN OrderedLocusNames=TM_1550 {ECO:0000313|EMBL:AAD36616.1}; GN ORFNames=Tmari_1558 {ECO:0000313|EMBL:AGL50482.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36616.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36616.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36616.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50482.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50482.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36616.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50482.1; -; Genomic_DNA. DR PIR; A72239; A72239. DR RefSeq; NP_229350.1; NC_000853.1. DR RefSeq; WP_004081944.1; NZ_CP011107.1. DR STRING; 243274.TM1550; -. DR EnsemblBacteria; AAD36616; AAD36616; TM_1550. DR EnsemblBacteria; AGL50482; AGL50482; Tmari_1558. DR GeneID; 897971; -. DR KEGG; tma:TM1550; -. DR KEGG; tmi:THEMA_06530; -. DR KEGG; tmm:Tmari_1558; -. DR KEGG; tmw:THMA_1585; -. DR PATRIC; 23938062; VBITheMar51294_1568. DR eggNOG; ENOG4105CBJ; Bacteria. DR eggNOG; COG3872; LUCA. DR OMA; VFEYHGA; -. DR OrthoDB; EOG6KWXWQ; -. DR BioCyc; TMAR243274:GC6P-1591-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IBA:GO_Central. DR GO; GO:0009691; P:cytokinin biosynthetic process; IBA:GO_Central. DR InterPro; IPR010787; DUF1385. DR Pfam; PF07136; DUF1385; 1. DR ProDom; PD131510; DUF1385; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 63 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 110 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 116 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 182 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 216 236 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 296 AA; 33124 MW; A66FD30ABEDC42C8 CRC64; MKAGGQAVIE GVLMIARKVS LAVRNPDGNI EVRELGKVKF PGWAKIPFLR GFYSLFVSLY FGIKALNLSS EISSGEKLKE SEKFFSLITA VGLAVGLFVV VPIFLTNFLV TKKGEFLYSL VEGFIRVGLF LLYVWIISLF KDVKRVFQYH GAEHMTIHAY EHGEELTPEN VRKYSTIHPR CGTNFLMIFL IVAILLLSLV GVVVEMNTWT RIVSRLVLLP FAAGISYELL KVIAFFNGKG LVKLLYLPGY LLQYLTTAKP DDSQLEVAIT ALKYAVGEEK DTTEDNVKED EVELLG // ID Q9X2F7_THEMA Unreviewed; 443 AA. AC Q9X2F7; G4FGM6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Carbohydrate-binding domain containing protein {ECO:0000313|EMBL:AGL50773.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36903.1}; GN OrderedLocusNames=TM_1841 {ECO:0000313|EMBL:AAD36903.1}; GN ORFNames=Tmari_1849 {ECO:0000313|EMBL:AGL50773.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36903.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36903.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36903.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50773.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50773.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36903.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50773.1; -; Genomic_DNA. DR PIR; D72204; D72204. DR RefSeq; NP_229637.1; NC_000853.1. DR RefSeq; WP_004082385.1; NZ_CP011107.1. DR STRING; 243274.TM1841; -. DR EnsemblBacteria; AAD36903; AAD36903; TM_1841. DR EnsemblBacteria; AGL50773; AGL50773; Tmari_1849. DR GeneID; 897814; -. DR KEGG; tma:TM1841; -. DR KEGG; tmi:THEMA_05000; -. DR KEGG; tmm:Tmari_1849; -. DR KEGG; tmw:THMA_1884; -. DR PATRIC; 23938671; VBITheMar51294_1862. DR eggNOG; ENOG4107074; Bacteria. DR eggNOG; ENOG410YWTH; LUCA. DR OMA; DSKWGAD; -. DR OrthoDB; EOG6FFS2J; -. DR BioCyc; TMAR243274:GC6P-1892-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro. DR Gene3D; 2.60.40.1190; -; 1. DR InterPro; IPR010502; Carb-bd_dom_fam9. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 443 AA; 47416 MW; 066705D14BBA0890 CRC64; MKKLFLVLAV LSLVLYGCLR TPPVVKDMVT TDGSLSDWGS KIKEDAADDS KWGADNELLK AGLLFDGANI YIAGEYVIGG DGNVNVFLVL IDLVGVTGAQ TVSYTGLNDG NRNFTNPNGD IDLIVEVNQS NEYKVWRVSQ DGSLTDITDQ VTAQFGTGST IAELKIPISE QVNQVKAVFA ISGGTGGGNQ WVGDFYPNQP DHDSAENGGI PQPAPVVNFV VCDKEGNVSE EINQTSEPEQ PTESVIVVDG DLSDFGTPVA TSTNPGGGNG ANLYRLYVTY DATYLYIGFD TQNSGSWDVA YGIGIDTKPS GYTGDSDAWG RKISFGADYA VDYEIYFWWA GGSGLDSNNF CEWNGLDWNY RSIADAGGTF DYTGDTSSGL QTMEIAIPWS AIGGKQDVAL IVWITGGSGS AVDSIPDDDS TIDNADEWND SDTFTNLYLL QVN // ID Q9X1R3_THEMA Unreviewed; 408 AA. AC Q9X1R3; G4FFW5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36644.1}; GN OrderedLocusNames=TM_1577 {ECO:0000313|EMBL:AAD36644.1}; GN ORFNames=Tmari_1585 {ECO:0000313|EMBL:AGL50509.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36644.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36644.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36644.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50509.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50509.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36644.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50509.1; -; Genomic_DNA. DR PIR; B72238; B72238. DR RefSeq; NP_229377.1; NC_000853.1. DR RefSeq; WP_004082000.1; NZ_CP011107.1. DR STRING; 243274.TM1577; -. DR EnsemblBacteria; AAD36644; AAD36644; TM_1577. DR EnsemblBacteria; AGL50509; AGL50509; Tmari_1585. DR GeneID; 897957; -. DR KEGG; tma:TM1577; -. DR KEGG; tmi:THEMA_06395; -. DR KEGG; tmm:Tmari_1585; -. DR KEGG; tmw:THMA_1612; -. DR PATRIC; 23938118; VBITheMar51294_1596. DR eggNOG; ENOG4109089; Bacteria. DR eggNOG; ENOG4111PX0; LUCA. DR OMA; DLMENIP; -. DR OrthoDB; EOG680WZT; -. DR BioCyc; TMAR243274:GC6P-1618-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 408 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006753496. SQ SEQUENCE 408 AA; 46633 MW; 074BCA865CE90F46 CRC64; MKKTVFFLLL MASLSFSVPV LQNYDYFIHL KNTGELYSAL KKLPLFEFLF LEGVGYEETV VEWVESRLND PEEFFQGISS EIVICGKGDI SNLFTLDINE ILSLSEKING FIAFKTPAPE RFIEDFAKVK DRTFIKRDDL YVLGNTTPLF SKISGNYVLI SSTETVFEKI GESEDTTDKP FFARIKKMSV FGREGEVEIV GQVKESHLTV EITQKASPFR VSAREDIGKL PYLGDLFAFT SDPEILRWFF MNMFRGSDVE KFFNTISSEG SSMFLVSLYG TPRFAFLMEN KTLDEVTSDL VSRGAKFVGE ELQLDVGGLL LHFFNYNGKI VVSSMKKVGF LQTLNRKRLE NHPSFVFLEK EVPKSVFLEV FVDLYTLFDK LLGFSPRSSL LLIGYEEDGL IKYRLEVM // ID Q9WZT1_THEMA Unreviewed; 482 AA. AC Q9WZT1; G4FD00; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=AstB/chuR-related protein {ECO:0000313|EMBL:AAD35906.1}; DE SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:AGL49750.1}; GN OrderedLocusNames=TM_0824 {ECO:0000313|EMBL:AAD35906.1}; GN ORFNames=Tmari_0825 {ECO:0000313|EMBL:AGL49750.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35906.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35906.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35906.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49750.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49750.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35906.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49750.1; -; Genomic_DNA. DR PIR; C72330; C72330. DR RefSeq; NP_228633.1; NC_000853.1. DR RefSeq; WP_004080829.1; NZ_CP011107.1. DR STRING; 243274.TM0824; -. DR EnsemblBacteria; AAD35906; AAD35906; TM_0824. DR EnsemblBacteria; AGL49750; AGL49750; Tmari_0825. DR GeneID; 898494; -. DR KEGG; tma:TM0824; -. DR KEGG; tmi:THEMA_00520; -. DR KEGG; tmm:Tmari_0825; -. DR KEGG; tmw:THMA_0845; -. DR PATRIC; 23936572; VBITheMar51294_0836. DR eggNOG; ENOG4107RPP; Bacteria. DR eggNOG; COG0535; LUCA. DR OMA; YADKLWY; -. DR OrthoDB; EOG66XB8X; -. DR BioCyc; TMAR243274:GC6P-853-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF13186; SPASM; 1. DR SMART; SM00729; Elp3; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00421379}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|SAAS:SAAS00421379}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00421379}; KW Metal-binding {ECO:0000256|SAAS:SAAS00421379}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00421341}. FT DOMAIN 110 305 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 482 AA; 55809 MW; 981D4831F4B0065D CRC64; MAVGGIKGMI YRQAGKLVGS FVRNAEVETL GKIFGTLSMF TKEPAKSGLR KLADLAKERH PMVMSWVNVF KKASPRCVEG VINNLIINEF ALGEPIRQEK MHEYKTVLPK LLVLSPTYAC NLNCVGCYAG LYGRKYELSH DEVRDILKQA NDLGIYFFII TGGEPFFWPH LMDIFEEFKD SYFLVYSNGT LIKEETAKKL AELGNVTVSI SVEGFETDTD WRRGRGIFKR VLEAWERLRR HGVIFGASVT ATRMNHDTIM KDEFWDFLEE QGVSYVWVYQ FMPVGMNPTM DLVPTPQQRY ERFHKLEQLR LSGRFAFVAD FWNHGFLTNG CLAAGAKYLH INAKGYVEPC VFQQFAVDSI REKKLIDILR SPFFEAYKRM IPYSDNLFRP CPIIDNPKVF RAMVRAFNAK PQHEGSERVI TDLAPELDKL AAEWKKYADK LWYEEGYSEI YPANRGVYSY EVRMRRYADK EKLLAVDKRY RD // ID Q9X0W1_THEMA Unreviewed; 281 AA. AC Q9X0W1; G4FEB2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD36309.1}; GN OrderedLocusNames=TM_1234 {ECO:0000313|EMBL:AAD36309.1}; GN ORFNames=Tmari_1241 {ECO:0000313|EMBL:AGL50165.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36309.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36309.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36309.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50165.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50165.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36309.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50165.1; -; Genomic_DNA. DR PIR; C72279; C72279. DR RefSeq; NP_229039.1; NC_000853.1. DR RefSeq; WP_004080044.1; NZ_CP011107.1. DR STRING; 243274.TM1234; -. DR EnsemblBacteria; AAD36309; AAD36309; TM_1234. DR EnsemblBacteria; AGL50165; AGL50165; Tmari_1241. DR GeneID; 898250; -. DR KEGG; tma:TM1234; -. DR KEGG; tmi:THEMA_08160; -. DR KEGG; tmm:Tmari_1241; -. DR KEGG; tmw:THMA_1260; -. DR PATRIC; 23937410; VBITheMar51294_1252. DR eggNOG; ENOG4107G03; Bacteria. DR eggNOG; COG1175; LUCA. DR KO; K02025; -. DR OMA; YWILYLM; -. DR OrthoDB; EOG6QK4QB; -. DR BioCyc; TMAR243274:GC6P-1264-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 7 27 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 61 81 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 93 115 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 147 170 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 208 226 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 250 271 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 57 268 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 281 AA; 32119 MW; 62EE8DC4B552C19D CRC64; MRGKWISFLL ILPAVLYLVL LMGYPLFETF RLAFTSDEGF LGNFKRLVEN GGFWGAMKNT ILLTAVIVPL QLIFALGLAL FVNQKFKGYT TVLYFIAIPL ALSDVTAALM SYTIFSPNGY LNKILMNLHL IERPIYFFGY MFKAREFWVI VLTEVWRATP LVFIILLAGL QSINKEYLEA ADLFGFSRWK KFTKIILPLL KPSIMSALLL RTLFAFQIFG VVWLLAGRDI PVLAGETYYW YTFMNDPKMA SAYALVIALV TIVVSWFYIT FLSAKHLEGA R // ID Q9X1Y2_THEMA Unreviewed; 93 AA. AC Q9X1Y2; G4FG38; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36716.1}; DE SubName: Full=YlxP-like protein {ECO:0000313|EMBL:AGL50582.1}; GN OrderedLocusNames=TM_1649 {ECO:0000313|EMBL:AAD36716.1}; GN ORFNames=Tmari_1658 {ECO:0000313|EMBL:AGL50582.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36716.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36716.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36716.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50582.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50582.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36716.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50582.1; -; Genomic_DNA. DR PIR; F72227; F72227. DR RefSeq; NP_229449.1; NC_000853.1. DR RefSeq; WP_004082152.1; NZ_CP011107.1. DR STRING; 243274.TM1649; -. DR EnsemblBacteria; AAD36716; AAD36716; TM_1649. DR EnsemblBacteria; AGL50582; AGL50582; Tmari_1658. DR GeneID; 896827; -. DR KEGG; tma:TM1649; -. DR KEGG; tmi:THEMA_06000; -. DR KEGG; tmm:Tmari_1658; -. DR KEGG; tmw:THMA_1690; -. DR PATRIC; 23938272; VBITheMar51294_1668. DR eggNOG; ENOG410854P; Bacteria. DR eggNOG; COG1550; LUCA. DR KO; K09764; -. DR OMA; RWIEEER; -. DR OrthoDB; EOG69WFP9; -. DR BioCyc; TMAR243274:GC6P-1695-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.30.70.1120; -; 1. DR InterPro; IPR007546; DUF503. DR Pfam; PF04456; DUF503; 1. DR SUPFAM; SSF103007; SSF103007; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 93 AA; 10779 MW; E9511C5642530CD0 CRC64; MSVGVVSLRV RLFGVRSLKE KRGILKRLMN DLRKKYNISI SEVGAHDSKS FFEIGIAMVN TDRAVIERVF DSIIDYLDLY PGMEVEEIER EVW // ID Q9WZI7_THEMA Unreviewed; 276 AA. AC Q9WZI7; G4FD95; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Permease of the drug/metabolite transporter (DMT) superfamily {ECO:0000313|EMBL:AGL49654.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35810.1}; GN OrderedLocusNames=TM_0728 {ECO:0000313|EMBL:AAD35810.1}; GN ORFNames=Tmari_0729 {ECO:0000313|EMBL:AGL49654.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35810.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35810.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35810.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49654.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49654.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35810.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49654.1; -; Genomic_DNA. DR PIR; F72342; F72342. DR RefSeq; NP_228537.1; NC_000853.1. DR RefSeq; WP_004080999.1; NZ_CP011107.1. DR STRING; 243274.TM0728; -. DR EnsemblBacteria; AAD35810; AAD35810; TM_0728. DR EnsemblBacteria; AGL49654; AGL49654; Tmari_0729. DR GeneID; 898395; -. DR KEGG; tma:TM0728; -. DR KEGG; tmi:THEMA_01020; -. DR KEGG; tmm:Tmari_0729; -. DR KEGG; tmw:THMA_0744; -. DR PATRIC; 23936376; VBITheMar51294_0741. DR eggNOG; COG0697; LUCA. DR OMA; GERWHLN; -. DR OrthoDB; EOG6X6RHW; -. DR BioCyc; TMAR243274:GC6P-754-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 78 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 105 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 112 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 156 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 168 186 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 198 215 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 227 245 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 251 270 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 7 129 EamA. {ECO:0000259|Pfam:PF00892}. FT DOMAIN 137 265 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 276 AA; 30796 MW; 75B7DE7AC2C056E9 CRC64; MWRENKALAF LVLTAVLQGS TFPLQKLVLG GVSPFVYNTV RFGSAALLSL FVFGPGRFVK GFLLGLVLCG AYIFQLWGLK FTSAVKSGFI VSSFVFLVPL FAFLLEREKL RKIHFISFTS GFLGLYLLTG GVSQITLGNL FQFFCAVLFA LHVVLITRFS RSEEEKNMLF WQFVTVGAVN FLFGLGERWH LNLEAISVGI YSGVFATTLG ILWQMRYQKE VGNNTTALVY MTQPFVSLVL SFLLLGERMS FLQLLGGILV LVALFTGTTL RPRESN // ID Q9X1W9_THEMA Unreviewed; 128 AA. AC Q9X1W9; G4FG23; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 98. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36701.1}; GN OrderedLocusNames=TM_1634 {ECO:0000313|EMBL:AAD36701.1}; GN ORFNames=Tmari_1643 {ECO:0000313|EMBL:AGL50567.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36701.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36701.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36701.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50567.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50567.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36701.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50567.1; -; Genomic_DNA. DR PIR; B72230; B72230. DR RefSeq; NP_229434.1; NC_000853.1. DR RefSeq; WP_004082112.1; NZ_CP011107.1. DR PDB; 2VKJ; X-ray; 1.65 A; A/B=27-128. DR PDB; 2VKO; X-ray; 1.79 A; A/B/C/D=27-128. DR PDBsum; 2VKJ; -. DR PDBsum; 2VKO; -. DR STRING; 243274.TM1634; -. DR DNASU; 897924; -. DR EnsemblBacteria; AAD36701; AAD36701; TM_1634. DR EnsemblBacteria; AGL50567; AGL50567; Tmari_1643. DR GeneID; 897924; -. DR KEGG; tma:TM1634; -. DR KEGG; tmi:THEMA_06075; -. DR KEGG; tmm:Tmari_1643; -. DR KEGG; tmw:THMA_1675; -. DR PATRIC; 23938242; VBITheMar51294_1653. DR OMA; ADYVEKE; -. DR OrthoDB; EOG6VXFBQ; -. DR BioCyc; TMAR243274:GC6P-1680-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR PROSITE; PS50005; TPR; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2VKJ, ECO:0000213|PDB:2VKO}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 75 108 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 128 AA; 15105 MW; 143854FE1B24FF8D CRC64; MKRDIFYVII LTVFAVLFML TYFSYRNLAV KLTRMEKTLK AYELYIFSDY ENFENYVKKE GLKIEGMELL KEKKARSLIA EGKDLFETAN YGEALVFFEK ALNLSDNEEI KKIASFYLEE CRKKLAGD // ID Q9WXR6_THEMA Unreviewed; 328 AA. AC Q9WXR6; G4FGX5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35154.1}; DE SubName: Full=Xylose-regulated ABC transporter, permease component 1 {ECO:0000313|EMBL:AGL48983.1}; GN OrderedLocusNames=TM_0060 {ECO:0000313|EMBL:AAD35154.1}; GN ORFNames=Tmari_0057 {ECO:0000313|EMBL:AGL48983.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35154.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35154.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35154.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48983.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48983.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35154.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48983.1; -; Genomic_DNA. DR PIR; E72424; E72424. DR RefSeq; NP_227876.1; NC_000853.1. DR RefSeq; WP_004082548.1; NZ_CP011107.1. DR STRING; 243274.TM0060; -. DR TCDB; 3.A.1.5.29; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35154; AAD35154; TM_0060. DR EnsemblBacteria; AGL48983; AGL48983; Tmari_0057. DR GeneID; 896884; -. DR KEGG; tma:TM0060; -. DR KEGG; tmi:THEMA_04505; -. DR KEGG; tmm:Tmari_0057; -. DR KEGG; tmw:THMA_0056; -. DR PATRIC; 23934960; VBITheMar51294_0058. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR KO; K02033; -. DR OMA; TRIIGQR; -. DR OrthoDB; EOG66F098; -. DR BioCyc; TMAR243274:GC6P-60-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 9 27 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 102 125 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 137 163 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 195 214 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 248 275 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 295 321 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 102 314 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 328 AA; 36536 MW; 2A2B76ABDB7232E7 CRC64; MLAYIAKRVL YAIPLLFVIS IVSFIIIELP PGDYLTTYVM TLRQSGETID QAALEVLKKR YGLDKPVIVR YFYWIGNIIT KGDFGYSFMW EKPVSDLLNQ RVWWTILISV LSTAFAWVFG FLIGVYSGTH QYSIGDYVFT VLGYIGLATP NFLLALILLW FMFVTTGVSL GGLFSPEYAG APWSWAKFVD LLKHIWIPVV VLGTGSMAGL IRVLRANLLD EINKPYVVAA RARGVPEREL VWKYPLRVAV IPFASTAGWA LPQIVSGAVV TGIVLNLPTV GTLLLDALTS QDMYLAGSLV LILSVFTIIG TLISDILLAW LDPRIRFE // ID Q9X1S5_THEMA Unreviewed; 979 AA. AC Q9X1S5; G4FFX7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Clostripain-related protein {ECO:0000313|EMBL:AAD36656.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AGL50521.1}; GN OrderedLocusNames=TM_1589 {ECO:0000313|EMBL:AAD36656.1}; GN ORFNames=Tmari_1597 {ECO:0000313|EMBL:AGL50521.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36656.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36656.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36656.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50521.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50521.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36656.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50521.1; -; Genomic_DNA. DR PIR; E72236; E72236. DR RefSeq; NP_229389.1; NC_000853.1. DR RefSeq; WP_004082025.1; NZ_CP011107.1. DR STRING; 243274.TM1589; -. DR EnsemblBacteria; AAD36656; AAD36656; TM_1589. DR EnsemblBacteria; AGL50521; AGL50521; Tmari_1597. DR GeneID; 897374; -. DR KEGG; tma:TM1589; -. DR KEGG; tmi:THEMA_06325; -. DR KEGG; tmm:Tmari_1597; -. DR KEGG; tmw:THMA_1626; -. DR PATRIC; 23938146; VBITheMar51294_1608. DR eggNOG; ENOG4108X2E; Bacteria. DR eggNOG; ENOG4111KB4; LUCA. DR OrthoDB; EOG6RNQ8K; -. DR BioCyc; TMAR243274:GC6P-1632-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 2.60.40.920; -; 1. DR InterPro; IPR003344; Big_1_dom. DR InterPro; IPR008964; Invasin/intimin_cell_adhesion. DR InterPro; IPR005077; Peptidase_C11. DR Pfam; PF03415; Peptidase_C11; 1. DR SUPFAM; SSF49373; SSF49373; 1. DR PROSITE; PS51127; BIG1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 471 578 Big-1 (bacterial Ig-like domain 1). FT {ECO:0000259|PROSITE:PS51127}. SQ SEQUENCE 979 AA; 110279 MW; 276A1BFC685DB88C CRC64; MRLRKSFFVS ILAAFMVLVI LSGCAQPSLV PSSEKITAEI HLTLNFPFTK AFQDELPISK FQVRVLNSSG TVIYSGEFTS SEISITVQTY PGVHTIEVEA YTDNSELYDK ETKIMEGSSQ VNLRDGANDV FIALEFLSGQ FSLNMSLNPD APYIIESSEI QMVHSANNSE LNLDHTVNST EDTYTISDLE PGVWHIVYSA TLTNINDNTV TNLQEEFDVT IYPARMSEIN FSVGDDLVLT NPQITITASL PYLPPVSNLT ASLENEEIVL SWDYNIENAV FMVHKKYVSE NFWRYVGETT EKFFSIPLVQ GDEEIAMVGV NAVANGMESG ITYVGPAYIV DFEYGIPVDW ILGGDALPFV QDSVFYEGNH SLQFGDIDNY EKSWVEFTVN YNVPVILSFW VKVSSEEDFD YFRFYVDNVL WDELSGEVDW TPLAYLLPPG EHTIRFAYKK DSSVSEGYDT AWVDYIIIQP EEQISTTSAQ IIADNETHVV GRIGYIDVQV VDESGVPIPG VNVQLLYQES DGNWYPLSDA ITEENSFTTD SNGIAKIRIW PVQSGTVTFK ARLVGNPSIE TQFDVTFQGL NWFFLVWMCA DNNLESFALN DLSEMLNSNE NVSVVVIFDG FFHSDWIYVL NEEGEWEGGP ADAEIDSGNI SELINYMEYA SNLEASHRAI ILWDHGNAWL YDAKARYSPR AICFDETSGN HITTPELRQA LEEYNSYGLP RIDILGMDAC LMGSIEVLYE LRGLVDYIVA SSFTEPGDGW DYSFLANITS SDDALDVGMK IVDAYRNFYD ETFWENYGLS LAVYDANQVT GVTDSLNSLA SRLVSIMDDS LRITINSFYP SLMQYYPDYN LLVDLNNCAI SMQDINNSDV QTYANEVSQS LEQLVIYEYA EKSGTSIENP VSIFMPDDPD SLIYWGSDYN SLLFSQELLW SNFLESWHQT GDVLSYKSGA TAFLGNSLKK KELKSPFLSL RRLLRDLPE // ID Q9WZ05_THEMA Unreviewed; 205 AA. AC Q9WZ05; G4FDT6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35620.1}; GN OrderedLocusNames=TM_0535 {ECO:0000313|EMBL:AAD35620.1}; GN ORFNames=Tmari_0532 {ECO:0000313|EMBL:AGL49457.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35620.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35620.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35620.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49457.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49457.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35620.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49457.1; -; Genomic_DNA. DR PIR; E72367; E72367. DR RefSeq; NP_228345.1; NC_000853.1. DR RefSeq; WP_004081371.1; NZ_CP011107.1. DR STRING; 243274.TM0535; -. DR EnsemblBacteria; AAD35620; AAD35620; TM_0535. DR EnsemblBacteria; AGL49457; AGL49457; Tmari_0532. DR GeneID; 897587; -. DR KEGG; tma:TM0535; -. DR KEGG; tmi:THEMA_02000; -. DR KEGG; tmm:Tmari_0532; -. DR KEGG; tmw:THMA_0548; -. DR PATRIC; 23935977; VBITheMar51294_0543. DR eggNOG; ENOG4105NWC; Bacteria. DR eggNOG; ENOG4111X38; LUCA. DR OMA; KTYFSRE; -. DR OrthoDB; EOG64V2DP; -. DR BioCyc; TMAR243274:GC6P-559-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 31 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 32 63 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 205 AA; 24116 MW; 57B35E6189216CCE CRC64; MKKDSLVTFF ASLIVIAILL FFVLSVFNFY FLKKLEARMD EVEKQFQTTL ESYEERLKIL EELLKPNSII SRYITAYEYF EKASVDFERI FSEIEDDPTT GYMRIFVIGN DPVWITVKDG NEVLFSRDVK PGLSPYRFFY YKKPKISTEY DIVIPRDATL IVGIPNRVFL LVFGVGTTYH PTKIVQVQQT RIDNIERDLK LYIPK // ID Q9X149_THEMA Unreviewed; 285 AA. AC Q9X149; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE RecName: Full=Transport permease protein {ECO:0000256|RuleBase:RU361157}; GN OrderedLocusNames=TM_1326 {ECO:0000313|EMBL:AAD36398.1}; GN ORFNames=Tmari_1333 {ECO:0000313|EMBL:AGL50257.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36398.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36398.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36398.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50257.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50257.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU361157}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU361157}. CC -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family. CC {ECO:0000256|RuleBase:RU361157}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-2 domain. CC {ECO:0000256|RuleBase:RU361157}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36398.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50257.1; -; Genomic_DNA. DR PIR; B72267; B72267. DR RefSeq; NP_229128.1; NC_000853.1. DR RefSeq; WP_010865313.1; NC_000853.1. DR STRING; 243274.TM1326; -. DR EnsemblBacteria; AAD36398; AAD36398; TM_1326. DR EnsemblBacteria; AGL50257; AGL50257; Tmari_1333. DR GeneID; 898156; -. DR KEGG; tma:TM1326; -. DR KEGG; tmm:Tmari_1333; -. DR PATRIC; 23937589; VBITheMar51294_1340. DR eggNOG; ENOG4107WTT; Bacteria. DR eggNOG; COG0842; LUCA. DR KO; K01992; -. DR OMA; YYFVGTS; -. DR OrthoDB; EOG64V2BM; -. DR BioCyc; TMAR243274:GC6P-1357-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR InterPro; IPR013525; ABC_2_trans. DR InterPro; IPR000412; ABC_2_transport. DR Pfam; PF01061; ABC2_membrane; 1. DR PRINTS; PR00164; ABC2TRNSPORT. DR PROSITE; PS51012; ABC_TM2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU361157}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU361157}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU361157}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361157}; KW Transport {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 40 57 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 77 98 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 124 151 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 163 186 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 193 211 Helical. {ECO:0000256|RuleBase:RU361157}. FT TRANSMEM 250 269 Helical. {ECO:0000256|RuleBase:RU361157}. FT DOMAIN 34 238 ABC2_membrane. FT {ECO:0000259|Pfam:PF01061}. SQ SEQUENCE 285 AA; 31874 MW; C1F619C5AA3B1E07 CRC64; MFHGGSEFSS GGEGHLKLLI KTLYFIRKDI LIWLSYRTQL VLGLLSGFVG IVQFGFIGKF IAQGNYFPLI ERYGGDILAY FITGSVFMSY TNLALMTFKG VIQREQSMGT LEYILLSKTP LWQLFLFSFV SSFFFTTLNI TLIFLGLVYL FSVHITPNFL EALVVLFTVM LPLMGIGLLS ASIVLVTKRG DPVGWLYTTL SGLFSGIYFP VEILPDWIRP VSYLIPSTYG IDLLRRVLMR GEHLSSVSEG LVLLAATGTV LISAGIVAFK RSFNQARLRG SLSWY // ID Q9WYZ3_THEMA Unreviewed; 209 AA. AC Q9WYZ3; G4FDU8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35608.1}; GN OrderedLocusNames=TM_0523 {ECO:0000313|EMBL:AAD35608.1}; GN ORFNames=Tmari_0519 {ECO:0000313|EMBL:AGL49444.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35608.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35608.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35608.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49444.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49444.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35608.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49444.1; -; Genomic_DNA. DR PIR; A72366; A72366. DR RefSeq; NP_228333.1; NC_000853.1. DR RefSeq; WP_004081399.1; NZ_CP011107.1. DR STRING; 243274.TM0523; -. DR EnsemblBacteria; AAD35608; AAD35608; TM_0523. DR EnsemblBacteria; AGL49444; AGL49444; Tmari_0519. DR GeneID; 897575; -. DR KEGG; tma:TM0523; -. DR KEGG; tmi:THEMA_02060; -. DR KEGG; tmm:Tmari_0519; -. DR KEGG; tmw:THMA_0535; -. DR PATRIC; 23935951; VBITheMar51294_0530. DR OMA; PVYNGEF; -. DR OrthoDB; EOG6SV585; -. DR BioCyc; TMAR243274:GC6P-547-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 209 AA; 23210 MW; B7667C5C37F8B239 CRC64; MRVLLPAFLL LLAVGCALVS PGKADLYVYL FNVGTDENVT VDLESSHLSV NGKEYTLKDV LANEGVLLNT VDIPFDLSDF ELTVAATIVF DEQTEEVSFK TTPVVLYHSA GKFSTDTVLR SNAYQLLDLE NKKIFAVEDP VKVYGELTSE GSVVTLSFGE YEMKVPVYNG EFLFYLPGTD ESYDVDVFFD SDSTSLTIQE GRDEYEVPF // ID Q9X1I7_THEMA Unreviewed; 250 AA. AC Q9X1I7; G4FFL5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 115. DE RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974}; DE Short=MAP {ECO:0000256|HAMAP-Rule:MF_01974}; DE Short=MetAP {ECO:0000256|HAMAP-Rule:MF_01974}; DE EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_01974}; DE AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01974}; GN Name=map {ECO:0000256|HAMAP-Rule:MF_01974}; GN OrderedLocusNames=TM_1478 {ECO:0000313|EMBL:AAD36544.1}; GN ORFNames=Tmari_1486 {ECO:0000313|EMBL:AGL50410.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36544.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36544.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36544.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50410.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50410.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. CC The N-terminal methionine is often cleaved when the second residue CC in the primary sequence is small and uncharged (Met-Ala-, Cys, CC Gly, Pro, Ser, Thr, or Val). Requires deformylation of the CC N(alpha)-formylated initiator methionine before it can be CC hydrolyzed. {ECO:0000256|HAMAP-Rule:MF_01974}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids, CC preferentially methionine, from peptides and arylamides. CC {ECO:0000256|HAMAP-Rule:MF_01974}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974}; CC Note=Binds 2 divalent metal cations per subunit. Has a high- CC affinity and a low affinity metal-binding site. The true nature of CC the physiological cofactor is under debate. The enzyme is active CC with cobalt, zinc, manganese or divalent iron ions. Most likely, CC methionine aminopeptidases function as mononuclear Fe(2+)- CC metalloproteases under physiological conditions, and the CC catalytically relevant metal-binding site has been assigned to the CC histidine-containing high-affinity site. {ECO:0000256|HAMAP- CC Rule:MF_01974}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01974}. CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP- CC Rule:MF_01974}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36544.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50410.1; -; Genomic_DNA. DR PIR; F72247; F72247. DR RefSeq; NP_229278.1; NC_000853.1. DR RefSeq; WP_004081791.1; NZ_CP011107.1. DR PDB; 1O0X; X-ray; 1.90 A; A=1-250. DR PDBsum; 1O0X; -. DR STRING; 243274.TM1478; -. DR EnsemblBacteria; AAD36544; AAD36544; TM_1478. DR EnsemblBacteria; AGL50410; AGL50410; Tmari_1486. DR GeneID; 898008; -. DR KEGG; tma:TM1478; -. DR KEGG; tmi:THEMA_06910; -. DR KEGG; tmm:Tmari_1486; -. DR KEGG; tmw:THMA_1510; -. DR PATRIC; 23937914; VBITheMar51294_1495. DR eggNOG; ENOG4105CA1; Bacteria. DR eggNOG; COG0024; LUCA. DR KO; K01265; -. DR OMA; PYPATLC; -. DR OrthoDB; EOG6MWNDS; -. DR BioCyc; TMAR243274:GC6P-1518-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.230.10; -; 1. DR HAMAP; MF_01974; MetAP_1; 1. DR InterPro; IPR001714; Pept_M24_MAP. DR InterPro; IPR000994; Pept_M24_structural-domain. DR InterPro; IPR002467; Pept_M24A_MAP1. DR Pfam; PF00557; Peptidase_M24; 1. DR PRINTS; PR00599; MAPEPTIDASE. DR SUPFAM; SSF55920; SSF55920; 1. DR TIGRFAMs; TIGR00500; met_pdase_I; 1. DR PROSITE; PS00680; MAP_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O0X}; KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000313|EMBL:AAD36544.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000313|EMBL:AAD36544.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000313|EMBL:AAD36544.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 11 240 Peptidase_M24. FT {ECO:0000259|Pfam:PF00557}. FT METAL 95 95 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 106 106 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 106 106 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 169 169 Divalent metal cation 2; catalytic; via FT tele nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01974}. FT METAL 202 202 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 233 233 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 233 233 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT BINDING 77 77 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01974}. FT BINDING 176 176 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01974}. SQ SEQUENCE 250 AA; 27489 MW; B259C59CC1B66E29 CRC64; MIRIKTPSEI EKMKKAGKAV AVALREVRKV IVPGKTAWDV ETLVLEIFKK LRVKPAFKGY GGYKYATCVS VNEEVVHGLP LKEKVFKEGD IVSVDVGAVY QGLYGDAAVT YIVGETDERG KELVRVTREV LEKAIKMIKP GIRLGDVSHC IQETVESVGF NVIRDYVGHG VGRELHEDPQ IPNYGTPGTG VVLRKGMTLA IEPMVSEGDW RVVVKEDGWT AVTVDGSRCA HFEHTILITE NGAEILTKEG // ID Q9WYE1_THEMA Unreviewed; 707 AA. AC Q9WYE1; G4FHL9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Endoglucanase, putative {ECO:0000313|EMBL:AAD35393.1}; DE SubName: Full=Secreted cellulase {ECO:0000313|EMBL:AGL49229.1}; GN OrderedLocusNames=TM_0305 {ECO:0000313|EMBL:AAD35393.1}; GN ORFNames=Tmari_0303 {ECO:0000313|EMBL:AGL49229.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35393.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35393.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35393.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49229.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49229.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35393.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49229.1; -; Genomic_DNA. DR PIR; F72393; F72393. DR RefSeq; NP_228117.1; NC_000853.1. DR RefSeq; WP_004083030.1; NZ_CP011107.1. DR STRING; 243274.TM0305; -. DR CAZy; GH74; Glycoside Hydrolase Family 74. DR EnsemblBacteria; AAD35393; AAD35393; TM_0305. DR EnsemblBacteria; AGL49229; AGL49229; Tmari_0303. DR GeneID; 897235; -. DR KEGG; tma:TM0305; -. DR KEGG; tmi:THEMA_03200; -. DR KEGG; tmm:Tmari_0303; -. DR KEGG; tmw:THMA_0312; -. DR PATRIC; 23935489; VBITheMar51294_0310. DR eggNOG; ENOG4107RF2; Bacteria. DR eggNOG; ENOG410ZVF4; LUCA. DR OMA; YSSWWPD; -. DR OrthoDB; EOG6V7BGX; -. DR BioCyc; TMAR243274:GC6P-318-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR002860; BNR_rpt. DR Pfam; PF15899; BNR_6; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 707 AA; 79496 MW; 8CD8743CBDA6A99F CRC64; MLRSFLILFL AILGVVFGAT FEWKSVEING GGFVPGIIFH PASPGLLYAR TDVGGLYRWD EETKRWKQLF DFLRRDQSDY MGVLSVALDP SDPKRIYAMT GKYTQDWAGY GAILISEDYG ETWTIVNLDK YGIKVGGNED GRNAGERLQV DPNFSSVLFM GTTKYGLWKS EDFGKNWKKV DSFPSTSVTF VLFDEKSGEK GSPTPRIFVG CSEPKGIFVT EDGGTTWNVL PNLPNDLIPL RGKIHDGILY VTLSNALGPN GATRGAVMKY VIADQKWYDV TPMKGDFGYC GIDVQENVVI VSTLDRWYPH DEIFISLNGG ETWRPLLEKA NFDINKAPWI KDLNPHWISD VKIDPFDMNR AIFTTGYGVW VTYELKKSFE GMGKPVKWIF ENRGLEETVV LQLVPPIGER PLLSAIADWG GFRHESLDTP PSSMYKPLKW TSLGIAFAYQ NSKFVARVHT YTYPFLSYSE DGGINWREIE TVPEGITDGG RLSLAVSNDG KTLVWSPANH EVIVSSDKGK SWKKAISVPV PEFNYFPASD PVNPSKFYIF DWKNGDFLIS KDGGKSFMKG AKLPSFDNWW VSLYSFPVLA PDREGDIWLA LQWNGLYRSK DGGITFERLG NVDIAYVIGF GAPKPGTDYP AIYLNGMVNG VYGIFMSTDE GKTWMRINND KHQFGWIHYM IGDMNEFGRI FLGTEGRGII VGEVKEE // ID Q9X0K6_THEMA Unreviewed; 276 AA. AC Q9X0K6; G4FEM6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 94. DE SubName: Full=Glycerol-3-phosphate ABC transporter, permease protein {ECO:0000313|EMBL:AAD36198.1}; DE SubName: Full=SN-glycerol-3-phosphate transport system permease protein UgpE {ECO:0000313|EMBL:AGL50052.1}; GN OrderedLocusNames=TM_1122 {ECO:0000313|EMBL:AAD36198.1}; GN ORFNames=Tmari_1128 {ECO:0000313|EMBL:AGL50052.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36198.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36198.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36198.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50052.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50052.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36198.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50052.1; -; Genomic_DNA. DR PIR; G72292; G72292. DR RefSeq; NP_228928.1; NC_000853.1. DR RefSeq; WP_004080295.1; NZ_CP011107.1. DR STRING; 243274.TM1122; -. DR EnsemblBacteria; AAD36198; AAD36198; TM_1122. DR EnsemblBacteria; AGL50052; AGL50052; Tmari_1128. DR GeneID; 898642; -. DR KEGG; tma:TM1122; -. DR KEGG; tmi:THEMA_08735; -. DR KEGG; tmm:Tmari_1128; -. DR KEGG; tmw:THMA_1145; -. DR PATRIC; 23937179; VBITheMar51294_1138. DR eggNOG; ENOG4105EX2; Bacteria. DR eggNOG; COG0395; LUCA. DR KO; K05815; -. DR OMA; FLLMREF; -. DR OrthoDB; EOG693GR8; -. DR BioCyc; TMAR243274:GC6P-1151-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0015169; F:glycerol-3-phosphate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0001406; F:glycerophosphodiester transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015794; P:glycerol-3-phosphate transport; IBA:GO_Central. DR GO; GO:0001407; P:glycerophosphodiester transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR030165; UgpE. DR PANTHER; PTHR32243:SF31; PTHR32243:SF31; 1. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 9 34 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 69 95 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 107 130 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 193 214 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 240 266 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 70 261 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 276 AA; 31378 MW; 6D7663F4C11EFC36 CRC64; MRRKRSITIL YEIILVMVTF IMALPLFLAI TISFQKPEAV FSYPPKFFPT SFYWKNYVEA FKYVPLARLF LNSLIVASLI TLGKLTTGAL AGFAFSHFNF KSKKIMFATL FATLFLPAET VMILPLFLIM KTFGWVNTYW ALTIPFMASA TNTFLMRQHF LTIPRELQDA ALIDGASYMQ FFWKVLIPLS KHMLAGASII NFVYAWNMYL WPLIVSMEDK MKTVQVGVKM LMQAESANNW GVIMAGTVVA LAPTVVMFLA LQNLFVKSLV RSGMKG // ID Q9X202_THEMA Unreviewed; 237 AA. AC Q9X202; G4FG61; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Putative membrane protein {ECO:0000313|EMBL:AGL50606.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36741.1}; GN OrderedLocusNames=TM_1674 {ECO:0000313|EMBL:AAD36741.1}; GN ORFNames=Tmari_1682 {ECO:0000313|EMBL:AGL50606.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36741.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36741.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36741.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50606.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50606.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36741.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50606.1; -; Genomic_DNA. DR PIR; H72225; H72225. DR RefSeq; NP_229474.1; NC_000853.1. DR RefSeq; WP_004082190.1; NZ_CP011107.1. DR STRING; 243274.TM1674; -. DR DNASU; 897276; -. DR EnsemblBacteria; AAD36741; AAD36741; TM_1674. DR EnsemblBacteria; AGL50606; AGL50606; Tmari_1682. DR GeneID; 897276; -. DR KEGG; tma:TM1674; -. DR KEGG; tmi:THEMA_05870; -. DR KEGG; tmm:Tmari_1682; -. DR KEGG; tmw:THMA_1716; -. DR PATRIC; 23938322; VBITheMar51294_1691. DR eggNOG; ENOG4107B04; Bacteria. DR eggNOG; COG1434; LUCA. DR OMA; WLGYWKE; -. DR OrthoDB; EOG6SBT3M; -. DR BioCyc; TMAR243274:GC6P-1722-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR003848; DUF218. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF02698; DUF218; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 56 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 73 228 DUF218. {ECO:0000259|Pfam:PF02698}. SQ SEQUENCE 237 AA; 27026 MW; 8FFAD29B75B56B3D CRC64; MFLQKILGAF LVTPGLFILL LIVGSFFFKK ARWFLLALAA IVYLFSSYVG EFLFLWPLEK NLDVPATLPN DAVIVVLGGG VERNTKAGDN LSDATLRRLL TGVQIYQKTK MPILVTGGSL TGLRSEAMIM KDYLVSLGVP EEKITVEDRS RNTYENALFT REKIGDVPII LVTDSIHMRR AVFTFKRFFQ SVTPYPAGFY FGDPEFVDFL PNATSFYLNS RAIYEWIGLV WYNFRWR // ID Q9WY35_THEMA Unreviewed; 87 AA. AC Q9WY35; G4FHA6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 76. DE SubName: Full=SpoVS-related protein {ECO:0000313|EMBL:AAD35284.1}; DE SubName: Full=SpoVS-related protein, type 2 {ECO:0000313|EMBL:AGL49116.1}; GN OrderedLocusNames=TM_0192 {ECO:0000313|EMBL:AAD35284.1}; GN ORFNames=Tmari_0190 {ECO:0000313|EMBL:AGL49116.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35284.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35284.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35284.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49116.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49116.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35284.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49116.1; -; Genomic_DNA. DR PIR; H72406; H72406. DR RefSeq; NP_228007.1; NC_000853.1. DR RefSeq; WP_004082838.1; NZ_CP011107.1. DR SMR; Q9WY35; 2-85. DR STRING; 243274.TM0192; -. DR EnsemblBacteria; AAD35284; AAD35284; TM_0192. DR EnsemblBacteria; AGL49116; AGL49116; Tmari_0190. DR GeneID; 897040; -. DR KEGG; tma:TM0192; -. DR KEGG; tmi:THEMA_03805; -. DR KEGG; tmm:Tmari_0190; -. DR KEGG; tmw:THMA_0194; -. DR PATRIC; 23935244; VBITheMar51294_0194. DR eggNOG; ENOG4105MCT; Bacteria. DR eggNOG; COG2359; LUCA. DR KO; K06416; -. DR OMA; AIKFIIE; -. DR OrthoDB; EOG6ND0PF; -. DR BioCyc; TMAR243274:GC6P-199-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR007347; SpoVS. DR Pfam; PF04232; SpoVS; 1. DR ProDom; PD061837; SpoVS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 87 AA; 8961 MW; 132173DDCF9221DA CRC64; MEVLKVASNS NPNKVAGALA GVIREKGKAE LQAIGAGAVN QAVKAIAIAR GYLAPSGINL VCVPAFAEVQ INGETRTAIK FIVFPKD // ID Q9X124_THEMA Unreviewed; 89 AA. AC Q9X124; G4FE51; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36372.1}; GN OrderedLocusNames=TM_1298 {ECO:0000313|EMBL:AAD36372.1}; GN ORFNames=Tmari_1306 {ECO:0000313|EMBL:AGL50230.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36372.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36372.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36372.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50230.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50230.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36372.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50230.1; -; Genomic_DNA. DR PIR; D72269; D72269. DR RefSeq; NP_229102.1; NC_000853.1. DR RefSeq; WP_004079925.1; NZ_CP011107.1. DR STRING; 243274.TM1298; -. DR EnsemblBacteria; AAD36372; AAD36372; TM_1298. DR EnsemblBacteria; AGL50230; AGL50230; Tmari_1306. DR GeneID; 898184; -. DR KEGG; tma:TM1298; -. DR KEGG; tmi:THEMA_07845; -. DR KEGG; tmm:Tmari_1306; -. DR KEGG; tmw:THMA_1324; -. DR PATRIC; 23937536; VBITheMar51294_1314. DR eggNOG; COG0457; LUCA. DR OMA; LVRILHW; -. DR OrthoDB; EOG62K250; -. DR BioCyc; TMAR243274:GC6P-1329-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 89 AA; 11158 MW; 2C5C0D10D25F6585 CRC64; MKRKKLERFT LKYIEMKEPD RKFLDRFLRN YGRYDGVRFG IRLRKPDVVR EFAKRHSLKV QPLFVAFWCE EDGRARRRLV RILHWMTQE // ID Q9X280_THEMA Unreviewed; 77 AA. AC Q9X280; G4FGE4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 100. DE SubName: Full=2-oxoisovalerate oxidoreductase, gamma subunit, putative {ECO:0000313|EMBL:AAD36823.1}; DE SubName: Full=Ketoisovalerate oxidoreductase subunit VorC {ECO:0000313|EMBL:AGL50690.1}; DE EC=1.2.7.7 {ECO:0000313|EMBL:AGL50690.1}; GN OrderedLocusNames=TM_1758 {ECO:0000313|EMBL:AAD36823.1}; GN ORFNames=Tmari_1766 {ECO:0000313|EMBL:AGL50690.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36823.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36823.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36823.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50690.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50690.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36823.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50690.1; -; Genomic_DNA. DR PIR; G72214; G72214. DR RefSeq; NP_229556.1; NC_000853.1. DR RefSeq; WP_004082295.1; NZ_CP011107.1. DR STRING; 243274.TM1758; -. DR EnsemblBacteria; AAD36823; AAD36823; TM_1758. DR EnsemblBacteria; AGL50690; AGL50690; Tmari_1766. DR GeneID; 897093; -. DR KEGG; tma:TM1758; -. DR KEGG; tmi:THEMA_05445; -. DR KEGG; tmm:Tmari_1766; -. DR KEGG; tmw:THMA_1800; -. DR PATRIC; 23938492; VBITheMar51294_1776. DR eggNOG; ENOG4105WAN; Bacteria. DR eggNOG; COG1146; LUCA. DR KO; K00176; -. DR OMA; IGCANCA; -. DR OrthoDB; EOG6CVV7G; -. DR BioCyc; TMAR243274:GC6P-1806-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0043807; F:3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF12838; Fer4_7; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50690.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 32 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 38 68 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 77 AA; 8661 MW; 47CA033D695D1830 CRC64; MRGYITIDSE RCKGCGLCIS VCPAKVIEFS HRYNSKGYHP AVYRGDDCIA CGFCYLTCPD VCITVFREVQ KKTNVKV // ID Q9WXW2_THEMA Unreviewed; 190 AA. AC Q9WXW2; G4FH22; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Diguanylate cyclase/phosphodiesterase-domain containing protein {ECO:0000313|EMBL:AGL49030.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35201.1}; GN OrderedLocusNames=TM_0107 {ECO:0000313|EMBL:AAD35201.1}; GN ORFNames=Tmari_0104 {ECO:0000313|EMBL:AGL49030.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35201.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35201.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35201.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49030.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49030.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains GGDEF domain. CC {ECO:0000256|SAAS:SAAS00496774}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35201.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49030.1; -; Genomic_DNA. DR PIR; B72416; B72416. DR RefSeq; NP_227923.1; NC_000853.1. DR RefSeq; WP_004082673.1; NZ_CP011107.1. DR STRING; 243274.TM0107; -. DR EnsemblBacteria; AAD35201; AAD35201; TM_0107. DR EnsemblBacteria; AGL49030; AGL49030; Tmari_0104. DR GeneID; 896934; -. DR KEGG; tma:TM0107; -. DR KEGG; tmi:THEMA_04270; -. DR KEGG; tmm:Tmari_0104; -. DR KEGG; tmw:THMA_0103; -. DR PATRIC; 23935054; VBITheMar51294_0105. DR eggNOG; ENOG4105JDT; Bacteria. DR eggNOG; COG2199; LUCA. DR OMA; ISYYHQK; -. DR OrthoDB; EOG66MQQ7; -. DR BioCyc; TMAR243274:GC6P-107-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR Pfam; PF00990; GGDEF; 1. DR SUPFAM; SSF55073; SSF55073; 1. DR PROSITE; PS50887; GGDEF; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 87 190 GGDEF. {ECO:0000259|PROSITE:PS50887}. FT COILED 4 41 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 190 AA; 22415 MW; B24C65BF5CEA683B CRC64; MDERTELLKR IEELEEKLRQ CQQREQELEA LIEEYNEVMK KQFQVFDDFF EKLGTTKMID PLTRVYAKDH FLRLLSYQHQ RAFEENTPYT IFFVKTKVSK NEREKALMKI GKILKECVRV PLDSVGRYSD DTFALFVIGV GKETAPNIEE RIKNHIESIG GIEYSIAYKS YPEDFMDLEK AILDLEKAVA // ID Q9WYL2_THEMA Unreviewed; 449 AA. AC Q9WYL2; G4FHU2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 127. DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692}; DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692}; GN OrderedLocusNames=TM_0381 {ECO:0000313|EMBL:AAD35466.1}; GN ORFNames=Tmari_0379 {ECO:0000313|EMBL:AGL49304.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35466.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35466.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35466.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49304.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49304.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = CC protein N(6)-(lipoyl)lysine + NADH. CC {ECO:0000256|RuleBase:RU003692}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003692}; CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003692}; CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC {ECO:0000256|RuleBase:RU003692}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35466.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49304.1; -; Genomic_DNA. DR PIR; E72383; E72383. DR RefSeq; NP_228191.1; NC_000853.1. DR RefSeq; WP_004083198.1; NZ_CP011107.1. DR STRING; 243274.TM0381; -. DR EnsemblBacteria; AAD35466; AAD35466; TM_0381. DR EnsemblBacteria; AGL49304; AGL49304; Tmari_0379. DR GeneID; 897357; -. DR KEGG; tma:TM0381; -. DR KEGG; tmi:THEMA_02815; -. DR KEGG; tmm:Tmari_0379; -. DR KEGG; tmw:THMA_0388; -. DR PATRIC; 23935645; VBITheMar51294_0387. DR eggNOG; ENOG4107QN2; Bacteria. DR eggNOG; COG1249; LUCA. DR KO; K00382; -. DR OMA; RKANHYG; -. DR OrthoDB; EOG6QCD6D; -. DR BioCyc; TMAR243274:GC6P-395-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR006258; Lipoamide_DH. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR SUPFAM; SSF51905; SSF51905; 1. DR SUPFAM; SSF55424; SSF55424; 1. DR TIGRFAMs; TIGR01350; lipoamide_DH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW FAD {ECO:0000256|RuleBase:RU003692}; KW Flavoprotein {ECO:0000256|RuleBase:RU003692}; KW Glycolysis {ECO:0000256|SAAS:SAAS00436429}; KW NAD {ECO:0000256|RuleBase:RU003692}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003692, KW ECO:0000313|EMBL:AGL49304.1}; KW Redox-active center {ECO:0000256|RuleBase:RU003692}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 313 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. FT DOMAIN 332 435 Pyr_redox_dim. FT {ECO:0000259|Pfam:PF02852}. SQ SEQUENCE 449 AA; 48166 MW; DEBD7BE52FC93D88 CRC64; MYDAVIIGGG PGGYVCAIKL AQLGKKVALV EKDALGGTCT NRGCIPTKAM LTVSHLMDEM KEKASKYGLK VSGVEYDVAA IMKHVQKSVM MSRKGIEYLL KKNGVEVFKG TAVVENKNTV VVQETGEKLE AKNLVLAHGS VPSVFSPFDI DGVWTSDDVF NLKEFPKSLV IVGGGVIGVE FATFFGSFGV DVTIVEIAEH ILPYEDSDVA EEVKKALKRK GVKILEKTKI SSLSKVDDGF EVALENGETL KAEKVLLAAG RKPNIPEDVK ALGVKIEKGV VTDSRMRTNV ENVYAIGDIR SGIMLAHVAM YEGIVAAKNI AGEEEEMDYS AVPSIIFSSP EVASVGVREK DVNPEEVVIS KFPVSANGRA RTMLENIGFA KVIADKKDGT VLGMSIVSPS ATDMIMEGVI AVKFRMKAED LEKAIHPHPT LTETILGALE GVSGKPIHL // ID Q9X190_THEMA Unreviewed; 368 AA. AC Q9X190; G4FFA6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Iron-sulfur cluster assembly protein SufD {ECO:0000313|EMBL:AGL50301.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36441.1}; GN OrderedLocusNames=TM_1370 {ECO:0000313|EMBL:AAD36441.1}; GN ORFNames=Tmari_1377 {ECO:0000313|EMBL:AGL50301.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36441.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36441.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36441.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50301.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50301.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36441.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50301.1; -; Genomic_DNA. DR PIR; C72260; C72260. DR RefSeq; NP_229171.1; NC_000853.1. DR RefSeq; WP_004081566.1; NZ_CP011107.1. DR STRING; 243274.TM1370; -. DR EnsemblBacteria; AAD36441; AAD36441; TM_1370. DR EnsemblBacteria; AGL50301; AGL50301; Tmari_1377. DR GeneID; 898109; -. DR KEGG; tma:TM1370; -. DR KEGG; tmi:THEMA_07485; -. DR KEGG; tmm:Tmari_1377; -. DR KEGG; tmw:THMA_1396; -. DR PATRIC; 23937680; VBITheMar51294_1382. DR eggNOG; ENOG4105IEU; Bacteria. DR eggNOG; COG0719; LUCA. DR KO; K07033; -. DR OMA; SERFCSE; -. DR OrthoDB; EOG6VTK32; -. DR BioCyc; TMAR243274:GC6P-1404-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR InterPro; IPR000825; SUF_FeS_clus_asmbl_SufBD. DR Pfam; PF01458; UPF0051; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 368 AA; 42191 MW; EBC09077366137AC CRC64; MEKTLVIEHD GEKAVVWETP QIFSENDYDY EVLEKALENT GGPLKEWRKK KYQEYKEWGF PRWKRCNLDG MSLPELSFKR IDLDVDISLL EKLDFEGAHR KFVLLGDTFF TDFRVYGDGK HMMRFDGDGI ENVLVVVEKE AEIYKLSSTD RFRNTVMRIL VKKNASLKFF NLDFFGNFSF DNVFIVLEEG ARLVLRDFKA FGYRKTGHIL VKLNKSSKAD MKSFFYQNGS GITDLLYLMR FEGEDAEGKL KGNGVVDGAG KIVFRGILDV KRGSKNIVAE ETEHTLVLSP DARMDAIPSL WVDENDVTAS HSASSSSLDE DELFYLMTRG VDEIESKKLI VRGVFNELLD ELDESVKGEV ENVVNRIV // ID Q9WXR7_THEMA Unreviewed; 179 AA. AC Q9WXR7; G4FGX7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 86. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35156.1}; GN OrderedLocusNames=TM_0062 {ECO:0000313|EMBL:AAD35156.1}; GN ORFNames=Tmari_0059 {ECO:0000313|EMBL:AGL48985.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35156.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35156.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35156.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48985.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48985.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35156.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48985.1; -; Genomic_DNA. DR PIR; B72422; B72422. DR RefSeq; NP_227878.1; NC_000853.1. DR RefSeq; WP_004082552.1; NZ_CP011107.1. DR STRING; 243274.TM0062; -. DR CAZy; CBM22; Carbohydrate-Binding Module Family 22. DR DNASU; 896886; -. DR EnsemblBacteria; AAD35156; AAD35156; TM_0062. DR EnsemblBacteria; AGL48985; AGL48985; Tmari_0059. DR GeneID; 896886; -. DR KEGG; tma:TM0062; -. DR KEGG; tmi:THEMA_04495; -. DR KEGG; tmm:Tmari_0059; -. DR KEGG; tmw:THMA_0058; -. DR PATRIC; 23934964; VBITheMar51294_0060. DR OMA; ITQNDTE; -. DR OrthoDB; EOG65J521; -. DR BioCyc; TMAR243274:GC6P-62-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro. DR Gene3D; 2.60.120.260; -; 1. DR InterPro; IPR003305; CenC_carb-bd. DR InterPro; IPR008979; Galactose-bd-like. DR Pfam; PF02018; CBM_4_9; 1. DR SUPFAM; SSF49785; SSF49785; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 179 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006972317. FT DOMAIN 33 128 CBM-cenC (cenC-type cellulose-binding). FT {ECO:0000259|Pfam:PF02018}. SQ SEQUENCE 179 AA; 19845 MW; EE80E7D73B467BF9 CRC64; MKKWFLMSVL GVFAFLIILS GCVSAPGTGG ALNKVLKVET GDQGWKTAWF YGIGNYINAD ATYTYSVRIY HEEATSVKFN LTLKTTTNQY KSIFWGREVL PATWVTIEAT YTLNSSDGNP SDIYIEPQTP GITFYLDDFV IKDESGKVVL KTDFEDGTEQ GWSGNNATVS VVYDPAQSQ // ID Q9WXY2_THEMA Unreviewed; 462 AA. AC Q9WXY2; G4FH43; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Oxaloacetate decarboxylase, alpha subunit {ECO:0000313|EMBL:AAD35222.1}; DE SubName: Full=Pyruvate:Oxaloacetate transcarboxylase domain protein {ECO:0000313|EMBL:AGL49052.1}; GN OrderedLocusNames=TM_0128 {ECO:0000313|EMBL:AAD35222.1}; GN ORFNames=Tmari_0126 {ECO:0000313|EMBL:AGL49052.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35222.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35222.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35222.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49052.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49052.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35222.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49052.1; -; Genomic_DNA. DR PIR; H72415; H72415. DR RefSeq; NP_227944.1; NC_000853.1. DR RefSeq; WP_004082715.1; NZ_CP011107.1. DR STRING; 243274.TM0128; -. DR EnsemblBacteria; AAD35222; AAD35222; TM_0128. DR EnsemblBacteria; AGL49052; AGL49052; Tmari_0126. DR GeneID; 896955; -. DR KEGG; tma:TM0128; -. DR KEGG; tmi:THEMA_04165; -. DR KEGG; tmm:Tmari_0126; -. DR KEGG; tmw:THMA_0124; -. DR PATRIC; 23935094; VBITheMar51294_0125. DR eggNOG; ENOG4107QSA; Bacteria. DR eggNOG; COG5016; LUCA. DR KO; K01571; -. DR OMA; MLHAVKG; -. DR OrthoDB; EOG6CVV6Z; -. DR BioCyc; TMAR243274:GC6P-128-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003379; Carboxylase_cons_dom. DR InterPro; IPR005776; OadA. DR InterPro; IPR000891; PYR_CT. DR Pfam; PF00682; HMGL-like; 1. DR Pfam; PF02436; PYC_OADA; 1. DR TIGRFAMs; TIGR01108; oadA; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Pyruvate {ECO:0000313|EMBL:AGL49052.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 261 PYR_CT. {ECO:0000259|PROSITE:PS50991}. SQ SEQUENCE 462 AA; 53122 MW; 3AEDDFF97A446A3C CRC64; MFVDTTLRDG HQSLIATRMR TEDMLPALEA FDRMNFHSME VWGGATFDVA VRFLNENPWE RLKKIREGLK NTKIQMLLRG QNLVGYRHYA DDVVELFIKK VAEYGLDIIR IFDALNDERN LQKSIEESKK HGLHVQVAIS YTVSPVHTLD YYLDFARKLL DMGVDSICIK DMAGLLTPKR AYELVRALKE KFGVPVEVHS HCTTGFAPLA YQAAYEAGAD FFDTAISPFS MGTSQPTFET MYYAFRGNGK EDFDREALKF LVDHFTKVRM KYIEYDVGMK YPDSRIIFSQ IPGGMYSNLL KQLKEQRMEH LLDKVLEEVP RVQKDLGYPP LVTPTSQIVG VQAFLNVVYG RYERITNETR NYVKGLYGRP PAPIDPELMR KILGDEKPID CRPADLLEPE LDKTRKELGI LVETDEDLLI AVILGEVGKK FLRKKYEEKI GVDFNYLESL SDFTDDMPVY PV // ID G4FFG1_THEMA Unreviewed; 645 AA. AC G4FFG1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-MAR-2016, entry version 43. DE SubName: Full=Fe-hydrogenase, subunit alpha {ECO:0000313|EMBL:AAD36496.1}; DE SubName: Full=Periplasmic [Fe] hydrogenase large subunit {ECO:0000313|EMBL:AGL50356.1}; DE EC=1.12.7.2 {ECO:0000313|EMBL:AGL50356.1}; GN OrderedLocusNames=TM_1426 {ECO:0000313|EMBL:AAD36496.1}; GN ORFNames=Tmari_1432 {ECO:0000313|EMBL:AGL50356.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AGL50356.1, ECO:0000313|Proteomes:UP000013901}; RN [1] {ECO:0000313|EMBL:AAD36496.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36496.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50356.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50356.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36496.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50356.1; -; Genomic_DNA. DR PIR; G72256; G72256. DR RefSeq; NP_229226.1; NC_000853.1. DR RefSeq; WP_004081677.1; NZ_CP011107.1. DR STRING; 243274.TM1426; -. DR EnsemblBacteria; AAD36496; AAD36496; TM_1426. DR EnsemblBacteria; AGL50356; AGL50356; Tmari_1432. DR GeneID; 898049; -. DR KEGG; tma:TM1426; -. DR KEGG; tmi:THEMA_07185; -. DR KEGG; tmm:Tmari_1432; -. DR KEGG; tmw:THMA_1456; -. DR eggNOG; ENOG4107QHI; Bacteria. DR eggNOG; COG1034; LUCA. DR eggNOG; COG1905; LUCA. DR eggNOG; COG4624; LUCA. DR KO; K17997; -. DR OMA; CGDCVRM; -. DR BioCyc; TMAR243274:GC6P-1464-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR Gene3D; 4.10.260.20; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR009016; Fe_hydrogenase. DR InterPro; IPR004108; Fe_hydrogenase_lsu_C. DR InterPro; IPR003149; Fe_hydrogenase_ssu. DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS. DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF02906; Fe_hyd_lg_C; 1. DR Pfam; PF02256; Fe_hyd_SSU; 1. DR Pfam; PF12838; Fer4_7; 1. DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1. DR SMART; SM00902; Fe_hyd_SSU; 1. DR SMART; SM00929; NADH-G_4Fe-4S_3; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF53920; SSF53920; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. DR PROSITE; PS00641; COMPLEX1_75K_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Oxidoreductase {ECO:0000313|EMBL:AGL50356.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 76 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. FT DOMAIN 133 164 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 178 206 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 645 AA; 72254 MW; 817111261966B58F CRC64; MKIYVDGREV IINDNERNLL EALKNVGIEI PNLCYLSEAS IYGACRMCLV EINGQITTSC TLKPYEGMKV KTNTPEIYEM RRNILELILA THNRDCTTCD RNGSCKLQKY AEDFGIRKIR FEALKKEHVR DESAPVVRDT SKCILCGDCV RVCEEIQGVG VIEFAKRGFE SVVTTAFDTP LIETECVLCG QCVAYCPTGA LSIRNDIDKL IEALESDKIV IGMIAPAVRA AIQEEFGIDE DVAMAEKLVS FLKTIGFDKV FDVSFGADLV AYEEAHEFYE RLKKGERLPQ FTSCCPAWVK HAEHTYPQYL QNLSSVKSPQ QALGTVIKKI YARKLGVPEE KIFLVSFMPC TAKKFEAERE EHEGIVDIVL TTRELAQLIK MSRIDINRVE PQPFDRPYGV SSQAGLGFGK AGGVFSCVLS VLNEEIGIEK VDVKSPEDGI RVAEVTLKDG TSFKGAVIYG LGKVKKFLEE RKDVEIIEVM ACNYGCVGGG GQPYPNDSRI REHRAKVLRD TMGIKSLLTP VENLFLMKLY EEDLKDEHTR HEILHTTYRP RRRYPEKDVE ILPVPNGEKR TVKVCLGTSC YTKGSYEILK KLVDYVKEND MEGKIEVLGT FCVENCGASP NVIVDDKIIG GATFEKVLEE LSKNG // ID Q9X188_THEMA Unreviewed; 246 AA. AC Q9X188; G4FFA4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 118. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36439.1}; DE SubName: Full=Iron-sulfur cluster assembly ATPase protein SufC {ECO:0000313|EMBL:AGL50299.1}; GN OrderedLocusNames=TM_1368 {ECO:0000313|EMBL:AAD36439.1}; GN ORFNames=Tmari_1375 {ECO:0000313|EMBL:AGL50299.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36439.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36439.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36439.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50299.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50299.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36439.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50299.1; -; Genomic_DNA. DR PIR; A72260; A72260. DR RefSeq; NP_229169.1; NC_000853.1. DR RefSeq; WP_004081564.1; NZ_CP011107.1. DR STRING; 243274.TM1368; -. DR EnsemblBacteria; AAD36439; AAD36439; TM_1368. DR EnsemblBacteria; AGL50299; AGL50299; Tmari_1375. DR GeneID; 898111; -. DR KEGG; tma:TM1368; -. DR KEGG; tmi:THEMA_07495; -. DR KEGG; tmm:Tmari_1375; -. DR KEGG; tmw:THMA_1394; -. DR PATRIC; 23937676; VBITheMar51294_1380. DR eggNOG; ENOG4105C3K; Bacteria. DR eggNOG; COG0396; LUCA. DR KO; K09013; -. DR OMA; CHGNPRE; -. DR OrthoDB; EOG6J74ZM; -. DR BioCyc; TMAR243274:GC6P-1402-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR010230; FeS-cluster_ATPase_SufC. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01978; sufC; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAD36439.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000313|EMBL:AAD36439.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 245 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT COILED 108 139 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 246 AA; 27836 MW; 9B3EEBDA5A0D5621 CRC64; MLRIVNLHAK LRDEDKEILK GVNLEIEKGE VHVLMGPNGS GKSTLANVIM GNPRYIVTEG DIVFEGNSIK DLPPNERAKL GIMMTFQNPY EVEGVKLSQF LITAHRRIHG EDKNYLELRK ELEETAEKLG LDKDFLERYL NVGFSGGEKK RSEILQSLFL RPKLLILDEI DSGLDVDALR LIANLIARLN EEGVTLLIIT HYKRLLDHLK RIDKVHVYVD GRIVTSGGPE LADEIEEKGY SLEGVR // ID Q9WYX3_THEMA Unreviewed; 345 AA. AC Q9WYX3; G4FDW7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 95. DE SubName: Full=Dipeptide transport system permease protein DppB {ECO:0000313|EMBL:AGL49425.1}; DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35588.1}; GN OrderedLocusNames=TM_0503 {ECO:0000313|EMBL:AAD35588.1}; GN ORFNames=Tmari_0500 {ECO:0000313|EMBL:AGL49425.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35588.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35588.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35588.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49425.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49425.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35588.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49425.1; -; Genomic_DNA. DR PIR; F72371; F72371. DR RefSeq; NP_228313.1; NC_000853.1. DR RefSeq; WP_004081437.1; NZ_CP011107.1. DR STRING; 243274.TM0503; -. DR EnsemblBacteria; AAD35588; AAD35588; TM_0503. DR EnsemblBacteria; AGL49425; AGL49425; Tmari_0500. DR GeneID; 897544; -. DR KEGG; tma:TM0503; -. DR KEGG; tmi:THEMA_02155; -. DR KEGG; tmm:Tmari_0500; -. DR KEGG; tmw:THMA_0516; -. DR PATRIC; 23935911; VBITheMar51294_0510. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR KO; K02033; -. DR OMA; TIELALY; -. DR OrthoDB; EOG66F098; -. DR BioCyc; TMAR243274:GC6P-527-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 106 127 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 139 164 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 212 231 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 266 292 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 312 338 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 100 331 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 345 AA; 38929 MW; 7C2E0025F12BCAEA CRC64; MTAYIIRRLL LLPLILLGVT FIVFSMIQSL GPDKLLAAYV NPNMLDKLTP EQMDALKEKY GLNDFFVVRY VKWLANTLRG DLGWSLVGKE PVKDALLRRL PYTVELALYA IFPVVFVGIW LGVKAAVHRG KFLDHFIRIF AVVGWSFPDF VFGLLVLMIF YSILNWLPPG NLSMWAEEVI KSPEFHRYTK LITIDALLNG RLDIFWDGLK HLIGPIITLS WLWWAYLLRI TRSSMLEVLN KEYVRTARAK GLPEDVVINK HARRNALIPV TTVAGGMVIG LFSGTVIVET VFNRTGVGSF TAQAALQLDY ASVMASALFF STILVVGNLI IDILYALIDP RIRLG // ID Q9X2A6_THEMA Unreviewed; 59 AA. AC Q9X2A6; G4FGH3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36849.1}; GN OrderedLocusNames=TM_1786 {ECO:0000313|EMBL:AAD36849.1}; GN ORFNames=Tmari_1795 {ECO:0000313|EMBL:AGL50719.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36849.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36849.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36849.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50719.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50719.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36849.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50719.1; -; Genomic_DNA. DR PIR; E72211; E72211. DR RefSeq; NP_229583.1; NC_000853.1. DR RefSeq; WP_004082332.1; NZ_CP011107.1. DR EnsemblBacteria; AAD36849; AAD36849; TM_1786. DR EnsemblBacteria; AGL50719; AGL50719; Tmari_1795. DR GeneID; 897738; -. DR KEGG; tma:TM1786; -. DR KEGG; tmi:THEMA_05270; -. DR KEGG; tmm:Tmari_1795; -. DR KEGG; tmw:THMA_1830; -. DR PATRIC; 23938557; VBITheMar51294_1806. DR OMA; PYIYRCT; -. DR BioCyc; TMAR243274:GC6P-1836-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 59 AA; 6952 MW; 19F54C257EE7AA42 CRC64; MPYIYRCKKC GAIYYSATSI EYQLNKYCEK CGGELEQLGE EGEVMEKEEE KKSEKKKKE // ID Q9WXN9_THEMA Unreviewed; 381 AA. AC Q9WXN9; G4FGU9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 100. DE SubName: Full=Cellobiose-responsive regulator of beta-glucosides utilization, ROK family {ECO:0000313|EMBL:AGL48955.1}; DE SubName: Full=Transcriptional regulator, XylR-related {ECO:0000313|EMBL:AAD35126.1}; GN OrderedLocusNames=TM_0032 {ECO:0000313|EMBL:AAD35126.1}; GN ORFNames=Tmari_0029 {ECO:0000313|EMBL:AGL48955.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35126.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35126.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35126.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL48955.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL48955.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35126.1; -; Genomic_DNA. DR EMBL; CP004077; AGL48955.1; -; Genomic_DNA. DR PIR; B72429; B72429. DR RefSeq; NP_227848.1; NC_000853.1. DR RefSeq; WP_004082489.1; NZ_CP011107.1. DR STRING; 243274.TM0032; -. DR EnsemblBacteria; AAD35126; AAD35126; TM_0032. DR EnsemblBacteria; AGL48955; AGL48955; Tmari_0029. DR GeneID; 896853; -. DR KEGG; tma:TM0032; -. DR KEGG; tmi:THEMA_04640; -. DR KEGG; tmm:Tmari_0029; -. DR KEGG; tmw:THMA_0028; -. DR PATRIC; 23934904; VBITheMar51294_0030. DR eggNOG; ENOG4106CW9; Bacteria. DR eggNOG; COG1940; LUCA. DR OMA; AQSAIWR; -. DR OrthoDB; EOG64R61Z; -. DR BioCyc; TMAR243274:GC6P-32-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR000600; ROK. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00480; ROK; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 381 AA; 43424 MW; B1E93781CF023764 CRC64; MHKKLNPKSM KRENKKMVLR YLIESGPHSR VEIARKTGLA QSAIWRIIEE LVNEGLVEEK GTATGRRRKA VTYGPTRSFI TSIIYNVEVL ETLVAVGFLD GAWRIIERFS TPKDFDEFKQ RVTSSYENIL KSHVLNKNIS KVVFSLPGIV NTESKFLIHA PNLGWRNIDF RREFGNLDLE VLVENDSNLS LLAEEFFSQD VKESDVAFFL YFGEGIGGAI SVNGKIVRGE NFAAGEIGHV VLDVKNGKEV EEFLSISKLV ERMEKFVELQ GESLDEKFRY IKRLWFSGEK NVKETMEEFL QHVAVVLKNI IYFLNPGVIV LGGVVNDLWD TFGSFIKREL EKITDREIAN VLIRDTIFKE ISPSLVGGNV LAIEEFLRQI T // ID Q9WZU1_THEMA Unreviewed; 566 AA. AC Q9WZU1; G4FCY7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 113. DE SubName: Full=General secretion pathway protein E {ECO:0000313|EMBL:AAD35919.1}; DE SubName: Full=Type II secretory pathway, ATPase PulE {ECO:0000313|EMBL:AGL49764.1}; GN OrderedLocusNames=TM_0837 {ECO:0000313|EMBL:AAD35919.1}; GN ORFNames=Tmari_0839 {ECO:0000313|EMBL:AGL49764.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35919.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35919.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35919.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49764.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49764.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35919.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49764.1; -; Genomic_DNA. DR PIR; A72329; A72329. DR RefSeq; NP_228646.1; NC_000853.1. DR RefSeq; WP_004080797.1; NZ_CP011107.1. DR SMR; Q9WZU1; 177-563. DR STRING; 243274.TM0837; -. DR EnsemblBacteria; AAD35919; AAD35919; TM_0837. DR EnsemblBacteria; AGL49764; AGL49764; Tmari_0839. DR GeneID; 898508; -. DR KEGG; tma:TM0837; -. DR KEGG; tmi:THEMA_00455; -. DR KEGG; tmm:Tmari_0839; -. DR KEGG; tmw:THMA_0858; -. DR PATRIC; 23936600; VBITheMar51294_0850. DR eggNOG; ENOG4107QHF; Bacteria. DR eggNOG; COG2804; LUCA. DR KO; K02652; -. DR OMA; CGHNGYR; -. DR OrthoDB; EOG63Z76W; -. DR BioCyc; TMAR243274:GC6P-866-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR007831; GSPII_E_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001482; T2SS_protein-E. DR Pfam; PF00437; T2SSE; 1. DR Pfam; PF05157; T2SSE_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00662; T2SP_E; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 381 395 T2SP_E. {ECO:0000259|PROSITE:PS00662}. SQ SEQUENCE 566 AA; 64066 MW; B9641C16CEB7C080 CRC64; MLRRYRKLGE ILLEKGFITR EELDKALEIQ KEERKPLGEV LIETGYITED QLLEALSEQY GVPILKELPK NIPLNVVGSI PKNIIESLHV IPVEKKEDGT LVVVTDNGTN IPRIKQEIRF LTGKNPEIYL VTSRDFSVLY QTYVLGVPLE LFEEPYVAIE ETPEQVEEEE EEEREVEEAP IVRLVNNIVN RAIEMGASDI HIEPMKRTVR VRFRIDGILR KVLEYQKPQH NSVVARIKIM SGLDVSERRL PQDGKFYTIK GGEQYDFRVS TMPSTFGEKV VMRILKVSDA NKRLEELGYS EYNLKRILSL LEKPYGIILV TGPTGSGKST TLVAMINYLK SESVNIVTAE DPVEYTIEGV TQCQVFPEIG LTFARYLRAF LRQDPDIIMV GEIRDRETAQ LAVEASLTGH LVLSTLHTNT AAGAVSRLIE MGIDPHLLGA SLIGIIGQRL VRKLCDECKM PGEVRDEQVK SYFEQFFGKV PDQIYYPSEE GCPACKGMRY RGRMAIGEVL IVDEELRELI SSKASETEIA KLAVKKGMRT MFQDALEKVL LGQTSIEEVF RVTTPL // ID Q9WYV1_THEMA Unreviewed; 382 AA. AC Q9WYV1; G4FDY9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35565.1}; GN OrderedLocusNames=TM_0481 {ECO:0000313|EMBL:AAD35565.1}; GN ORFNames=Tmari_0478 {ECO:0000313|EMBL:AGL49403.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35565.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35565.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35565.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49403.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49403.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35565.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49403.1; -; Genomic_DNA. DR PIR; A72373; A72373. DR RefSeq; NP_228291.1; NC_000853.1. DR RefSeq; WP_004081485.1; NZ_CP011107.1. DR STRING; 243274.TM0481; -. DR DNASU; 897516; -. DR EnsemblBacteria; AAD35565; AAD35565; TM_0481. DR EnsemblBacteria; AGL49403; AGL49403; Tmari_0478. DR GeneID; 897516; -. DR KEGG; tma:TM0481; -. DR KEGG; tmi:THEMA_02280; -. DR KEGG; tmm:Tmari_0478; -. DR KEGG; tmw:THMA_0491; -. DR PATRIC; 23935861; VBITheMar51294_0488. DR eggNOG; ENOG4108WGH; Bacteria. DR eggNOG; COG1906; LUCA. DR KO; K09133; -. DR OMA; PVHLCLV; -. DR OrthoDB; EOG6XQ3H5; -. DR BioCyc; TMAR243274:GC6P-502-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005253; CHP00529. DR InterPro; IPR007294; DUF401. DR Pfam; PF04165; DUF401; 1. DR TIGRFAMs; TIGR00529; AF0261; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 94 115 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 154 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 166 184 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 235 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 287 317 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 329 351 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 363 381 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 382 AA; 42885 MW; 7E94449DED0162CF CRC64; MNTLSVLLSL FTVIVVQRVF KKLSISLLSG VIVMILSLKV RNILEIFFWT VSSDSFWSLI VTVFLIYLLS GMMEKSGDYS RFSEEMRTIF SKNVDSFVPA LIGLMPMPGG ALFTAPIVKN SLPEENSLKL AVKNYWFRHT IEFFWPIYPA VVLVSELSGI HPGKVSLTLF PVFAIAFFLG WFFFNGKQLP CLSKPRSFFN LFPLIPVLGT GVLILLFKVS GWFALLLSTS GYAVFRRRYL LKTLKQVFNK WDVFLVLFFV YIYKVVVEHS GVGEGIAAEF VRWNLSPWIL LIFLPLVSGI STGITQAAVG ISLPVLMEVF SSKYAVYTYM FAVGGVILSP VHLCVVLSAK FFEVEVFDIL KKVFLPLVLT LILGALVLGV IL // ID Q9WY34_THEMA Unreviewed; 258 AA. AC Q9WY34; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 113. DE SubName: Full=Iron(III) ABC transporter, ATP-binding protein, putative {ECO:0000313|EMBL:AAD35283.1}; GN OrderedLocusNames=TM_0191 {ECO:0000313|EMBL:AAD35283.1}; GN ORFNames=Tmari_0189 {ECO:0000313|EMBL:AGL49115.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35283.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35283.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35283.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49115.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49115.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35283.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49115.1; -; Genomic_DNA. DR PIR; G72406; G72406. DR RefSeq; NP_228006.1; NC_000853.1. DR RefSeq; WP_010865069.1; NZ_CP011107.1. DR STRING; 243274.TM0191; -. DR DNASU; 897039; -. DR EnsemblBacteria; AAD35283; AAD35283; TM_0191. DR EnsemblBacteria; AGL49115; AGL49115; Tmari_0189. DR GeneID; 897039; -. DR KEGG; tma:TM0191; -. DR KEGG; tmi:THEMA_03810; -. DR KEGG; tmm:Tmari_0189; -. DR KEGG; tmw:THMA_0193; -. DR PATRIC; 23935242; VBITheMar51294_0193. DR eggNOG; ENOG4105E0A; Bacteria. DR eggNOG; COG1120; LUCA. DR KO; K02013; -. DR OMA; MEIVQDF; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; TMAR243274:GC6P-198-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35283.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35283.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 232 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 258 AA; 29143 MW; 15E5FADEC5E0B064 CRC64; MLRIRNLSFS YRNKKILDNV TFSAQKGELI AILGPNGAGK STLLKCIAGI LKCQGVEIFS KPLEQYTRRD LARIVGYVPQ RIDPGMLNVY NLILLGRKPY VSVSPSKEDI EIVNRVVERL NLQHLVFQRA KNLSGGELQK VSIARALVQE PEILLLDEPT NNLDPKNQIE IMEIVQDFVK SRKMALVVMH EINLALRFAD RFIFMKDGKI VRDGERSILT PDLFWEVYGV NGVVKEILDT PVFVLRGKES PGSRENAG // ID Q9X2B0_THEMA Unreviewed; 139 AA. AC Q9X2B0; G4FGH7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36853.1}; GN OrderedLocusNames=TM_1790 {ECO:0000313|EMBL:AAD36853.1}; GN ORFNames=Tmari_1799 {ECO:0000313|EMBL:AGL50723.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36853.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36853.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36853.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50723.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50723.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36853.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50723.1; -; Genomic_DNA. DR PIR; A72212; A72212. DR RefSeq; NP_229587.1; NC_000853.1. DR RefSeq; WP_004082336.1; NZ_CP011107.1. DR STRING; 243274.TM1790; -. DR EnsemblBacteria; AAD36853; AAD36853; TM_1790. DR EnsemblBacteria; AGL50723; AGL50723; Tmari_1799. DR GeneID; 896906; -. DR KEGG; tma:TM1790; -. DR KEGG; tmi:THEMA_05245; -. DR KEGG; tmm:Tmari_1799; -. DR KEGG; tmw:THMA_1835; -. DR PATRIC; 23938567; VBITheMar51294_1810. DR OrthoDB; EOG6384Q6; -. DR BioCyc; TMAR243274:GC6P-1841-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 139 AA; 16115 MW; 296BE6DC4C6412CC CRC64; MISNKTRRRI RNELLPFVGK RVSVRGKIKA FGTTRSPFSK KPTILITNVT VRYLDKKVKV DHLWVAIKRI PENMDIAVGD VVSFEADVVK YKLLPDFKTK DDILHPRYNY GVENPKSFKI IKRTAEPSMT LRDAFLRVL // ID Q9X0B6_THEMA Unreviewed; 402 AA. AC Q9X0B6; G4FEX2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Transposase, putative {ECO:0000313|EMBL:AAD36103.1}; GN OrderedLocusNames=TM_1026 {ECO:0000313|EMBL:AAD36103.1}; GN ORFNames=Tmari_1030 {ECO:0000313|EMBL:AGL49954.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36103.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36103.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36103.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49954.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49954.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36103.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49954.1; -; Genomic_DNA. DR PIR; A72303; A72303. DR RefSeq; NP_228832.1; NC_000853.1. DR RefSeq; WP_004080500.1; NZ_CP011107.1. DR STRING; 243274.TM1026; -. DR EnsemblBacteria; AAD36103; AAD36103; TM_1026. DR EnsemblBacteria; AGL49954; AGL49954; Tmari_1030. DR GeneID; 898618; -. DR KEGG; tma:TM1026; -. DR KEGG; tmi:THEMA_09230; -. DR KEGG; tmm:Tmari_1030; -. DR KEGG; tmw:THMA_1048; -. DR PATRIC; 23936981; VBITheMar51294_1039. DR eggNOG; ENOG4108K3X; Bacteria. DR eggNOG; COG0675; LUCA. DR KO; K07496; -. DR OMA; ESREACK; -. DR OrthoDB; EOG6DRPD6; -. DR BioCyc; TMAR243274:GC6P-1055-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR024064; FdhE-like. DR InterPro; IPR001959; Transposase_2. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR Pfam; PF01385; OrfB_IS605; 1. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR SUPFAM; SSF144020; SSF144020; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 164 281 OrfB_IS605. {ECO:0000259|Pfam:PF01385}. FT DOMAIN 300 366 OrfB_Zn_ribbon. FT {ECO:0000259|Pfam:PF07282}. SQ SEQUENCE 402 AA; 46062 MW; 0A867EB69AC4E68D CRC64; MPRRVIRTYK LAIPGHLNQI CEELNRIAAR IYNKTMSLVQ KIHQKKGFWL SWPTADKYIL RWAENIKIHV HSKQAFVQLY FQALKGYFKA AKKNQDAKPP YKKKRYLPFI WKESAVKLLS DGTLRLSLGK EREPFVVQTP LKPPLRIKQA RLVFEDGYYL HLAIEVEIEE KSANSGVMAV DLGVLRPITC FDGKEVISYH GGVLSSVLRY RNKRLASLQS AIAECKKGSR RYNKLVRAKK RVLRRLKNQI NDIMHKITSS FIGLCLRKQI GTIVIGDVTG IRERADYSDN ANQKIHQWQF RKLIEMIRYK AEQFGIEVKL ISEANTSKTC PVCGAKNKPN GRRYHCKTCG FEYHRDGVGA INIWKRYPGT GQVVAGLAPV RGVRFHPHLC GHGASLAPWK VA // ID Q9X0V4_THEMA Unreviewed; 669 AA. AC Q9X0V4; G4FEB9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE SubName: Full=Endo-1,4-beta-mannosidase {ECO:0000313|EMBL:AAD36302.1}; GN OrderedLocusNames=TM_1227 {ECO:0000313|EMBL:AAD36302.1}; GN ORFNames=Tmari_1234 {ECO:0000313|EMBL:AGL50158.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36302.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36302.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36302.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50158.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50158.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) CC family. {ECO:0000256|RuleBase:RU361153}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36302.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50158.1; -; Genomic_DNA. DR PIR; D72278; D72278. DR RefSeq; NP_229032.1; NC_000853.1. DR RefSeq; WP_004080058.1; NZ_CP011107.1. DR SMR; Q9X0V4; 496-669. DR STRING; 243274.TM1227; -. DR CAZy; CBM27; Carbohydrate-Binding Module Family 27. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR EnsemblBacteria; AAD36302; AAD36302; TM_1227. DR EnsemblBacteria; AGL50158; AGL50158; Tmari_1234. DR GeneID; 898257; -. DR KEGG; tma:TM1227; -. DR KEGG; tmi:THEMA_08195; -. DR KEGG; tmm:Tmari_1234; -. DR KEGG; tmw:THMA_1253; -. DR PATRIC; 23937396; VBITheMar51294_1245. DR eggNOG; ENOG41081JG; Bacteria. DR eggNOG; COG3934; LUCA. DR KO; K19355; -. DR OMA; CEILEYD; -. DR OrthoDB; EOG6VHZBC; -. DR BioCyc; TMAR243274:GC6P-1257-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IBA:GO_Central. DR GO; GO:0046355; P:mannan catabolic process; IBA:GO_Central. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR015295; Carb-bd_module_27. DR InterPro; IPR008979; Galactose-bd-like. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF09212; CBM27; 1. DR Pfam; PF00150; Cellulase; 1. DR SUPFAM; SSF49785; SSF49785; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361153}; KW Hydrolase {ECO:0000256|RuleBase:RU361153}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 34 351 Cellulase. {ECO:0000259|Pfam:PF00150}. FT DOMAIN 497 665 CBM27. {ECO:0000259|Pfam:PF09212}. SQ SEQUENCE 669 AA; 76932 MW; 5659B727305688F5 CRC64; MRRFMFILLI VELSFVLFAS DEFVKVENGK FALNGKEFRF IGSNNYYMHY KSNRMIDSVL ESARDMGIKV LRIWGFLDGE SYCRDKNTYM HPEPGVFGVP EGISNAQSGF ERLDYTVAKA KELGIKLVIV LVNNWDDFGG MNQYVRWFGG THHDDFYRDE KIKEEYKKYV SFLVNHVNTY TGVPYREEPT IMAWELANEP RCETDKSGNT LVEWVKEMSS YIKSLDPNHL VAVGDEGFFS NYEGFKPYGG EAEWAYNGWS GVDWKKLLSI ETVDFGTFHL YPSHWGVSPE NYAQWGAKWI EDHIKIAKEI GKPVVLEEYG IPKSAPVNRT AIYRLWNDLV YDLGGDGAMF WMLAGIGEGS DRDERGYYPD YDGFRIVNDD SPEAELIREY AKLFNTGEDI REDTCSFILP KDGMEIKKTV EVRAGVFDYS NTFEKLSVKV EDLVFENEIE HLGYGIYGFD LDTTRIPDGE HEMFLEGHFQ GKTVKDSIKA KVVNEARYVL AEEVDFSSPE EVKNWWNSGT WQAEFGSPDI EWNGEVGNGA LQLNVKLPGK SDWEEVRVAR KFERLSECEI LEYDIYIPNV EGLKGRLRPY AVLNPGWVKI GLDMNNANVE SAEIITFGGK EYRRFHVRIE FDRTAGVKEL HIGVVGDHLR YDGPIFIDNV RLYKRTGGM // ID Q9WZK8_THEMA Unreviewed; 148 AA. AC Q9WZK8; G4FD74; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35830.1}; GN OrderedLocusNames=TM_0749 {ECO:0000313|EMBL:AAD35830.1}; GN ORFNames=Tmari_0750 {ECO:0000313|EMBL:AGL49675.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35830.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35830.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35830.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49675.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49675.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35830.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49675.1; -; Genomic_DNA. DR PIR; H72340; H72340. DR RefSeq; NP_228558.1; NC_000853.1. DR RefSeq; WP_004080964.1; NZ_CP011107.1. DR STRING; 243274.TM0749; -. DR EnsemblBacteria; AAD35830; AAD35830; TM_0749. DR EnsemblBacteria; AGL49675; AGL49675; Tmari_0750. DR GeneID; 898416; -. DR KEGG; tma:TM0749; -. DR KEGG; tmi:THEMA_00910; -. DR KEGG; tmm:Tmari_0750; -. DR KEGG; tmw:THMA_0767; -. DR PATRIC; 23936418; VBITheMar51294_0762. DR eggNOG; ENOG4107BF6; Bacteria. DR eggNOG; ENOG410Z886; LUCA. DR OMA; LNAYYFV; -. DR OrthoDB; EOG6WMJ09; -. DR BioCyc; TMAR243274:GC6P-775-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR InterPro; IPR019606; GerMN. DR Pfam; PF10646; Germane; 1. DR SMART; SM00909; Germane; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 44 128 Germane. {ECO:0000259|SMART:SM00909}. SQ SEQUENCE 148 AA; 17304 MW; 0FED5545F973F492 CRC64; MRKSVFVLVF LMASVLFSVE LKICYLNEDL LPIVKVTEGR DNPVLEIFEA LSSPPEGLKT FVPEGVLRAY FFVGDYLILD FYGEKLKGMN FDSERYFLHQ VLYTTFLNVK GVNNVYIIID GKKRDVLAKH VDIRFSFPRE VWEKWPIR // ID Q9WZ51_THEMA Unreviewed; 486 AA. AC Q9WZ51; G4FDN8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 105. DE SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:AGL49505.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35667.1}; GN OrderedLocusNames=TM_0582 {ECO:0000313|EMBL:AAD35667.1}; GN ORFNames=Tmari_0580 {ECO:0000313|EMBL:AGL49505.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35667.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35667.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35667.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49505.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49505.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35667.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49505.1; -; Genomic_DNA. DR PIR; G72358; G72358. DR RefSeq; NP_228392.1; NC_000853.1. DR RefSeq; WP_004081275.1; NZ_CP011107.1. DR STRING; 243274.TM0582; -. DR EnsemblBacteria; AAD35667; AAD35667; TM_0582. DR EnsemblBacteria; AGL49505; AGL49505; Tmari_0580. DR GeneID; 897652; -. DR KEGG; tma:TM0582; -. DR KEGG; tmi:THEMA_01755; -. DR KEGG; tmm:Tmari_0580; -. DR KEGG; tmw:THMA_0597; -. DR PATRIC; 23936075; VBITheMar51294_0591. DR eggNOG; ENOG4108PVV; Bacteria. DR eggNOG; COG1032; LUCA. DR OMA; AHAGKEE; -. DR OrthoDB; EOG683S6D; -. DR BioCyc; TMAR243274:GC6P-607-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 222 428 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 486 AA; 56549 MW; AA89FEC9427C036A CRC64; MRRPRRPQDF LEYEKVLKFK ESEKQIEETE TKGDVRVALV VPSGYEVAAS GLAFHYVQKL LNSHPRIRCE RFFYDETFKK FYSLETQTPI DEFPIWLFSV SFENDFSNLL DILKKKDVPL SWKEREDYHP LIIIGGAVTY LNEEFLIPVA DAVYYGELEK YLDLFTEALT GETKQEILSS LSRIPSVEVP SLKEHSEIAT GVDLNDFLPH SSVVPSRGVF PGKLLVEVGR GCIRRCAFCI FGKNLKPARF VKPERFEELV KNTPYSEYGL ISATITDYPW LEDLLDTVEK YQLKISVSSL RLDRLSERLL RTLKDSGQRS FTIAPEAGSQ RIRDILKKDI TDEQIENALK LARKLDFDRV KMYFIYGLEE ETEEDLEAFK KLGDLAVRLG YREVHMSFNP LIPKPGTEFE RRKMEPVDVL RKKEKILKNL LKGFRVDFES IRESVVQYTI AHAGKEEVES WLKFFEKSDK KLLGKLIYEE GRKRLC // ID Q9X1B0_THEMA Unreviewed; 335 AA. AC Q9X1B0; G4FFC6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Integral membrane protein {ECO:0000313|EMBL:AGL50321.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36461.1}; GN OrderedLocusNames=TM_1390 {ECO:0000313|EMBL:AAD36461.1}; GN ORFNames=Tmari_1397 {ECO:0000313|EMBL:AGL50321.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36461.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36461.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36461.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50321.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50321.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36461.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50321.1; -; Genomic_DNA. DR PIR; G72258; G72258. DR RefSeq; NP_229191.1; NC_000853.1. DR RefSeq; WP_004081596.1; NZ_CP011107.1. DR STRING; 243274.TM1390; -. DR EnsemblBacteria; AAD36461; AAD36461; TM_1390. DR EnsemblBacteria; AGL50321; AGL50321; Tmari_1397. DR GeneID; 898086; -. DR KEGG; tma:TM1390; -. DR KEGG; tmi:THEMA_07365; -. DR KEGG; tmm:Tmari_1397; -. DR KEGG; tmw:THMA_1419; -. DR PATRIC; 23937726; VBITheMar51294_1402. DR eggNOG; ENOG4108AEA; Bacteria. DR eggNOG; COG0392; LUCA. DR KO; K07027; -. DR OMA; SAEHFIY; -. DR OrthoDB; EOG6DZDXF; -. DR BioCyc; TMAR243274:GC6P-1427-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR022791; L-PG_synthase/AglD. DR Pfam; PF03706; LPG_synthase_TM; 1. DR TIGRFAMs; TIGR00374; TIGR00374; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 112 135 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 147 167 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 222 243 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 310 326 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 335 AA; 37557 MW; A8AB9C23E68BBE2E CRC64; MKRNLLLALI IGLGATALIV SFWGSGDAWK ELKNVEPIFL MVLSLNFLGI VLVDASRTKI LLKDVPFGTC VANSLWGFYV GAITPFAAGG QPFQIYHLTK AGIPFEKSAS AVAVRFFSSF SFSIISGFAF FMVYLDTFEE LGILGDLFFA GIVLAFLFYV FIILLSFSKG FLRRFFMSRP VLKIFMFFSR KSEYDMKRLV EERILGYVSA TREFWRASKL KFLAVVILSG LMVVLIHSST YFAMKAVNLN VNVSLFQVVS IQLALSLIVY FAPTPGASGA TELAYYVVYS NIIEKTDAMV SMLVWRFFNY YLFIILGILL GLGRLTKKPE ERSSG // ID Q9X1H0_THEMA Unreviewed; 114 AA. AC Q9X1H0; G4FFJ4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36527.1}; GN OrderedLocusNames=TM_1459 {ECO:0000313|EMBL:AAD36527.1}; GN ORFNames=Tmari_1465 {ECO:0000313|EMBL:AGL50389.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36527.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36527.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36527.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50389.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50389.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36527.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50389.1; -; Genomic_DNA. DR PIR; D72251; D72251. DR RefSeq; NP_229258.1; NC_000853.1. DR RefSeq; WP_004081748.1; NZ_CP011107.1. DR PDB; 1VJ2; X-ray; 1.65 A; A/B=1-114. DR PDBsum; 1VJ2; -. DR STRING; 243274.TM1459; -. DR EnsemblBacteria; AAD36527; AAD36527; TM_1459. DR EnsemblBacteria; AGL50389; AGL50389; Tmari_1465. DR GeneID; 898018; -. DR KEGG; tma:TM1459; -. DR KEGG; tmi:THEMA_07020; -. DR KEGG; tmm:Tmari_1465; -. DR KEGG; tmw:THMA_1489; -. DR PATRIC; 23937870; VBITheMar51294_1473. DR eggNOG; ENOG4105N83; Bacteria. DR eggNOG; COG1917; LUCA. DR OMA; AGTVHWY; -. DR OrthoDB; EOG64BQ6J; -. DR BioCyc; TMAR243274:GC6P-1497-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR013096; Cupin_2. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF07883; Cupin_2; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VJ2}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Manganese {ECO:0000213|PDB:1VJ2}; KW Metal-binding {ECO:0000213|PDB:1VJ2}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 40 107 Cupin_2. {ECO:0000259|Pfam:PF07883}. FT METAL 52 52 Manganese; via tele nitrogen. FT {ECO:0000213|PDB:1VJ2}. FT METAL 54 54 Manganese; via tele nitrogen. FT {ECO:0000213|PDB:1VJ2}. FT METAL 58 58 Manganese; via tele nitrogen. FT {ECO:0000213|PDB:1VJ2}. FT METAL 92 92 Manganese; via tele nitrogen. FT {ECO:0000213|PDB:1VJ2}. SQ SEQUENCE 114 AA; 13109 MW; E1556D9CB2119D15 CRC64; MILKRAYDVT PQKISTDKVR GVRKRVLIGL KDAPNFVMRL FTVEPGGLID RHSHPWEHEI FVLKGKLTVL KEQGEETVEE GFYIFVEPNE IHGFRNDTDS EVEFLCLIPK EGGE // ID Q9X0Z7_THEMA Unreviewed; 379 AA. AC Q9X0Z7; G4FE78; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 87. DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AAD36345.1}; DE EC=2.5.1.48 {ECO:0000313|EMBL:AGL50199.1}; GN OrderedLocusNames=TM_1270 {ECO:0000313|EMBL:AAD36345.1}; GN ORFNames=Tmari_1275 {ECO:0000313|EMBL:AGL50199.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36345.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36345.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36345.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50199.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50199.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU362118}; CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. CC {ECO:0000256|RuleBase:RU362118}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36345.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50199.1; -; Genomic_DNA. DR PIR; E72274; E72274. DR RefSeq; NP_229075.1; NC_000853.1. DR RefSeq; WP_004079973.1; NZ_CP011107.1. DR STRING; 243274.TM1270; -. DR EnsemblBacteria; AAD36345; AAD36345; TM_1270. DR EnsemblBacteria; AGL50199; AGL50199; Tmari_1275. DR GeneID; 898213; -. DR KEGG; tma:TM1270; -. DR KEGG; tmi:THEMA_07985; -. DR KEGG; tmm:Tmari_1275; -. DR KEGG; tmw:THMA_1295; -. DR PATRIC; 23937480; VBITheMar51294_1286. DR eggNOG; ENOG4105C28; Bacteria. DR eggNOG; COG0626; LUCA. DR KO; K01739; -. DR OMA; TICDNSY; -. DR OrthoDB; EOG67DPN3; -. DR BioCyc; TMAR243274:GC6P-1301-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11808; PTHR11808; 1. DR Pfam; PF01053; Cys_Met_Meta_PP; 1. DR PIRSF; PIRSF001434; CGS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00868; CYS_MET_METAB_PP; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2, KW ECO:0000256|RuleBase:RU362118}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AGL50199.1}. FT MOD_RES 202 202 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR001434-2}. SQ SEQUENCE 379 AA; 42753 MW; E522AACAC3DDBD7A CRC64; MNTDDILFSY GEEDIPLKAL SFPIFETTNF YFDSFDEMSK ALRNGDYEFV YKRGSNPTTR LVEKKLAALE ECEDARLVAS GMSAISLSIL HFLSSGDHVV CVDEAYSWAK KFFNYLSKKF DIEVSYVPPD AERIVEAITK KTKLIYLESP TSMRMKVIDI RKVTEAAGEL KIKTVIDNTW ASPIFQKPKL LGVDVVVHSA TKYISGHGDV MAGVIAGDVE DMKNIFVDEY KNIGPVLSPI EAWLILRGLR TLELRMKKHY ENALVVSDFL MDHPKVLEVN YPMNPRSPQY ELASSQMSGG SGLMSFRLKT DSAEKVKEFV ESLRVFRMAV SWGSHENLVV PRVAYGDCPK KDVNLIRIHV GLGDPEKLVE DLDQALKKI // ID Q9WZ37_THEMA Unreviewed; 137 AA. AC Q9WZ37; G4FDQ3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Rrf2 family transcriptional regulator {ECO:0000313|EMBL:AGL49490.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35652.1}; GN OrderedLocusNames=TM_0567 {ECO:0000313|EMBL:AAD35652.1}; GN ORFNames=Tmari_0565 {ECO:0000313|EMBL:AGL49490.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35652.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35652.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD35652.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL49490.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL49490.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35652.1; -; Genomic_DNA. DR EMBL; CP004077; AGL49490.1; -; Genomic_DNA. DR PIR; F72361; F72361. DR RefSeq; NP_228377.1; NC_000853.1. DR RefSeq; WP_004081299.1; NZ_CP011107.1. DR STRING; 243274.TM0567; -. DR EnsemblBacteria; AAD35652; AAD35652; TM_0567. DR EnsemblBacteria; AGL49490; AGL49490; Tmari_0565. DR GeneID; 897631; -. DR KEGG; tma:TM0567; -. DR KEGG; tmi:THEMA_01835; -. DR KEGG; tmm:Tmari_0565; -. DR KEGG; tmw:THMA_0581; -. DR PATRIC; 23936043; VBITheMar51294_0576. DR eggNOG; ENOG4108ZF1; Bacteria. DR eggNOG; COG1959; LUCA. DR OMA; DIATGNN; -. DR OrthoDB; EOG6Q5NXK; -. DR BioCyc; TMAR243274:GC6P-591-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR030489; TR_Rrf2-type_CS. DR InterPro; IPR000944; Tscrpt_reg_Rrf2-type. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02082; Rrf2; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR TIGRFAMs; TIGR00738; rrf2_super; 1. DR PROSITE; PS01332; HTH_RRF2_1; 1. DR PROSITE; PS51197; HTH_RRF2_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 137 AA; 15986 MW; 58BB7E8B39F5B797 CRC64; MFTMRSEYAL RLMIVMAKEY GNYLSMTEIL EKAKQSVPRE FAEKILYTLK KAGLVKTRRG KSGGYMLSRP PKEIKVSEIV FLLDRKSKVF FDMPGCPDEL DCVIRALWKR VENEIEKILS GVTLEDLVRE QEEKMKQ // ID Q9X116_THEMA Unreviewed; 116 AA. AC Q9X116; G4FE59; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Glycine-rich cell wall structural protein {ECO:0000313|EMBL:AGL50222.1}; DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36364.1}; GN OrderedLocusNames=TM_1290 {ECO:0000313|EMBL:AAD36364.1}; GN ORFNames=Tmari_1298 {ECO:0000313|EMBL:AGL50222.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36364.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36364.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}, and RC MSB8 {ECO:0000313|EMBL:AAD36364.1}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000313|EMBL:AGL50222.1, ECO:0000313|Proteomes:UP000013901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000013901}, and RC MSB8 {ECO:0000313|EMBL:AGL50222.1}; RX PubMed=23637642; RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H., RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y., RA Zengler K.; RT "The genome organization of Thermotoga maritima reflects its RT lifestyle."; RL PLoS Genet. 9:E1003485-E1003485(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36364.1; -; Genomic_DNA. DR EMBL; CP004077; AGL50222.1; -; Genomic_DNA. DR PIR; A72272; A72272. DR RefSeq; NP_229094.1; NC_000853.1. DR RefSeq; WP_004079939.1; NZ_CP011107.1. DR PDB; 1RDU; NMR; -; A=1-116. DR PDBsum; 1RDU; -. DR STRING; 243274.TM1290; -. DR EnsemblBacteria; AAD36364; AAD36364; TM_1290. DR EnsemblBacteria; AGL50222; AGL50222; Tmari_1298. DR GeneID; 898193; -. DR KEGG; tma:TM1290; -. DR KEGG; tmi:THEMA_07885; -. DR KEGG; tmm:Tmari_1298; -. DR KEGG; tmw:THMA_1316; -. DR PATRIC; 23937520; VBITheMar51294_1306. DR eggNOG; ENOG4105XWZ; Bacteria. DR eggNOG; COG1433; LUCA. DR OMA; TPRCGEN; -. DR OrthoDB; EOG6FBX0Q; -. DR BioCyc; TMAR243274:GC6P-1321-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Proteomes; UP000013901; Chromosome. DR Gene3D; 3.30.420.130; -; 1. DR InterPro; IPR003731; Di-Nase_FeMo-co_biosynth. DR Pfam; PF02579; Nitro_FeMo-Co; 1. DR SUPFAM; SSF53146; SSF53146; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1RDU}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 14 102 Nitro_FeMo-Co. FT {ECO:0000259|Pfam:PF02579}. SQ SEQUENCE 116 AA; 12538 MW; 855B73AD89A8F491 CRC64; MARVAIPSVG KDLSSMVSDR FARAEYFIIY DTESGNVEVV ENTIADAHGT GPKVVQSLVS KGVEYLIASN VGRNAFETLK AAGVKVYRFE GGTVQEAIDA FSEGRLEELT TFTREG // ID Q9X0U7_THEMA Unreviewed; 326 AA. AC Q9X0U7; G4FEC6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 118. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36295.1}; GN OrderedLocusNames=TM_1220 {ECO:0000313|EMBL:AAD36295.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36295.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36295.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36295.1; -; Genomic_DNA. DR PIR; B72282; B72282. DR RefSeq; NP_229025.1; NC_000853.1. DR RefSeq; WP_004080073.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0U7; -. DR STRING; 243274.TM1220; -. DR TCDB; 3.A.1.5.14; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36295; AAD36295; TM_1220. DR GeneID; 898264; -. DR KEGG; tma:TM1220; -. DR KEGG; tmw:THMA_1246; -. DR PATRIC; 23937382; VBITheMar51294_1238. DR eggNOG; ENOG41060CX; Bacteria. DR eggNOG; ENOG410Y04P; LUCA. DR InParanoid; Q9X0U7; -. DR KO; K02031; -. DR OMA; HATERCK; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1250-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36295.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36295.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 11 256 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 326 AA; 36686 MW; 97209CA573881F26 CRC64; MIGVAEVVLD VRDLRIYYRT LYGYVKAVDG VSFDIKRGEI LGIAGESGCG KSTLGNGLIL LKPPMKYMGG EAILDGKNIM ALSPKELRKV RYEKISIIPQ YAMDAMNPTK KIKQIIDDLL HEHGESFERK KDVIEERLEI VNLGKKVLNM YPIELSGGMK QRMVMVISTL MNPDVLIADE ITSALDVSSQ RSVIQMLYEM REKEIMGSLA FITHDLSVLY QIADKVMVLY AGRVAEISPM EDIIQEPLHP YTKMLLSSLP KIGVRYSQTK LKGIPGYPPS LLNIGPGCRF RDRCPYAFEK CEQDPPVFDV DGRKVSCWLF ERGDAN // ID Q9WYU6_THEMA Unreviewed; 214 AA. AC Q9WYU6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 75. DE SubName: Full=Pyrazinamidase/nicotinamidase-related protein {ECO:0000313|EMBL:AAD35560.1}; GN OrderedLocusNames=TM_0475 {ECO:0000313|EMBL:AAD35560.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35560.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35560.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35560.1; -; Genomic_DNA. DR PIR; C72372; C72372. DR RefSeq; NP_228285.1; NC_000853.1. DR RefSeq; WP_010865129.1; NC_000853.1. DR ProteinModelPortal; Q9WYU6; -. DR STRING; 243274.TM0475; -. DR DNASU; 897507; -. DR EnsemblBacteria; AAD35560; AAD35560; TM_0475. DR GeneID; 897507; -. DR KEGG; tma:TM0475; -. DR PATRIC; 23935847; VBITheMar51294_0482. DR eggNOG; ENOG4108RWI; Bacteria. DR eggNOG; COG1335; LUCA. DR InParanoid; Q9WYU6; -. DR KO; K08281; -. DR OMA; GHTGDKF; -. DR OrthoDB; EOG6NWBV7; -. DR BioCyc; TMAR243274:GC6P-495-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.50.850; -; 1. DR InterPro; IPR000868; Isochorismatase-like. DR Pfam; PF00857; Isochorismatase; 1. DR SUPFAM; SSF52499; SSF52499; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 43 209 Isochorismatase. FT {ECO:0000259|Pfam:PF00857}. SQ SEQUENCE 214 AA; 24695 MW; 25AED11B210CE90A CRC64; MSELAKEPVL KTGGPEGPCG FESHRLRQPR TGLFFLGGEN VRALLVVDLQ RDFVDEGGAL YFEGAEKVIN PILKWVEEFK KENLPIITTQ DWHDPEDREF NIWPKHCVAN TDGARLTEKL EKALKDYPNH FSVKKNRYSA FYNTNLEKII RDNEIDEIYV CGVVTHICVL FTVEELRNRD IPVKIITEGV ASYDEELHRF ALREMKEILG AEFI // ID Q9X293_THEMA Unreviewed; 497 AA. AC Q9X293; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36835.1}; GN OrderedLocusNames=TM_1772 {ECO:0000313|EMBL:AAD36835.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36835.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36835.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36835.1; -; Genomic_DNA. DR PIR; C72213; C72213. DR RefSeq; NP_229569.1; NC_000853.1. DR RefSeq; WP_010865399.1; NC_000853.1. DR ProteinModelPortal; Q9X293; -. DR STRING; 243274.TM1772; -. DR EnsemblBacteria; AAD36835; AAD36835; TM_1772. DR GeneID; 897850; -. DR KEGG; tma:TM1772; -. DR PATRIC; 23938526; VBITheMar51294_1792. DR eggNOG; ENOG4105DP4; Bacteria. DR eggNOG; COG1461; LUCA. DR InParanoid; Q9X293; -. DR KO; K07030; -. DR OMA; KVKIDNM; -. DR OrthoDB; EOG60PHBN; -. DR BioCyc; TMAR243274:GC6P-1821-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro. DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro. DR InterPro; IPR019986; DAK2_dom-cont_prot_YloV. DR InterPro; IPR004007; DhaL_dom. DR InterPro; IPR033470; UPF_DhaK. DR Pfam; PF13684; Dak1_2; 1. DR Pfam; PF02734; Dak2; 1. DR SMART; SM01121; Dak1_2; 1. DR SMART; SM01120; Dak2; 1. DR SUPFAM; SSF101473; SSF101473; 1. DR TIGRFAMs; TIGR03599; YloV; 1. DR PROSITE; PS51480; DHAL; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 165 DhaL. {ECO:0000259|PROSITE:PS51480}. SQ SEQUENCE 497 AA; 55866 MW; 6AD1E22229C25D43 CRC64; MFPVPDGDTG SNMCSTMLEA CKYIDNVKSD DLIEVWKAVK EGALMGARGN SGVILSQILR GMADASPREY ITPADFVKMI SNARKVAYSA VMRPVEGTML TVVRVLDERL QGKNFETFEE LFDWIVEIAR DTVNRTPHML QKLREAGVVD AGAKGLYYIF EGMRDAVKGN IQVNLEEVEQ ASVEELQRMA FEEITNRYCT EVAVRRNQVV EKSELEAFLN EIGDSVVLVE QDDLIKLHVH TNHPGQVLEK VIEFGEIVKV KIDNMKLQHE HVISTQPTKE IGVVAVSPGK GISDILKSLG VDVIVPGGQT MNPSFADLKA AVEQTHAKNV FLFPNNANVL LTAKQIAEAF DDRRVIVVPT SFVQECVAAM VEYDPDAEPE DLLKRFEEAI SQCVPISVTR AVRDSRYGNR RIRKGEYLLF VRKELVSHGF SLVKVLKEAL EKENAHEKEI LTVFLGDNYR KPELEKIQKL IGEEFPNLDL EIYEGGQPHY PYLMLLQ // ID Q9X1N9_THEMA Unreviewed; 352 AA. AC Q9X1N9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=FAD:protein FMN transferase {ECO:0000256|RuleBase:RU363002}; DE EC=2.7.1.180 {ECO:0000256|RuleBase:RU363002}; GN OrderedLocusNames=TM_1553 {ECO:0000313|EMBL:AAD36619.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36619.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36619.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1VRM} RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 40-352. RX PubMed=16779835; DOI=10.1002/prot.20950; RA Han G.W., Sri Krishna S., Schwarzenbacher R., McMullan D., RA Ginalski K., Elsliger M.A., Brittain S.M., Abdubek P., Agarwalla S., RA Ambing E., Astakhova T., Axelrod H., Canaves J.M., Chiu H.J., RA DiDonato M., Grzechnik S.K., Hale J., Hampton E., Haugen J., RA Jaroszewski L., Jin K.K., Klock H.E., Knuth M.W., Koesema E., RA Kreusch A., Kuhn P., Miller M.D., Morse A.T., Moy K., Nigoghossian E., RA Oommachen S., Ouyang J., Paulsen J., Quijano K., Reyes R., Rife C., RA Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., Wang X., RA West B., White A., Wolf G., Xu Q., Hodgson K.O., Wooley J., RA Deacon A.M., Godzik A., Lesley S.A., Wilson I.A.; RT "Crystal structure of the ApbE protein (TM1553) from Thermotoga RT maritima at 1.58 A resolution."; RL Proteins 64:1083-1090(2006). CC -!- FUNCTION: Flavin transferase that catalyzes the transfer of the CC FMN moiety of FAD and its covalent binding to the hydroxyl group CC of a threonine residue in a target flavoprotein. CC {ECO:0000256|RuleBase:RU363002}. CC -!- CATALYTIC ACTIVITY: FAD + [protein]-L-threonine = [protein]-FMN-L- CC threonine + AMP. {ECO:0000256|RuleBase:RU363002}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR006268-2}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR006268-2}; CC Note=Magnesium. Can also use manganese. CC {ECO:0000256|PIRSR:PIRSR006268-2}; CC -!- SIMILARITY: Belongs to the ApbE family. CC {ECO:0000256|RuleBase:RU363002}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36619.1; -; Genomic_DNA. DR PIR; D72239; D72239. DR RefSeq; NP_229353.1; NC_000853.1. DR RefSeq; WP_010865358.1; NC_000853.1. DR PDB; 1VRM; X-ray; 1.58 A; A=40-352. DR PDBsum; 1VRM; -. DR ProteinModelPortal; Q9X1N9; -. DR SMR; Q9X1N9; 44-352. DR STRING; 243274.TM1553; -. DR EnsemblBacteria; AAD36619; AAD36619; TM_1553. DR GeneID; 897605; -. DR KEGG; tma:TM1553; -. DR PATRIC; 23938068; VBITheMar51294_1571. DR eggNOG; ENOG4105CJ2; Bacteria. DR eggNOG; COG1477; LUCA. DR InParanoid; Q9X1N9; -. DR KO; K03734; -. DR OMA; YIYLKSG; -. DR OrthoDB; EOG6CGCF7; -. DR BioCyc; TMAR243274:GC6P-1594-MONOMER; -. DR EvolutionaryTrace; Q9X1N9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0017013; P:protein flavinylation; IEA:InterPro. DR InterPro; IPR024932; ApbE. DR InterPro; IPR003374; ApbE-like. DR PANTHER; PTHR30040:SF2; PTHR30040:SF2; 1. DR Pfam; PF02424; ApbE; 1. DR PIRSF; PIRSF006268; ApbE; 1. DR SUPFAM; SSF143631; SSF143631; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VRM}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW FAD {ECO:0000256|RuleBase:RU363002}; KW Flavoprotein {ECO:0000256|RuleBase:RU363002}; KW Magnesium {ECO:0000256|PIRSR:PIRSR006268-2, KW ECO:0000256|RuleBase:RU363002}; Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR006268-2, KW ECO:0000256|RuleBase:RU363002}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU363002}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 39 Helical. {ECO:0000256|SAM:Phobius}. FT METAL 191 191 Magnesium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR006268-2}. FT METAL 303 303 Magnesium. FT {ECO:0000256|PIRSR:PIRSR006268-2}. FT METAL 307 307 Magnesium. FT {ECO:0000256|PIRSR:PIRSR006268-2}. SQ SEQUENCE 352 AA; 39542 MW; 5A6DEE3F4653A0A6 CRC64; MHKMWPSDSN DHRVTRRNVI IFSSLLLGSL AILLALLLIR TKDQYYELRD FALGTSVRIV VSSQKINPRT IAEAILEDMK RITYKFSFTD ERSVVKKIND HPNEWVEVDE ETYSLIKAAC AFAELTDGAF DPTVGRLLEL WGFTGNYENL RVPSREEIEE ALKHTGYKNV LFDDKNMRVM VKNGVKIDLG GIAKGYALDR ARQIALSFDE NATGFVEAGG DVRIIGPKFG KYPWVIGVKD PRGDDVIDYI YLKSGAVATS GDYERYFVVD GVRYHHILDP STGYPARGVW SVTIIAEDAT TADALSTAGF VMAGKDWRKV VLDFPNMGAH LLIVLEGGAI ERSETFKLFE RE // ID Q9X281_THEMA Unreviewed; 356 AA. AC Q9X281; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=2-oxoisovalerate oxidoreductase, beta subunit, putative {ECO:0000313|EMBL:AAD36824.1}; GN OrderedLocusNames=TM_1759 {ECO:0000313|EMBL:AAD36824.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36824.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36824.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36824.1; -; Genomic_DNA. DR PIR; H72214; H72214. DR RefSeq; NP_229557.1; NC_000853.1. DR RefSeq; WP_010865396.1; NC_000853.1. DR ProteinModelPortal; Q9X281; -. DR STRING; 243274.TM1759; -. DR EnsemblBacteria; AAD36824; AAD36824; TM_1759. DR GeneID; 897859; -. DR KEGG; tma:TM1759; -. DR PATRIC; 23938494; VBITheMar51294_1777. DR eggNOG; ENOG4105DI2; Bacteria. DR eggNOG; COG0674; LUCA. DR InParanoid; Q9X281; -. DR KO; K00174; -. DR OMA; YLQATKG; -. DR OrthoDB; EOG6GTZJW; -. DR BioCyc; TMAR243274:GC6P-1807-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR033412; PFOR_II. DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR Pfam; PF17147; PFOR_II; 1. DR Pfam; PF01855; POR_N; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR SUPFAM; SSF52922; SSF52922; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 18 195 POR_N. {ECO:0000259|Pfam:PF01855}. SQ SEQUENCE 356 AA; 39743 MW; 4B72E1117E29A15E CRC64; MVLMKKLMMK GNEAIAESAI RAGCRLYFAY PITPQSEIAE YMARRLPEVG GVFLQTESEI ATVNMVYGAA CTGKRVMTST SSPGFSLMQE GISYIAGAEL PCVFVDVVRG GPGLGNIQPS QGDYFQAVKG GGHGDYRLIV LAPSTLQEAV DLTQLAFDLA DRYRNPVLIL ADGMIGQMME PVELPEMRDL STLPDHSDWA LRGARNREPH RIAAFNIDPV GLEKMNKRLQ EKYRLIEASE QRWEEYRVDG AEYLMVGYGT MGRILKSVVD SLREEGIPAG LFRPVTLWPF PKRRLKELAK KVQLIFVVEM SSGQMVEDVQ ISVEGKVPVH FYGRMGGVVP TPEEILFAFK EVRKWK // ID Q9WZS5_THEMA Unreviewed; 274 AA. AC Q9WZS5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Lipopolysaccharide biosynthesis protein, putative {ECO:0000313|EMBL:AAD35900.1}; GN OrderedLocusNames=TM_0818 {ECO:0000313|EMBL:AAD35900.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35900.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35900.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the glycosyltransferase 26 family. CC {ECO:0000256|SAAS:SAAS00571257}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35900.1; -; Genomic_DNA. DR PIR; E72329; E72329. DR RefSeq; NP_228627.1; NC_000853.1. DR RefSeq; WP_010865210.1; NC_000853.1. DR STRING; 243274.TM0818; -. DR CAZy; GT26; Glycosyltransferase Family 26. DR EnsemblBacteria; AAD35900; AAD35900; TM_0818. DR GeneID; 898487; -. DR KEGG; tma:TM0818; -. DR PATRIC; 23936558; VBITheMar51294_0830. DR eggNOG; ENOG4108UHC; Bacteria. DR eggNOG; COG1922; LUCA. DR InParanoid; Q9WZS5; -. DR KO; K05946; -. DR OMA; ATPNAEI; -. DR OrthoDB; EOG6C8N17; -. DR BioCyc; TMAR243274:GC6P-846-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR InterPro; IPR004629; WecB_TagA_CpsF. DR Pfam; PF03808; Glyco_tran_WecB; 1. DR TIGRFAMs; TIGR00696; wecG_tagA_cpsF; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000256|SAAS:SAAS00461039}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00461039}. SQ SEQUENCE 274 AA; 31350 MW; 2D07440C2371B4F9 CRC64; MWGFPRAGSS PALGTSRKRR SFLRFFLEEN GVKEIELFGT KVLSGTRREF LNAIEERIEK NIKTFVVTMN ASILLKAIED AGYRAIVNSA DLVVPDGFGV VWAMKTLTGE TTERLPGVEI MKHLCERSKE KGWKVYLLGT KREIVEKAKQ VLERSGVRVV GCHDGFFSEK ESPKIVEDVN RSSTDLLFVG MGVPRQEEWI YRNFPQLNVK LAMGVGGSID VVSGKKKRAP EWVQRMNLEW LYRFFQSPLS KRKVPVQVSK FVFFVLREKL KNRN // ID Q9X1U6_THEMA Unreviewed; 273 AA. AC Q9X1U6; G4FFZ9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=ATP synthase gamma chain {ECO:0000256|HAMAP-Rule:MF_00815}; DE AltName: Full=ATP synthase F1 sector gamma subunit {ECO:0000256|HAMAP-Rule:MF_00815}; DE AltName: Full=F-ATPase gamma subunit {ECO:0000256|HAMAP-Rule:MF_00815}; GN Name=atpG {ECO:0000256|HAMAP-Rule:MF_00815}; GN OrderedLocusNames=TM_1611 {ECO:0000313|EMBL:AAD36678.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36678.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36678.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The gamma chain is believed to be CC important in regulating ATPase activity and the flow of protons CC through the CF(0) complex. {ECO:0000256|HAMAP-Rule:MF_00815, CC ECO:0000256|SAAS:SAAS00011807}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. {ECO:0000256|HAMAP- CC Rule:MF_00815, ECO:0000256|SAAS:SAAS00343210}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00815}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00815}. CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. CC {ECO:0000256|HAMAP-Rule:MF_00815, ECO:0000256|SAAS:SAAS00539378}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36678.1; -; Genomic_DNA. DR PIR; E72231; E72231. DR RefSeq; NP_229411.1; NC_000853.1. DR RefSeq; WP_004082062.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1U6; -. DR STRING; 243274.TM1611; -. DR EnsemblBacteria; AAD36678; AAD36678; TM_1611. DR GeneID; 897680; -. DR KEGG; tma:TM1611; -. DR KEGG; tmw:THMA_1651; -. DR PATRIC; 23938196; VBITheMar51294_1630. DR eggNOG; ENOG4105J80; Bacteria. DR eggNOG; COG0224; LUCA. DR InParanoid; Q9X1U6; -. DR KO; K02115; -. DR OMA; DRGMCGG; -. DR OrthoDB; EOG6R5C97; -. DR BioCyc; TMAR243274:GC6P-1657-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00815; ATP_synth_gamma_bact; 1. DR InterPro; IPR000131; ATPase_F1-cplx_gsu. DR InterPro; IPR023632; ATPase_F1_gsu_CS. DR InterPro; IPR023633; ATPase_F1_gsu_dom. DR PANTHER; PTHR11693; PTHR11693; 1. DR Pfam; PF00231; ATP-synt; 1. DR PRINTS; PR00126; ATPASEGAMMA. DR SUPFAM; SSF52943; SSF52943; 1. DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1. DR PROSITE; PS00153; ATPASE_GAMMA; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|HAMAP-Rule:MF_00815, KW ECO:0000256|SAAS:SAAS00421850}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00815}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00815}; KW CF(1) {ECO:0000256|HAMAP-Rule:MF_00815, KW ECO:0000256|SAAS:SAAS00421850}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00815, KW ECO:0000256|SAAS:SAAS00421832}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_00815, KW ECO:0000256|SAAS:SAAS00421832}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00815}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00815, KW ECO:0000256|SAAS:SAAS00421832}. SQ SEQUENCE 273 AA; 31911 MW; 3F7517BB4741AC83 CRC64; MLQIKRKINA TQSLMKITRA MEMVARAKVR KIESEYQKFK PFYDEVKRLW ALVPAESLDP IFFEEGNRDL IVVITSDMGL CGSFNSEILR EAERVISESR DPHLILVGLK AINHFKDGKV LKMYDRFYEI PDFRNGSTIV EDILNFLDGK PARVRVIFSR FKNVLIQRPE VHELLPIKKE EKKREDFEYE PRLEQIAPLI FHYYLSATLM ELMFQTKIGE YYARQNAMKN ATDNAQEVIR ELTLAYNKAR QASITQELIE IVTGAEALKE IEK // ID Q9X0Y6_THEMA Unreviewed; 229 AA. AC Q9X0Y6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 98. DE SubName: Full=Phosphate regulon transcriptional regulatory protein PhoB {ECO:0000313|EMBL:AAD36333.1}; GN OrderedLocusNames=TM_1259 {ECO:0000313|EMBL:AAD36333.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36333.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36333.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains OmpR/PhoB-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00583175}. CC -!- SIMILARITY: Contains response regulatory domain. CC {ECO:0000256|SAAS:SAAS00122778}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36333.1; -; Genomic_DNA. DR PIR; F72275; F72275. DR RefSeq; NP_229064.1; NC_000853.1. DR RefSeq; WP_010865291.1; NC_000853.1. DR ProteinModelPortal; Q9X0Y6; -. DR DIP; DIP-60577N; -. DR STRING; 243274.TM1259; -. DR EnsemblBacteria; AAD36333; AAD36333; TM_1259. DR GeneID; 898224; -. DR KEGG; tma:TM1259; -. DR PATRIC; 23937458; VBITheMar51294_1275. DR eggNOG; ENOG4105EFQ; Bacteria. DR eggNOG; COG0745; LUCA. DR InParanoid; Q9X0Y6; -. DR KO; K02483; -. DR OMA; ASNKNRV; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1290-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF00486; Trans_reg_C; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00862; Trans_reg_C; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS51755; OMPR_PHOB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00582919}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00478953}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00478953}; KW Two-component regulatory system {ECO:0000256|SAAS:SAAS00478431}. FT DOMAIN 7 121 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT DOMAIN 128 221 OmpR/PhoB-type DNA-binding. FT {ECO:0000259|PROSITE:PS51755}. SQ SEQUENCE 229 AA; 26341 MW; 8810B58A65C2E9D4 CRC64; MLRVGVKVLI AEDDEDIRSV LKRYLETEGY ECDEAESLFD LKKKLSEGTY NVLLLDLMFP DGVAMDEIPE MKVSHPEMAI IIISARDRDM DRIFGIELGA DDYVTKPFNP REVLARVKAV LRRMGKEQKV LRFGRLEIFP EDYIVRYDGK NVEMTAKEFE LLKLLATTPN KVFSREEILN RVWGDDYVSD RVVDVHISAI RSKIGKGWIK TVRGLGYKFS TRGDEGDRA // ID Q9WZZ0_THEMA Unreviewed; 173 AA. AC Q9WZZ0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35969.1}; GN OrderedLocusNames=TM_0888 {ECO:0000313|EMBL:AAD35969.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35969.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35969.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35969.1; -; Genomic_DNA. DR PIR; A72321; A72321. DR RefSeq; NP_228696.1; NC_000853.1. DR RefSeq; WP_010865218.1; NC_000853.1. DR ProteinModelPortal; Q9WZZ0; -. DR STRING; 243274.TM0888; -. DR EnsemblBacteria; AAD35969; AAD35969; TM_0888. DR GeneID; 898562; -. DR KEGG; tma:TM0888; -. DR PATRIC; 23936707; VBITheMar51294_0902. DR eggNOG; ENOG4105FJ0; Bacteria. DR eggNOG; COG1564; LUCA. DR InParanoid; Q9WZZ0; -. DR KO; K00949; -. DR OMA; RTEGLYY; -. DR OrthoDB; EOG62NX6M; -. DR BioCyc; TMAR243274:GC6P-918-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0030975; F:thiamine binding; IEA:InterPro. DR GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:InterPro. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro. DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.10240; -; 1. DR InterPro; IPR006282; Thi_PPkinase. DR InterPro; IPR007373; Thiamin_PyroPKinase_B1-bd. DR InterPro; IPR007371; TPK_catalytic. DR Pfam; PF04265; TPK_B1_binding; 1. DR Pfam; PF04263; TPK_catalytic; 1. DR SUPFAM; SSF63999; SSF63999; 1. DR TIGRFAMs; TIGR01378; thi_PPkinase; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 18 113 TPK_catalytic. FT {ECO:0000259|Pfam:PF04263}. FT DOMAIN 141 170 TPK_B1_binding. FT {ECO:0000259|Pfam:PF04265}. SQ SEQUENCE 173 AA; 19446 MW; 271D0745B2411BC4 CRC64; MVCIFANGSY EEFVDVSRCE KIVAVDGGAN YLRTRNIVPD FFIGDADSAK EETMEWLKQH GVTLKIFPKE KDEIDLELAL REFEEEEKVV FGWKGDRLDM VLALFYLLRR FKNTILESPS LTVGYVEGAK TLSAVPGEKW SILPLGGDAE GVTLKGFKYT LEDAVMPITK PTV // ID Q9X234_THEMA Unreviewed; 295 AA. AC Q9X234; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Putative sporulation transcription regulator WhiA {ECO:0000256|SAAS:SAAS00015186}; GN OrderedLocusNames=TM_1708 {ECO:0000313|EMBL:AAD36775.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36775.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36775.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:3HYI, ECO:0000213|PDB:3HYJ} RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS). RX PubMed=19836336; DOI=10.1016/j.str.2009.08.008; RA Kaiser B.K., Clifton M.C., Shen B.W., Stoddard B.L.; RT "The structure of a bacterial DUF199/WhiA protein: domestication of an RT invasive endonuclease."; RL Structure 17:1368-1376(2009). CC -!- FUNCTION: May be required for sporulation. CC {ECO:0000256|SAAS:SAAS00015191}. CC -!- SIMILARITY: Belongs to the WhiA transcriptional regulatory family. CC {ECO:0000256|SAAS:SAAS00545653}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36775.1; -; Genomic_DNA. DR PIR; F72221; F72221. DR RefSeq; NP_229508.1; NC_000853.1. DR RefSeq; WP_010865387.1; NC_000853.1. DR PDB; 3HYI; X-ray; 2.34 A; A=1-295. DR PDB; 3HYJ; X-ray; 2.60 A; A/D=1-198. DR PDBsum; 3HYI; -. DR PDBsum; 3HYJ; -. DR STRING; 243274.TM1708; -. DR EnsemblBacteria; AAD36775; AAD36775; TM_1708. DR GeneID; 897285; -. DR KEGG; tma:TM1708; -. DR KEGG; tmi:THEMA_05700; -. DR PATRIC; 23938390; VBITheMar51294_1725. DR eggNOG; ENOG4105CIE; Bacteria. DR eggNOG; COG1481; LUCA. DR KO; K09762; -. DR OMA; RVQIFIP; -. DR OrthoDB; EOG68WR87; -. DR BioCyc; TMAR243274:GC6P-1756-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.10.28.10; -; 1. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR018478; Sporu_reg_WhiA_N_dom. DR InterPro; IPR023054; Sporulation_regulator_WhiA_C. DR Pfam; PF02650; HTH_WhiA; 1. DR Pfam; PF10298; WhiA_N; 1. DR SUPFAM; SSF55608; SSF55608; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3HYI, ECO:0000213|PDB:3HYJ}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00429667}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00429670}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00429670}. FT DOMAIN 27 88 WhiA_N. {ECO:0000259|Pfam:PF10298}. FT DOMAIN 207 288 HTH_WhiA. {ECO:0000259|Pfam:PF02650}. SQ SEQUENCE 295 AA; 34244 MW; 442A432806A54DC8 CRC64; MVSLLRRTFS EEIKEELVNV PFGSREEVIS ELLGFIKARG DLDVKSRHIV FSLHSFAASR RLLNLMKYLS KPVSEIIVEK SHNIKKRYIK ITAEYSESFM VIEPFFDVAL FVSFLRGLFL SGGSMTNPRY HYHLEINLFE EETLALTRKS LKDFFNINAG IIELRNTRKL YIKSIKDILV FLEAIGVQRK LEEIDRIVTE RKVIGDVNRT VNFIEANAIR TANSTARQIR AIELIKENMG LENLPEDLRR VALVRLRNKE LSLRELGKKL NLTKSQIYSK LKRIIKIAER FGDVK // ID Q9WZ84_THEMA Unreviewed; 360 AA. AC Q9WZ84; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35700.1}; GN OrderedLocusNames=TM_0615 {ECO:0000313|EMBL:AAD35700.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35700.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35700.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35700.1; -; Genomic_DNA. DR PIR; C72356; C72356. DR RefSeq; NP_228425.1; NC_000853.1. DR RefSeq; WP_010865164.1; NC_000853.1. DR ProteinModelPortal; Q9WZ84; -. DR EnsemblBacteria; AAD35700; AAD35700; TM_0615. DR GeneID; 897698; -. DR KEGG; tma:TM0615; -. DR PATRIC; 23936143; VBITheMar51294_0625. DR eggNOG; ENOG4108KNV; Bacteria. DR eggNOG; COG4928; LUCA. DR OMA; CKDWITE; -. DR OrthoDB; EOG6ZSP4D; -. DR BioCyc; TMAR243274:GC6P-640-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13401; AAA_22; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 360 AA; 41332 MW; 943ED7913E3494CB CRC64; MNRAREINYL NSIALHQPFG IVGVSGETGI GKTTVLNFVN PEGVFTVRVN ISLRDSMESI LYDLLHSLAL SLEKVEEVSD LAKEVRKWIT DEVSTIKGFS LGVSFGVNAS LTHEKSIRPR FNFFKAREKL GELIKQTVQR KGKFLLIIDE LDKEKKEDVL RVIDSIKNFI IMEDFVVILS LPFSIYREYA ADRLRWNEAG NLENIFTDIV FVEPLKKLEI KELIIKRLGS YIELIEDGVL DIVADFSDGN PRDGLWILTK AIYDNIHKEL LSKEDLINTI NRTISEYTGL TLNLTENQKK AIRVLRGSVY SREKIIETLQ KEGFKRTTAY SVMDQLLQKR ILLVEKEGYR ISGKFSYMEI // ID Q9X1X0_THEMA Unreviewed; 385 AA. AC Q9X1X0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=Nuclease SbcCD subunit D {ECO:0000256|RuleBase:RU363069}; GN Name=sbcD {ECO:0000256|RuleBase:RU363069}; GN OrderedLocusNames=TM_1635 {ECO:0000313|EMBL:AAD36702.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36702.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36702.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:2Q8U} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-324. RX PubMed=20122942; DOI=10.1016/j.jmb.2010.01.049; RA Das D., Moiani D., Axelrod H.L., Miller M.D., McMullan D., Jin K.K., RA Abdubek P., Astakhova T., Burra P., Carlton D., Chiu H.J., Clayton T., RA Deller M.C., Duan L., Ernst D., Feuerhelm J., Grant J.C., RA Grzechnik A., Grzechnik S.K., Han G.W., Jaroszewski L., Klock H.E., RA Knuth M.W., Kozbial P., Krishna S.S., Kumar A., Marciano D., RA Morse A.T., Nigoghossian E., Okach L., Paulsen J., Reyes R., RA Rife C.L., Sefcovic N., Tien H.J., Trame C.B., van den Bedem H., RA Weekes D., Xu Q., Hodgson K.O., Wooley J., Elsliger M.A., Deacon A.M., RA Godzik A., Lesley S.A., Tainer J.A., Wilson I.A.; RT "Crystal structure of the first eubacterial Mre11 nuclease reveals RT novel features that may discriminate substrates during DNA repair."; RL J. Mol. Biol. 397:647-663(2010). RN [3] {ECO:0000213|PDB:3QF7, ECO:0000213|PDB:3QG5} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 343-385. RX PubMed=21458667; DOI=10.1016/j.cell.2011.02.038; RA Lammens K., Bemeleit D.J., Mockel C., Clausing E., Schele A., RA Hartung S., Schiller C.B., Lucas M., Angermuller C., Soding J., RA Strasser K., Hopfner K.P.; RT "The Mre11:Rad50 structure shows an ATP-dependent molecular clamp in RT DNA double-strand break repair."; RL Cell 145:54-66(2011). RN [4] {ECO:0000213|PDB:3THN, ECO:0000213|PDB:3THO} RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 8-385 IN COMPLEX WITH RP MANGANESE. RX PubMed=21937514; DOI=10.1093/nar/gkr749; RA Mockel C., Lammens K., Schele A., Hopfner K.P.; RT "ATP driven structural changes of the bacterial Mre11:Rad50 catalytic RT head complex."; RL Nucleic Acids Res. 40:914-927(2012). RN [5] {ECO:0000213|PDB:4W9M} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 347-383. RX PubMed=25349191; DOI=10.15252/embj.201488889; RA Rojowska A., Lammens K., Seifert F.U., Direnberger C., Feldmann H., RA Hopfner K.P.; RT "Structure of the Rad50 DNA double-strand break repair protein in RT complex with DNA."; RL EMBO J. 33:2847-2859(2014). RN [6] {ECO:0000213|PDB:4NZV, ECO:0000213|PDB:4O24, ECO:0000213|PDB:4O43} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-324 IN COMPLEX WITH RP MANGANESE. RX PubMed=24316220; DOI=10.1016/j.molcel.2013.11.003; RA Shibata A., Moiani D., Arvai A.S., Perry J., Harding S.M., RA Genois M.M., Maity R., van Rossum-Fikkert S., Kertokalio A., RA Romoli F., Ismail A., Ismalaj E., Petricci E., Neale M.J., RA Bristow R.G., Masson J.Y., Wyman C., Jeggo P.A., Tainer J.A.; RT "DNA double-strand break repair pathway choice is directed by distinct RT MRE11 nuclease activities."; RL Mol. Cell 53:7-18(2014). CC -!- FUNCTION: SbcCD cleaves DNA hairpin structures. These structures CC can inhibit DNA replication and are intermediates in certain DNA CC recombination reactions. The complex acts as a 3'->5' double CC strand exonuclease that can open hairpins. It also has a 5' CC single-strand endonuclease activity. CC {ECO:0000256|RuleBase:RU363069}. CC -!- SUBUNIT: Heterodimer of SbcC and SbcD. CC {ECO:0000256|RuleBase:RU363069}. CC -!- SIMILARITY: Belongs to the SbcD family. CC {ECO:0000256|RuleBase:RU363069}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36702.1; -; Genomic_DNA. DR PIR; C72230; C72230. DR RefSeq; NP_229435.1; NC_000853.1. DR RefSeq; WP_010865373.1; NC_000853.1. DR PDB; 2Q8U; X-ray; 2.20 A; A/B=1-324. DR PDB; 3QF7; X-ray; 1.90 A; C/D=343-385. DR PDB; 3QG5; X-ray; 3.40 A; C/D=8-385. DR PDB; 3THN; X-ray; 2.81 A; A=8-325. DR PDB; 3THO; X-ray; 2.61 A; B=8-385. DR PDB; 4NZV; X-ray; 1.90 A; A/B=2-324. DR PDB; 4O24; X-ray; 2.30 A; A/B=2-324. DR PDB; 4O43; X-ray; 2.40 A; A/B=2-324. DR PDB; 4O4K; X-ray; 2.10 A; A/B=2-324. DR PDB; 4O5G; X-ray; 2.30 A; A/B=2-324. DR PDB; 4W9M; X-ray; 2.70 A; D/F/J/L=347-383. DR PDBsum; 2Q8U; -. DR PDBsum; 3QF7; -. DR PDBsum; 3QG5; -. DR PDBsum; 3THN; -. DR PDBsum; 3THO; -. DR PDBsum; 4NZV; -. DR PDBsum; 4O24; -. DR PDBsum; 4O43; -. DR PDBsum; 4O4K; -. DR PDBsum; 4O5G; -. DR PDBsum; 4W9M; -. DR ProteinModelPortal; Q9X1X0; -. DR SMR; Q9X1X0; 1-324. DR IntAct; Q9X1X0; 1. DR STRING; 243274.TM1635; -. DR EnsemblBacteria; AAD36702; AAD36702; TM_1635. DR GeneID; 897574; -. DR KEGG; tma:TM1635; -. DR KEGG; tmi:THEMA_06070; -. DR PATRIC; 23938244; VBITheMar51294_1654. DR eggNOG; ENOG4107RH8; Bacteria. DR eggNOG; COG0420; LUCA. DR KO; K03547; -. DR OMA; LGNHDWR; -. DR OrthoDB; EOG60CWP4; -. DR BioCyc; TMAR243274:GC6P-1681-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IMP:CACAO. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006259; P:DNA metabolic process; IEA:InterPro. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR004593; SbcD. DR Pfam; PF00149; Metallophos; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00619; sbcd; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2Q8U, ECO:0000213|PDB:3QF7, KW ECO:0000213|PDB:3QG5, ECO:0000213|PDB:3THN}; KW Coiled coil {ECO:0000256|RuleBase:RU363069}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA recombination {ECO:0000256|RuleBase:RU363069}; KW DNA replication {ECO:0000256|RuleBase:RU363069}; KW Endonuclease {ECO:0000256|RuleBase:RU363069}; KW Exonuclease {ECO:0000256|RuleBase:RU363069, KW ECO:0000313|EMBL:AAD36702.1}; KW Hydrolase {ECO:0000256|RuleBase:RU363069, KW ECO:0000313|EMBL:AAD36702.1}; KW Manganese {ECO:0000213|PDB:3THN, ECO:0000213|PDB:3THO, KW ECO:0000213|PDB:4NZV, ECO:0000213|PDB:4O24}; KW Metal-binding {ECO:0000213|PDB:3THN, ECO:0000213|PDB:3THO, KW ECO:0000213|PDB:4NZV, ECO:0000213|PDB:4O24}; KW Nuclease {ECO:0000256|RuleBase:RU363069, ECO:0000313|EMBL:AAD36702.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 219 Metallophos. {ECO:0000259|Pfam:PF00149}. FT COILED 28 51 {ECO:0000256|RuleBase:RU363069}. FT COILED 359 385 {ECO:0000256|RuleBase:RU363069}. FT METAL 14 14 Manganese 1. {ECO:0000213|PDB:3THN, FT ECO:0000213|PDB:3THO, FT ECO:0000213|PDB:4NZV}. FT METAL 16 16 Manganese 1; via tele nitrogen. FT {ECO:0000213|PDB:3THN, FT ECO:0000213|PDB:3THO, FT ECO:0000213|PDB:4NZV}. FT METAL 58 58 Manganese 1. {ECO:0000213|PDB:3THN, FT ECO:0000213|PDB:3THO, FT ECO:0000213|PDB:4NZV}. FT METAL 58 58 Manganese 2. {ECO:0000213|PDB:3THN, FT ECO:0000213|PDB:3THO, FT ECO:0000213|PDB:4NZV}. FT METAL 93 93 Manganese 2. {ECO:0000213|PDB:3THN, FT ECO:0000213|PDB:3THO, FT ECO:0000213|PDB:4NZV}. FT METAL 180 180 Manganese 2; via tele nitrogen. FT {ECO:0000213|PDB:3THN, FT ECO:0000213|PDB:3THO, FT ECO:0000213|PDB:4NZV}. FT METAL 216 216 Manganese 1; via carbonyl oxygen. FT {ECO:0000213|PDB:4O4K, FT ECO:0000213|PDB:4O5G}. FT METAL 216 216 Manganese 2; via pros nitrogen. FT {ECO:0000213|PDB:3THN, FT ECO:0000213|PDB:3THO, FT ECO:0000213|PDB:4NZV}. FT METAL 218 218 Manganese 1; via tele nitrogen. FT {ECO:0000213|PDB:3THN, FT ECO:0000213|PDB:3THO, FT ECO:0000213|PDB:4NZV}. SQ SEQUENCE 385 AA; 44686 MW; F8ECCA6B72798430 CRC64; MINLKELKIL HTSDWHLGVT SWTSSRPVDR REELKKALDK VVEEAEKREV DLILLTGDLL HSRNNPSVVA LHDLLDYLKR MMRTAPVVVL PGNHDWKGLK LFGNFVTSIS SDITFVMSFE PVDVEAKRGQ KVRILPFPYP DESEALRKNE GDFRFFLESR LNKLYEEALK KEDFAIFMGH FTVEGLAGYA GIEQGREIII NRALIPSVVD YAALGHIHSF REIQKQPLTI YPGSLIRIDF GEEADEKGAV FVELKRGEPP RYERIDASPL PLKTLYYKKI DTSALKSIRD FCRNFPGYVR VVYEEDSGIL PDLMGEIDNL VKIERKSRRE IEEVLRESPE EFKEELDKLD YFELFKEYLK KREENHEKLL KILDELLDEV KKSEA // ID Q9WZY0_THEMA Unreviewed; 386 AA. AC Q9WZY0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Pyruvate:ferredoxin 2-oxidoreductase-related protein {ECO:0000313|EMBL:AAD35959.1}; GN OrderedLocusNames=TM_0878 {ECO:0000313|EMBL:AAD35959.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35959.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35959.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35959.1; -; Genomic_DNA. DR PIR; H72323; H72323. DR RefSeq; NP_228686.1; NC_000853.1. DR RefSeq; WP_010865215.1; NC_000853.1. DR ProteinModelPortal; Q9WZY0; -. DR STRING; 243274.TM0878; -. DR EnsemblBacteria; AAD35959; AAD35959; TM_0878. DR GeneID; 898552; -. DR KEGG; tma:TM0878; -. DR PATRIC; 23936687; VBITheMar51294_0892. DR eggNOG; ENOG4105DI2; Bacteria. DR eggNOG; COG0674; LUCA. DR InParanoid; Q9WZY0; -. DR KO; K00174; -. DR OMA; QEMYDFT; -. DR OrthoDB; EOG6GTZJW; -. DR BioCyc; TMAR243274:GC6P-908-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR033412; PFOR_II. DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR Pfam; PF17147; PFOR_II; 1. DR Pfam; PF01855; POR_N; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR SUPFAM; SSF52922; SSF52922; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Pyruvate {ECO:0000313|EMBL:AAD35959.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 18 247 POR_N. {ECO:0000259|Pfam:PF01855}. SQ SEQUENCE 386 AA; 42816 MW; 0C3893B6F9894196 CRC64; MRMPEMMFLQ GNEACALGAI KAGCRFFAGY PITPSTEIAE VMARELPKVG GVFVQMEDEI ASAAAVVGAS LAGVKSMTAT SGPGFSLIQE VIGYAIMTET PCVFANVMRL GPSTGLPTKP AQGDIMQTRW GTHGDHAIIA LYPSSVAEVY RYIITAFNLA EEYRTPVVFL MDAMLGHMRE SFYPPKDEEL FIIERLKDTS FGEEDLFVPF SESEYAEPTP FPMAEMGKTK FHVSGLVHDE SGFPLSSPDA AEKLIRRLTN KIRLHADEIA FYEEYETEDA EILVVAYGIV ARSAMKAVKI ARRDRIKVGL FKPITIWPAP VSRFRKLAEK VNTIVIAEMN LGQYAKELIS SIDRRSKVIR TINKVNGELI KPEEILDVIT ETQIEI // ID Q9X103_THEMA Unreviewed; 369 AA. AC Q9X103; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 127. DE SubName: Full=Sugar ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36351.1}; GN OrderedLocusNames=TM_1276 {ECO:0000313|EMBL:AAD36351.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36351.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36351.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00562907}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36351.1; -; Genomic_DNA. DR PIR; H72272; H72272. DR RefSeq; NP_229081.1; NC_000853.1. DR RefSeq; WP_010865294.1; NC_000853.1. DR ProteinModelPortal; Q9X103; -. DR SMR; Q9X103; 3-369. DR STRING; 243274.TM1276; -. DR TCDB; 3.A.1.1.22; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36351; AAD36351; TM_1276. DR GeneID; 898207; -. DR KEGG; tma:TM1276; -. DR PATRIC; 23937490; VBITheMar51294_1291. DR eggNOG; ENOG4108IJ9; Bacteria. DR eggNOG; COG3839; LUCA. DR InParanoid; Q9X103; -. DR KO; K10112; -. DR OMA; DYPENIF; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1307-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005116; Transp-assoc_OB_typ1. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF03459; TOBE; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00452173, ECO:0000313|EMBL:AAD36351.1}; KW Cell membrane {ECO:0000256|SAAS:SAAS00452105}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00452105}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00452173, ECO:0000313|EMBL:AAD36351.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00452289}. FT DOMAIN 6 237 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 369 AA; 41539 MW; AA589E22C2A56F43 CRC64; MRMAQVVLEN VTKVYENKVV AVKNANLVVE DKEFVVLLGP SGCGKTTTLR MIAGLEEITD GKIYIDGKVV NDVEPKDRDI AMVFQNYALY PHMTVYENMA FGLKLRKYPK DEIDRRVREA AKILGIENLL DRKPRQLSGG QRQRVAVGRA IVRNPKVFLF DEPLSNLDAK LRVQMRSELK KLHHRLQATI IYVTHDQVEA MTMADKIVVM KDGEIQQIGT PHEIYNSPAN VFVAGFIGSP PMNFVNARVV RGEGGLWIQA SGFKVKVPKE FEDKLANYID KEIIFGIRPE DIYDKLFALA PSPENTITGV VDVVEPLGSE TILHVKVGDD LIVASVNPRT QAKEEQKIDL VLDMTRMHAF DKETEKAII // ID Q9WXR5_THEMA Unreviewed; 362 AA. AC Q9WXR5; G4FGX4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 95. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35153.1}; GN OrderedLocusNames=TM_0059 {ECO:0000313|EMBL:AAD35153.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35153.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35153.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032, CC ECO:0000256|SAAS:SAAS00537635}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35153.1; -; Genomic_DNA. DR PIR; D72424; D72424. DR RefSeq; NP_227875.1; NC_000853.1. DR RefSeq; WP_004082547.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXR5; -. DR STRING; 243274.TM0059; -. DR TCDB; 3.A.1.5.29; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35153; AAD35153; TM_0059. DR GeneID; 896883; -. DR KEGG; tma:TM0059; -. DR KEGG; tmw:THMA_0055; -. DR PATRIC; 23934958; VBITheMar51294_0057. DR eggNOG; ENOG4105C2T; Bacteria. DR eggNOG; COG1173; LUCA. DR InParanoid; Q9WXR5; -. DR KO; K02034; -. DR OMA; AQNIRTV; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-59-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR025966; OppC_N. DR Pfam; PF00528; BPD_transp_1; 1. DR Pfam; PF12911; OppC_N; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00496716}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496716, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00496724}. FT TRANSMEM 25 47 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 160 184 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 196 217 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 223 242 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 281 306 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 326 349 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 154 350 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 362 AA; 41333 MW; 79F5438E8DC646CB CRC64; MDKTEELYLA SEWKLMWWRF KKNKLAVIGM VILGILYVLG IFCEFFSPYD PNRIFARYVY APPQKIHFFH EGKFIGPFVY GYKMERDPET FRRIYKEDKT KIYKIRLFVH GDKYKLWNTW ESDVHFFGVE EGTIFLFGTD RLGRDVFSRI LYGARISTTI GLVGVFLSMV LGIIIGGISG YYGGKIDNFI QRTIEFLISI PTIPLWMALA AALPRYWSQI KVYFAITVIL SLIGWTGLAR VVRSKFLSLK DEDFVVAARL AGASEWRIIF KHMLPSLTSH LIASATLSIP GMILGETGLS FLGLGLRPPA ISWGVLLQEA QNIRTVALYP WLLIPGLFVI ITVLCFNFVG DGLRDAADPY KT // ID Q9WZE4_THEMA Unreviewed; 289 AA. AC Q9WZE4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Motility protein B {ECO:0000313|EMBL:AAD35760.1}; GN OrderedLocusNames=TM_0677 {ECO:0000313|EMBL:AAD35760.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35760.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35760.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains OmpA-like domain. CC {ECO:0000256|SAAS:SAAS00509386}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35760.1; -; Genomic_DNA. DR PIR; C72347; C72347. DR RefSeq; NP_228485.1; NC_000853.1. DR RefSeq; WP_010865181.1; NC_000853.1. DR ProteinModelPortal; Q9WZE4; -. DR STRING; 243274.TM0677; -. DR EnsemblBacteria; AAD35760; AAD35760; TM_0677. DR GeneID; 898345; -. DR KEGG; tma:TM0677; -. DR PATRIC; 23936270; VBITheMar51294_0688. DR eggNOG; ENOG4107WER; Bacteria. DR eggNOG; COG1360; LUCA. DR InParanoid; Q9WZE4; -. DR KO; K02557; -. DR OMA; EFRRIDI; -. DR BioCyc; TMAR243274:GC6P-702-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.30.1330.60; -; 1. DR InterPro; IPR025713; MotB_N_dom. DR InterPro; IPR006665; OmpA-like. DR Pfam; PF13677; MotB_plug; 1. DR Pfam; PF00691; OmpA; 1. DR SUPFAM; SSF103088; SSF103088; 1. DR PROSITE; PS51123; OMPA_2; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 103 231 OmpA-like. {ECO:0000259|PROSITE:PS51123}. FT COILED 220 283 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 289 AA; 33417 MW; 15DA7A98BCE31BE2 CRC64; MMAKKREEEQ KGSPQWMTTY SDMVTLLLTF FVALISMSTI SPGKFQQVAV GLRIALSGRP PSVLMGGKSI NEEPLITSKR GIYQELMRLS EEYKGKITVE ERDEGTLIVL KDMVFFEPGS AKLTAEAKEL LAKVGQIVIE HTTNVLEVYG YADDRPPLPN SIYVSNWHLS SARAASVVNF FLTELKEKRM IERAADIKLG RFNIDLFYNP DRFYPIGLGD REIKKKIQDL ENQINVEKAL LNEKFRNGEI SQAEYELELR KLEEKYQQEL DRLRREFRRI DILIKREKM // ID Q9WYR8_THEMA Unreviewed; 448 AA. AC Q9WYR8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=Exo-poly-alpha-D-galacturonosidase, putative {ECO:0000313|EMBL:AAD35522.1}; GN OrderedLocusNames=TM_0437 {ECO:0000313|EMBL:AAD35522.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35522.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35522.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:3JUR} RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). RX PubMed=19854184; DOI=10.1016/j.febslet.2009.10.047; RA Pijning T., van Pouderoyen G., Kluskens L., van der Oost J., RA Dijkstra B.W.; RT "The crystal structure of a hyperthermoactive exopolygalacturonase RT from Thermotoga maritima reveals a unique tetramer."; RL FEBS Lett. 583:3665-3670(2009). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. CC {ECO:0000256|RuleBase:RU361169}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35522.1; -; Genomic_DNA. DR PIR; H72376; H72376. DR RefSeq; NP_228247.1; NC_000853.1. DR RefSeq; WP_010865120.1; NC_000853.1. DR PDB; 3JUR; X-ray; 2.05 A; A/B/C/D=1-448. DR PDBsum; 3JUR; -. DR ProteinModelPortal; Q9WYR8; -. DR STRING; 243274.TM0437; -. DR CAZy; GH28; Glycoside Hydrolase Family 28. DR EnsemblBacteria; AAD35522; AAD35522; TM_0437. DR GeneID; 897452; -. DR KEGG; tma:TM0437; -. DR PATRIC; 23935759; VBITheMar51294_0443. DR eggNOG; ENOG4105E4I; Bacteria. DR eggNOG; COG5434; LUCA. DR InParanoid; Q9WYR8; -. DR OMA; GHYLRPS; -. DR OrthoDB; EOG6X10TQ; -. DR BioCyc; MetaCyc:MONOMER-17963; -. DR BioCyc; TMAR243274:GC6P-452-MONOMER; -. DR EvolutionaryTrace; Q9WYR8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.160.20.10; -; 1. DR InterPro; IPR000743; Glyco_hydro_28. DR InterPro; IPR024535; Pectate_lyase_SF_prot. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR Pfam; PF00295; Glyco_hydro_28; 1. DR Pfam; PF12708; Pectate_lyase_3; 1. DR SUPFAM; SSF51126; SSF51126; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3JUR}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361169}; KW Hydrolase {ECO:0000256|RuleBase:RU361169}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 448 AA; 50484 MW; C18A6741BC0D0C09 CRC64; MIMEELAKKI EEEILNHVRE PQIPDREVNL LDFGARGDGR TDCSESFKRA IEELSKQGGG RLIVPEGVFL TGPIHLKSNI ELHVKGTIKF IPDPERYLPV VLTRFEGIEL YNYSPLVYAL DCENVAITGS GVLDGSADNE HWWPWKGKKD FGWKEGLPNQ QEDVKKLKEM AERGTPVEER VFGKGHYLRP SFVQFYRCRN VLVEGVKIIN SPMWCVHPVL SENVIIRNIE ISSTGPNNDG IDPESCKYML IEKCRFDTGD DSVVIKSGRD ADGRRIGVPS EYILVRDNLV ISQASHGGLV IGSEMSGGVR NVVARNNVYM NVERALRLKT NSRRGGYMEN IFFIDNVAVN VSEEVIRINL RYDNEEGEYL PVVRSVFVKN LKATGGKYAV RIEGLENDYV KDILISDTII EGAKISVLLE FGQLGMENVI MNGSRFEKLY IEGKALLK // ID Q9WYN5_THEMA Unreviewed; 201 AA. AC Q9WYN5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 96. DE SubName: Full=Deoxycytidylate deaminase, putative {ECO:0000313|EMBL:AAD35489.1}; GN OrderedLocusNames=TM_0404 {ECO:0000313|EMBL:AAD35489.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35489.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35489.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35489.1; -; Genomic_DNA. DR PIR; B72380; B72380. DR RefSeq; NP_228214.1; NC_000853.1. DR RefSeq; WP_010865113.1; NC_000853.1. DR ProteinModelPortal; Q9WYN5; -. DR STRING; 243274.TM0404; -. DR EnsemblBacteria; AAD35489; AAD35489; TM_0404. DR GeneID; 897403; -. DR KEGG; tma:TM0404; -. DR PATRIC; 23935691; VBITheMar51294_0409. DR eggNOG; ENOG4108UK2; Bacteria. DR eggNOG; COG2131; LUCA. DR InParanoid; Q9WYN5; -. DR KO; K01493; -. DR OMA; RIDEYAI; -. DR OrthoDB; EOG6Z6FT0; -. DR BioCyc; TMAR243274:GC6P-419-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn-bd. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR015517; dCMP_deaminase-rel. DR InterPro; IPR028883; tRNA_aden_deaminase. DR PANTHER; PTHR11086; PTHR11086; 1. DR Pfam; PF14437; MafB19-deam; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 55 188 CMP/dCMP-type deaminase. FT {ECO:0000259|PROSITE:PS51747}. SQ SEQUENCE 201 AA; 23212 MW; 4F32FDD79A9D8700 CRC64; MKRRLGLKLY YRRRGHVKPS LLFVIQSHKG EFVKDRLEEY LNNLKIEKKP DSRESWDSYF MRIARMVSER STCVHRKVGA VIVKDHRILA TGYNQPPSKF PHCNEIGCIR DDLEINSGEH QEICYALHAE QNALMQAAKF GIAVNGATIY VTHKPCSICA RLIVNAGIKR VVYEKDYPDP LTDFFFKFTG VESVRFVGDE M // ID Q9X0C2_THEMA Unreviewed; 381 AA. AC Q9X0C2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 86. DE SubName: Full=Permease, putative {ECO:0000313|EMBL:AAD36109.1}; GN OrderedLocusNames=TM_1032 {ECO:0000313|EMBL:AAD36109.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36109.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36109.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36109.1; -; Genomic_DNA. DR PIR; G72303; G72303. DR RefSeq; NP_228838.1; NC_000853.1. DR RefSeq; WP_010865248.1; NC_000853.1. DR ProteinModelPortal; Q9X0C2; -. DR STRING; 243274.TM1032; -. DR EnsemblBacteria; AAD36109; AAD36109; TM_1032. DR GeneID; 897718; -. DR KEGG; tma:TM1032; -. DR KEGG; tmi:THEMA_09200; -. DR PATRIC; 23936993; VBITheMar51294_1045. DR eggNOG; ENOG410813Z; Bacteria. DR eggNOG; COG0477; LUCA. DR KO; K05820; -. DR OMA; DRTGMRS; -. DR OrthoDB; EOG615VM7; -. DR BioCyc; TMAR243274:GC6P-1061-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR024989; MFS_assoc_dom. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF12832; MFS_1_like; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 66 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 124 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 136 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 159 180 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 201 223 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 235 256 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 263 282 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 294 315 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 327 347 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 353 374 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 201 381 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 381 AA; 43220 MW; E1CE8F8BA615479E CRC64; MLQFLLCKGG SFVRYRLMSI EFFVYGTMAV YSLLSQFLAN EELSKSQIGI LMAILPITSL YANHLNFEIA STIGRVNWLK RVILFAGILF WGLFLFDEFY LKLLFMAVFA FFFSAVTPLS ESVIVDITYQ MKMNYGRIRL FGTFGFSFTA LLMSGLIRLG FVTIFCTFTT LMFLTFLILN PMKEVELGEE EKRKSKKPLP TFFWLLLPVV IFGIAANNFN FVFLPVLMKE RNYDVSLASI ALSLMAITET PFLLWADEIV KKLGVGFMLA SGVFVVGLRN LLVTMTGSPA ALLMVQLLQG WTYIVIYYSM MFLIRTFGSA RIRAQKYFWV AMGIGPFIGS SVGGVLAENL GLINSYRILG LVPMIVSLFV FLFLRKYERA S // ID Q9WZ78_THEMA Unreviewed; 366 AA. AC Q9WZ78; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35694.1}; GN OrderedLocusNames=TM_0609 {ECO:0000313|EMBL:AAD35694.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35694.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35694.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35694.1; -; Genomic_DNA. DR PIR; E72355; E72355. DR RefSeq; NP_228419.1; NC_000853.1. DR RefSeq; WP_010865160.1; NC_000853.1. DR ProteinModelPortal; Q9WZ78; -. DR STRING; 243274.TM0609; -. DR EnsemblBacteria; AAD35694; AAD35694; TM_0609. DR GeneID; 897690; -. DR KEGG; tma:TM0609; -. DR PATRIC; 23936133; VBITheMar51294_0620. DR eggNOG; ENOG4108TYC; Bacteria. DR eggNOG; COG0438; LUCA. DR OMA; KYDKRVF; -. DR OrthoDB; EOG65QWF8; -. DR BioCyc; TMAR243274:GC6P-634-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 322 349 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 366 AA; 42956 MW; 3EE5A29EC351666B CRC64; MSDLKVLVIG YMHPRNDKRV FRTVQALSKR SEVIYQYWTE KEELPFKENN IRYIPVKCSN RGNIFQKAVK RKQVDEKIRH LVETEDYDIL YMHHFPATKP LKPFVVAKKR GKKIVYDIHE YHPQNFLSTL PRPLSDLKGF VMWRIFKKQL QLSDLCIFVS EETRNDVVAK TGLDPEKTFI VPNYASMKIE PDPDKKKMEI VLVGKTPRNL IHEKKLIRAL VERGFSFRII GMDSEAFSDV PHTYTSFLPY EKMMEELSKS MFSLISYKPT GKEDKNYLYS LPHKFYDSIA AGTPVIVKNS FVSMAKMVED LGIGVVIDPA NVEESLKRIE NACQRYEEIL ENIRRHQEGF VWDEKKEEEF LERVMG // ID Q9WZU3_THEMA Unreviewed; 340 AA. AC Q9WZU3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 81. DE SubName: Full=Rod shape-determining protein RodA {ECO:0000313|EMBL:AAD35921.1}; GN OrderedLocusNames=TM_0839 {ECO:0000313|EMBL:AAD35921.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35921.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35921.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the SEDS family. CC {ECO:0000256|SAAS:SAAS00587907}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35921.1; -; Genomic_DNA. DR PIR; H72325; H72325. DR RefSeq; NP_228648.1; NC_000853.1. DR RefSeq; WP_010865212.1; NC_000853.1. DR STRING; 243274.TM0839; -. DR DNASU; 898510; -. DR EnsemblBacteria; AAD35921; AAD35921; TM_0839. DR GeneID; 898510; -. DR KEGG; tma:TM0839; -. DR KEGG; tmi:THEMA_00445; -. DR PATRIC; 23936604; VBITheMar51294_0852. DR eggNOG; ENOG4105CNI; Bacteria. DR eggNOG; COG0772; LUCA. DR KO; K05837; -. DR OMA; ATIAWYL; -. DR OrthoDB; EOG68M4JQ; -. DR BioCyc; TMAR243274:GC6P-868-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:InterPro. DR GO; GO:0051301; P:cell division; IEA:InterPro. DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro. DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS. DR InterPro; IPR001182; Cell_cycle_FtsW/RodA. DR InterPro; IPR011923; RodA_shape. DR PANTHER; PTHR30474; PTHR30474; 1. DR PANTHER; PTHR30474:SF1; PTHR30474:SF1; 1. DR Pfam; PF01098; FTSW_RODA_SPOVE; 1. DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00481328, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00481328, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00481328, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 28 44 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 69 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 150 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 156 174 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 195 214 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 234 260 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 272 289 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 309 334 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 340 AA; 38255 MW; AF616F60D800A61D CRC64; MSILMLFGLA TLRSATYGEN EQLFTRQIVW DIAGFSLMFL VLFIKDRTIR NFSIILYVFS VVLLAALLVK GTPIGGSKRW FRVMGFSFQP SDFAKLSLIV LLPYLLEKRW FWRSFFLTVV PAVLIFLEPD LGTTLSVGLI WLFAVLASNV NKKPLVILLI LVLVFLPVFF FFGLKDYQRA RILSFLNPEE YGESYSYNVL QSIHAIGAGG LFGAGYMKGK ANLMGYVPVS YTDFIVSVIG EEFGFIGIVF LLSLFGLLFF EVSRWILNVK DEYWEILMVS ACGLIWFHVF ENVSMNLGLL PVTGVPLPFI SYGGTSTLVF SILVGLILKG IALARVEKKL // ID Q9WZU0_THEMA Unreviewed; 419 AA. AC Q9WZU0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=Cell division protein FtsA {ECO:0000256|HAMAP-Rule:MF_02033}; GN Name=ftsA {ECO:0000256|HAMAP-Rule:MF_02033}; GN OrderedLocusNames=TM_0835 {ECO:0000313|EMBL:AAD35917.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35917.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35917.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1E4F, ECO:0000213|PDB:1E4G} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ATP. RX PubMed=11032797; DOI=10.1093/emboj/19.20.5300; RA van den Ent F., Lowe J.; RT "Crystal structure of the cell division protein FtsA from Thermotoga RT maritima."; RL EMBO J. 19:5300-5307(2000). RN [3] {ECO:0000213|PDB:4A2A, ECO:0000213|PDB:4A2B} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ATP. RX PubMed=22473211; DOI=10.1038/emboj.2012.76; RA Szwedziak P., Wang Q., Freund S.M., Lowe J.; RT "FtsA forms actin-like protofilaments."; RL EMBO J. 31:2249-2260(2012). CC -!- FUNCTION: Cell division protein that is involved in the assembly CC of the Z ring. May serve as a membrane anchor for the Z ring. CC {ECO:0000256|HAMAP-Rule:MF_02033}. CC -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000256|HAMAP- CC Rule:MF_02033}. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-7808292, EBI-7808292; CC O08398:ftsZ; NbExp=4; IntAct=EBI-7808292, EBI-7808310; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_02033}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_02033}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_02033}. Note=Localizes to the Z ring in an FtsZ-dependent CC manner. Targeted to the membrane through a conserved C-terminal CC amphiphatic helix. {ECO:0000256|HAMAP-Rule:MF_02033}. CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000256|HAMAP- CC Rule:MF_02033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35917.1; -; Genomic_DNA. DR PIR; G72328; G72328. DR RefSeq; NP_228644.1; NC_000853.1. DR RefSeq; WP_010865211.1; NC_000853.1. DR PDB; 1E4F; X-ray; 1.90 A; T=1-419. DR PDB; 1E4G; X-ray; 2.60 A; T=1-419. DR PDB; 4A2A; X-ray; 1.80 A; A/B=1-419. DR PDB; 4A2B; X-ray; 1.80 A; A=1-419. DR PDBsum; 1E4F; -. DR PDBsum; 1E4G; -. DR PDBsum; 4A2A; -. DR PDBsum; 4A2B; -. DR ProteinModelPortal; Q9WZU0; -. DR SMR; Q9WZU0; 7-390. DR IntAct; Q9WZU0; 1. DR MINT; MINT-8382765; -. DR STRING; 243274.TM0835; -. DR EnsemblBacteria; AAD35917; AAD35917; TM_0835. DR GeneID; 898506; -. DR KEGG; tma:TM0835; -. DR KEGG; tmi:THEMA_00465; -. DR PATRIC; 23936596; VBITheMar51294_0848. DR eggNOG; ENOG4107ZUG; Bacteria. DR eggNOG; COG0849; LUCA. DR KO; K03590; -. DR OMA; AKIPRIN; -. DR OrthoDB; EOG60PH7X; -. DR BioCyc; TMAR243274:GC6P-864-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_02033; FtsA; 1. DR InterPro; IPR020823; Cell_div_FtsA. DR InterPro; IPR003494; SHS2_FtsA. DR Pfam; PF02491; SHS2_FTSA; 1. DR SMART; SM00842; FtsA; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1E4F, ECO:0000213|PDB:1E4G, KW ECO:0000213|PDB:4A2A, ECO:0000213|PDB:4A2B}; KW ATP-binding {ECO:0000213|PDB:1E4G, ECO:0000213|PDB:4A2A}; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02033, KW ECO:0000313|EMBL:AAD35917.1}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_02033, KW ECO:0000313|EMBL:AAD35917.1}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02033}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02033}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02033}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_02033}; KW Nucleotide-binding {ECO:0000213|PDB:1E4G, ECO:0000213|PDB:4A2A}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT NP_BIND 17 21 ATP. {ECO:0000213|PDB:1E4G, FT ECO:0000213|PDB:4A2A}. FT BINDING 84 84 ATP. {ECO:0000213|PDB:1E4G}. FT BINDING 215 215 ATP; via amide nitrogen. FT {ECO:0000213|PDB:1E4G, FT ECO:0000213|PDB:4A2A}. FT BINDING 257 257 ATP. {ECO:0000213|PDB:1E4G, FT ECO:0000213|PDB:4A2A}. FT BINDING 337 337 ATP. {ECO:0000213|PDB:1E4G, FT ECO:0000213|PDB:4A2A}. SQ SEQUENCE 419 AA; 47016 MW; 3A41B479596B4927 CRC64; MIDLSKTVFY TSIDIGSRYI KGLVLGKRDQ EWEALAFSSV KSRGLDEGEI KDAIAFKESV NTLLKELEEQ LQKSLRSDFV ISFSSVSFER EDTVIERDFG EEKRSITLDI LSEMQSEALE KLKENGKTPL HIFSKRYLLD DERIVFNPLD MKASKIAIEY TSIVVPLKVY EMFYNFLQDT VKSPFQLKSS LVSTAEGVLT TPEKDRGVVV VNLGYNFTGL IAYKNGVPIK ISYVPVGMKH VIKDVSAVLD TSFEESERLI ITHGNAVYND LKEEEIQYRG LDGNTIKTTT AKKLSVIIHA RLREIMSKSK KFFREVEAKI VEEGEIGIPG GVVLTGGGAK IPRINELATE VFKSPVRTGC YANSDRPSII NADEVANDPS FAAAFGNVFA VSENPYEETP VKSENPLKKI FRLFKELME // ID Q9WXQ6_THEMA Unreviewed; 261 AA. AC Q9WXQ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 88. DE SubName: Full=Iron-sulfur cluster-binding protein {ECO:0000313|EMBL:AAD35142.1}; GN OrderedLocusNames=TM_0049 {ECO:0000313|EMBL:AAD35142.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35142.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35142.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35142.1; -; Genomic_DNA. DR PIR; F72426; F72426. DR RefSeq; NP_227865.1; NC_000853.1. DR RefSeq; WP_010865039.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXQ6; -. DR STRING; 243274.TM0049; -. DR EnsemblBacteria; AAD35142; AAD35142; TM_0049. DR GeneID; 896873; -. DR KEGG; tma:TM0049; -. DR KEGG; tmi:THEMA_04560; -. DR KEGG; tmw:THMA_0045; -. DR PATRIC; 23934938; VBITheMar51294_0047. DR eggNOG; ENOG4105E2G; Bacteria. DR eggNOG; COG1145; LUCA. DR eggNOG; COG2006; LUCA. DR OMA; THELTYY; -. DR OrthoDB; EOG664CDM; -. DR BioCyc; TMAR243274:GC6P-49-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR007160; DUF362. DR Pfam; PF04015; DUF362; 1. DR Pfam; PF00037; Fer4; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|RuleBase:RU003429}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|RuleBase:RU003429}; KW Iron-sulfur {ECO:0000256|RuleBase:RU003429}; KW Metal-binding {ECO:0000256|RuleBase:RU003429}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 203 232 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 233 259 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 261 AA; 29239 MW; 7948C55680DE9858 CRC64; MRGCFSVTGV EDVCERLGVP CVPLDDPVEV SGEVFQKIKI SRKVLEADKV VNLPKLKTHS QMVMTLGVKN TFGCVVGLEK SSWHMRAKNY DDFANLLIDI HRIVSPVLTI LDGVEGMEGN GPTNGKKKHF GLVAVSKNAF ALDDAVCKAL GIDHVVYTVQ HARKRRVVPD YEIVGTFHAS IQLPSTVSTL DRLSRTFSRF FVKYPKIDTR KCVKCRLCEE RCPASAIDIS SQRIDYQKCI RCYVCHEVCP QDAIKLVRRL V // ID Q9X169_THEMA Unreviewed; 352 AA. AC Q9X169; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36419.1}; GN OrderedLocusNames=TM_1348 {ECO:0000313|EMBL:AAD36419.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36419.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36419.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36419.1; -; Genomic_DNA. DR PIR; D72264; D72264. DR RefSeq; NP_229149.1; NC_000853.1. DR RefSeq; WP_010865323.1; NC_000853.1. DR STRING; 243274.TM1348; -. DR EnsemblBacteria; AAD36419; AAD36419; TM_1348. DR GeneID; 898132; -. DR KEGG; tma:TM1348; -. DR KEGG; tmi:THEMA_07600; -. DR PATRIC; 23937634; VBITheMar51294_1360. DR eggNOG; ENOG4106FDK; Bacteria. DR eggNOG; ENOG410YSTI; LUCA. DR OMA; GMHEEAM; -. DR OrthoDB; EOG6FJNBN; -. DR BioCyc; TMAR243274:GC6P-1381-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR SUPFAM; SSF48452; SSF48452; 2. DR PROSITE; PS50293; TPR_REGION; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 276 295 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 288 352 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 352 AA; 41237 MW; 47EF0B432D421CB8 CRC64; MRVLRIIFIL LLLIPSLLTM ALSLEEIKSL SKTNLDNAID LFLDYMKKHP SDPELENVGE FLFAKKKLVE KHPSLSREII SEDFHGLLEK LRDTEEMFSE EEVPLLEEIF PELKSFAEKL QDVEEFLSSP FFWKLGISLK IENPEKFAED LVNRFLEDPF VFSFEVVEAL SKVENAEEIA YHLVRKAKEI PLKEESYSYI LRLFEVAHHL GYSETDELEE QIKKYFSISA KVNASGNVEE ILDEYEQLTI PKEKLREKLA AVSKKSKVSE EKRGRYYPFL LVLLALPFLS ARFRASFYRR IGMKKRAASI YLKLLQKQPE NVKLRLKLAR LYEEIGMHEE AMKEYEIIKK LS // ID Q9X114_THEMA Unreviewed; 308 AA. AC Q9X114; G4FE61; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36362.1}; GN OrderedLocusNames=TM_1288 {ECO:0000313|EMBL:AAD36362.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36362.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36362.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36362.1; -; Genomic_DNA. DR PIR; G72271; G72271. DR RefSeq; NP_229092.1; NC_000853.1. DR RefSeq; WP_004079946.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X114; -. DR STRING; 243274.TM1288; -. DR EnsemblBacteria; AAD36362; AAD36362; TM_1288. DR GeneID; 898195; -. DR KEGG; tma:TM1288; -. DR KEGG; tmi:THEMA_07895; -. DR KEGG; tmw:THMA_1314; -. DR PATRIC; 23937516; VBITheMar51294_1304. DR eggNOG; ENOG41082XB; Bacteria. DR eggNOG; COG0731; LUCA. DR OMA; QPDRIDI; -. DR OrthoDB; EOG6TTVP9; -. DR BioCyc; TMAR243274:GC6P-1319-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 26 191 Radical_SAM. {ECO:0000259|Pfam:PF04055}. SQ SEQUENCE 308 AA; 35250 MW; BEAB502A88155046 CRC64; MSSNSRVYGI VPSKRLGRSL GVSPIPFKTC TYSCVYCQLG RTTNFTVKRQ TFFPLKVFEE ELKGFVKRHR YDFDVVSIVG EGEPTLYTPL DALIDLCKSI TGKPVVLITN GSLFWSEKVR KEAKLSDIIM PTLSAWDEKS FRTIHKPHKN LSFQKVFEGL KKFRREYSGE IWLEVMLVKG LNDFALEELK EKISQVESDR VYVNVPVRPP AEGWVEPPDE ETIEKAKELF NAASIETPAA SRFIAAGEGI DAVLNVIKRH PMNEEEVRDL LTSQKIDPKP VLEKLRSCKN VKIIEYSGRR YYRYTTAE // ID Q9X2H5_THEMA Unreviewed; 178 AA. AC Q9X2H5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 88. DE SubName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000313|EMBL:AAD36923.1}; GN OrderedLocusNames=TM_1861 {ECO:0000313|EMBL:AAD36923.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36923.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36923.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase CC class-I family. {ECO:0000256|RuleBase:RU003750, CC ECO:0000256|SAAS:SAAS00571358}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36923.1; -; Genomic_DNA. DR PIR; F72201; F72201. DR RefSeq; NP_229657.1; NC_000853.1. DR RefSeq; WP_010865420.1; NC_000853.1. DR STRING; 243274.TM1861; -. DR EnsemblBacteria; AAD36923; AAD36923; TM_1861. DR GeneID; 897501; -. DR KEGG; tma:TM1861; -. DR PATRIC; 23938711; VBITheMar51294_1882. DR eggNOG; ENOG4105BZQ; Bacteria. DR eggNOG; COG0558; LUCA. DR InParanoid; Q9X2H5; -. DR KO; K00995; -. DR OMA; WWLFWPS; -. DR OrthoDB; EOG6WMJ3D; -. DR BioCyc; TMAR243274:GC6P-1912-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:InterPro. DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central. DR InterPro; IPR000462; CDP-OH_P_trans. DR InterPro; IPR004570; Phosphatidylglycerol_P_synth. DR Pfam; PF01066; CDP-OH_P_transf; 1. DR PIRSF; PIRSF000847; Phos_ph_gly_syn; 1. DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lipid biosynthesis {ECO:0000256|SAAS:SAAS00461556}; KW Lipid metabolism {ECO:0000256|SAAS:SAAS00461556}; KW Membrane {ECO:0000256|SAAS:SAAS00461540, ECO:0000256|SAM:Phobius}; KW Phospholipid biosynthesis {ECO:0000256|SAAS:SAAS00461556}; KW Phospholipid metabolism {ECO:0000256|SAAS:SAAS00461556}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU003750, KW ECO:0000256|SAAS:SAAS00461509, ECO:0000313|EMBL:AAD36923.1}; KW Transmembrane {ECO:0000256|SAAS:SAAS00461540, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00461540, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 52 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 146 166 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 178 AA; 20005 MW; 928FB9DF321B20BA CRC64; MGVSDMNLAN FFSLLRAALV IPVVWFYMEG WISLSFLIFV FAAFTDYLDG FFARKKNQVT DFGKVFDQVS DKILVISTAV AMLDVLPLWY VLVVFARDTF VNGLRILAAS RGNVVPARWI GKAKTVSQFV VLIAAYLFKM GFLSNALLMF FVVLSLTVTV ISWITYTIDI ARITKLEG // ID Q9WYS2_THEMA Unreviewed; 255 AA. AC Q9WYS2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 112. DE SubName: Full=Oxidoreductase, short chain dehydrogenase/reductase family {ECO:0000313|EMBL:AAD35526.1}; GN OrderedLocusNames=TM_0441 {ECO:0000313|EMBL:AAD35526.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35526.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35526.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1VL8} RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH NADP. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of Gluconate 5-dehydrogenase (TM0441) from RT Thermotoga maritima at 2.07 A resolution."; RL Submitted (JUL-2004) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35526.1; -; Genomic_DNA. DR PIR; D72377; D72377. DR RefSeq; NP_228251.1; NC_000853.1. DR RefSeq; WP_010865121.1; NC_000853.1. DR PDB; 1VL8; X-ray; 2.07 A; A/B=1-255. DR PDBsum; 1VL8; -. DR ProteinModelPortal; Q9WYS2; -. DR SMR; Q9WYS2; 4-255. DR STRING; 243274.TM0441; -. DR DNASU; 897456; -. DR EnsemblBacteria; AAD35526; AAD35526; TM_0441. DR GeneID; 897456; -. DR KEGG; tma:TM0441; -. DR KEGG; tmi:THEMA_02520; -. DR PATRIC; 23935767; VBITheMar51294_0447. DR eggNOG; ENOG4105CHR; Bacteria. DR eggNOG; ENOG410XNW1; LUCA. DR KO; K00046; -. DR OMA; PSIINIG; -. DR OrthoDB; EOG6N3CR8; -. DR BioCyc; MetaCyc:MONOMER-17953; -. DR BioCyc; TMAR243274:GC6P-456-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24322; PTHR24322; 2. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VL8}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW NADP {ECO:0000213|PDB:1VL8}; KW Nucleotide-binding {ECO:0000213|PDB:1VL8}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT NP_BIND 16 21 NADP. {ECO:0000213|PDB:1VL8}. FT NP_BIND 41 42 NADP. {ECO:0000213|PDB:1VL8}. FT NP_BIND 67 68 NADP. {ECO:0000213|PDB:1VL8}. FT NP_BIND 193 195 NADP. {ECO:0000213|PDB:1VL8}. FT BINDING 94 94 NADP; via carbonyl oxygen. FT {ECO:0000213|PDB:1VL8}. FT BINDING 160 160 NADP. {ECO:0000213|PDB:1VL8}. FT BINDING 164 164 NADP. {ECO:0000213|PDB:1VL8}. SQ SEQUENCE 255 AA; 27917 MW; BAB56B3FB337725C CRC64; MKEVFDLRGR VALVTGGSRG LGFGIAQGLA EAGCSVVVAS RNLEEASEAA QKLTEKYGVE TMAFRCDVSN YEEVKKLLEA VKEKFGKLDT VVNAAGINRR HPAEEFPLDE FRQVIEVNLF GTYYVCREAF SLLRESDNPS IINIGSLTVE EVTMPNISAY AASKGGVASL TKALAKEWGR YGIRVNVIAP GWYRTKMTEA VFSDPEKLDY MLKRIPLGRT GVPEDLKGVA VFLASEEAKY VTGQIIFVDG GWTAN // ID Q9WYX1_THEMA Unreviewed; 327 AA. AC Q9WYX1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 117. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35586.1}; GN OrderedLocusNames=TM_0501 {ECO:0000313|EMBL:AAD35586.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35586.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35586.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35586.1; -; Genomic_DNA. DR PIR; D72371; D72371. DR RefSeq; NP_228311.1; NC_000853.1. DR RefSeq; WP_010865137.1; NC_000853.1. DR ProteinModelPortal; Q9WYX1; -. DR STRING; 243274.TM0501; -. DR EnsemblBacteria; AAD35586; AAD35586; TM_0501. DR GeneID; 897542; -. DR KEGG; tma:TM0501; -. DR PATRIC; 23935907; VBITheMar51294_0508. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR InParanoid; Q9WYX1; -. DR KO; K02031; -. DR OMA; YSDYPHE; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-525-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35586.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35586.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 1 249 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 327 AA; 36918 MW; 623D2A5E3CB3F34D CRC64; MENLKTYFYT EDGVVKAVDG VSFEVREGET LGIVGESGSG KSVTSLSIMR LLDQNGKIVD GKIIFKGRNL LELSENEMRK IRGKEIAMIF QEPMVALNPV FTIGDQIMEA IILHQNVSEK EARKMAIDLL RKVGIPEPEK RVDEYPHQLS GGMRQRAMIA MALSCRPSLL IADEPTTALD VTIQAQILEL MKELQKEYGM AIILITHDMG VVAEMSDKVA VMYAGKVVEY GDVKTIFTEP KHPYTYALLE SIPRIDVEQE RLKSIPGNVP DPLNFPPGCK FHPRCEFFEK GKCDVEEPEL EDLDGNHKVR CFFWQKLDEM RHAKSEV // ID Q9WYN0_THEMA Unreviewed; 225 AA. AC Q9WYN0; G4FHV8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 122. DE SubName: Full=Response regulator {ECO:0000313|EMBL:AAD35484.1}; GN OrderedLocusNames=TM_0399 {ECO:0000313|EMBL:AAD35484.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35484.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35484.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1KGS} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS). RX PubMed=11839301; DOI=10.1016/S0969-2126(01)00706-7; RA Buckler D.R., Zhou Y., Stock A.M.; RT "Evidence of intradomain and interdomain flexibility in an OmpR/PhoB RT homolog from Thermotoga maritima."; RL Structure 10:153-164(2002). RN [3] {ECO:0000213|PDB:3NNN} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-122 IN COMPLEX WITH RP MAGNESIUM. RX PubMed=20702407; DOI=10.1074/jbc.M110.157164; RA Barbieri C.M., Mack T.R., Robinson V.L., Miller M.T., Stock A.M.; RT "Regulation of response regulator autophosphorylation through RT interdomain contacts."; RL J. Biol. Chem. 285:32325-32335(2010). CC -!- SIMILARITY: Contains OmpR/PhoB-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00583175}. CC -!- SIMILARITY: Contains response regulatory domain. CC {ECO:0000256|SAAS:SAAS00122778}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35484.1; -; Genomic_DNA. DR PIR; H72382; H72382. DR RefSeq; NP_228209.1; NC_000853.1. DR RefSeq; WP_004083233.1; NC_000853.1. DR PDB; 1KGS; X-ray; 1.50 A; A=1-225. DR PDB; 3NNN; X-ray; 2.20 A; A/B=1-122. DR PDBsum; 1KGS; -. DR PDBsum; 3NNN; -. DR ProteinModelPortal; Q9WYN0; -. DR SMR; Q9WYN0; 2-225. DR STRING; 243274.TM0399; -. DR EnsemblBacteria; AAD35484; AAD35484; TM_0399. DR GeneID; 897392; -. DR KEGG; tma:TM0399; -. DR PATRIC; 23935681; VBITheMar51294_0404. DR eggNOG; ENOG4105CK6; Bacteria. DR eggNOG; COG0745; LUCA. DR InParanoid; Q9WYN0; -. DR OMA; EVWNINF; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-414-MONOMER; -. DR EvolutionaryTrace; Q9WYN0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF00486; Trans_reg_C; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00862; Trans_reg_C; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS51755; OMPR_PHOB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1KGS, ECO:0000213|PDB:3NNN}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00582919}; KW Magnesium {ECO:0000213|PDB:3NNN}; KW Metal-binding {ECO:0000213|PDB:3NNN}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00478953}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00478953}; KW Two-component regulatory system {ECO:0000256|SAAS:SAAS00478431}. FT DOMAIN 4 118 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT DOMAIN 126 224 OmpR/PhoB-type DNA-binding. FT {ECO:0000259|PROSITE:PS51755}. FT METAL 10 10 Magnesium. {ECO:0000213|PDB:3NNN}. FT METAL 53 53 Magnesium. {ECO:0000213|PDB:3NNN}. FT METAL 55 55 Magnesium. {ECO:0000213|PDB:3NNN}. SQ SEQUENCE 225 AA; 26015 MW; 4CB1F2CC82A218F7 CRC64; MNVRVLVVED ERDLADLITE ALKKEMFTVD VCYDGEEGMY MALNEPFDVV ILDIMLPVHD GWEILKSMRE SGVNTPVLML TALSDVEYRV KGLNMGADDY LPKPFDLREL IARVRALIRR KSESKSTKLV CGDLILDTAT KKAYRGSKEI DLTKKEYQIL EYLVMNKNRV VTKEELQEHL WSFDDEVFSD VLRSHIKNLR KKVDKGFKKK IIHTVRGIGY VARDE // ID Q9X223_THEMA Unreviewed; 391 AA. AC Q9X223; G4FG84; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 88. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36764.1}; GN OrderedLocusNames=TM_1697 {ECO:0000313|EMBL:AAD36764.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36764.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36764.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00026557}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmI CC family. {ECO:0000256|SAAS:SAAS00545036}. CC -!- SIMILARITY: Contains PUA domain. {ECO:0000256|SAAS:SAAS00026697}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36764.1; -; Genomic_DNA. DR PIR; C72220; C72220. DR RefSeq; NP_229497.1; NC_000853.1. DR RefSeq; WP_004082213.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X223; -. DR STRING; 243274.TM1697; -. DR EnsemblBacteria; AAD36764; AAD36764; TM_1697. DR GeneID; 897890; -. DR KEGG; tma:TM1697; -. DR KEGG; tmi:THEMA_05755; -. DR KEGG; tmw:THMA_1739; -. DR PATRIC; 23938368; VBITheMar51294_1714. DR eggNOG; ENOG4107RPU; Bacteria. DR eggNOG; COG1092; LUCA. DR KO; K06969; -. DR OMA; AKKEIRQ; -. DR OrthoDB; EOG6DG2T1; -. DR BioCyc; TMAR243274:GC6P-1745-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 2.30.130.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR019614; SAM-dep_methyl-trfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF10672; Methyltrans_SAM; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR PROSITE; PS50890; PUA; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00428966}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00429068}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW RNA-binding {ECO:0000256|SAAS:SAAS00469861}; KW rRNA processing {ECO:0000256|SAAS:SAAS00429013}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00429032}; KW Transferase {ECO:0000256|SAAS:SAAS00429068}. FT DOMAIN 1 77 PUA. {ECO:0000259|PROSITE:PS50890}. SQ SEQUENCE 391 AA; 45045 MW; 1C5858FC7F8342AF CRC64; MAKVFLKRMN RRISGGHLWI FYNEILKVEG EYENGSVVDV FRPDGSFFGK GYINDNSKIR VRILTWKNEV IDRNFIKNRI ESALKRKKKL VKETTAFRVV HSEGDFLPGL IVDLFGDYLV FQITTLGMEK MKDWILDSLV EIFKPKGIYE KSEGTFREKE GLDNREEWVY GKGPELIEFE MNGFKFLADT RGQKTGFFLD QRENARMVMD LAEGKVCLDV FSYTGNFAVH LLKGGAKHVT LVDYSERALE VAREILKLNG FDSSRYDLLP GNAFDILKSF DREGRKYDLV VLDPPSFAKS SSNLESARRG YKEINLRAMR ILKKPGVLVT SSCTQIVSEE LFREILFDAS FDTKTSLTVL RRGGQPPDHP VLMNVPETQY LKFYILQVDK R // ID Q9WXW4_THEMA Unreviewed; 328 AA. AC Q9WXW4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Pyruvate formate lyase activating enzyme, putative {ECO:0000313|EMBL:AAD35203.1}; GN OrderedLocusNames=TM_0109 {ECO:0000313|EMBL:AAD35203.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35203.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35203.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|PIRSR:PIRSR004869-50}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|PIRSR:PIRSR004869-50}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35203.1; -; Genomic_DNA. DR PIR; D72416; D72416. DR RefSeq; NP_227925.1; NC_000853.1. DR RefSeq; WP_010865053.1; NC_000853.1. DR ProteinModelPortal; Q9WXW4; -. DR STRING; 243274.TM0109; -. DR DNASU; 896936; -. DR EnsemblBacteria; AAD35203; AAD35203; TM_0109. DR GeneID; 896936; -. DR KEGG; tma:TM0109; -. DR PATRIC; 23935058; VBITheMar51294_0107. DR eggNOG; ENOG4105KN9; Bacteria. DR eggNOG; COG1313; LUCA. DR InParanoid; Q9WXW4; -. DR KO; K04070; -. DR OMA; RNINHVG; -. DR OrthoDB; EOG6677SM; -. DR BioCyc; TMAR243274:GC6P-109-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004869; PflX_prd; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|PIRSR:PIRSR004869-50}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR004869-50}; KW Lyase {ECO:0000313|EMBL:AAD35203.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR004869-50}; KW Pyruvate {ECO:0000313|EMBL:AAD35203.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR004869-50}. FT DOMAIN 79 239 Radical_SAM. {ECO:0000259|Pfam:PF04055}. FT METAL 84 84 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. FT METAL 88 88 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. FT METAL 91 91 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004869-50}. SQ SEQUENCE 328 AA; 37531 MW; 3DF24F86FA4EB760 CRC64; MNWEQKSSML KKKIERIKEI ETTLWGNLEK CELCPRKCGV DRYRTTGICG LPARAKISNA VLHFGEEPPI SGKTGAGTVF FSGCNMKCVY CQNMGFSQKG IGTEVEVEDL AEIFLILQKH GAKTLNLVTP TPHLPFIISA LRIAIENGLN LPIVYNTSGY EDPEILRLLE GVVDIYLSDV RYSDNEASKK YSKTPDYWTV VQKAIVEMFR QVGIFDEEKM KGLIVRILVL PGNVVDYSEI FSFLSSLSTR IPLSIMNQYI PHFDAQKFPE ISRKLNQNEY EKILELAERY GFTEGWYQSE EKERVTTRGL KEISEKLQFL RLKTHNSY // ID Q9X226_THEMA Unreviewed; 202 AA. AC Q9X226; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 85. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36767.1}; GN OrderedLocusNames=TM_1700 {ECO:0000313|EMBL:AAD36767.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36767.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36767.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36767.1; -; Genomic_DNA. DR PIR; F72220; F72220. DR RefSeq; NP_229500.1; NC_000853.1. DR RefSeq; WP_010865385.1; NC_000853.1. DR ProteinModelPortal; Q9X226; -. DR STRING; 243274.TM1700; -. DR EnsemblBacteria; AAD36767; AAD36767; TM_1700. DR GeneID; 897286; -. DR KEGG; tma:TM1700; -. DR PATRIC; 23938374; VBITheMar51294_1717. DR eggNOG; ENOG4108UZW; Bacteria. DR eggNOG; COG1011; LUCA. DR InParanoid; Q9X226; -. DR KO; K07025; -. DR OMA; TENDIAC; -. DR OrthoDB; EOG6K403K; -. DR BioCyc; TMAR243274:GC6P-1748-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR Pfam; PF13419; HAD_2; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 201 HAD-like_dom. {ECO:0000259|Pfam:PF13419}. SQ SEQUENCE 202 AA; 23469 MW; F041A430F835E0D0 CRC64; MSVRIFLFDY DGTLAEDNGF AEEYFKKLTS FFRDRGVSIS PELVLGCVEE ITRNPDGSTN LERYMKCLEK RTSQCAEKWK ELFMEFYESE LFDSLKGTVE PVKGTVDLLK EKKKEGKVVL ATNPVFPRIA ILKRLNWIGL SEDDFHLITD MESFHFCKPD PRYYLEICEK MGVSPEDCVM YGDDELNDGE CEKVGMKFIR VR // ID Q9WZ95_THEMA Unreviewed; 393 AA. AC Q9WZ95; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 79. DE SubName: Full=Lipopolysaccharide biosynthesis protein {ECO:0000313|EMBL:AAD35711.1}; GN OrderedLocusNames=TM_0627 {ECO:0000313|EMBL:AAD35711.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35711.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35711.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35711.1; -; Genomic_DNA. DR PIR; H72352; H72352. DR RefSeq; NP_228436.1; NC_000853.1. DR RefSeq; WP_010865170.1; NC_000853.1. DR ProteinModelPortal; Q9WZ95; -. DR STRING; 243274.TM0627; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAD35711; AAD35711; TM_0627. DR GeneID; 897715; -. DR KEGG; tma:TM0627; -. DR KEGG; tmi:THEMA_01525; -. DR PATRIC; 23936167; VBITheMar51294_0637. DR eggNOG; ENOG4107T8Q; Bacteria. DR eggNOG; COG0438; LUCA. DR OMA; ICINDIR; -. DR OrthoDB; EOG6VXF9W; -. DR BioCyc; TMAR243274:GC6P-652-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 196 369 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 393 AA; 45853 MW; F70C3460AD96C6BC CRC64; MNMKVLLVNP VGEWGGAEKI FFLVSQIFQK TGFELYVLLG SRGILYEKLR NLNFNISIMN FPDLSENSIV IAGRRFQLPH HLLKNLRKIK ILSKKFWDYL RILKPDIIYL NNLRSLVLYY ETVRTYGKPC EAVVIWHEHG YQRSIIRQLI LDKIYLKFVD AVICVSKHLA NKHLKDVQQK LYVVHNGIPD ELNAIEKENV RYEYNNNKVL IIHPAFITYW KGQHLALKAV DLLVKRGVRN FEIWFFGEPR SKQDYKYFKK LKQFVRSKNL EKQVFFKGFS ANIIDEMLKA DIVISTSVED DPFPTILLEA SMIGKPVVTT DAGGSGEIVK NGETGFVVKK DKRELASALC ELIQNKELRD VFSKNARDRF LKEFSILAFE KRFLETLESI LRR // ID Q9WY48_THEMA Unreviewed; 780 AA. AC Q9WY48; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 110. DE RecName: Full=ATP-dependent DNA helicase RecG {ECO:0000256|RuleBase:RU363016}; DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363016}; GN Name=recG {ECO:0000256|RuleBase:RU363016}; GN OrderedLocusNames=TM_0205 {ECO:0000313|EMBL:AAD35297.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35297.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35297.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1GM5} RP X-RAY CRYSTALLOGRAPHY (3.24 ANGSTROMS) IN COMPLEX WITH ADP, AND RP DISULFIDE BONDS. RX PubMed=11595187; DOI=10.1016/S0092-8674(01)00501-3; RA Singleton M.R., Scaife S., Wigley D.B.; RT "Structural analysis of DNA replication fork reversal by RecG."; RL Cell 107:79-89(2001). CC -!- FUNCTION: Critical role in recombination and DNA repair. Helps CC process Holliday junction intermediates to mature products by CC catalyzing branch migration. Has a DNA unwinding activity CC characteristic of a DNA helicase with a 3'- to 5'- polarity. CC Unwinds branched duplex DNA (Y-DNA). CC {ECO:0000256|RuleBase:RU363016}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000256|RuleBase:RU363016}. CC -!- SIMILARITY: Belongs to the helicase family. RecG subfamily. CC {ECO:0000256|RuleBase:RU363016}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000256|RuleBase:RU363016}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35297.1; -; Genomic_DNA. DR PIR; G72405; G72405. DR RefSeq; NP_228020.1; NC_000853.1. DR RefSeq; WP_010865074.1; NC_000853.1. DR PDB; 1GM5; X-ray; 3.24 A; A=1-780. DR PDBsum; 1GM5; -. DR ProteinModelPortal; Q9WY48; -. DR SMR; Q9WY48; 7-755. DR STRING; 243274.TM0205; -. DR EnsemblBacteria; AAD35297; AAD35297; TM_0205. DR GeneID; 897075; -. DR KEGG; tma:TM0205; -. DR PATRIC; 23935282; VBITheMar51294_0207. DR eggNOG; ENOG4105CB5; Bacteria. DR eggNOG; COG1200; LUCA. DR InParanoid; Q9WY48; -. DR KO; K03655; -. DR OMA; IMSETND; -. DR OrthoDB; EOG6FNHKW; -. DR BioCyc; TMAR243274:GC6P-218-MONOMER; -. DR BRENDA; 3.6.4.12; 6331. DR EvolutionaryTrace; Q9WY48; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central. DR Gene3D; 1.20.120.630; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR004609; ATP-dep_DNA_helicase_RecG. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR028993; RecG_N. DR InterPro; IPR033454; RecG_wedge. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF17190; RecG_N; 1. DR Pfam; PF17191; RecG_wedge; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF69008; SSF69008; 1. DR TIGRFAMs; TIGR00643; recG; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1GM5}; KW ATP-binding {ECO:0000256|RuleBase:RU363016, KW ECO:0000313|EMBL:AAD35297.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA damage {ECO:0000256|RuleBase:RU363016}; KW DNA recombination {ECO:0000256|RuleBase:RU363016}; KW DNA repair {ECO:0000256|RuleBase:RU363016}; KW Helicase {ECO:0000256|RuleBase:RU363016, ECO:0000313|EMBL:AAD35297.1}; KW Hydrolase {ECO:0000256|RuleBase:RU363016, KW ECO:0000313|EMBL:AAD35297.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363016, KW ECO:0000313|EMBL:AAD35297.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 383 544 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 563 728 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT NP_BIND 367 369 ADP. {ECO:0000213|PDB:1GM5}. FT NP_BIND 399 403 ADP. {ECO:0000213|PDB:1GM5}. FT BINDING 436 436 ADP. {ECO:0000213|PDB:1GM5}. FT DISULFID 106 282 {ECO:0000213|PDB:1GM5}. SQ SEQUENCE 780 AA; 89931 MW; E7C7FDE6B6B85D41 CRC64; MLCSRYFTSS LFLWGEALPT LLEEFLNEVE KMLKNQVNTR RIHQLLKELD DPLLENKDLE EKLQAFLDYV KEIPNLPEAR KRYRIQKSLE MIEKLRSWFL IDYLECSGEE VDLSTDIQYA KGVGPNRKKK LKKLGIETLR DLLEFFPRDY EDRRKIFKLN DLLPGEKVTT QGKIVSVETK KFQNMNILTA VLSDGLVHVP LKWFNQDYLQ TYLKQLTGKE VFVTGTVKSN AYTGQYEIHN AEVTPKEGEY VRRILPIYRL TSGISQKQMR KIFEENIPSL CCSLKETLPE RILEKRKLLG VKDAYYGMHF PKTFYHLEKA RERLAYEELF VLQLAFQKIR KEREKHGGIP KKIEGKLAEE FIKSLPFKLT NAQKRAHQEI RNDMISEKPM NRLLQGDVGS GKTVVAQLAI LDNYEAGFQT AFMVPTSILA IQHYRRTVES FSKFNIHVAL LIGATTPSEK EKIKSGLRNG QIDVVIGTHA LIQEDVHFKN LGLVIIDEQH RFGVKQREAL MNKGKMVDTL VMSATPIPRS MALAFYGDLD VTVIDEMPPG RKEVQTMLVP MDRVNEVYEF VRQEVMRGGQ AFIVYPLIEE SDKLNVKSAV EMYEYLSKEV FPEFKLGLMH GRLSQEEKDR VMLEFAEGRY DILVSTTVIE VGIDVPRANV MVIENPERFG LAQLHQLRGR VGRGGQEAYC FLVVGDVGEE AMERLRFFTL NTDGFKIAEY DLKTRGPGEF FGVKQHGLSG FKVADLYRDL KLLEWAREDV QEIDVEGIEL PEEIKLIEVG // ID Q9X0L5_THEMA Unreviewed; 413 AA. AC Q9X0L5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Aminotransferase, putative {ECO:0000313|EMBL:AAD36207.1}; GN OrderedLocusNames=TM_1131 {ECO:0000313|EMBL:AAD36207.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36207.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36207.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1VP4} RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT RP LYS-248. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of Aminotransferase, putative (TM1131) from RT Thermotoga maritima at 1.82 A resolution."; RL Submitted (OCT-2004) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36207.1; -; Genomic_DNA. DR PIR; H72293; H72293. DR RefSeq; NP_228937.1; NC_000853.1. DR RefSeq; WP_010865270.1; NC_000853.1. DR PDB; 1VP4; X-ray; 1.82 A; A/B=1-413. DR PDBsum; 1VP4; -. DR ProteinModelPortal; Q9X0L5; -. DR SMR; Q9X0L5; 1-413. DR STRING; 243274.TM1131; -. DR EnsemblBacteria; AAD36207; AAD36207; TM_1131. DR GeneID; 898633; -. DR KEGG; tma:TM1131; -. DR PATRIC; 23937197; VBITheMar51294_1147. DR eggNOG; ENOG4105C1I; Bacteria. DR eggNOG; COG1167; LUCA. DR InParanoid; Q9X0L5; -. DR OMA; RLNFTYV; -. DR OrthoDB; EOG699754; -. DR BioCyc; TMAR243274:GC6P-1160-MONOMER; -. DR EvolutionaryTrace; Q9X0L5; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VP4}; KW Aminotransferase {ECO:0000313|EMBL:AAD36207.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD36207.1}. FT DOMAIN 50 398 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. FT MOD_RES 248 248 N6-(pyridoxal phosphate)lysine. FT {ECO:0000213|PDB:1VP4}. SQ SEQUENCE 413 AA; 47136 MW; 045709F43CB93894 CRC64; MVVNLEGKIS KIGQNMKSSI IREILKFAAD KDAISFGGGV PDPETFPRKE LAEIAKEIIE KEYHYTLQYS TTEGDPVLKQ QILKLLERMY GITGLDEDNL IFTVGSQQAL DLIGKLFLDD ESYCVLDDPA YLGAINAFRQ YLANFVVVPL EDDGMDLNVL ERKLSEFDKN GKIKQVKFIY VVSNFHNPAG VTTSLEKRKA LVEIAEKYDL FIVEDDPYGA LRYEGETVDP IFKIGGPERV VLLNTFSKVL APGLRIGMVA GSKEFIRKIV QAKQSADLCS PAITHRLAAR YLERYDLLEQ LKPTIELYRR KRTVMLNALE EYFSDIPGVK WVKSEGGLFI WLTLPEGFDT WEMFEYAKRK KVFYVPGRVF KVYDEPSPSM RLSFCLPPDE KIVEGIKRLR EVVLEYGKEK HLL // ID Q9X011_THEMA Unreviewed; 374 AA. AC Q9X011; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 79. DE SubName: Full=Flagellar biosynthesis protein FlhB {ECO:0000313|EMBL:AAD35990.1}; GN OrderedLocusNames=TM_0909 {ECO:0000313|EMBL:AAD35990.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35990.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35990.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35990.1; -; Genomic_DNA. DR PIR; D72319; D72319. DR RefSeq; NP_228717.1; NC_000853.1. DR RefSeq; WP_008193133.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X011; -. DR STRING; 243274.TM0909; -. DR EnsemblBacteria; AAD35990; AAD35990; TM_0909. DR GeneID; 898583; -. DR KEGG; tma:TM0909; -. DR KEGG; tmw:THMA_0931; -. DR PATRIC; 23936749; VBITheMar51294_0923. DR eggNOG; ENOG4105D00; Bacteria. DR eggNOG; COG1377; LUCA. DR InParanoid; Q9X011; -. DR KO; K02401; -. DR OMA; KMMQEIP; -. DR OrthoDB; EOG6FRD1F; -. DR BioCyc; TMAR243274:GC6P-939-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR Gene3D; 3.40.1690.10; -; 1. DR InterPro; IPR006136; FlhB. DR InterPro; IPR006135; T3SS_substrate_exporter. DR InterPro; IPR029025; T3SS_substrate_exporter_C. DR PANTHER; PTHR30531; PTHR30531; 1. DR Pfam; PF01312; Bac_export_2; 1. DR PRINTS; PR00950; TYPE3IMSPROT. DR SUPFAM; SSF160544; SSF160544; 1. DR TIGRFAMs; TIGR00328; flhB; 1. PE 4: Predicted; KW Cell projection {ECO:0000313|EMBL:AAD35990.1}; KW Cilium {ECO:0000313|EMBL:AAD35990.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35990.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 78 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 108 129 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 374 AA; 43012 MW; 7F5DB5AE434EB0B6 CRC64; MGGHGSENLS TQLERYSGTS WEIELLLFAE AERTERATPR KRRRVREEGR APVSRELNMA VTFLVFALAL KIFGYQGVER ITEDVQVFLS FEETEDLLMN AVNIFKDVLL IVGAFVVFSM VAGVMIGALQ TRFLFAPKAL KPDLNRINPI EGFKRLFSLR SLVELLKSVL KVAIVGIVVY QVLKNRWDEM ILLTEMSVND AFANFWDITS EITLKSGMIL LALAVFDYFY QRWEFEKSIR MTKQEVKDEL KEVEGNPEIK RRQRQMMYDI LRRRMLEEVP KADVVITNPT HFAVALKYDP DTMNAPVVVA KGVDHLAFKI IEIAKENDVP VLRNPSLARA LYYKTEIGEE IPVEFYRIVA EVLVYVYAKK GVRI // ID Q9X0M0_THEMA Unreviewed; 299 AA. AC Q9X0M0; G4FEL2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Branched chain amino acid ABC transporter, permease protein {ECO:0000313|EMBL:AAD36212.1}; GN OrderedLocusNames=TM_1136 {ECO:0000313|EMBL:AAD36212.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36212.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36212.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|SAAS:SAAS00582814}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36212.1; -; Genomic_DNA. DR PIR; D72290; D72290. DR RefSeq; NP_228942.1; NC_000853.1. DR RefSeq; WP_004080271.1; NZ_CP011107.1. DR STRING; 243274.TM1136; -. DR EnsemblBacteria; AAD36212; AAD36212; TM_1136. DR GeneID; 898628; -. DR KEGG; tma:TM1136; -. DR KEGG; tmi:THEMA_08665; -. DR KEGG; tmw:THMA_1159; -. DR PATRIC; 23937207; VBITheMar51294_1152. DR eggNOG; ENOG4105C32; Bacteria. DR eggNOG; COG0559; LUCA. DR KO; K01997; -. DR OMA; YRTKIGM; -. DR OrthoDB; EOG6H1Q47; -. DR BioCyc; TMAR243274:GC6P-1165-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00476327}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAAS:SAAS00476327, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00476193}. FT TRANSMEM 12 35 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 117 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 142 165 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 213 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 273 292 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 299 AA; 32109 MW; 6419DC7B25DEED93 CRC64; MVFFLQNLFN GIMLGGLYAL IAIGYTMVYG ILRLINFAHG DVMMMGVYFA FYAATLLSLN PLFSAIVAIL GAALLGFLID RVAYKPLRNA PRISALITAI GVSFFLESLA VVVFGAIPKS FLKVFKDRTI LNKVLTVAGA RIPLLTFLVI FITAVILIVL FFIVYRTKIG MAMRAISMDI PTTALMGVNV DAVIGFTFAL GSALAAASGI MWAMRFPNVH PYMGFMPGLK AFIAAVFGGI GSIPGAVLGG VLLGLIEIFL AAYFPAVMGY RDAFAFIILI IILLVKPSGL LGKKIVEKV // ID Q9X1U2_THEMA Unreviewed; 454 AA. AC Q9X1U2; G4FFZ4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 87. DE SubName: Full=Cytoplasmic axial filament protein, putative {ECO:0000313|EMBL:AAD36673.1}; GN OrderedLocusNames=TM_1606 {ECO:0000313|EMBL:AAD36673.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36673.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36673.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36673.1; -; Genomic_DNA. DR PIR; B72235; B72235. DR RefSeq; NP_229406.1; NC_000853.1. DR RefSeq; WP_004082053.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1U2; -. DR STRING; 243274.TM1606; -. DR EnsemblBacteria; AAD36673; AAD36673; TM_1606. DR GeneID; 897938; -. DR KEGG; tma:TM1606; -. DR KEGG; tmw:THMA_1646; -. DR PATRIC; 23938186; VBITheMar51294_1625. DR eggNOG; ENOG4105C03; Bacteria. DR eggNOG; COG1530; LUCA. DR InParanoid; Q9X1U2; -. DR KO; K08301; -. DR OMA; QVDSREN; -. DR OrthoDB; EOG6PCPTH; -. DR BioCyc; TMAR243274:GC6P-1652-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GOC. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G. DR InterPro; IPR004659; RNase_E/G. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF10150; RNase_E_G; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00757; RNaseEG; 1. DR PROSITE; PS50126; S1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 19 98 S1 motif. {ECO:0000259|PROSITE:PS50126}. SQ SEQUENCE 454 AA; 52417 MW; 4F24BDB71AD55EC2 CRC64; MDDGELEEVF FDEIETIAGK IYLGRIEKIV PGLEAAFVKI GKGRNAFLKL SEINEAYRKT VLKGQEVKEG QKILVQVKKD ASGKKGPQVT PQIGIADRFV VIFPFKKVIG VSRKIEDASE RRRLRTIAFS LRKKYGVGVI MRTAAEGVDE EEIIKNFERA LEKWNQVLQK FRRSRKPKLL YEEDPVEQII KEKVNSKIDK LIYNDRSLLE TLQKYLQNLP KKPEIEYVEG DLFEKFSVYE RLKKLLSRTV PLKSGGNIVI DRTEALTVID VNSESYTDAE NQEELALKTN MEAIEEIVRQ LILRNIGGIV VIDFIKQKDP KSYEKLLSRF KEVAKRDGTR IEIFGFTNLG LLEITRKRTT RPLDTLLFTR CPVCSGTGKV LSQKILLKRI REDLKKLKDF EEVTLKVHPN MSGYFKREDI KKLQKEFKVK LNLDYGWHDP NSYEIKAKTK KGGK // ID Q9WZ99_THEMA Unreviewed; 434 AA. AC Q9WZ99; G4FDJ2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 87. DE SubName: Full=Lipopolysaccharide biosynthesis protein {ECO:0000313|EMBL:AAD35715.1}; GN OrderedLocusNames=TM_0631 {ECO:0000313|EMBL:AAD35715.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35715.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35715.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35715.1; -; Genomic_DNA. DR PIR; D72353; D72353. DR RefSeq; NP_228440.1; NC_000853.1. DR RefSeq; WP_004081170.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ99; -. DR STRING; 243274.TM0631; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAD35715; AAD35715; TM_0631. DR GeneID; 897727; -. DR KEGG; tma:TM0631; -. DR KEGG; tmi:THEMA_01505; -. DR KEGG; tmw:THMA_0647; -. DR PATRIC; 23936175; VBITheMar51294_0641. DR eggNOG; ENOG4107W3N; Bacteria. DR eggNOG; ENOG410ZWDI; LUCA. DR OMA; RFNIIGN; -. DR OrthoDB; EOG6J48J1; -. DR BioCyc; TMAR243274:GC6P-656-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 243 407 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 434 AA; 49787 MW; 49923502F59FDDED CRC64; MEKRGEVKEK RKLSILLINN YFPPEIGAAS HLYFYLAREL SKRGHEVTVL TGIPRYNIPK ETYNQYLRRM KNKKFVIENI SDCADIEVIR VRLPYIERHQ LLRRGVEHFE IALKMFSYAK EYLRNKRVDV SLVYSPPITL YKTAWKVKRL KDAPFVLNVQ DLFPQAAIDL GILKNPLLIR LFKQVEKKAY QLADLITVHS ERNKEFVKSV LNGDGRKVLV MENWVDENEI KPGDKINDFS IKHGLTEKFV VSFAGTLGFS QDMEVIIRAA NELKEYKDIV FIIVGNGVRL EESKKLAESL NLQNIRFIPS VPREIYPLVL HSSDVSLATL TKDVKTPVVP SKILSIMSAG IPVIAVMNLE GDAPKLVEKA NAGFAIPAGD YKSLAEKILL LYKNPELRES LGRNGRRYIE ENLSSRKAAE KYEKIFLDAL RRDK // ID Q9S5Y0_THEMA Unreviewed; 247 AA. AC Q9S5Y0; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 11-MAY-2016, entry version 113. DE SubName: Full=Response regulator DrrA {ECO:0000313|EMBL:AAD36722.1}; GN OrderedLocusNames=TM_1655 {ECO:0000313|EMBL:AAD36722.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36722.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36722.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains OmpR/PhoB-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00583175}. CC -!- SIMILARITY: Contains response regulatory domain. CC {ECO:0000256|SAAS:SAAS00122777}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36722.1; -; Genomic_DNA. DR PIR; D72228; D72228. DR RefSeq; NP_229455.1; NC_000853.1. DR RefSeq; WP_010865376.1; NC_000853.1. DR ProteinModelPortal; Q9S5Y0; -. DR STRING; 243274.TM1655; -. DR EnsemblBacteria; AAD36722; AAD36722; TM_1655. DR GeneID; 897913; -. DR KEGG; tma:TM1655; -. DR PATRIC; 23938284; VBITheMar51294_1674. DR eggNOG; ENOG4105CK6; Bacteria. DR eggNOG; COG0745; LUCA. DR InParanoid; Q9S5Y0; -. DR KO; K02483; -. DR OMA; ICNIIER; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1701-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd. DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF00486; Trans_reg_C; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00862; Trans_reg_C; 1. DR SUPFAM; SSF46894; SSF46894; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS51755; OMPR_PHOB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00582919}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00275006}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00275006}; KW Two-component regulatory system {ECO:0000256|SAAS:SAAS00583142}. FT DOMAIN 13 129 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT DOMAIN 143 242 OmpR/PhoB-type DNA-binding. FT {ECO:0000259|PROSITE:PS51755}. SQ SEQUENCE 247 AA; 28423 MW; 4D4D9FC0E0903F4B CRC64; MYPLGGSKMA KKKILVVDDD PAILELVGYN LSKEGYEVLK AYDGEEALKI ANDEDVDMFI VDIMLPGIDG FELVRKIRSM EKYKNTPVIF LSAKGEEFDK VLGLELGADD YITKPFSVRE LLARVKAIFR RLSTATQSKE ERPKKIIAKD LEIDVEKYEV KVRGKKVNLT PLEFELLRFL AENEGKVFSR DVLLDKLWGY DYYGDTRTVD VHIRRLRTKI EEDPSNPKYI ITVRGKGYKF RDPGKED // ID Q9WXU3_THEMA Unreviewed; 1285 AA. AC Q9WXU3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 85. DE SubName: Full=ComE protein, putative {ECO:0000313|EMBL:AAD35182.1}; GN OrderedLocusNames=TM_0088 {ECO:0000313|EMBL:AAD35182.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35182.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35182.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the GSP D family. CC {ECO:0000256|RuleBase:RU004003}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35182.1; -; Genomic_DNA. DR PIR; B72420; B72420. DR RefSeq; NP_227904.1; NC_000853.1. DR RefSeq; WP_010865047.1; NC_000853.1. DR STRING; 243274.TM0088; -. DR EnsemblBacteria; AAD35182; AAD35182; TM_0088. DR GeneID; 896915; -. DR KEGG; tma:TM0088; -. DR KEGG; tmi:THEMA_04365; -. DR PATRIC; 23935016; VBITheMar51294_0086. DR eggNOG; ENOG4105E4G; Bacteria. DR eggNOG; COG4796; LUCA. DR OMA; FPRSKER; -. DR OrthoDB; EOG6423BN; -. DR BioCyc; TMAR243274:GC6P-88-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR004846; T2SS/T3SS. DR Pfam; PF00263; Secretin; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 501 528 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1285 AA; 145210 MW; 057435F821FB0EA5 CRC64; MVSVRRILLI LVMLMFSVLF SAELVGVLPK IENDRVIIEI QISSPVEDVS AEMNSSKTVF SIFMKGVQMK ISRFMVPVGV GPVEGVRVVN VGNGVMVSAS LLVPFSGSYR VEDKTIVMEF PRSKERIDVS FENMPFEDMV KYLAERLNLN VIVSDSVKSA TTSLKLNDVT PEDALRDLLV TFGEVAYAYF PDGTMFIGKY EEVSGRFQRF WGIYRVENQT VADRIKSLIS QEAMIDYLPS KSVLFVYGTS EEHDLVASLL SVSPPLQQKE VSFSVDSGRV EELLTALKSV YQFEYHLLKP VSRMILVGDS ETISKVERYI KILETREQVS VEEQVQIPAK KFVFYAYDPE SAASLITLLL GIDAQPFKDM NLVVCQVPID EEQKLIDFIA ENNLELGEMF YLDIKKGEED FLREAAQFLG IPDSRLKFLN IDGENVKAAI SVPKAAYEKV SPVLEKLLSL RRKNFIVKSV ELKEEIQQEM IDAITRMYGV SMEKIGNFLF IEGARSSVEN VEEQLKKLLS EHTQFLKIAL KTENVEDLGR FMKEKYGVEF EYFSSLKVAM LSGKEEENVQ KAAEELQIIS SEERIIRFVK KTENVPIDKA KNVVLQLYSV SIEELGNELV VIGEREEVEK AADLLQKIFS SEVEISRDFV KLPSWIDEQE KLLEVVKNSA GITYEILDGV VYFEGTKENV EKAKELFSDI VEKLGEVRKE ETVEFLEVNS SFPVDEFINL SGKLYPDVTC FSLDQLGLLV LKGSSEAVED LSSMYRSFFE RHQKIVKENV FDRLMLEVPS GFSFEEFKTF LEVLVPEVKQ VVYLDKLNLL LVEVPVSQSE RVKSLLDTFL KKEEAVSEKK AVKSVTIPSG VNPDELSSYL KKLLRNVEIT VFPNMGQMIV EGPENEVEKA VELVEAEKEK IVLKERKDYV KVSDGKLTIN AEDAPLYDLL EEIASELGIS VMFVSIPSEK ITMKADNVAW EKFIDLISQN YGYLFDNKNG VYVVSKPKQD LARRYIYDVP HNFDQIKALI EFYGGTVYVD SLNNFMVVTG ISETIKRELD NIIEKLKKPT KQIEISAKIV DRSLIDRLSK ETGLELTGEN VNVGSSGAEI SFSVTDYLDF EKIFGEILNN TLSLQFSDQK TNTLDDILAS PRIVTTSGKE ARILIGDRIP YVTDTNGDGT PEVQFLETGI ELSITPFVRS DDTIELDLFV KASEPGNYIN EVPGERTREA QTHLIVKNGS TITIGGLIRE VTNVTESKLP FLGDLPVIGQ FFRTKSENKE KRDLVIFLTV RVVEP // ID Q9X0I5_THEMA Unreviewed; 189 AA. AC Q9X0I5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 84. DE RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039}; DE EC=3.1.4.- {ECO:0000256|RuleBase:RU362039}; GN OrderedLocusNames=TM_1101 {ECO:0000313|EMBL:AAD36177.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36177.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36177.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|RuleBase:RU362039}; CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CC YfcE family. {ECO:0000256|RuleBase:RU362039}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36177.1; -; Genomic_DNA. DR PIR; G72294; G72294. DR RefSeq; NP_228907.1; NC_000853.1. DR RefSeq; WP_010865263.1; NC_000853.1. DR ProteinModelPortal; Q9X0I5; -. DR STRING; 243274.TM1101; -. DR EnsemblBacteria; AAD36177; AAD36177; TM_1101. DR GeneID; 898664; -. DR KEGG; tma:TM1101; -. DR PATRIC; 23937135; VBITheMar51294_1116. DR eggNOG; ENOG4108RE9; Bacteria. DR eggNOG; COG0622; LUCA. DR InParanoid; Q9X0I5; -. DR KO; K07095; -. DR OMA; DILYHGP; -. DR OrthoDB; EOG6W45XC; -. DR BioCyc; TMAR243274:GC6P-1130-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29. DR PANTHER; PTHR11124; PTHR11124; 1. DR Pfam; PF12850; Metallophos_2; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00040; yfcE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000256|RuleBase:RU362039}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 168 Metallophos_2. FT {ECO:0000259|Pfam:PF12850}. SQ SEQUENCE 189 AA; 20881 MW; 3B52858DE5D1915A CRC64; MTLRILVISD THGSLSCTEK ALKSAGNFDE IWHLGDVLYH GPRNPLPEGY SPKELASLLK KHRVKYIRGN CDADVDIRVL EIPEMPRIGM EFLGDVKILL VHGDQFEYEG GDPVSLAQAH GCSVVLFGHT HVPLAERCEG VLLLNPGSVS LPKSEAGPTF GIIDMDEKKF YLCSLEGDVL KEVMLVERE // ID Q9WXQ5_THEMA Unreviewed; 108 AA. AC Q9WXQ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAD35143.1}; GN OrderedLocusNames=TM_0048 {ECO:0000313|EMBL:AAD35143.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35143.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35143.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35143.1; -; Genomic_DNA. DR PIR; E72426; E72426. DR RefSeq; NP_227864.1; NC_000853.1. DR RefSeq; WP_010865038.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WXQ5; -. DR STRING; 243274.TM0048; -. DR EnsemblBacteria; AAD35143; AAD35143; TM_0048. DR GeneID; 896872; -. DR KEGG; tma:TM0048; -. DR KEGG; tmw:THMA_0044; -. DR PATRIC; 23934936; VBITheMar51294_0046. DR eggNOG; ENOG4108VIJ; Bacteria. DR eggNOG; COG1943; LUCA. DR InParanoid; Q9WXQ5; -. DR KO; K07491; -. DR OMA; HIHILAE; -. DR OrthoDB; EOG6PP9P5; -. DR BioCyc; TMAR243274:GC6P-48-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR Gene3D; 3.30.70.1290; -; 1. DR InterPro; IPR002686; Transposase_17. DR Pfam; PF01797; Y1_Tnp; 1. DR SMART; SM01321; Y1_Tnp; 1. DR SUPFAM; SSF143422; SSF143422; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 108 AA; 12548 MW; 390323CB077CD45C CRC64; MTEKQPRKPF RFRGTGKRLA CWSCSCYDWV LSLSIQPDHV HLFVSAPPRL APAQIVNLFK GVSSKKLLEK FPHLRTREGL WSRTYYVGSV GTVSEETIRR YIEECQDM // ID Q9S5Y2_THEMA Unreviewed; 556 AA. AC Q9S5Y2; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134}; DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134}; GN OrderedLocusNames=TM_1840 {ECO:0000313|EMBL:AAD36902.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36902.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36902.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic CC linkages in polysaccharides containing three or more (1->4)-alpha- CC linked D-glucose units. {ECO:0000256|RuleBase:RU361134}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000256|RuleBase:RU361134}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36902.1; -; Genomic_DNA. DR PIR; C72204; C72204. DR RefSeq; NP_229636.1; NC_000853.1. DR RefSeq; WP_010865416.1; NC_000853.1. DR ProteinModelPortal; Q9S5Y2; -. DR STRING; 243274.TM1840; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblBacteria; AAD36902; AAD36902; TM_1840. DR GeneID; 897109; -. DR KEGG; tma:TM1840; -. DR PATRIC; 23938669; VBITheMar51294_1861. DR eggNOG; ENOG4108IUK; Bacteria. DR eggNOG; COG0366; LUCA. DR InParanoid; Q9S5Y2; -. DR KO; K01176; -. DR OMA; IREPFLW; -. DR OrthoDB; EOG6RZB0T; -. DR BioCyc; TMAR243274:GC6P-1891-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.80; -; 2. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR015902; Glyco_hydro_13. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10357; PTHR10357; 2. DR Pfam; PF00128; Alpha-amylase; 2. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; SSF51445; 2. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361134}; KW Hydrolase {ECO:0000256|RuleBase:RU361134}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 556 Alpha-amylase. {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004332512. FT DOMAIN 60 425 Aamy. {ECO:0000259|SMART:SM00642}. SQ SEQUENCE 556 AA; 65068 MW; 8D6CE1BF400C8195 CRC64; MKVVKKPFLL LAFVFLLFLT SCFQTSMSQS LVSSNPHSNS TNTDGTSSNL EEVKYPVVYE IFIRSFYDRD GNGVGDLNGV SQKVDYLKEL GVDAVWFMPF NEAVSYHGYD ITDYYNVEKD YGTMEDLENM IQVLHENGIK VIMDLVINHT SDEHPWFKDA VENTTSSPYW DYYIMSLEDH SGQDHWHWKI NSKGQKVWYF GLFGYNMPDL NHDSQKVREE VKKIVDFWIS KGVDGFRIDA AKHIYGWSWD DGIQESAEYF EWFRDYVLSK KPDAILVGEV FSGNTYDLSL YPIPVFNFAL MYSIRNYPEG QDGMIENNWV EESFLFLENH DLHRFFSHLQ EHYKKFSESD YEFIKKRAAL WYFLIFTLKG SPVIYYGGEI GTRGFKWHGP VYDEPVREPM QWYASGTGEG QTFWTKEVYK NAGITFGNAD VDGCIYDDPY DGFSVEEQES DPKSLLNFIR FILNFRKDHD AILNGDQTIF RDWKNLIAFY RESSNEKLLV VLNPDPVWQN SFTFEENMTM ILEVDFENFI WNESNVSFSA GESFTVDPMK AYIFKK // ID Q9WYE2_THEMA Unreviewed; 449 AA. AC Q9WYE2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 107. DE SubName: Full=Alpha-L-fucosidase, putative {ECO:0000313|EMBL:AAD35394.1}; GN OrderedLocusNames=TM_0306 {ECO:0000313|EMBL:AAD35394.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35394.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35394.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1HL8, ECO:0000213|PDB:1HL9, ECO:0000213|PDB:1ODU} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=14715651; DOI=10.1074/jbc.M313783200; RA Sulzenbacher G., Bignon C., Nishimura T., Tarling C.A., Withers S.G., RA Henrissat B., Bourne Y.; RT "Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights RT into the catalytic mechanism and the molecular basis for RT fucosidosis."; RL J. Biol. Chem. 279:13119-13128(2004). RN [3] {ECO:0000213|PDB:2ZWY} RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS), AND DISULFIDE BONDS. RA Wu H.-J., Ho C.-W., Ko T.P., Popat S.D., Lin C.-H., Wang A.H.-J.; RT "Structural Basis of alpha-Fucosidase Inhibition by Iminocyclitols RT with Ki Ranging from Micro- to Picomolar."; RL Submitted (DEC-2008) to the PDB data bank. RN [4] {ECO:0000213|PDB:2WSP} RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH FUCOSE, AND RP DISULFIDE BONDS. RX PubMed=19875083; DOI=10.1016/j.chembiol.2009.09.013; RA Cobucci-Ponzano B., Conte F., Bedini E., Corsaro M.M., Parrilli M., RA Sulzenbacher G., Lipski A., Dal Piaz F., Lepore L., Rossi M., RA Moracci M.; RT "beta-Glycosyl azides as substrates for alpha-glycosynthases: RT preparation of efficient alpha-L-fucosynthases."; RL Chem. Biol. 16:1097-1108(2009). RN [5] {ECO:0000213|PDB:2ZWZ, ECO:0000213|PDB:2ZX5, ECO:0000213|PDB:2ZX6} RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=19967696; DOI=10.1002/anie.200905597; RA Wu H.J., Ho C.W., Ko T.P., Popat S.D., Lin C.H., Wang A.H.; RT "Structural basis of alpha-fucosidase inhibition by iminocyclitols RT with K(i) values in the micro- to picomolar range."; RL Angew. Chem. Int. Ed. 49:337-340(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35394.1; -; Genomic_DNA. DR PIR; G72393; G72393. DR RefSeq; NP_228118.1; NC_000853.1. DR RefSeq; WP_010865090.1; NC_000853.1. DR PDB; 1HL8; X-ray; 2.40 A; A/B=1-449. DR PDB; 1HL9; X-ray; 2.25 A; A/B=1-449. DR PDB; 1ODU; X-ray; 2.80 A; A/B=1-449. DR PDB; 2WSP; X-ray; 2.65 A; A/B=1-449. DR PDB; 2ZWY; X-ray; 2.75 A; A/B=1-449. DR PDB; 2ZWZ; X-ray; 2.36 A; A/B=1-449. DR PDB; 2ZX5; X-ray; 2.65 A; A/B=1-449. DR PDB; 2ZX6; X-ray; 2.42 A; A/B=1-449. DR PDB; 2ZX7; X-ray; 2.48 A; A/B=1-449. DR PDB; 2ZX8; X-ray; 2.33 A; A/B=1-449. DR PDB; 2ZX9; X-ray; 2.62 A; A/B=1-449. DR PDB; 2ZXA; X-ray; 2.57 A; A/B=1-449. DR PDB; 2ZXB; X-ray; 2.61 A; A/B=1-449. DR PDB; 2ZXD; X-ray; 2.15 A; A/B=1-449. DR PDBsum; 1HL8; -. DR PDBsum; 1HL9; -. DR PDBsum; 1ODU; -. DR PDBsum; 2WSP; -. DR PDBsum; 2ZWY; -. DR PDBsum; 2ZWZ; -. DR PDBsum; 2ZX5; -. DR PDBsum; 2ZX6; -. DR PDBsum; 2ZX7; -. DR PDBsum; 2ZX8; -. DR PDBsum; 2ZX9; -. DR PDBsum; 2ZXA; -. DR PDBsum; 2ZXB; -. DR PDBsum; 2ZXD; -. DR ProteinModelPortal; Q9WYE2; -. DR SMR; Q9WYE2; 7-448. DR STRING; 243274.TM0306; -. DR CAZy; GH29; Glycoside Hydrolase Family 29. DR DNASU; 897238; -. DR EnsemblBacteria; AAD35394; AAD35394; TM_0306. DR GeneID; 897238; -. DR KEGG; tma:TM0306; -. DR KEGG; tmi:THEMA_03195; -. DR PATRIC; 23935491; VBITheMar51294_0311. DR eggNOG; ENOG4105ENQ; Bacteria. DR eggNOG; COG3669; LUCA. DR KO; K01206; -. DR OMA; TREYSNT; -. DR OrthoDB; EOG6GXTRQ; -. DR BioCyc; TMAR243274:GC6P-319-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro. DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR016286; FUC_metazoa-typ. DR InterPro; IPR000933; Glyco_hydro_29. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10030; PTHR10030; 2. DR Pfam; PF01120; Alpha_L_fucos; 1. DR PIRSF; PIRSF001092; Alpha-L-fucosidase; 1. DR PRINTS; PR00741; GLHYDRLASE29. DR SMART; SM00812; Alpha_L_fucos; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1HL8, ECO:0000213|PDB:1HL9, KW ECO:0000213|PDB:1ODU, ECO:0000213|PDB:2WSP}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT REGION 66 67 Fucose binding. {ECO:0000213|PDB:2WSP}. FT REGION 128 129 Fucose binding. {ECO:0000213|PDB:2WSP}. FT BINDING 34 34 Fucose. {ECO:0000213|PDB:2WSP}. FT BINDING 290 290 Fucose. {ECO:0000213|PDB:2WSP}. FT DISULFID 364 365 {ECO:0000213|PDB:1HL8, FT ECO:0000213|PDB:1HL9, FT ECO:0000213|PDB:1ODU}. FT DISULFID 380 380 Interchain. {ECO:0000213|PDB:2WSP, FT ECO:0000213|PDB:2ZWY, FT ECO:0000213|PDB:2ZWZ}. SQ SEQUENCE 449 AA; 52205 MW; B213C72A1ED9EA5C CRC64; MISMKPRYKP DWESLREHTV PKWFDKAKFG IFIHWGIYSV PGWATPTGEL GKVPMDAWFF QNPYAEWYEN SLRIKESPTW EYHVKTYGEN FEYEKFADLF TAEKWDPQEW ADLFKKAGAK YVIPTTKHHD GFCLWGTKYT DFNSVKRGPK RDLVGDLAKA VREAGLRFGV YYSGGLDWRF TTEPIRYPED LSYIRPNTYE YADYAYKQVM ELVDLYLPDV LWNDMGWPEK GKEDLKYLFA YYYNKHPEGS VNDRWGVPHW DFKTAEYHVN YPGDLPGYKW EFTRGIGLSF GYNRNEGPEH MLSVEQLVYT LVDVVSKGGN LLLNVGPKGD GTIPDLQKER LLGLGEWLRK YGDAIYGTSV WERCCAKTED GTEIRFTRKC NRIFVIFLGI PTGEKIVIED LNLSAGTVRH FLTGERLSFK NVGKNLEITV PKKLLETDSI TLVLEAVEE // ID Q9X004_THEMA Unreviewed; 220 AA. AC Q9X004; G4FCS4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 111. DE SubName: Full=RNA polymerase sigma-28 factor, putative {ECO:0000313|EMBL:AAD35983.1}; GN OrderedLocusNames=TM_0902 {ECO:0000313|EMBL:AAD35983.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35983.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35983.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the sigma-70 factor family. CC {ECO:0000256|SAAS:SAAS00565852}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35983.1; -; Genomic_DNA. DR PIR; E72318; E72318. DR RefSeq; NP_228710.1; NC_000853.1. DR RefSeq; WP_004080667.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X004; -. DR STRING; 243274.TM0902; -. DR EnsemblBacteria; AAD35983; AAD35983; TM_0902. DR GeneID; 898576; -. DR KEGG; tma:TM0902; -. DR KEGG; tmi:THEMA_00125; -. DR KEGG; tmw:THMA_0924; -. DR PATRIC; 23936735; VBITheMar51294_0916. DR eggNOG; ENOG4105DN4; Bacteria. DR eggNOG; COG1191; LUCA. DR KO; K02405; -. DR OMA; HEEANPL; -. DR OrthoDB; EOG661H9F; -. DR BioCyc; TMAR243274:GC6P-932-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:InterPro. DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR000943; RNA_pol_sigma70. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR007630; RNA_pol_sigma70_r4. DR InterPro; IPR012845; RNA_pol_sigma_FliA_WhiG. DR InterPro; IPR013325; RNA_pol_sigma_r2. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04542; Sigma70_r2; 1. DR Pfam; PF04545; Sigma70_r4; 1. DR PRINTS; PR00046; SIGMA70FCT. DR SUPFAM; SSF88659; SSF88659; 2. DR SUPFAM; SSF88946; SSF88946; 1. DR TIGRFAMs; TIGR02479; FliA_WhiG; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00457605}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Sigma factor {ECO:0000256|SAAS:SAAS00458134}; KW Transcription {ECO:0000256|SAAS:SAAS00458134}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00458134}. FT DOMAIN 8 78 Sigma70_r2. {ECO:0000259|Pfam:PF04542}. FT DOMAIN 162 211 Sigma70_r4. {ECO:0000259|Pfam:PF04545}. SQ SEQUENCE 220 AA; 25438 MW; F25780346B63C0E3 CRC64; MWNKESVIRS LLPFIKRIAE DLAQTLPPNV EVDDLIQEGI VAALSSLERY DPSKASFTTF IMKRVKGAMY DYLRKIDWMP RNLRKNVKMI ERVIYESEEF PSDEEIARKT GLELKEVVRA RNEMMRKQLL MIDAMEDEIV LKTEGPDENA YRELLVEEMK KAIEKLSDKE KLVLSLRFEK GLSLKEIARV LGVSESRVSQ IISKSLLKIK KEVMGDDQAG // ID Q9X0A4_THEMA Unreviewed; 365 AA. AC Q9X0A4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36076.1}; GN OrderedLocusNames=TM_1011 {ECO:0000313|EMBL:AAD36076.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36076.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36076.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36076.1; -; Genomic_DNA. DR PIR; C72308; C72308. DR RefSeq; NP_228817.1; NC_000853.1. DR RefSeq; WP_010865242.1; NC_000853.1. DR ProteinModelPortal; Q9X0A4; -. DR STRING; 243274.TM1011; -. DR EnsemblBacteria; AAD36076; AAD36076; TM_1011. DR GeneID; 897199; -. DR KEGG; tma:TM1011; -. DR PATRIC; 23936951; VBITheMar51294_1024. DR eggNOG; ENOG4107G4B; Bacteria. DR eggNOG; COG1672; LUCA. DR InParanoid; Q9X0A4; -. DR KO; K06921; -. DR OMA; GINTWSA; -. DR OrthoDB; EOG67Q97C; -. DR BioCyc; TMAR243274:GC6P-1040-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 19 259 ATPase_2. {ECO:0000259|Pfam:PF01637}. SQ SEQUENCE 365 AA; 42368 MW; 44AB71B438979E7F CRC64; MEVIDLLFSL TPKTKKEDLF DRERELKDLE KLLETYPIVV ITGLRRVGKS SLVKVFLNKS DLLHITVDGR RLYETSGGNI SSHHLTRFLG EELSRISKSQ KLLNVLKRVR GITVSGTSIE LNPKEFSLSD LLEKLNETAK RRKKKIVIFF DEAQYLRYYG SRGGNDLLAL FAYCYDNFEN VRFIISGSEV GVLHDFLKLE DYSSPLHGRG IGFLTVRPFT FDQSVDFLME GFREVGEKIN FDVEEIVREI DGIVGYLVLF GVKYLEKKKK DEALKEVFHA VKALFEKEME ELRKRSERYP FILRQIARGI NTWSALKNIF RAKGDFIGDS RLYSLLETLE KMSFIEKTQS GYRIVDPVFE RILRE // ID Q9X067_THEMA Unreviewed; 422 AA. AC Q9X067; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36051.1}; GN OrderedLocusNames=TM_0972 {ECO:0000313|EMBL:AAD36051.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36051.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36051.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains GGDEF domain. CC {ECO:0000256|SAAS:SAAS00496774}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36051.1; -; Genomic_DNA. DR PIR; A72309; A72309. DR RefSeq; NP_228780.1; NC_000853.1. DR RefSeq; WP_010865229.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X067; -. DR STRING; 243274.TM0972; -. DR EnsemblBacteria; AAD36051; AAD36051; TM_0972. DR GeneID; 898718; -. DR KEGG; tma:TM0972; -. DR KEGG; tmw:THMA_0995; -. DR PATRIC; 23936873; VBITheMar51294_0985. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR InParanoid; Q9X067; -. DR OMA; HTIIEFF; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1002-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR033425; MASE3. DR InterPro; IPR029787; Nucleotide_cyclase. DR Pfam; PF00990; GGDEF; 1. DR Pfam; PF17159; MASE3; 1. DR SMART; SM00267; GGDEF; 1. DR SUPFAM; SSF55073; SSF55073; 1. DR TIGRFAMs; TIGR00254; GGDEF; 1. DR PROSITE; PS50887; GGDEF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 85 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 147 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 185 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 197 216 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 298 422 GGDEF. {ECO:0000259|PROSITE:PS50887}. SQ SEQUENCE 422 AA; 48690 MW; EF96A6496A8BB005 CRC64; MWRGLALKAI TKRFIFIYIP VLAALFFLSR INYLLYHTVI EFFAIFTGLS IGLIAYATRG FNQNRIFIKF GIVYIFVAIV DFLHTLAYKG MGVFPNWTSN QPTQFWIAGR LLETLGFVLI LYFPKLSERT LFFLFGPLTT FLITSIWTGV FPDCFIEGFG LTEFKISMEY IIIFVLLAVL VRTLRSKDIS ISTFRKPLVA AVILTIFGEL SFTLYSDVYG FFNFLGHVFR FLSYMVILRG MIVNALANPV RALLFELHEE KEKLKEIAHR DSLTGLFNRA FFNEWIQDQV RKAQFQNVPL SFIMIDVDDF KQINDTYGHL TGDKVLKFVA RCISDSIRSS DFAVRYGGDE FLVVLYNTSK QQAERVASRI REKIRNSNEL GVDVDISYGV AELNPGDNYL KFLQKADEEM YGMKREKKSC CD // ID Q9S5X2_THEMA Unreviewed; 639 AA. AC Q9S5X2; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 11-MAY-2016, entry version 89. DE SubName: Full=Maltodextrin glycosyltransferase {ECO:0000313|EMBL:AAD35849.1}; GN OrderedLocusNames=TM_0767 {ECO:0000313|EMBL:AAD35849.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35849.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35849.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35849.1; -; Genomic_DNA. DR PIR; E72336; E72336. DR RefSeq; NP_228576.1; NC_000853.1. DR RefSeq; WP_010865200.1; NC_000853.1. DR ProteinModelPortal; Q9S5X2; -. DR SMR; Q9S5X2; 3-638. DR STRING; 243274.TM0767; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR DNASU; 898435; -. DR EnsemblBacteria; AAD35849; AAD35849; TM_0767. DR GeneID; 898435; -. DR KEGG; tma:TM0767; -. DR KEGG; tmi:THEMA_00815; -. DR PATRIC; 23936456; VBITheMar51294_0780. DR eggNOG; ENOG4107TFH; Bacteria. DR eggNOG; COG0366; LUCA. DR OMA; IDMGHAL; -. DR OrthoDB; EOG67DPGN; -. DR BioCyc; TMAR243274:GC6P-794-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR015167; DUF1923. DR InterPro; IPR015902; Glyco_hydro_13. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10357; PTHR10357; 3. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF09083; DUF1923; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35849.1}. SQ SEQUENCE 639 AA; 73908 MW; 214D178A7E96857E CRC64; MIVLLREINR YCKEKATGKR IYAVPKLWIP GFFKKFDEKS GRCFVDPYEL GAEITDWILN QSREWDYSQP LSFLKGEKTP DWIKRSVVYG SLPRTTAAYN HKGSGYYEEN DVLGFREAGT FFKMMLLLPF VKSLGADAIY LLPVSRMSDL FKKGDAPSPY SVKNPMELDE RYHDPLLEPF KVDEEFKAFV EACHILGIRV ILDFIPRTAA RDSDLIREHP DWFYWIKVEE LADYTPPRAE ELPFKVPDED ELEIIYNKEN VKRHLKKFTL PPNLIDPQKW EKIKREEGNI LELIVKEFGI ITPPGFSDLI NDPQPTWDDV TFLRLYLDHP EASKRFLDPN QPPYVLYDVI KASKFPGKEP NRELWEYLAG VIPHYQKKYG IDGARLDMGH ALPKELLDLI IKNVKEYDPA FVMIAEELDM EKDKASKEAG YDVILGSSWY FAGRVEEIGK LPDIAEELVL PFLASVETPD TPRIATRKYA SKMKKLAPFV TYFLPNSIPY VNTGQEIGEK QPMNLGLDTD PNLRKVLSPT DEFFGKLAFF DHYVLHWDSP DRGVLNFIKK LIKVRQQFLD FVLNGKFENL TTKDLVMYSY EKNGQKIVIA ANVGKEPKEI TGGRVWNGKW SDEEKVVLKP LEFALVVQE // ID Q9X0M1_THEMA Unreviewed; 359 AA. AC Q9X0M1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 77. DE SubName: Full=Branched chain amino acid ABC transporter, permease protein {ECO:0000313|EMBL:AAD36213.1}; GN OrderedLocusNames=TM_1137 {ECO:0000313|EMBL:AAD36213.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36213.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36213.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|SAAS:SAAS00582814}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36213.1; -; Genomic_DNA. DR PIR; E72290; E72290. DR RefSeq; NP_228943.1; NC_000853.1. DR RefSeq; WP_010865271.1; NC_000853.1. DR STRING; 243274.TM1137; -. DR EnsemblBacteria; AAD36213; AAD36213; TM_1137. DR GeneID; 898627; -. DR KEGG; tma:TM1137; -. DR PATRIC; 23937209; VBITheMar51294_1153. DR eggNOG; ENOG4105CF8; Bacteria. DR eggNOG; COG4177; LUCA. DR InParanoid; Q9X0M1; -. DR KO; K01998; -. DR OMA; GREELTW; -. DR BioCyc; TMAR243274:GC6P-1166-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015658; F:branched-chain amino acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015803; P:branched-chain amino acid transport; IBA:GOC. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00476327}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAAS:SAAS00476327, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00476288, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00476193}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 134 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 140 160 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 200 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 249 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 261 291 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 311 330 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 359 AA; 39879 MW; 41A1027202EC3964 CRC64; MMKMEKKLSA RTNFILTVVF LIFMALLLYL ADRYMDSYKL RVVRLIAIYG IMAVSLNLIN GITGIFSLGH AGFILIGAYT ASLLTLSPEQ KAMSFIIEPI VPWLANAHTD FFTATVAGGV LAAVFAFLIG WPVLRLSGDY LAIASLGFAE VIRIIALNAI SITNGPLGLK GIPEYSNIWW CYGWLFVTVL FMASLVNSSY GRALKAIRED RIAAEAMGIN VFKHQLLSFV IGAFFAGVSG SLYAHWLTTI DPRTTTLGPM LTFYVLIMIV LGGLGSISGS LIGAALFAIL FEWLRDLEEP FTFFGIHVPG IKGMRILVIS AIFILVMIFW QRGIMGREEL TWNNLYRWLF ARRRGGEEK // ID Q9WYB0_THEMA Unreviewed; 315 AA. AC Q9WYB0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 90. DE SubName: Full=Fructose-bisphosphate aldolase {ECO:0000313|EMBL:AAD35362.1}; GN OrderedLocusNames=TM_0273 {ECO:0000313|EMBL:AAD35362.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35362.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35362.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. {ECO:0000256|SAAS:SAAS00591215}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35362.1; -; Genomic_DNA. DR PIR; G72397; G72397. DR RefSeq; NP_228086.1; NC_000853.1. DR RefSeq; WP_010865086.1; NC_000853.1. DR ProteinModelPortal; Q9WYB0; -. DR SMR; Q9WYB0; 7-315. DR STRING; 243274.TM0273; -. DR EnsemblBacteria; AAD35362; AAD35362; TM_0273. DR GeneID; 897188; -. DR KEGG; tma:TM0273; -. DR PATRIC; 23935423; VBITheMar51294_0277. DR eggNOG; ENOG4105D2N; Bacteria. DR eggNOG; COG0191; LUCA. DR InParanoid; Q9WYB0; -. DR KO; K01624; -. DR OMA; VNTREMF; -. DR OrthoDB; EOG6HXJ7B; -. DR BioCyc; TMAR243274:GC6P-286-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011289; Fruc_bis_ald_class-2. DR InterPro; IPR000771; Ketose_bisP_aldolase_II. DR Pfam; PF01116; F_bP_aldolase; 1. DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1. DR TIGRFAMs; TIGR00167; cbbA; 1. DR TIGRFAMs; TIGR01859; fruc_bis_ald_; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000256|SAAS:SAAS00485079}; KW Metal-binding {ECO:0000256|SAAS:SAAS00485111}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000256|SAAS:SAAS00485107}. FT REGION 219 221 Dihydroxyacetone phosphate binding. FT {ECO:0000256|PIRSR:PIRSR001359-2}. FT REGION 261 264 Dihydroxyacetone phosphate binding. FT {ECO:0000256|PIRSR:PIRSR001359-2}. FT ACT_SITE 92 92 Proton donor. FT {ECO:0000256|PIRSR:PIRSR001359-1}. FT BINDING 189 189 Dihydroxyacetone phosphate; via amide FT nitrogen. {ECO:0000256|PIRSR:PIRSR001359- FT 2}. SQ SEQUENCE 315 AA; 34923 MW; 7D3D5F89BBE2845E CRC64; MTMPYVKNTK EILEKASKER YAIGAFNFNN MEFLQAILEA AEEEKAPVIV ATSEGAIKYI GKGDIETGAK LAVEMVRTYA EKLSVPVALH LDHGRDFKVI MAAIKAGYSS VMIDASHLPF EENLRETKRI VEIAHAVGIS VEAELGKLKG IEDNVVEKES VLVDPEEAKV FVKETEVDFL APAIGTSHGA FKFKGEAQLD FERLKKVKEY TQIPLVLHGA SMVPQDIVKL ANEYGAELSG AKGVPEDMLK KAIELGINKI NTDTDLRITF VAYLRKVLSE DKSQIDPRKI FKPVFEQVKE IVKERIRIFG SSGKA // ID Q9WYW8_THEMA Unreviewed; 333 AA. AC Q9WYW8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 117. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35583.1}; GN OrderedLocusNames=TM_0498 {ECO:0000313|EMBL:AAD35583.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35583.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35583.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35583.1; -; Genomic_DNA. DR PIR; A72371; A72371. DR RefSeq; NP_228308.1; NC_000853.1. DR RefSeq; WP_010865136.1; NC_000853.1. DR ProteinModelPortal; Q9WYW8; -. DR STRING; 243274.TM0498; -. DR EnsemblBacteria; AAD35583; AAD35583; TM_0498. DR GeneID; 897539; -. DR KEGG; tma:TM0498; -. DR PATRIC; 23935901; VBITheMar51294_0505. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR InParanoid; Q9WYW8; -. DR KO; K02031; -. DR OMA; DICQKVI; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-522-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35583.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD35583.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 8 258 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 333 AA; 37914 MW; 521049B38200010B CRC64; MNGLATLLEV KNLSTWFYME EGIVKAVNDV SFSLNSNEVL GIVGETGSGK SVTVKSIMRL IKPPGKIVSG EIIYKGQDIL KIPEKEMHRI RGKEIAMIFQ DPMMSLNPLY TIGDQLMETI RYHLGYDKRR AYLRAVEMLE LVGIPEPEKR MNNYPFEFSG GMRQRVVIAI ALSCNPSVLI ADEPTTALDV TIQAQILELM KELQKEFKTG LIFITHDLGV IASMADRIMV MYGGRQVEIG TSDQIFYSPR HPYTKMLLRS VPRVDKRLEK LESIPGQPPR MVDIPPVCPF LPRCPRRVER CLKELPELSE IEENHYVRCF NPVEEEVSLE RNS // ID Q9X0V3_THEMA Unreviewed; 562 AA. AC Q9X0V3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 73. DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein, putative {ECO:0000313|EMBL:AAD36301.1}; GN OrderedLocusNames=TM_1226 {ECO:0000313|EMBL:AAD36301.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36301.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36301.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36301.1; -; Genomic_DNA. DR PIR; C72278; C72278. DR RefSeq; NP_229031.1; NC_000853.1. DR RefSeq; WP_010865283.1; NC_000853.1. DR ProteinModelPortal; Q9X0V3; -. DR SMR; Q9X0V3; 25-559. DR STRING; 243274.TM1226; -. DR EnsemblBacteria; AAD36301; AAD36301; TM_1226. DR GeneID; 898258; -. DR KEGG; tma:TM1226; -. DR PATRIC; 23937394; VBITheMar51294_1244. DR eggNOG; ENOG4107VN3; Bacteria. DR eggNOG; COG0747; LUCA. DR InParanoid; Q9X0V3; -. DR KO; K02035; -. DR OMA; PANDAIH; -. DR OrthoDB; EOG6SV54Z; -. DR BioCyc; TMAR243274:GC6P-1256-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0042884; P:microcin transport; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 73 454 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. SQ SEQUENCE 562 AA; 65452 MW; 345F12AB6A483037 CRC64; MNMKRFLLVF VVVFLFSSLF SQVLERNETM YYGGSLWSPP SNWNPFTPWN AVPGTTGLVY ETMFFYDPLT GNFDPWLAEK GEWLDSKTYR VVLREGIYWH DNVPLTSEDV RFTFEIAKKY KGIHYSSVWE WLDHIETPDN RTVIFVFKDP RYHEWNELLY TLPIVPKHIW EEKDETTILQ SSNEYPLGSG PYVAHSWDQN KMIFERFENW WGTKVMGVKP APKYVVIVRV LSNNVALGML MKGELDFSNF MLPGVPILKK VYNLNTWYDE PPYHLSSTVV GLFLNARKYP LSLPEFRRAI AMSINADPIV QRVYEGAVLK ADPLGFLPNS VWMKYYPKEV VEKHGFKYDP EEAKSILDKL GFRDVNGDGF RETPDGKPIK LTIECPYGWT DWMQAIQVIV DQLKVVGINA EPYFPDSSKY YENMYKGEFD IEMNANGTGI SSTPWTYFNT IFYPDALESE FSYTGNYGRY QNPEVESLLE ELNRTPLDNV EKVTELCGKL GEILLKDLPF IPLWYGAMAF ITQDNVWTNW PNEHNPYAWP CGWANWWQTG ALKILFNLKP AK // ID Q9WYL3_THEMA Unreviewed; 232 AA. AC Q9WYL3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=Endonuclease III {ECO:0000256|PIRNR:PIRNR001435}; DE EC=4.2.99.18 {ECO:0000256|PIRNR:PIRNR001435}; GN OrderedLocusNames=TM_0382 {ECO:0000313|EMBL:AAD35467.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35467.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35467.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase CC activity and AP-lyase activity. {ECO:0000256|PIRNR:PIRNR001435}. CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. {ECO:0000256|PIRNR:PIRNR001435}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|PIRNR:PIRNR001435}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|PIRNR:PIRNR001435}; CC -!- SIMILARITY: Belongs to the Nth/MutY family. CC {ECO:0000256|PIRNR:PIRNR001435}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35467.1; -; Genomic_DNA. DR PIR; F72383; F72383. DR RefSeq; NP_228192.1; NC_000853.1. DR RefSeq; WP_010865108.1; NC_000853.1. DR ProteinModelPortal; Q9WYL3; -. DR STRING; 243274.TM0382; -. DR EnsemblBacteria; AAD35467; AAD35467; TM_0382. DR GeneID; 897359; -. DR KEGG; tma:TM0382; -. DR KEGG; tmi:THEMA_02810; -. DR PATRIC; 23935647; VBITheMar51294_0388. DR eggNOG; ENOG4108VTX; Bacteria. DR eggNOG; COG2231; LUCA. DR KO; K07457; -. DR OMA; WWPADTP; -. DR OrthoDB; EOG65J50F; -. DR BioCyc; TMAR243274:GC6P-396-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR Gene3D; 1.10.1670.10; -; 1. DR Gene3D; 1.10.340.30; -; 1. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR023170; HTH_base_excis_C. DR InterPro; IPR005759; Nth. DR Pfam; PF00730; HhH-GPD; 1. DR PIRSF; PIRSF001435; Nth; 1. DR SMART; SM00478; ENDO3c; 1. DR SMART; SM00278; HhH1; 1. DR SUPFAM; SSF48150; SSF48150; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR001435}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA damage {ECO:0000256|PIRNR:PIRNR001435}; KW DNA repair {ECO:0000256|PIRNR:PIRNR001435}; KW Endonuclease {ECO:0000313|EMBL:AAD35467.1}; KW Glycosidase {ECO:0000256|PIRNR:PIRNR001435}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR001435, KW ECO:0000313|EMBL:AAD35467.1}; Iron {ECO:0000256|PIRNR:PIRNR001435}; KW Iron-sulfur {ECO:0000256|PIRNR:PIRNR001435}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR001435}; KW Nuclease {ECO:0000313|EMBL:AAD35467.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 46 205 ENDO3c. {ECO:0000259|SMART:SM00478}. FT DOMAIN 127 146 HhH1. {ECO:0000259|SMART:SM00278}. SQ SEQUENCE 232 AA; 27279 MW; 90353F96DA1F262A CRC64; MLIWFTPRII LSMRLTELYR KLLEIHGSVG KWWPGTPEEI VITAVLTQNT NWKNVERAME NIKNEVKGNN LLKELDSLPE EKVAELIRPA GFFNIKTKRL KELLKFLKEY NYNLSRLRDL PTHILRERLL KIKGIGKETA DAILLYALEK PVFVVDSYTR RLLKRIFNIE LNDYDEVQKL FMTHYPEDVR LYQEFHGLIV EHAKKFCSKT PKCGVCPLKK ECCHVSQMNG FS // ID Q9X272_THEMA Unreviewed; 328 AA. AC Q9X272; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 120. DE SubName: Full=Oligopeptide ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36815.1}; GN OrderedLocusNames=TM_1750 {ECO:0000313|EMBL:AAD36815.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36815.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36815.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|SAAS:SAAS00555009}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36815.1; -; Genomic_DNA. DR PIR; A72216; A72216. DR RefSeq; NP_229548.1; NC_000853.1. DR RefSeq; WP_010865394.1; NC_000853.1. DR ProteinModelPortal; Q9X272; -. DR STRING; 243274.TM1750; -. DR TCDB; 3.A.1.5.15; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36815; AAD36815; TM_1750. DR GeneID; 897787; -. DR KEGG; tma:TM1750; -. DR PATRIC; 23938476; VBITheMar51294_1768. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR InParanoid; Q9X272; -. DR KO; K02032; -. DR OMA; IMEPMEI; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1798-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36815.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00554975, ECO:0000313|EMBL:AAD36815.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transport {ECO:0000256|SAAS:SAAS00554993}. FT DOMAIN 14 257 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 328 AA; 37153 MW; B9D826625D641AB6 CRC64; MPFDQGGIKM KPLLQTVDLK KYFPQGKRIL KAVDGISIEI KEGETLGLVG ESGCGKSTLG RTILKLLRPD GGKIFFEGKD ITNLNDKEMK PYRKKMQIIF QDPLGSLNPQ MTVGRIIEDP LIIHKIGTKK ERRKRVEELL DMVGIGREFI NSFPHEFSGG QQQRIGIARA LALNPKFIVC DEPVSALDVS IQAQIIDLLE EIQQKMGISY LFIAHNLAVV EHISHKVAVM YLGKIVEYGD VDKIFLNPIH PYTRALLKSV PKIPWDGQKQ RFYSLKGELP SPIDLPKGCR FQTRCTEKKA ICFEKEPELT EVEKNHFVSC HLVRSYRG // ID Q9X047_THEMA Unreviewed; 509 AA. AC Q9X047; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36031.1}; GN OrderedLocusNames=TM_0950 {ECO:0000313|EMBL:AAD36031.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36031.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36031.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36031.1; -; Genomic_DNA. DR PIR; A72314; A72314. DR RefSeq; NP_228758.1; NC_000853.1. DR RefSeq; WP_010865224.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X047; -. DR STRING; 243274.TM0950; -. DR EnsemblBacteria; AAD36031; AAD36031; TM_0950. DR GeneID; 898687; -. DR KEGG; tma:TM0950; -. DR KEGG; tmw:THMA_0973; -. DR PATRIC; 23936831; VBITheMar51294_0964. DR eggNOG; ENOG4108M7K; Bacteria. DR eggNOG; ENOG410XPYR; LUCA. DR InParanoid; Q9X047; -. DR OMA; GTTCYAW; -. DR OrthoDB; EOG67DPK2; -. DR BioCyc; TMAR243274:GC6P-980-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR032260; DUF5060. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF16586; DUF5060; 1. DR SUPFAM; SSF51445; SSF51445; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 8 75 DUF5060. {ECO:0000259|Pfam:PF16586}. SQ SEQUENCE 509 AA; 60276 MW; D69EADED245F658A CRC64; MISMTQNNVE KWGTYEITLK GKAEGNPFTD VEIKAVFTSE AGDSFEVEGF YDGEDTFKIR FMPNRTGLWK YEVRSDIKDL DGMKGEFLCV DPSEGNHGPV RVCNTYHFCY EDGTPYHPFG TTLYAWVHQR EELIQQTLES LRNSPFNKVR MCVFPKYYAY NREEPPMLPM SWREEDGRYQ VEFNVKFFQH FERLVKELMD MGIEADVILF HPYDKWGFCS MPEEVDKAYL RYLIARISSY RNVWWSMANE YDLIKPQKDW DGYFHFIVEK DPYNHLRSVH QCFKFYDHTK PWITHASIQW QGSLRSWSGE PEIDIGINLI PKWREMYKKP VIIDECGYEG NIEYGWGNLP PQEMMNRFWE GVTSGGYVTH GETYYSEDEV LWWSKGGRLK GESPKRIAFL RTIIEEAPPF LKPIKLDPMM DWDVHCIGKE GEYYLIYFDI NRPVKRTLKL PEGKYRVDLV DCWETEIHSL GIFQGQVVIR LPGKSYVALR IQKMENNDDW IILREDAKL // ID Q9X1Q8_THEMA Unreviewed; 306 AA. AC Q9X1Q8; G4FFW0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 107. DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042}; DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042}; GN OrderedLocusNames=TM_1572 {ECO:0000313|EMBL:AAD36639.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36639.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36639.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or CC leader sequences from secreted and periplasmic proteins. CC {ECO:0000256|RuleBase:RU362042}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; CC Single-pass type II membrane protein CC {ECO:0000256|RuleBase:RU362042}. CC -!- SIMILARITY: Belongs to the peptidase S26 family. CC {ECO:0000256|RuleBase:RU362042}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36639.1; -; Genomic_DNA. DR PIR; E72237; E72237. DR RefSeq; NP_229372.1; NC_000853.1. DR RefSeq; WP_004081991.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1Q8; -. DR STRING; 243274.TM1572; -. DR EnsemblBacteria; AAD36639; AAD36639; TM_1572. DR GeneID; 897380; -. DR KEGG; tma:TM1572; -. DR KEGG; tmi:THEMA_06420; -. DR KEGG; tmw:THMA_1607; -. DR PATRIC; 23938106; VBITheMar51294_1590. DR eggNOG; ENOG4107XQR; Bacteria. DR eggNOG; COG0681; LUCA. DR KO; K03100; -. DR OMA; DINRDEQ; -. DR OrthoDB; EOG6KDKTM; -. DR BioCyc; TMAR243274:GC6P-1613-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central. DR Gene3D; 2.10.109.10; -; 2. DR InterPro; IPR000223; Pept_S26A_signal_pept_1. DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR InterPro; IPR019533; Peptidase_S26. DR PANTHER; PTHR12383; PTHR12383; 3. DR Pfam; PF00717; Peptidase_S24; 1. DR Pfam; PF10502; Peptidase_S26; 1. DR PRINTS; PR00727; LEADERPTASE. DR SUPFAM; SSF51306; SSF51306; 1. DR TIGRFAMs; TIGR02227; sigpep_I_bact; 2. DR PROSITE; PS00760; SPASE_I_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000256|RuleBase:RU362042}; KW Membrane {ECO:0000256|RuleBase:RU362042}; KW Protease {ECO:0000256|RuleBase:RU362042}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU362042}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}. FT TRANSMEM 12 29 Helical. {ECO:0000256|RuleBase:RU362042}. FT DOMAIN 34 69 Peptidase_S24. FT {ECO:0000259|Pfam:PF00717}. FT DOMAIN 256 288 Peptidase_S26. FT {ECO:0000259|Pfam:PF10502}. SQ SEQUENCE 306 AA; 36082 MW; 466E1FE29C17019F CRC64; MNLKKESVEW IKALLYALVA ATIVRLYIFE TMLVPTGSMI PTIQIGDRLF VEKITYTVRE PQIGEIVVFW SPFVDERASH MLRLFDKFMD LFSPSKFRGH VKYVKRLVGK GGDVLEIKDG KLYVNGEVPE VLKDRYYEPE GIFKYEDFYE WLYTASKLRK DKQAYRDFIY DIAKNYGRTA AVLVFSLIGE EGLSYGEAFL PGLLNYFDPS MVYYDEKTKS YYIPGMIYHE FYEEYYSKLD LKKYVGKTDD GTIRIRVPEG FYFLMGDNTK ESLDCRYFGF VPKDHIIGWP ILRIWPFERF GPIQKY // ID Q9X012_THEMA Unreviewed; 258 AA. AC Q9X012; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Flagellar biosynthetic protein FliR {ECO:0000256|RuleBase:RU362071}; GN OrderedLocusNames=TM_0910 {ECO:0000313|EMBL:AAD35991.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35991.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35991.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Role in flagellar biosynthesis. CC {ECO:0000256|RuleBase:RU362071}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU362071}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU362071}. Bacterial flagellum basal body CC {ECO:0000256|RuleBase:RU362071}. CC -!- SIMILARITY: Belongs to the FliR/MopE/SpaR family. CC {ECO:0000256|RuleBase:RU362071}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35991.1; -; Genomic_DNA. DR PIR; E72319; E72319. DR RefSeq; NP_228718.1; NC_000853.1. DR RefSeq; WP_010865219.1; NC_000853.1. DR STRING; 243274.TM0910; -. DR DNASU; 898584; -. DR EnsemblBacteria; AAD35991; AAD35991; TM_0910. DR GeneID; 898584; -. DR KEGG; tma:TM0910; -. DR PATRIC; 23936751; VBITheMar51294_0924. DR eggNOG; ENOG4105D19; Bacteria. DR eggNOG; COG1684; LUCA. DR InParanoid; Q9X012; -. DR KO; K02421; -. DR OMA; NLAFGVM; -. DR OrthoDB; EOG6FBWVR; -. DR BioCyc; TMAR243274:GC6P-940-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro. DR GO; GO:0006605; P:protein targeting; IEA:InterPro. DR InterPro; IPR006303; FliR. DR InterPro; IPR002010; T3SS_IM_R. DR Pfam; PF01311; Bac_export_1; 1. DR PRINTS; PR00953; TYPE3IMRPROT. DR TIGRFAMs; TIGR01400; fliR; 1. PE 3: Inferred from homology; KW Bacterial flagellum {ECO:0000256|RuleBase:RU362071}; KW Cell membrane {ECO:0000256|RuleBase:RU362071}; KW Cell projection {ECO:0000313|EMBL:AAD35991.1}; KW Cilium {ECO:0000313|EMBL:AAD35991.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flagellum {ECO:0000313|EMBL:AAD35991.1}; KW Membrane {ECO:0000256|RuleBase:RU362071}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU362071}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362071}. FT TRANSMEM 14 34 Helical. {ECO:0000256|RuleBase:RU362071}. FT TRANSMEM 41 63 Helical. {ECO:0000256|RuleBase:RU362071}. FT TRANSMEM 69 94 Helical. {ECO:0000256|RuleBase:RU362071}. FT TRANSMEM 130 148 Helical. {ECO:0000256|RuleBase:RU362071}. FT TRANSMEM 180 205 Helical. {ECO:0000256|RuleBase:RU362071}. FT TRANSMEM 217 238 Helical. {ECO:0000256|RuleBase:RU362071}. SQ SEQUENCE 258 AA; 28758 MW; 6ED3A49B7A7323DA CRC64; MILETIFSFL EEKFLAWMCI FTRFTGFFLI APFFSERAFP VVVRVLLGLF TSWLMLFTVD VSIPLNTPVL SFTLNLFFNF LVGFGIGFIV YLFLQAFNGA GYIFGFQIGF GMEEVLAFGE EETNPTGELV YFIALTVFVL IKGPVLLFEG LKDSIDVFPV NLTGVTDGFF SYIVGRSSDF FVLILKIGAP VIAFMLIISI VLGIVSRLIP QMNVFMVGLP LKVIIGVILI LGMLPIWADM AQKISALSWN AIQELLGK // ID Q9WYR7_THEMA Unreviewed; 368 AA. AC Q9WYR7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 94. DE SubName: Full=Alcohol dehydrogenase, zinc-containing {ECO:0000313|EMBL:AAD35521.1}; GN OrderedLocusNames=TM_0436 {ECO:0000313|EMBL:AAD35521.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35521.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35521.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1VJ0} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of Alcohol dehydrogenase (TM0436) from Thermotoga RT maritima at 2.00 A resolution."; RL Submitted (DEC-2003) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35521.1; -; Genomic_DNA. DR PIR; G72376; G72376. DR RefSeq; NP_228246.1; NC_000853.1. DR RefSeq; WP_010865119.1; NC_000853.1. DR PDB; 1VJ0; X-ray; 2.00 A; A/B/C/D=1-368. DR PDBsum; 1VJ0; -. DR ProteinModelPortal; Q9WYR7; -. DR SMR; Q9WYR7; 2-367. DR STRING; 243274.TM0436; -. DR EnsemblBacteria; AAD35521; AAD35521; TM_0436. DR GeneID; 897451; -. DR KEGG; tma:TM0436; -. DR PATRIC; 23935757; VBITheMar51294_0442. DR eggNOG; ENOG4105CPQ; Bacteria. DR eggNOG; COG1063; LUCA. DR InParanoid; Q9WYR7; -. DR OMA; GSDVHMF; -. DR OrthoDB; EOG68Q0M3; -. DR BioCyc; TMAR243274:GC6P-451-MONOMER; -. DR EvolutionaryTrace; Q9WYR7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020843; PKS_ER. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VJ0}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000213|PDB:1VJ0}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Zinc {ECO:0000213|PDB:1VJ0}. FT METAL 43 43 Zinc 1. {ECO:0000213|PDB:1VJ0}. FT METAL 65 65 Zinc 1; via tele nitrogen. FT {ECO:0000213|PDB:1VJ0}. FT METAL 66 66 Zinc 1. {ECO:0000213|PDB:1VJ0}. FT METAL 100 100 Zinc 2. {ECO:0000213|PDB:1VJ0}. FT METAL 103 103 Zinc 2. {ECO:0000213|PDB:1VJ0}. FT METAL 106 106 Zinc 2. {ECO:0000213|PDB:1VJ0}. FT METAL 115 115 Zinc 2. {ECO:0000213|PDB:1VJ0}. FT METAL 166 166 Zinc 1. {ECO:0000213|PDB:1VJ0}. SQ SEQUENCE 368 AA; 40558 MW; 47DEB57CD23AB081 CRC64; MMGLKAHAMV LEKFNQPLVY KEFEISDIPR GSILVEILSA GVCGSDVHMF RGEDPRVPLP IILGHEGAGR VVEVNGEKRD LNGELLKPGD LIVWNRGITC GECYWCKVSK EPYLCPNRKV YGINRGCSEY PHLRGCYSSH IVLDPETDVL KVSEKDDLDV LAMAMCSGAT AYHAFDEYPE SFAGKTVVIQ GAGPLGLFGV VIARSLGAEN VIVIAGSPNR LKLAEEIGAD LTLNRRETSV EERRKAIMDI THGRGADFIL EATGDSRALL EGSELLRRGG FYSVAGVAVP QDPVPFKVYE WLVLKNATFK GIWVSDTSHF VKTVSITSRN YQLLSKLITH RLPLKEANKA LELMESREAL KVILYPEG // ID Q9WXY0_THEMA Unreviewed; 220 AA. AC Q9WXY0; G4FH41; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 130. DE SubName: Full=Response regulator {ECO:0000313|EMBL:AAD35220.1}; GN OrderedLocusNames=TM_0126 {ECO:0000313|EMBL:AAD35220.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35220.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35220.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1P2F} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 3-220. RX PubMed=12837793; DOI=10.1128/JB.185.14.4186-4194.2003; RA Robinson V.L., Wu T., Stock A.M.; RT "Structural analysis of the domain interface in DrrB, a response RT regulator of the OmpR/PhoB subfamily."; RL J. Bacteriol. 185:4186-4194(2003). RN [3] {ECO:0000213|PDB:3NNS} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-117 IN COMPLEX WITH RP MAGNESIUM. RX PubMed=20702407; DOI=10.1074/jbc.M110.157164; RA Barbieri C.M., Mack T.R., Robinson V.L., Miller M.T., Stock A.M.; RT "Regulation of response regulator autophosphorylation through RT interdomain contacts."; RL J. Biol. Chem. 285:32325-32335(2010). CC -!- SIMILARITY: Contains OmpR/PhoB-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00583175}. CC -!- SIMILARITY: Contains response regulatory domain. CC {ECO:0000256|SAAS:SAAS00122777}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35220.1; -; Genomic_DNA. DR PIR; F72415; F72415. DR RefSeq; NP_227942.1; NC_000853.1. DR RefSeq; WP_004082711.1; NZ_CP011107.1. DR PDB; 1P2F; X-ray; 1.80 A; A=3-220. DR PDB; 3NNS; X-ray; 1.90 A; A/B=1-117. DR PDBsum; 1P2F; -. DR PDBsum; 3NNS; -. DR ProteinModelPortal; Q9WXY0; -. DR SMR; Q9WXY0; 1-217. DR STRING; 243274.TM0126; -. DR EnsemblBacteria; AAD35220; AAD35220; TM_0126. DR GeneID; 896953; -. DR KEGG; tma:TM0126; -. DR KEGG; tmi:THEMA_04175; -. DR KEGG; tmw:THMA_0122; -. DR PATRIC; 23935092; VBITheMar51294_0124. DR eggNOG; ENOG4106NW0; Bacteria. DR eggNOG; ENOG410YGCR; LUCA. DR KO; K02483; -. DR OMA; IINDSSH; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-126-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd. DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF00486; Trans_reg_C; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00862; Trans_reg_C; 1. DR SUPFAM; SSF46894; SSF46894; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS51755; OMPR_PHOB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1P2F, ECO:0000213|PDB:3NNS}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|SAAS:SAAS00582919}; KW Magnesium {ECO:0000213|PDB:3NNS}; KW Metal-binding {ECO:0000213|PDB:3NNS}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|SAAS:SAAS00275006}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00275006}; KW Two-component regulatory system {ECO:0000256|SAAS:SAAS00583142}. FT DOMAIN 4 115 Response regulatory. FT {ECO:0000259|PROSITE:PS50110}. FT DOMAIN 120 217 OmpR/PhoB-type DNA-binding. FT {ECO:0000259|PROSITE:PS51755}. FT METAL 10 10 Magnesium. {ECO:0000213|PDB:3NNS}. FT METAL 50 50 Magnesium. {ECO:0000213|PDB:3NNS}. FT METAL 52 52 Magnesium; via carbonyl oxygen. FT {ECO:0000213|PDB:3NNS}. SQ SEQUENCE 220 AA; 25521 MW; 2581C6BF38452800 CRC64; MMWKIAVVDD DKNILKKVSE KLQQLGRVKT FLTGEDFLND EEAFHVVVLD VMLPDYSGYE ICRMIKETRP ETWVILLTLL SDDESVLKGF EAGADDYVTK PFNPEILLAR VKRFLEREKK GLYDFGDLKI DATGFTVFLK GKRIHLPKKE FEILLFLAEN AGKVVTREKL LETFWEDPVS PRVVDTVIKR IRKAIEDDPN RPRYIKTIWG VGYMFTGGER // ID Q9WZV6_THEMA Unreviewed; 335 AA. AC Q9WZV6; G4FCX2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000256|PIRNR:PIRNR004930}; DE Short=TC-AMP synthase {ECO:0000256|PIRNR:PIRNR004930}; DE EC=2.7.7.87 {ECO:0000256|PIRNR:PIRNR004930}; DE AltName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000256|PIRNR:PIRNR004930}; GN OrderedLocusNames=TM_0852 {ECO:0000313|EMBL:AAD35934.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35934.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35934.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. {ECO:0000256|PIRNR:PIRNR004930}. CC -!- CATALYTIC ACTIVITY: L-threonine + ATP + HCO(3)(-) = L- CC threonylcarbamoyladenylate + diphosphate + H(2)O. CC {ECO:0000256|PIRNR:PIRNR004930}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR004930}. CC -!- SIMILARITY: Belongs to the SUA5 family. CC {ECO:0000256|PIRNR:PIRNR004930}. CC -!- SIMILARITY: Contains YrdC-like domain. CC {ECO:0000256|SAAS:SAAS00501982}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35934.1; -; Genomic_DNA. DR PIR; E72324; E72324. DR RefSeq; NP_228661.1; NC_000853.1. DR RefSeq; WP_004080774.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZV6; -. DR STRING; 243274.TM0852; -. DR EnsemblBacteria; AAD35934; AAD35934; TM_0852. DR GeneID; 898524; -. DR KEGG; tma:TM0852; -. DR KEGG; tmi:THEMA_00375; -. DR KEGG; tmw:THMA_0874; -. DR PATRIC; 23936632; VBITheMar51294_0865. DR eggNOG; ENOG4105EK0; Bacteria. DR eggNOG; COG0009; LUCA. DR KO; K07566; -. DR OMA; AIRMPDH; -. DR OrthoDB; EOG6C5RT4; -. DR BioCyc; TMAR243274:GC6P-882-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:UniProtKB-EC. DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central. DR GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IBA:GO_Central. DR Gene3D; 3.90.870.10; -; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR005145; SUA5. DR InterPro; IPR010923; t(6)A37_SUA5. DR InterPro; IPR006070; YrdC-like_dom. DR Pfam; PF03481; SUA5; 1. DR Pfam; PF01300; Sua5_yciO_yrdC; 1. DR PIRSF; PIRSF004930; Tln_factor_SUA5; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00057; TIGR00057; 1. DR PROSITE; PS51163; YRDC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRNR:PIRNR004930, KW ECO:0000256|PIRSR:PIRSR004930-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR004930}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR004930, KW ECO:0000256|PIRSR:PIRSR004930-1}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004930}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|PIRNR:PIRNR004930}; KW tRNA processing {ECO:0000256|PIRNR:PIRNR004930}. FT DOMAIN 14 200 YrdC-like. {ECO:0000259|PROSITE:PS51163}. FT BINDING 36 36 L-threonine. FT {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 59 59 ATP. {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 63 63 ATP. {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 68 68 L-threonine. FT {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 118 118 ATP. {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 122 122 L-threonine. FT {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 142 142 L-threonine; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 144 144 ATP; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 152 152 ATP. {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 182 182 L-threonine. FT {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 196 196 ATP. {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 237 237 ATP. {ECO:0000256|PIRSR:PIRSR004930-1}. SQ SEQUENCE 335 AA; 37859 MW; 5DEB3A7C990791C2 CRC64; MTRVLKVDPL FPDEKVLKEA AELLRNGEVI IFPTETVYGI GADAYNEEAC KKIFKLKERP ADNPLIVHIH SFKQLEEIAE GYEPHLDFLK KFWPGPLTVI FRKKSEKIPP VVTADLPTVA VRMPAHPVAL KLIELFGHPI AAPSANISGR PSATNVKHVI EDFMGKVKLI IDAGDTPFGL ESTIVDLTKE KPVLLRPGPV EVERLKELFP ELVVPDFVRK GNFKGRPLAP GMKYRHYAPL KPLILVEDLT KMEEVLKKYP DHVVICVEER KELYDDRIVV GSLKNPYSIA QNIFSALREA EKMGKEYIIV EGFEERGILF AVMNRLRKAA TEIVR // ID Q9X1I0_THEMA Unreviewed; 317 AA. AC Q9X1I0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Glucokinase {ECO:0000313|EMBL:AAD36537.1}; GN OrderedLocusNames=TM_1469 {ECO:0000313|EMBL:AAD36537.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36537.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36537.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36537.1; -; Genomic_DNA. DR PIR; F72246; F72246. DR RefSeq; NP_229269.1; NC_000853.1. DR RefSeq; WP_010865348.1; NC_000853.1. DR ProteinModelPortal; Q9X1I0; -. DR STRING; 243274.TM1469; -. DR EnsemblBacteria; AAD36537; AAD36537; TM_1469. DR GeneID; 898013; -. DR KEGG; tma:TM1469; -. DR PATRIC; 23937894; VBITheMar51294_1485. DR eggNOG; ENOG4105DKQ; Bacteria. DR eggNOG; COG1940; LUCA. DR InParanoid; Q9X1I0; -. DR KO; K00845; -. DR OMA; ANDGNCA; -. DR OrthoDB; EOG6CGCDC; -. DR BioCyc; MetaCyc:MONOMER-6111; -. DR BioCyc; TMAR243274:GC6P-1508-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004340; F:glucokinase activity; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:InterPro. DR InterPro; IPR000600; ROK. DR InterPro; IPR004654; ROK_glcA. DR Pfam; PF00480; ROK; 1. DR TIGRFAMs; TIGR00744; ROK_glcA_fam; 1. DR PROSITE; PS01125; ROK; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000313|EMBL:AAD36537.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD36537.1}. SQ SEQUENCE 317 AA; 33891 MW; 30B1DE9D69FFFA3F CRC64; MPKLKLIGVD LGGTTFSVGL VSEDGKILKK VTRDTLVENG KEDVIRRIAE TILEVSDGEE APYVGIGSPG SIDRENGIVR FSPNFPDWHN VPLTDELAKR TGKKVFLEND ANAFVLGEKW FGAGRGHDHI VALTLGTGIG GGVVTHGYLL TGRDGIGAEL GHVVVEPNGP MCNCGTRGCL EAVASATAIR RFLREGYKKY HSSLVYKLAG SPEKADAKHL FDAARQGDRF ALMIRDRVVD ALARAVAGYI HIFNPEIVII GGGISRAGEI LFGPLREKVV DYIMPSFVGT YEVVASPLVE DAGILGAASI IKERIGG // ID Q9WZ87_THEMA Unreviewed; 1289 AA. AC Q9WZ87; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 103. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35703.1}; GN OrderedLocusNames=TM_0618 {ECO:0000313|EMBL:AAD35703.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35703.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35703.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35703.1; -; Genomic_DNA. DR PIR; B72354; B72354. DR RefSeq; NP_228428.1; NC_000853.1. DR RefSeq; WP_010865167.1; NC_000853.1. DR ProteinModelPortal; Q9WZ87; -. DR STRING; 243274.TM0618; -. DR EnsemblBacteria; AAD35703; AAD35703; TM_0618. DR GeneID; 897704; -. DR KEGG; tma:TM0618; -. DR KEGG; tmi:THEMA_01575; -. DR PATRIC; 23936147; VBITheMar51294_0627. DR eggNOG; ENOG4105DKE; Bacteria. DR eggNOG; COG1112; LUCA. DR OMA; FAKFLMY; -. DR OrthoDB; EOG6G4VR9; -. DR BioCyc; TMAR243274:GC6P-643-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR025103; DUF4011. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR Pfam; PF13195; DUF4011; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 5. DR SUPFAM; SSF52980; SSF52980; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 264 959 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 1289 AA; 150918 MW; E667E628253FA9BA CRC64; MSLSNPLLAV DRARVSKLLI KDSEMTDLFD LLVKRGLKLP VFKYDLTTDR YILEKPGEIN FEGTEEEIVR KISRLYSLSK LSIEEKGVVT LFMTFGVLKW NDPGFKTPYL SAPVVMVPCE FEKNKHTNQV SRINFFGEGI QFNPVLELLF REKYDLPLPQ IEEIDSKNFN EIIEHLGNLK TQFTIWKVIP QCWIISLNPE MFVLYSDLGK MMQNTEALTH PLINAFSGVL SLSKSSTESV SSVPLVPILR ADSSQRKILE MVREGENVVI HGPPGTGKSQ TIANIIADAV AREKTVLFVS AKKAALDVVY NRLKNAGLGR FCLEIHSTRK SKQELMFDLK RTIDLLQNFQ DVEQPADLLK QFEHLKNNLN NLLNSLHRTD HPLGMSIYDA ISRLEGLKDY PVIHSLHLSS IAEISKERFE KILQLMEKLE QLADVYNESQ HPWKGFKFSE NILSYPLKVI EMLEYVKMNL KNMKQMLEKA GFTDIGNLRF EDFQKILYLL KSLKNVDVLP GRWFQVEIEE LSTLREIVEI LRKRKVLMKK YFQHTEKSIE EMTEILQPVE RFSRSWLRIL NPSYWKWKKF VNRNLRYPHN FEEIQRLYEI SKNLIDTEIK YNDLKEKIPD QEFSFDEYRT KELEEIDFAL IKLDIALKIR KKLPIKIIKN DLILTRVSKD LISRAIEILE DTQLKKYMED LNRLWPDGFV GEKTLQTAPV DELIRKIDHL IANESKLHEW IQLQETLESL EKMELKTFIR SVEKEHVKNI RRIFEKSFYK QWIDNVCTLD KNLRDFSSER YEQDILTLEK AEEALRKRWV QYVKSLLAKK FRTILADTNH SQQIRILMRE TQKKRRHKPI RKFLLEISDI LRFVKPCILM SPLSVSSFLD LDKFINYFDI VIFDEASQLR TPEAISAVVR GKQIIVAGDP KQLPPTNFFK SYYELEDDED EREPLDSFLD ECIALPRVFK QGYLRWHYRS RDERLIAFSN HYFYGENPLI TFPSPKYRNS DQGIKLVYVE NGTWDRAGKR VNTMEALKVV DIVIEHFQKH PDRSIGVVTM NTSQSDLIEN LLQRRLMEYP HLMDVIFKES NEPFFIKSLE NVQGDERDTI IISIGYARTP SGELFYNFGP LNNEGGWRRL NVLITRARYQ IILVTSLRSE DLSRANSENK GVAALRNYLK YAEQNCKLEF CRSYGESDDI IPTSIARQLN NIGFLTDTNI GMGLCQVSVG IEDPEDPGRY KIGIIHDGKN HAMIQDVIDR EVLKFKVLES LGWKLKRLWT IEWYRDPEKV LKNIIEHLK // ID Q9X0E8_THEMA Unreviewed; 508 AA. AC Q9X0E8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE RecName: Full=Archaeal-type glutamate synthase [NADPH] {ECO:0000256|PIRNR:PIRNR006429}; DE EC=1.4.1.13 {ECO:0000256|PIRNR:PIRNR006429}; GN OrderedLocusNames=TM_1058 {ECO:0000313|EMBL:AAD36135.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36135.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36135.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: 2 L-glutamate + NADP(+) = L-glutamine + 2- CC oxoglutarate + NADPH. {ECO:0000256|PIRNR:PIRNR006429}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|PIRNR:PIRNR006429}; CC -!- SIMILARITY: Belongs to the glutamate synthase family. CC {ECO:0000256|PIRNR:PIRNR006429}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36135.1; -; Genomic_DNA. DR PIR; E72299; E72299. DR RefSeq; NP_228864.1; NC_000853.1. DR RefSeq; WP_010865255.1; NC_000853.1. DR ProteinModelPortal; Q9X0E8; -. DR STRING; 243274.TM1058; -. DR EnsemblBacteria; AAD36135; AAD36135; TM_1058. DR GeneID; 898736; -. DR KEGG; tma:TM1058; -. DR PATRIC; 23937045; VBITheMar51294_1071. DR eggNOG; ENOG4105EYY; Bacteria. DR eggNOG; COG0069; LUCA. DR InParanoid; Q9X0E8; -. DR OMA; QMNVEDT; -. DR OrthoDB; EOG61CKWN; -. DR BioCyc; TMAR243274:GC6P-1087-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR024188; GltB. DR InterPro; IPR002932; Glu_synthdom. DR Pfam; PF01645; Glu_synthase; 1. DR PIRSF; PIRSF006429; GOGAT_lg_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR006429}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Flavoprotein {ECO:0000256|PIRNR:PIRNR006429}; KW FMN {ECO:0000256|PIRNR:PIRNR006429}; KW Glutamate biosynthesis {ECO:0000256|PIRNR:PIRNR006429}; KW NADP {ECO:0000256|PIRNR:PIRNR006429}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006429}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 260 390 Glu_synthase. {ECO:0000259|Pfam:PF01645}. SQ SEQUENCE 508 AA; 55981 MW; 8F1BC2012347E338 CRC64; MSGLCAKCVD GCTGGCETWL ASFRGREVLY PGPFGDITAG AVKDYPVDYS HLNILGYARG AEGLPEGVEP GPDTAIFTNV DTTTEYGWDI KVKMKVPIFT GALGSTEIAR KNWDHIAVGA AISGITVVCG ENVAGVDPDL ELDSNGKVKK SPELDRRIEI YKRYHDGEYG EILIQMNVED TRLGVAEYVI NKHGIETIEL KWGQGAKSIG GEIKVRSLER ALELKRRGYI VLPDPELPEV QRAFKEGEIK EFERHSRLGF VSKESFLKEV ERLRKLGFKR ITLKTGAYSA VELAMALRYG AEAKVDLITV DGAPGGTGMS PWPMMNEWGI PTFYLEALTY QFAEKLSRRG IRVPDIAIAG GFSTEDGVLK AIAMGSPYVK AVCMGRALMI PAMVGKNIGE WLKSGNLPKT VSKYGTTVEE IFVTYEELRS RFGEEEVKKL PLGAIGVYTF VQKFKTGLQQ LMAGARKFRL SALSRKDLIA LTKDAAEISG IPYVMESYRD EAERILEE // ID Q9X2F3_THEMA Unreviewed; 220 AA. AC Q9X2F3; G4FGL9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Methyl-accepting chemotaxis-related protein {ECO:0000313|EMBL:AAD36896.1}; GN OrderedLocusNames=TM_1833 {ECO:0000313|EMBL:AAD36896.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36896.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36896.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36896.1; -; Genomic_DNA. DR PIR; E72205; E72205. DR RefSeq; NP_229630.1; NC_000853.1. DR RefSeq; WP_004082378.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2F3; -. DR STRING; 243274.TM1833; -. DR EnsemblBacteria; AAD36896; AAD36896; TM_1833. DR GeneID; 897818; -. DR KEGG; tma:TM1833; -. DR KEGG; tmw:THMA_1877; -. DR PATRIC; 23938653; VBITheMar51294_1853. DR eggNOG; ENOG4107KHF; Bacteria. DR eggNOG; ENOG410ZJF7; LUCA. DR OMA; FWKITIA; -. DR OrthoDB; EOG6Z6FVR; -. DR BioCyc; TMAR243274:GC6P-1884-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR029151; Sensor-like. DR SUPFAM; SSF103190; SSF103190; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 33 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 220 AA; 25627 MW; 93C0EABEE0AD88DD CRC64; MSSLKKELFW KITIALIVAF VVICVLSIFQ LYFSGIKTAR DFIRNVNNTV TSFINGYFRK FYVVDVLSRI PEVRYAPYLT DEERRKVLEI YRIFQEADRD IYYLYSGYEN GLLLINDYEP AEGYDPRVRP WYRAALESRP KPTGGIPYRE FKTKELLFSV SKVITDDEGN VTGVISVETL LERLLSNFPH SFDNHETVTE PQPLTILLQG DRFVVVLIIL // ID Q9WZ55_THEMA Unreviewed; 301 AA. AC Q9WZ55; G4FDN4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35671.1}; GN OrderedLocusNames=TM_0586 {ECO:0000313|EMBL:AAD35671.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35671.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35671.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35671.1; -; Genomic_DNA. DR PIR; C72359; C72359. DR RefSeq; NP_228396.1; NC_000853.1. DR RefSeq; WP_004081271.1; NZ_CP011107.1. DR STRING; 243274.TM0586; -. DR DNASU; 897658; -. DR EnsemblBacteria; AAD35671; AAD35671; TM_0586. DR GeneID; 897658; -. DR KEGG; tma:TM0586; -. DR KEGG; tmw:THMA_0601; -. DR PATRIC; 23936083; VBITheMar51294_0595. DR eggNOG; ENOG410631K; Bacteria. DR eggNOG; COG0697; LUCA. DR InParanoid; Q9WZ55; -. DR OMA; MAMEATS; -. DR OrthoDB; EOG622PSZ; -. DR BioCyc; TMAR243274:GC6P-611-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 87 106 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 115 133 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 169 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 200 220 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256 273 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 6 130 EamA. {ECO:0000259|Pfam:PF00892}. FT DOMAIN 142 272 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 301 AA; 33915 MW; FF253E9960A06DE1 CRC64; MILERFFAWL VVVFWGISFL ATKVVVQVLD PFFAGFLRFI FAFFFLFLIS GGRPKLFNKN IVMAGFWGVF SYFAFENSAL MFTEPTNAAI IVSSAPVFFL LFSHLVQKKK TTSKMYLGVI LSFLGVALVV LNGRFVLKLN PLGDLLAFGA ALSWVFYTHH IESLGSLSFR ENAGIMFWGV VFFLPFSAGK FQQIREMNSI VVISLLYLGL VCSGLAYFLW NKAIERLGSR TTTNMIYYIP VVTAVAEHLL KLKLPSALLV GGVVLVVIGL LIFEREVHYE TEDSTRGMRK DRTEETRPSA D // ID Q9WZE8_THEMA Unreviewed; 321 AA. AC Q9WZE8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35764.1}; GN OrderedLocusNames=TM_0682 {ECO:0000313|EMBL:AAD35764.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35764.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35764.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35764.1; -; Genomic_DNA. DR PIR; G72347; G72347. DR RefSeq; NP_228491.1; NC_000853.1. DR RefSeq; WP_010865185.1; NC_000853.1. DR STRING; 243274.TM0682; -. DR DNASU; 898349; -. DR EnsemblBacteria; AAD35764; AAD35764; TM_0682. DR GeneID; 898349; -. DR KEGG; tma:TM0682; -. DR PATRIC; 23936282; VBITheMar51294_0694. DR eggNOG; ENOG4108264; Bacteria. DR eggNOG; COG2327; LUCA. DR InParanoid; Q9WZE8; -. DR OMA; VISERFH; -. DR OrthoDB; EOG6ZSP4K; -. DR BioCyc; TMAR243274:GC6P-708-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR007345; Polysacch_pyruvyl_Trfase. DR InterPro; IPR019896; Polysacch_pyruvyl_Trfase_CsaB. DR Pfam; PF04230; PS_pyruv_trans; 1. DR TIGRFAMs; TIGR03609; S_layer_CsaB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 19 259 PS_pyruv_trans. FT {ECO:0000259|Pfam:PF04230}. SQ SEQUENCE 321 AA; 36640 MW; 4964CC675B17676D CRC64; MRWFSLATAF LWGYYGFDNF GDELMFKACV NLLRELGFGT IYTPLPKGKK SMGVTSVDRY SIKLLSLLKK SQVSIAGGGG LFQDVTSLRS LLYYYSISKA SLLMDKPLIF FGNSVGPLRR RLSKKLVWDV FKDKRTVFIA RDPASYRYVK MVGGNAVLGT DPAIIHLMES DMEKKTEKKA VFFLKSPMDV SYILKSLRDQ GINDFVISTA FPGDHSYLPP LRNGENLLEE IVSSSIVITE RFHPALVAAY FEIPFIIVDC QKARRFFARY TKEDHFFSKR DPLEISLKVP VVLKKELKLK EKMKNDAIEM KEMLKGVLKG W // ID Q9S5X8_THEMA Unreviewed; 258 AA. AC Q9S5X8; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:AAD36591.1}; GN OrderedLocusNames=TM_1524 {ECO:0000313|EMBL:AAD36591.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36591.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36591.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:3O7O} RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS). RX PubMed=21082721; DOI=10.1002/pro.550; RA Forse G.J., Ram N., Banatao D.R., Cascio D., Sawaya M.R., Klock H.E., RA Lesley S.A., Yeates T.O.; RT "Synthetic symmetrization in the crystallization and structure RT determination of CelA from Thermotoga maritima."; RL Protein Sci. 20:168-178(2011). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) CC family. {ECO:0000256|RuleBase:RU361163}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36591.1; -; Genomic_DNA. DR PIR; H72240; H72240. DR RefSeq; NP_229324.1; NC_000853.1. DR RefSeq; WP_010865354.1; NC_000853.1. DR PDB; 3O7O; X-ray; 2.41 A; A/B=1-258. DR PDBsum; 3O7O; -. DR ProteinModelPortal; Q9S5X8; -. DR STRING; 243274.TM1524; -. DR CAZy; GH12; Glycoside Hydrolase Family 12. DR DNASU; 897984; -. DR EnsemblBacteria; AAD36591; AAD36591; TM_1524. DR GeneID; 897984; -. DR KEGG; tma:TM1524; -. DR PATRIC; 23938008; VBITheMar51294_1542. DR eggNOG; ENOG4111VJ0; LUCA. DR InParanoid; Q9S5X8; -. DR KO; K01179; -. DR OMA; FAMETWL; -. DR OrthoDB; EOG6SJJH4; -. DR BioCyc; TMAR243274:GC6P-1564-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008810; F:cellulase activity; IEA:InterPro. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.180; -; 1. DR InterPro; IPR013320; ConA-like_dom. DR InterPro; IPR013319; GH11/12. DR InterPro; IPR002594; GH12. DR Pfam; PF01670; Glyco_hydro_12; 1. DR SUPFAM; SSF49899; SSF49899; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3O7O}; KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361163}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosidase {ECO:0000256|RuleBase:RU361163}; KW Hydrolase {ECO:0000256|RuleBase:RU361163}; KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361163}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 258 AA; 29833 MW; D515E14EE2417A6B CRC64; MVVLMTKPGT SDFVWNGIPL SMELNLWNIK EYSGSVAMKF DGEKITFDAD IQNLSPKEPE RYVLGYPEFY YGYKPWENHT AEGSKLPVPV SSMKSFSVEV SFDIHHEPSL PLNFAMETWL TREKYQTEAS IGDVEIMVWF YFNNLTPGGE KIEEFTIPFV LNGESVEGTW ELWLAEWGWD YLAFRLKDPV KKGRVKFDVR HFLDAAGKAL SSSARVKDFE DLYFTVWEIG TEFGSPETKS AQFGWKFENF SIDLEVRE // ID Q9X0D4_THEMA Unreviewed; 405 AA. AC Q9X0D4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Transposase, IS605-TnpB family {ECO:0000313|EMBL:AAD36121.1}; GN OrderedLocusNames=TM_1044 {ECO:0000313|EMBL:AAD36121.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36121.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36121.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36121.1; -; Genomic_DNA. DR PIR; C72305; C72305. DR RefSeq; NP_228850.1; NC_000853.1. DR RefSeq; WP_010865252.1; NC_000853.1. DR STRING; 243274.TM1044; -. DR EnsemblBacteria; AAD36121; AAD36121; TM_1044. DR GeneID; 897061; -. DR KEGG; tma:TM1044; -. DR PATRIC; 23937017; VBITheMar51294_1057. DR eggNOG; ENOG4105D7V; Bacteria. DR eggNOG; COG0675; LUCA. DR InParanoid; Q9X0D4; -. DR KO; K07496; -. DR OMA; LTISRDY; -. DR OrthoDB; EOG6JTC9V; -. DR BioCyc; TMAR243274:GC6P-1073-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR001959; Transposase_2. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR InterPro; IPR021027; Transposase_put_HTH. DR Pfam; PF12323; HTH_OrfB_IS605; 1. DR Pfam; PF01385; OrfB_IS605; 1. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 44 HTH_OrfB_IS605. FT {ECO:0000259|Pfam:PF12323}. FT DOMAIN 174 287 OrfB_IS605. {ECO:0000259|Pfam:PF01385}. FT DOMAIN 301 371 OrfB_Zn_ribbon. FT {ECO:0000259|Pfam:PF07282}. SQ SEQUENCE 405 AA; 47688 MW; 64D1405D5F8EF9D1 CRC64; MTKMLRTYKF RIYPTREQEE KLAKHFGHTR FVYNFFLNYA NIIYRVMERP TYYNEWASVL VKLKKTNKYS WLNEVNSQAL QQSLKDLERA FKNFFKKQAG YPKFKKKKFS RQTFRIPQHI QLYIKEDNPK YGCIFVPKFK EGIKVRLHRK LPKDGKIKQA TFIKTATNKY YAAIVFEVQD AEVQNTSTGI LGIDLGIKDT ITLSDGKKYK MPDLSKYERQ IKRLHRRLSR KQRGSKNWEK ARLCLAKLYE KIVNIKNDWL HKITHDLVSE SQAGKIVVED LNIKGMVQNH RLARHIHMQS WRRFLELLEY KAKRCGIEVI KANRYYPSSQ MCSECGYINK EVKDLSVREW TCPVCGAHHD RDVNAAKNLV RYGLMLSIGR EPSEFTPVDS ALAAEPERGL RAITG // ID Q9X0K5_THEMA Unreviewed; 302 AA. AC Q9X0K5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 84. DE SubName: Full=Glycerol-3-phosphate ABC transporter, permease protein {ECO:0000313|EMBL:AAD36197.1}; GN OrderedLocusNames=TM_1121 {ECO:0000313|EMBL:AAD36197.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36197.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36197.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36197.1; -; Genomic_DNA. DR PIR; F72292; F72292. DR RefSeq; NP_228927.1; NC_000853.1. DR RefSeq; WP_010865267.1; NC_000853.1. DR ProteinModelPortal; Q9X0K5; -. DR STRING; 243274.TM1121; -. DR EnsemblBacteria; AAD36197; AAD36197; TM_1121. DR GeneID; 898643; -. DR KEGG; tma:TM1121; -. DR PATRIC; 23937177; VBITheMar51294_1137. DR eggNOG; ENOG4105E4X; Bacteria. DR eggNOG; COG1175; LUCA. DR InParanoid; Q9X0K5; -. DR KO; K05814; -. DR OMA; DGANGWT; -. DR OrthoDB; EOG61307J; -. DR BioCyc; TMAR243274:GC6P-1150-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 21 39 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 82 103 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 115 135 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 163 186 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 221 241 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 273 292 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 78 291 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 302 AA; 34526 MW; FF71E04BBD99F4A3 CRC64; MFPLTPYHFS GGIKLKRVLP YLLLLPTFVI ITLFIYWPAV YSLRLSFYRI TPFGNRMVFV GLRNFQRLFQ SPEYLNAIKV TVVYVLASLF LTIFLAFFIA LLLNMNLPGN RIFRALIFTP YAISPAIAGV LWSFLLNPVV GHVNYILSKL FGLQVEWLTT KPYALIAVII ATVWKTLPFD IIFYLAGLQD IPQELIEASL VEGANSWART WKIVFPLLSP ITFYLVIMNL VSFMFSSFAI IDVTTKGGPG NYTTTLIYRL YLDAFAFQKI GPAAAQSVIL FLIMAIVTIF YFKFGERRVH YQ // ID Q9X0F1_THEMA Unreviewed; 387 AA. AC Q9X0F1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36137.1}; GN OrderedLocusNames=TM_1061 {ECO:0000313|EMBL:AAD36137.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36137.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36137.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36137.1; -; Genomic_DNA. DR PIR; H72299; H72299. DR RefSeq; NP_228867.1; NC_000853.1. DR RefSeq; WP_010865257.1; NC_000853.1. DR STRING; 243274.TM1061; -. DR EnsemblBacteria; AAD36137; AAD36137; TM_1061. DR GeneID; 896977; -. DR KEGG; tma:TM1061; -. DR PATRIC; 23937051; VBITheMar51294_1074. DR eggNOG; ENOG41069F1; Bacteria. DR eggNOG; COG4289; LUCA. DR InParanoid; Q9X0F1; -. DR OMA; GIAPWLE; -. DR OrthoDB; EOG66XBDD; -. DR BioCyc; TMAR243274:GC6P-1090-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR016624; UCP014753. DR Pfam; PF10022; DUF2264; 1. DR PIRSF; PIRSF014753; UCP014753; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 387 AA; 44848 MW; B04D226AA0725E76 CRC64; MRSMTDVRRY WISLLRKICE MPLELCASDR LKKSMPVEGK KSEERRKFTH LELLGRIFCG ISPFLELNRE SPSTDPEERK IATRLSEFAV KSLDVATNPN CKDYMNFKEG RQPLVDAAFL VEAILRAPKV LWEDLDVSTK KRLIRELKAT RKIEPYFSNW LLFSAMIETF FFFAGEEWDS TKVDLILKNV ESWYKGDGAY GDGPFFRWDY YNSFVIYPMT IDVLRIISEE KTEWKELYVK VLRRAQRYAV VLERMISPEG TFPIIGRSIT YRTAVFHLLS QLSLLHLLPA SLSPAQVRCA LTAVLRRIFE NPSTFDENGW LKIGVIGSQP SLGEEYITTG SLYLCTTVFL PLGLPTSDPF WRDPCKKWTN KKVWEGEDVA PDRALED // ID Q9WYV9_THEMA Unreviewed; 162 AA. AC Q9WYV9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35574.1}; GN OrderedLocusNames=TM_0489 {ECO:0000313|EMBL:AAD35574.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35574.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35574.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35574.1; -; Genomic_DNA. DR PIR; H72369; H72369. DR RefSeq; NP_228299.1; NC_000853.1. DR RefSeq; WP_010865132.1; NC_000853.1. DR STRING; 243274.TM0489; -. DR EnsemblBacteria; AAD35574; AAD35574; TM_0489. DR GeneID; 897530; -. DR KEGG; tma:TM0489; -. DR KEGG; tmi:THEMA_02225; -. DR PATRIC; 23935883; VBITheMar51294_0496. DR eggNOG; ENOG4106F56; Bacteria. DR eggNOG; ENOG410Y77X; LUCA. DR OMA; FRYMSAN; -. DR OrthoDB; EOG63Z7C1; -. DR BioCyc; TMAR243274:GC6P-513-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 46 80 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 162 AA; 18832 MW; CC578ACB79DE375A CRC64; MGTVVFSWTY LLLGRNGNTK EPNQEDIEER IMELMGKFRY LSANRLELLE KKTQELRKLI SEANTVMSRL MVKMSEIERE RIFSSENGGE KSEKMEKPII PVIQEQEETK VEEKEEELET AIEKRIVSMY DRGFSEVDIA KNLGITVGEV RLILQLFKRN AG // ID Q9X2D3_THEMA Unreviewed; 102 AA. AC Q9X2D3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36876.1}; GN OrderedLocusNames=TM_1813 {ECO:0000313|EMBL:AAD36876.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36876.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36876.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36876.1; -; Genomic_DNA. DR PIR; B72209; B72209. DR RefSeq; NP_229610.1; NC_000853.1. DR RefSeq; WP_010865409.1; NC_000853.1. DR STRING; 243274.TM1813; -. DR EnsemblBacteria; AAD36876; AAD36876; TM_1813. DR GeneID; 897828; -. DR KEGG; tma:TM1813; -. DR BioCyc; TMAR243274:GC6P-1864-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 102 AA; 11947 MW; 9E895B1941D1C917 CRC64; MGEVVKLVTF LGLGKYEESE IKINGNLLDG CVKNDDSQDI FCVRQSIFPL ALIEYLNHIG KQVETIFFLT KTVKESKTWD ECRRFLRSNI KDFEIPERRI FK // ID Q9X1Z3_THEMA Unreviewed; 186 AA. AC Q9X1Z3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 107. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36732.1}; GN OrderedLocusNames=TM_1665 {ECO:0000313|EMBL:AAD36732.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36732.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36732.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains histidine kinase domain. CC {ECO:0000256|SAAS:SAAS00102782}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36732.1; -; Genomic_DNA. DR PIR; G72224; G72224. DR RefSeq; NP_229465.1; NC_000853.1. DR RefSeq; WP_010865378.1; NC_000853.1. DR ProteinModelPortal; Q9X1Z3; -. DR STRING; 243274.TM1665; -. DR EnsemblBacteria; AAD36732; AAD36732; TM_1665. DR GeneID; 897907; -. DR KEGG; tma:TM1665; -. DR PATRIC; 23938304; VBITheMar51294_1684. DR eggNOG; ENOG4108ZFE; Bacteria. DR eggNOG; ENOG4111N8X; LUCA. DR InParanoid; Q9X1Z3; -. DR OMA; HIDRPPL; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1711-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF02518; HATPase_c; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00528924}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|SAAS:SAAS00529081}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00528924}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00529081}. FT DOMAIN 1 108 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. SQ SEQUENCE 186 AA; 20895 MW; 810DE9B2A268C898 CRC64; MNRLLRTIAD HLMDVAQNAV KAGAKNIKIE IEETDEWFSF VVEDDGPGIE NPERVFDPFF TTRDPRLRKV GLGLPFLKQA AEQTGGFVKL HTERGKGTKV EARFNLKSVD CQPVGDVAGA LASLILSDPD VNWYIIRKKN GDGYEINTIE LREKGLWDPE SPSFAVFLFE TLESLERELK GGENNE // ID Q9WZK9_THEMA Unreviewed; 291 AA. AC Q9WZK9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35831.1}; GN OrderedLocusNames=TM_0750 {ECO:0000313|EMBL:AAD35831.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35831.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35831.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35831.1; -; Genomic_DNA. DR PIR; A72341; A72341. DR RefSeq; NP_228559.1; NC_000853.1. DR RefSeq; WP_010865198.1; NC_000853.1. DR STRING; 243274.TM0750; -. DR DNASU; 898417; -. DR EnsemblBacteria; AAD35831; AAD35831; TM_0750. DR GeneID; 898417; -. DR KEGG; tma:TM0750; -. DR PATRIC; 23936420; VBITheMar51294_0763. DR eggNOG; ENOG41077K6; Bacteria. DR eggNOG; ENOG410ZCGJ; LUCA. DR OMA; YLEYNGH; -. DR OrthoDB; EOG6ZH2J2; -. DR BioCyc; TMAR243274:GC6P-776-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR032547; DUF4941. DR Pfam; PF16299; DUF4941; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 291 AA; 32742 MW; 41E2B1B80FEAFCFE CRC64; MRRLILLFAI FSVTLLAETI TLDATLLNFD DLLQLLEIHS RVFDVTPPST GTVGSMRYLE YNGHVLANVE DLYILDNNKL PSPGVPVETL KLFGVDYIQT GDGVKIITCR VNSIEEIGKT VVVNFEGEKN FDVEQTQNSV RIIAKDWLLF RGVVKMPEEV LYEKENVRIE RTAESDGQFR ILLSAESVGK YVVKPFGERV DPYEKDVVFL VGYGDGRIIV RSFSKDLNGL DLPAYSESLK LARKIANELG YKLEECPVYD IPVGVIGMIV LLKGKDEMPV FLNTVERLMA E // ID Q9WZM3_THEMA Unreviewed; 240 AA. AC Q9WZM3; G4FD59; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35846.1}; GN OrderedLocusNames=TM_0764 {ECO:0000313|EMBL:AAD35846.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35846.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35846.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35846.1; -; Genomic_DNA. DR PIR; B72336; B72336. DR RefSeq; NP_228573.1; NC_000853.1. DR RefSeq; WP_004080934.1; NC_000853.1. DR STRING; 243274.TM0764; -. DR EnsemblBacteria; AAD35846; AAD35846; TM_0764. DR GeneID; 898432; -. DR KEGG; tma:TM0764; -. DR PATRIC; 23936450; VBITheMar51294_0777. DR eggNOG; ENOG4108UPB; Bacteria. DR eggNOG; ENOG4111JPT; LUCA. DR KO; K01992; -. DR OMA; FNDQVKP; -. DR OrthoDB; EOG6DNTCF; -. DR BioCyc; TMAR243274:GC6P-791-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032688; ABC2_membrane_2. DR Pfam; PF12679; ABC2_membrane_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 91 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 112 137 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 149 170 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 177 194 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 214 232 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 240 AA; 27543 MW; 99BE245381208F88 CRC64; MKVRFLVMFF LLLGTFVLLV VMKDYTPALT EMLKNVPEGF LEKFGVTEDF IKKLSEWNFY IITQWYGKNL GQFVPILAII IAFPIFAREI ENETIELLLV RMSREKLFNV KFFAPLVFTF AALAVLALVP IPVSWFIGER LDTGLVFKYF LVEMITTYLW FSVTVFFSVI SSDQVKPLIA SIALLAGTTV LGGFVKTLST LNTYSYVLKG DVTLWPSLIY TLTGVVFTYL SWRSFKTRDF // ID Q9X092_THEMA Unreviewed; 365 AA. AC Q9X092; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36079.1}; GN OrderedLocusNames=TM_0997 {ECO:0000313|EMBL:AAD36079.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36079.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36079.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36079.1; -; Genomic_DNA. DR PIR; G72306; G72306. DR RefSeq; NP_228805.1; NC_000853.1. DR RefSeq; WP_010865238.1; NC_000853.1. DR STRING; 243274.TM0997; -. DR EnsemblBacteria; AAD36079; AAD36079; TM_0997. DR GeneID; 897721; -. DR KEGG; tma:TM0997; -. DR KEGG; tmi:THEMA_09365; -. DR PATRIC; 23936925; VBITheMar51294_1011. DR eggNOG; ENOG4105DSX; Bacteria. DR eggNOG; COG0701; LUCA. DR KO; K07089; -. DR OMA; VLAVCSC; -. DR OrthoDB; EOG66XBBJ; -. DR BioCyc; TMAR243274:GC6P-1027-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005524; DUF318. DR Pfam; PF03773; ArsP_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 45 64 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 108 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 136 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 148 166 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 211 229 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 249 267 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 279 298 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 318 338 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 345 364 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 365 AA; 39590 MW; 1B807F78F6B005B7 CRC64; MRNLATFILI ALIFVAFYFV PFGHPIVDQS ILNGFYLLHE YAREHVLLCL VPAFFIAGTI SVMLKKDAVL KLLGPNAKRI ISYPVAAISG GILAVCSCTI LPLFGGIYKK GAGIGPATTF LFAGPAINIA AIFLTARVLG WDLGLARLIA TITAAVLIGL IMEMIYQERG EGGLAFTSDD DQYGVRGIIF FLIQLGFLVT SSLGINQTLK YSLMTLLGIS ALFMALFGFK RDTVENWLYE TWDFAKKILP YLFIGVFFAG VLTRLLPQQV VTALLGSNSF LSNLVASVIG TLMYFATLTE VPIVQALREL GMAKGPTLAL LMAGNSLSLP SMIVITKLLG KKKAFTYFGL VVVFSTLFGM IYGVI // ID Q9X0N4_THEMA Unreviewed; 503 AA. AC Q9X0N4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein {ECO:0000313|EMBL:AAD36226.1}; GN OrderedLocusNames=TM_1150 {ECO:0000313|EMBL:AAD36226.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36226.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36226.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36226.1; -; Genomic_DNA. DR PIR; B72289; B72289. DR RefSeq; NP_228956.1; NC_000853.1. DR RefSeq; WP_010865272.1; NC_000853.1. DR ProteinModelPortal; Q9X0N4; -. DR STRING; 243274.TM1150; -. DR EnsemblBacteria; AAD36226; AAD36226; TM_1150. DR GeneID; 898336; -. DR KEGG; tma:TM1150; -. DR PATRIC; 23937237; VBITheMar51294_1167. DR eggNOG; ENOG4105DEF; Bacteria. DR eggNOG; COG0747; LUCA. DR InParanoid; Q9X0N4; -. DR KO; K02035; -. DR OMA; ATRNPKG; -. DR OrthoDB; EOG61P6QJ; -. DR BioCyc; TMAR243274:GC6P-1179-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GOC. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 503 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004336009. FT DOMAIN 67 422 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. SQ SEQUENCE 503 AA; 57762 MW; 9C8134EFD879388B CRC64; MGMKKLVWLF LILTVTLSFA AKDIIVVGTT DKIRTLDPAN CYDYFSSNIL QNVMVGLVDY EIGTSVLKPV LAERWEVDET GTVYTFYLRK DAKFEDGTPI DAHVFKYSFD RVMKLNGDPA FLLSDVVEKT EVVDDYTFRV TLKYPFSAFV SVLGYTVAYP VNPKVYPADS FYEGIPSASG PYRVKEWIRD VRIVLEANPN YFGEKPKTKT IVINFYENAS TLRLALETGE IDVAYRHLDP RDVIDLEGRE DIVVYKGNSP QIRYLVINVT QPPFDNVKVR QALAYSVNRD VIVEDVFVGL AKPLYSMIPE GMWGHKDVFP ERDLEKARAL LKEAGYDENN PLVIDLWYTP SHYGTTEADV AQVLKESFEE TGVIKVNLKY AEWSTYVEYF LNGTMGLFLL GWYPDYLDPD DYVWPFLSES GAKSLGSFYS NPEVENLMIE ARKLTDLEKR TEIYYKVQEI LARDVPYIPL WQGVATCAAK KQVKGILLEP TQIFRYYILY WEE // ID Q9WY10_THEMA Unreviewed; 278 AA. AC Q9WY10; G4FH77; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 88. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35256.1}; GN OrderedLocusNames=TM_0163 {ECO:0000313|EMBL:AAD35256.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35256.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35256.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35256.1; -; Genomic_DNA. DR PIR; A72411; A72411. DR RefSeq; NP_227978.1; NC_000853.1. DR RefSeq; WP_004082787.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WY10; -. DR STRING; 243274.TM0163; -. DR DNASU; 897002; -. DR EnsemblBacteria; AAD35256; AAD35256; TM_0163. DR GeneID; 897002; -. DR KEGG; tma:TM0163; -. DR KEGG; tmi:THEMA_03985; -. DR KEGG; tmw:THMA_0159; -. DR PATRIC; 23935174; VBITheMar51294_0164. DR eggNOG; ENOG41062I4; Bacteria. DR eggNOG; ENOG41126CF; LUCA. DR OMA; LKMGICA; -. DR OrthoDB; EOG6S7XSR; -. DR BioCyc; TMAR243274:GC6P-164-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50005; TPR; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 128 150 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 20 53 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 278 AA; 31859 MW; DB2E79495ED8FA00 CRC64; MVVVKGLILI FILLSLVSVA NDLYSSALSA YLEGDYRRAL ELFENALRED PTIEERDPLV KLKMGICAYA IGDYEKARAY LSNFPDNVVA QEILKRLSVP EEVWKKYIET EKAGSESKKV EATKSIPFWL PMVVSAATFL SVFFLQRFLM KRLAIRSEKK SSIAEETPEV VEELPEGTVE EIPEEKPSET FAEKLDFLEE LLGKVQESNR EEYVDVDEVK NRAREILENS EEIPDDLTAE EVNLDVEEVI KELEEKEAYD EEDARKLVLV AKNKLREE // ID Q9X0Z8_THEMA Unreviewed; 157 AA. AC Q9X0Z8; G4FE77; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Type IV pilin-related protein {ECO:0000313|EMBL:AAD36346.1}; GN OrderedLocusNames=TM_1271 {ECO:0000313|EMBL:AAD36346.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36346.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36346.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36346.1; -; Genomic_DNA. DR PIR; F72274; F72274. DR RefSeq; NP_229076.1; NC_000853.1. DR RefSeq; WP_004079971.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0Z8; -. DR STRING; 243274.TM1271; -. DR EnsemblBacteria; AAD36346; AAD36346; TM_1271. DR GeneID; 898212; -. DR KEGG; tma:TM1271; -. DR KEGG; tmi:THEMA_07980; -. DR KEGG; tmw:THMA_1296; -. DR eggNOG; ENOG41061W7; Bacteria. DR eggNOG; ENOG411258P; LUCA. DR OMA; NDEVDIK; -. DR OrthoDB; EOG6QP12Z; -. DR BioCyc; TMAR243274:GC6P-1302-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro. DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro. DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro. DR InterPro; IPR000983; Bac_GSPG_pilin. DR InterPro; IPR012902; N_methyl_site. DR Pfam; PF13544; N_methyl_2; 1. DR PRINTS; PR00813; BCTERIALGSPG. DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1. DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methylation {ECO:0000256|RuleBase:RU000388}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 27 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 157 AA; 17313 MW; B955E692E26E5E3D CRC64; MRKRAGFTLI ELLIVMAIIA ALMAVLIPTA TGAMRKARAT RIAVQLRNLE QGIEQYLMAT LPATEDVDGK TLTNWRSELQ GKGFVDDTIL TDPNLETLTT SATNSNTQIE IKIVYNTRSD NLPDLVVGAL KETYGNGVSK ADTTKVQIIK TIDAFWW // ID Q9WZW2_THEMA Unreviewed; 168 AA. AC Q9WZW2; G4FCW6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35940.1}; GN OrderedLocusNames=TM_0858 {ECO:0000313|EMBL:AAD35940.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35940.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35940.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35940.1; -; Genomic_DNA. DR PIR; C72325; C72325. DR RefSeq; NP_228667.1; NC_000853.1. DR RefSeq; WP_004080748.1; NZ_CP011107.1. DR STRING; 243274.TM0858; -. DR EnsemblBacteria; AAD35940; AAD35940; TM_0858. DR GeneID; 898531; -. DR KEGG; tma:TM0858; -. DR KEGG; tmi:THEMA_00345; -. DR KEGG; tmw:THMA_0880; -. DR PATRIC; 23936644; VBITheMar51294_0871. DR eggNOG; ENOG410903H; Bacteria. DR eggNOG; ENOG4111QB7; LUCA. DR OMA; LPMHIPV; -. DR OrthoDB; EOG6M0T6K; -. DR BioCyc; TMAR243274:GC6P-888-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR024529; ECF_trnsprt_substrate-spec. DR Pfam; PF12822; DUF3816; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 64 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 125 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 131 153 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 168 AA; 18507 MW; 3851207F7CD89B7A CRC64; MRMRKLTYTA MWLAVGVALA YLFHLLNLGR MFLPLHLVAM LAGATSGAFV GGVTGAVLPI LSFLTMGMPP FPMFLFMIPE VFTYGFVMGV MKKNIFVRIL IAVVLGRLVY SVSYYVLGAL IGIKLQPLTS ILLSFTTGIP GIVLQFILVP LVYRRLQLIF EKGGKENA // ID Q9WYF5_THEMA Unreviewed; 64 AA. AC Q9WYF5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35407.1}; GN OrderedLocusNames=TM_0319 {ECO:0000313|EMBL:AAD35407.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35407.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35407.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35407.1; -; Genomic_DNA. DR PIR; F72392; F72392. DR RefSeq; NP_228131.1; NC_000853.1. DR RefSeq; WP_010865094.1; NC_000853.1. DR ProteinModelPortal; Q9WYF5; -. DR STRING; 243274.TM0319; -. DR EnsemblBacteria; AAD35407; AAD35407; TM_0319. DR GeneID; 897261; -. DR KEGG; tma:TM0319; -. DR PATRIC; 23935517; VBITheMar51294_0324. DR OMA; DTCCAKM; -. DR OrthoDB; EOG6358H8; -. DR BioCyc; TMAR243274:GC6P-332-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR019903; RIC_family. DR Pfam; PF04405; ScdA_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 64 AA; 7618 MW; 55ECFBF32EB37B73 CRC64; METHERLEKA LRKYGFDTCC AKMASLKDAC EKKWLDVEKV LEDLNRVVEE INEEERIIIE SQFL // ID Q9X2F6_THEMA Unreviewed; 54 AA. AC Q9X2F6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36900.1}; GN OrderedLocusNames=TM_1838 {ECO:0000313|EMBL:AAD36900.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36900.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36900.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36900.1; -; Genomic_DNA. DR PIR; A72206; A72206. DR RefSeq; NP_229634.1; NC_000853.1. DR RefSeq; WP_010865415.1; NC_000853.1. DR STRING; 243274.TM1838; -. DR EnsemblBacteria; AAD36900; AAD36900; TM_1838. DR GeneID; 897529; -. DR KEGG; tma:TM1838; -. DR PATRIC; 23938665; VBITheMar51294_1859. DR KO; K10109; -. DR BioCyc; TMAR243274:GC6P-1889-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032605; DUF4896. DR Pfam; PF16237; DUF4896; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 41 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 2 44 DUF4896. {ECO:0000259|Pfam:PF16237}. SQ SEQUENCE 54 AA; 6183 MW; 29F3010A7C064FFA CRC64; MFLAVFNAGM VWAGIFLLQN SYYELGIVLL TLLVLIDYFI FNPKLILTDT PFPL // ID Q9X056_THEMA Unreviewed; 193 AA. AC Q9X056; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=LemA protein {ECO:0000313|EMBL:AAD36040.1}; GN OrderedLocusNames=TM_0961 {ECO:0000313|EMBL:AAD36040.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36040.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36040.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:2ETD} RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 35-193, AND METHYLATION AT RP LYS-45; LYS-68; LYS-75; LYS-87; LYS-92; LYS-122; LYS-153; LYS-154; RP LYS-160; LYS-161; LYS-169; LYS-176; LYS-182 AND LYS-192. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of LEMA protein (tm0961) from THERMOTOGA MARITIMA RT at 2.28 A resolution."; RL Submitted (OCT-2005) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36040.1; -; Genomic_DNA. DR PIR; F72311; F72311. DR RefSeq; NP_228769.1; NC_000853.1. DR RefSeq; WP_010865226.1; NC_000853.1. DR PDB; 2ETD; X-ray; 2.28 A; A=35-193. DR PDBsum; 2ETD; -. DR ProteinModelPortal; Q9X056; -. DR SMR; Q9X056; 33-181. DR STRING; 243274.TM0961; -. DR EnsemblBacteria; AAD36040; AAD36040; TM_0961. DR GeneID; 898698; -. DR KEGG; tma:TM0961; -. DR PATRIC; 23936853; VBITheMar51294_0975. DR eggNOG; ENOG4108V0P; Bacteria. DR eggNOG; COG1704; LUCA. DR InParanoid; Q9X056; -. DR KO; K03744; -. DR OMA; SKWSQID; -. DR OrthoDB; EOG6MM1RR; -. DR BioCyc; TMAR243274:GC6P-991-MONOMER; -. DR EvolutionaryTrace; Q9X056; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.20.1440.20; -; 1. DR InterPro; IPR007156; LemA. DR InterPro; IPR023353; LemA-like_dom. DR Pfam; PF04011; LemA; 1. DR SUPFAM; SSF140478; SSF140478; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2ETD}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 127 154 {ECO:0000256|SAM:Coils}. FT MOD_RES 45 45 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 68 68 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 75 75 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 87 87 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 92 92 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 122 122 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 153 153 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 154 154 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 160 160 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 161 161 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 169 169 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 176 176 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 182 182 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. FT MOD_RES 192 192 N6,N6-dimethyllysine. FT {ECO:0000213|PDB:2ETD}. SQ SEQUENCE 193 AA; 21635 MW; F2C04F81DAB9F257 CRC64; MEGGIRVKRG LIVLIVILVL VVVIIGTTVG YYNYLVSLEQ EVQEKYSQIQ NQLQRRADLI PNLVETVKGY AAHEKEILEE IANARAKLIG AKTPQESAQA DAELSSALSR LLAIAENYPN LKADANFRQL MDELAGTENR IAVARRDYNE AVKKYNTAIK KFPGVIFAKM FGFEEKQYFE AKPGAEEVPE VKF // ID Q9WXS8_THEMA Unreviewed; 287 AA. AC Q9WXS8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 84. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD35167.1}; GN OrderedLocusNames=TM_0073 {ECO:0000313|EMBL:AAD35167.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35167.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35167.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35167.1; -; Genomic_DNA. DR PIR; A72421; A72421. DR RefSeq; NP_227889.1; NC_000853.1. DR RefSeq; WP_010865042.1; NC_000853.1. DR STRING; 243274.TM0073; -. DR TCDB; 3.A.1.5.13; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35167; AAD35167; TM_0073. DR GeneID; 896898; -. DR KEGG; tma:TM0073; -. DR PATRIC; 23934986; VBITheMar51294_0071. DR eggNOG; ENOG4108PKC; Bacteria. DR eggNOG; COG1173; LUCA. DR HOGENOM; HOG000171368; -. DR InParanoid; Q9WXS8; -. DR KO; K02034; -. DR OMA; LGTMLQW; -. DR OrthoDB; EOG6WX4NQ; -. DR BioCyc; TMAR243274:GC6P-73-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 20 38 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 79 101 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 113 134 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 140 159 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 193 219 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 255 275 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 75 268 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 287 AA; 32477 MW; 24C0E65D94A2303C CRC64; MERMQVLKDL LRDTRFRFGF IVLLVLLTLS ILSFFSPYNP YLWNQVPRDL PPHWPHILGT NSMGQDIFWK LTFAVRNSLV MSLIAGLVSR IIAMIVGMIA GYKGGAADRV LTFLSDSFLV IPLFIIIVLV ASIVKGRLSL PMLGLLLGVF GWAWDARVIR SQVLSLRERD FTYTALLSGS KALSIVFKEY LPFLIPLIFA TLIGNMSWAI GMEITLAILG VSNLDIPTLG TMLQWSINYQ ALLLGYWWWV LTPVLTSIFL FIALYLISIS ISEYLDPRMR IQRIGQA // ID Q9WXX2_THEMA Unreviewed; 245 AA. AC Q9WXX2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35211.1}; GN OrderedLocusNames=TM_0117 {ECO:0000313|EMBL:AAD35211.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35211.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35211.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35211.1; -; Genomic_DNA. DR PIR; D72417; D72417. DR RefSeq; NP_227933.1; NC_000853.1. DR RefSeq; WP_010865055.1; NC_000853.1. DR ProteinModelPortal; Q9WXX2; -. DR STRING; 243274.TM0117; -. DR EnsemblBacteria; AAD35211; AAD35211; TM_0117. DR GeneID; 896944; -. DR KEGG; tma:TM0117; -. DR PATRIC; 23935074; VBITheMar51294_0115. DR eggNOG; ENOG4105DCH; Bacteria. DR eggNOG; COG1533; LUCA. DR InParanoid; Q9WXX2; -. DR OMA; YCYAMDF; -. DR OrthoDB; EOG679T8Q; -. DR BioCyc; TMAR243274:GC6P-117-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 21 245 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 245 AA; 29293 MW; C300794975FB8C66 CRC64; MKMRVKEINV KSALTYSESK RRYTLSPYVG CTNACVYCYA SDYARRYREM IWKSEIIVKR NIAEVLRKDI IKKKPHHVFM STMCDPYQPI EKEYKLTRRC LEVFLEFPLL EIEVMILTKS TLVLRDLDLF KKMRRISVGL SVTTDDDEIR KMFEPNSSSI EERVEALKVL KENGIRTCVF ISPMLPMNPK KLASMLKPHV DCVFIDDMHY RWRVKDFYEK LGFSWALENE YFERTRKELL AFFQE // ID Q9X045_THEMA Unreviewed; 258 AA. AC Q9X045; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36029.1}; GN OrderedLocusNames=TM_0948 {ECO:0000313|EMBL:AAD36029.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36029.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36029.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36029.1; -; Genomic_DNA. DR PIR; G72313; G72313. DR RefSeq; NP_228756.1; NC_000853.1. DR RefSeq; WP_010865223.1; NC_000853.1. DR ProteinModelPortal; Q9X045; -. DR STRING; 243274.TM0948; -. DR DNASU; 898685; -. DR EnsemblBacteria; AAD36029; AAD36029; TM_0948. DR GeneID; 898685; -. DR KEGG; tma:TM0948; -. DR PATRIC; 23936827; VBITheMar51294_0962. DR eggNOG; COG5014; LUCA. DR InParanoid; Q9X045; -. DR OMA; WDEESFE; -. DR OrthoDB; EOG6HMXCZ; -. DR BioCyc; TMAR243274:GC6P-978-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016771; Fe-S_OxRdtase_rSAM_TM0948_prd. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF020275; RadSAM_TM0948_prd; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 82 219 Radical_SAM. {ECO:0000259|Pfam:PF04055}. SQ SEQUENCE 258 AA; 30261 MW; 3A7D822E74A22919 CRC64; MFHESYLENP VSLHYRIHPS SPRTIHTGCD HRVHYTQGGG NMAFNPVQRA MEMESLVMKG ERRKYYRFRY SLYYGGIVTA DTVGCKFLCA YCWNYFRNLR PKRAGDFLSP EEVAERLLEI SKKRKCDLFR ISGAEPILGR RSAEHVRKVI ELVNNTFILE TNGLMFGFDP SLVDLFVNLN VLIRVSVKGW DEESFEKITG ASGEYFRYQL KALEHLHGKV HFWVAVVYDL FREKGLKELE KRLPIPCRIE KEYLEMYP // ID Q9WXV0_THEMA Unreviewed; 158 AA. AC Q9WXV0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35189.1}; GN OrderedLocusNames=TM_0095 {ECO:0000313|EMBL:AAD35189.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35189.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35189.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35189.1; -; Genomic_DNA. DR PIR; G72417; G72417. DR RefSeq; NP_227911.1; NC_000853.1. DR RefSeq; WP_010865049.1; NC_000853.1. DR ProteinModelPortal; Q9WXV0; -. DR STRING; 243274.TM0095; -. DR EnsemblBacteria; AAD35189; AAD35189; TM_0095. DR GeneID; 896922; -. DR KEGG; tma:TM0095; -. DR KEGG; tmi:THEMA_04330; -. DR PATRIC; 23935030; VBITheMar51294_0093. DR eggNOG; ENOG4105IM6; Bacteria. DR eggNOG; COG1633; LUCA. DR OMA; EHARTFE; -. DR OrthoDB; EOG6KQ6GS; -. DR BioCyc; TMAR243274:GC6P-95-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR003251; Rubrerythrin. DR Pfam; PF02915; Rubrerythrin; 1. DR SUPFAM; SSF47240; SSF47240; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 8 152 Rubrerythrin. {ECO:0000259|Pfam:PF02915}. SQ SEQUENCE 158 AA; 18730 MW; 2580C1A3EC094269 CRC64; MSMFSAKELL NIAVRVEKEG EEFYRKIAER FTQPDIKEFF SYMSRQEAEH ARTFEKIGEE VGAKEETYLD MEDTEEYLKS FVEGKFFPSP EVMERYLKEK SVEEAIDFSI SVEKETIIFY YEILELLKNE KARSLVKGII EQEKQHVVKL LRIKGMIT // ID Q9X1T3_THEMA Unreviewed; 354 AA. AC Q9X1T3; G4FFY5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36664.1}; GN OrderedLocusNames=TM_1597 {ECO:0000313|EMBL:AAD36664.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36664.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36664.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36664.1; -; Genomic_DNA. DR PIR; A72234; A72234. DR RefSeq; NP_229397.1; NC_000853.1. DR RefSeq; WP_004082040.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1T3; -. DR STRING; 243274.TM1597; -. DR EnsemblBacteria; AAD36664; AAD36664; TM_1597. DR GeneID; 897442; -. DR KEGG; tma:TM1597; -. DR KEGG; tmi:THEMA_06265; -. DR KEGG; tmw:THMA_1637; -. DR PATRIC; 23938168; VBITheMar51294_1616. DR eggNOG; ENOG4106M28; Bacteria. DR eggNOG; COG3457; LUCA. DR OMA; GTNLNCL; -. DR OrthoDB; EOG6V7BJP; -. DR BioCyc; TMAR243274:GC6P-1643-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.20.20.10; -; 1. DR InterPro; IPR001608; Ala_racemase_N. DR InterPro; IPR029066; PLP-binding_barrel. DR Pfam; PF01168; Ala_racemase_N; 1. DR SUPFAM; SSF51419; SSF51419; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 8 223 Ala_racemase_N. FT {ECO:0000259|Pfam:PF01168}. SQ SEQUENCE 354 AA; 39717 MW; FAF750F7823C42FE CRC64; MVYPRLLINL KEIEENARKV VEMASRRGIE IVGVTKVTLG DPRFAETLRK AGIGILGESR IRNVLRMKKA GIEGPFMLLR LPMMSELVED VKHFDYIMVS DPDVAKKVDE LSREMKRNVK IIYMIDVGDL REGVWFEKAV EEIAQCRGAN IVGIGTNFGC YGGIIPTREK FEILLDIKEK LEKNHGFNIE IVSGGNTPAL YALENGEIPE GINQLRIGEA IVLGRDITNN RVIDWLSQNT FLIEAEVIEV KEKPSVPLGK RGLDVFGRKV DFVDRGIRKR AICALGEQDI DSRGLIPVDK GVEVLHASSD HIVLDVTDFG DVKVGDVFRF RMTYSCLLKA MTSPFVEKVY EPSI // ID Q9WYM0_THEMA Unreviewed; 301 AA. AC Q9WYM0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35474.1}; GN OrderedLocusNames=TM_0389 {ECO:0000313|EMBL:AAD35474.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35474.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35474.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35474.1; -; Genomic_DNA. DR PIR; E72384; E72384. DR RefSeq; NP_228199.1; NC_000853.1. DR RefSeq; WP_010865109.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYM0; -. DR STRING; 243274.TM0389; -. DR EnsemblBacteria; AAD35474; AAD35474; TM_0389. DR GeneID; 897370; -. DR KEGG; tma:TM0389; -. DR KEGG; tmw:THMA_0396; -. DR PATRIC; 23935661; VBITheMar51294_0395. DR eggNOG; ENOG4105DA5; Bacteria. DR eggNOG; COG1131; LUCA. DR InParanoid; Q9WYM0; -. DR KO; K01990; -. DR OMA; EKKENHY; -. DR OrthoDB; EOG65J54C; -. DR BioCyc; TMAR243274:GC6P-403-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35474.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35474.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 15 240 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 301 AA; 34115 MW; 99F7E30271C4AE4B CRC64; MVVLHSKGGF FLEILKVVDL KKHYGDVKAV DGISFTVERG TVFSFLGPNG AGKTTTVEIL EGLRKKDSGE IYYFGERKDV LDRETKRKIG VCLQKSAFFE NLTVWETLKL FRGLYGTGLD LKEVMGLFSL ENIEKKMVKT LSGGQLQRLA VAVAFINDPE IVFLDEPTTG LDPQARRQIW DTIEHFKNLG KTIFLTTHYM EEAERLSDHV CIIDHGKIIA EGTPSSLISS SGLKTVVEFD CDQDVNVRYL EKKENHYVVE TDAPEELIKD LLKNWNVSNI VIRKPNLEDV FLKLTGRDLR E // ID Q9WYQ5_THEMA Unreviewed; 296 AA. AC Q9WYQ5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35509.1}; GN OrderedLocusNames=TM_0424 {ECO:0000313|EMBL:AAD35509.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35509.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35509.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35509.1; -; Genomic_DNA. DR PIR; H72378; H72378. DR RefSeq; NP_228234.1; NC_000853.1. DR RefSeq; WP_010865115.1; NC_000853.1. DR ProteinModelPortal; Q9WYQ5; -. DR STRING; 243274.TM0424; -. DR DNASU; 897430; -. DR EnsemblBacteria; AAD35509; AAD35509; TM_0424. DR GeneID; 897430; -. DR KEGG; tma:TM0424; -. DR PATRIC; 23935733; VBITheMar51294_0430. DR eggNOG; ENOG4107ZZ1; Bacteria. DR eggNOG; COG0679; LUCA. DR InParanoid; Q9WYQ5; -. DR KO; K07088; -. DR OMA; QIARNPM; -. DR OrthoDB; EOG61ZTCS; -. DR BioCyc; TMAR243274:GC6P-439-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004776; Auxin_eff. DR Pfam; PF03547; Mem_trans; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 51 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 78 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 90 111 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 117 137 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 149 168 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 174 198 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 210 235 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 269 291 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 296 AA; 32389 MW; 3DA8934E3E45BCC4 CRC64; MLYTTFSAII PSFLIILIGY TVGKIFSEET MGLASKVAIW VMVPTVTFTF INEYTPSFST LGEFGLGVAI IFVIFYLYSR LFKEKKEVIH VTAVTANVGY LGYPILLSLW GEEALSLGVV YATLNIIMFS AVLPMFLGEK VNVKNLFKLP YVYALVAGFL TGKLGWSFRE LPEWLVNAIL MLKQSAIPYL LIYVGLSVSK LKLGRHLSKI GGIIVVNKLF LAPLIALVFA LIYGLEGLTA KVFVLETAMP AAVNAVILTS ALGGDSETVS YGVTLTTFFA IFTLPVWAVI LESIFG // ID Q9WZD4_THEMA Unreviewed; 220 AA. AC Q9WZD4; G4FDF8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE RecName: Full=Serine acetyltransferase {ECO:0000256|PIRNR:PIRNR000441}; DE EC=2.3.1.30 {ECO:0000256|PIRNR:PIRNR000441}; GN OrderedLocusNames=TM_0666 {ECO:0000313|EMBL:AAD35754.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35754.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35754.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-serine = CoA + O-acetyl-L- CC serine. {ECO:0000256|PIRNR:PIRNR000441}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC {ECO:0000256|PIRNR:PIRNR000441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35754.1; -; Genomic_DNA. DR PIR; G72349; G72349. DR RefSeq; NP_228475.1; NC_000853.1. DR RefSeq; WP_004081107.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZD4; -. DR STRING; 243274.TM0666; -. DR EnsemblBacteria; AAD35754; AAD35754; TM_0666. DR GeneID; 897781; -. DR KEGG; tma:TM0666; -. DR KEGG; tmw:THMA_0681; -. DR PATRIC; 23936246; VBITheMar51294_0676. DR eggNOG; ENOG4105D7W; Bacteria. DR eggNOG; COG1045; LUCA. DR InParanoid; Q9WZD4; -. DR KO; K00640; -. DR OMA; HQIALLW; -. DR OrthoDB; EOG6HMXK6; -. DR BioCyc; TMAR243274:GC6P-691-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0009001; F:serine O-acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR005881; Ser_O-AcTrfase. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 1. DR PIRSF; PIRSF000441; CysE; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR01172; cysE; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|PIRNR:PIRNR000441}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|PIRNR:PIRNR000441}. SQ SEQUENCE 220 AA; 24782 MW; 7A2883244CA5E141 CRC64; MRLLFRKAGE FFRDFVSIFK HISDDLEMYL KLDPAAESKL QVFFFYASFQ GLMWYRFAHF FYKWKLKVLA YLIYYFVRVV FSMDIHPAAR IAPGVVIDHG IGVVIGSTAS VGRGTLIYHG VTLGTRKPCS GKRHPDVGEN VMIGTGAKIL GPIRVGNNAV VGANAVVLED VPDGAVVVGV PARIVKWRRD FCDDGKTDRE HSYSETRFDR LENLLETGKE // ID Q9X0W2_THEMA Unreviewed; 413 AA. AC Q9X0W2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36310.1}; GN OrderedLocusNames=TM_1235 {ECO:0000313|EMBL:AAD36310.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36310.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36310.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36310.1; -; Genomic_DNA. DR PIR; D72279; D72279. DR RefSeq; NP_229040.1; NC_000853.1. DR RefSeq; WP_010865286.1; NC_000853.1. DR ProteinModelPortal; Q9X0W2; -. DR STRING; 243274.TM1235; -. DR EnsemblBacteria; AAD36310; AAD36310; TM_1235. DR GeneID; 898249; -. DR KEGG; tma:TM1235; -. DR PATRIC; 23937412; VBITheMar51294_1253. DR eggNOG; ENOG4108N76; Bacteria. DR eggNOG; COG1653; LUCA. DR KO; K02027; -. DR OMA; WDHTARI; -. DR OrthoDB; EOG63JR5T; -. DR BioCyc; TMAR243274:GC6P-1265-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 413 AA; 46545 MW; 18CCA0A482BFC45D CRC64; MVLLIVAGLM FGKVNFASTQ MTPAAEREFM LNKLAEFSKK SGIDVEFLNF EYPQLYSRLQ AEIRAGKNTL NLIADLQGNL YIMASEGFLS DLKDLKFEGK TFIETLEKFA YVKGEKVFIP WLQATYVMAV NKKAFDYLPR GLSKEDVIRG TEKWTYDALL EWAKNIYEKT KQPLLGFPIG PKGLWHRFLH GYIYPSFTGA QALKFDSVRA VEMWNYLKEL FKYVHPASST WDGMADPLLR EEVWIAWDHT ARLKPAIVEK PNDFVVVPVP RGPMGRGYII VLVGLAIPKD ADFEEPAKVI DFLTSPEMQV EILKNVGFFP VVQEAVGAVP EGALKVLAEG VINQSATKDS IVSFIPSLGP KSGEFTETYR MAFTRIVFQG EDPAKVVKEL GERIRQLFKE SGAELPEPDA SLF // ID Q9X1R7_THEMA Unreviewed; 381 AA. AC Q9X1R7; G4FFW9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36648.1}; GN OrderedLocusNames=TM_1581 {ECO:0000313|EMBL:AAD36648.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36648.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36648.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36648.1; -; Genomic_DNA. DR PIR; E72235; E72235. DR RefSeq; NP_229381.1; NC_000853.1. DR RefSeq; WP_004082008.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1R7; -. DR STRING; 243274.TM1581; -. DR EnsemblBacteria; AAD36648; AAD36648; TM_1581. DR GeneID; 897955; -. DR KEGG; tma:TM1581; -. DR KEGG; tmi:THEMA_06375; -. DR KEGG; tmw:THMA_1616; -. DR PATRIC; 23938126; VBITheMar51294_1600. DR eggNOG; ENOG4107XUP; Bacteria. DR eggNOG; COG1524; LUCA. DR OMA; GFGWNIM; -. DR OrthoDB; EOG60SCMQ; -. DR BioCyc; TMAR243274:GC6P-1622-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR002591; Phosphodiest/P_Trfase. DR Pfam; PF01663; Phosphodiest; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 381 AA; 44635 MW; C8AEA1FA4E79B2A1 CRC64; MELKKLDEGL FWPDYKNSIV NFSNSILELF DEKPLHRPFR FPKRVLENVR KVIVMVIDGL SFEIFSDTIH DDDVQVFPCS AVFPTTTAAA LPSLYSALTP LEHGFLGYIL YLREVGSLVN MIEMSPPGLP RDSVLRFHDF KFTTIFQRLQ SKVKSFFLIP RYLLGTGFSR IMSQGSEQIG FSSFGDMIER TLEVLEKHDR TLVFIYWPTL DSIAHKNGVG REYIRELRWI YRILKSELLR RLKQDTLFFL VSDHGQISTP QDNEIWWNFS SEVMRFLDRP PAGEQRMMFL YTKKKRALIE YLKEKYGDFA VFLDTKDVVQ LFGTGRKHPE FFSRVGDAVL ITRETFSFNY RYTGKEESLS GRHGSLSYQE LVVPLVVYRR W // ID Q9X1K2_THEMA Unreviewed; 137 AA. AC Q9X1K2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36581.1}; GN OrderedLocusNames=TM_1514 {ECO:0000313|EMBL:AAD36581.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36581.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36581.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36581.1; -; Genomic_DNA. DR PIR; C72245; C72245. DR RefSeq; NP_229314.1; NC_000853.1. DR RefSeq; WP_010865351.1; NC_000853.1. DR STRING; 243274.TM1514; -. DR EnsemblBacteria; AAD36581; AAD36581; TM_1514. DR GeneID; 897989; -. DR KEGG; tma:TM1514; -. DR KEGG; tmi:THEMA_06730; -. DR PATRIC; 23937986; VBITheMar51294_1531. DR OMA; TMVSLAY; -. DR OrthoDB; EOG6HJ29C; -. DR BioCyc; TMAR243274:GC6P-1554-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 80 101 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 113 132 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 137 AA; 15416 MW; 8FB6A95ED9415AEB CRC64; MFEEGERLRY LVQLFSLLLV IIGILGLVVW AGLYFLAPYI EGFAGIKLPE NIANVLLACF LPILGSGILL NFYTSSGIKW FVVLGFVVLS VSFVSEIYGL YILRGIFSKI APAYLIFLLF TMVSLAYFLT IIRRDED // ID Q9WYX4_THEMA Unreviewed; 42 AA. AC Q9WYX4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35589.1}; GN OrderedLocusNames=TM_0504 {ECO:0000313|EMBL:AAD35589.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35589.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35589.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35589.1; -; Genomic_DNA. DR PIR; F72367; F72367. DR RefSeq; NP_228314.1; NC_000853.1. DR RefSeq; WP_010865138.1; NC_000853.1. DR STRING; 243274.TM0504; -. DR EnsemblBacteria; AAD35589; AAD35589; TM_0504. DR GeneID; 897547; -. DR KEGG; tma:TM0504; -. DR BioCyc; TMAR243274:GC6P-528-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 42 AA; 4280 MW; 532245F0A45DC4E7 CRC64; MEAGGFEPPS EDGGPWASPS AARVFALGRD LPRAGCPLPQ PS // ID Q9WXN8_THEMA Unreviewed; 606 AA. AC Q9WXN8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein {ECO:0000313|EMBL:AAD35125.1}; GN OrderedLocusNames=TM_0031 {ECO:0000313|EMBL:AAD35125.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35125.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35125.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:2O7I, ECO:0000213|PDB:3I5O} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 22-606. RX PubMed=19801540; DOI=10.1074/jbc.M109.041624; RA Cuneo M.J., Beese L.S., Hellinga H.W.; RT "Structural analysis of semi-specific oligosaccharide recognition by a RT cellulose-binding protein of thermotoga maritima reveals adaptations RT for functional diversification of the oligopeptide periplasmic binding RT protein fold."; RL J. Biol. Chem. 284:33217-33223(2009). RN [3] {ECO:0000213|PDB:4JSD, ECO:0000213|PDB:4JSO} RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 24-605 IN COMPLEX WITH RP CALCIUM. RX PubMed=24090243; DOI=10.1186/1472-6807-13-18; RA Munshi P., Stanley C.B., Ghimire-Rijal S., Lu X., Myles D.A., RA Cuneo M.J.; RT "Molecular details of ligand selectivity determinants in a promiscuous RT beta-glucan periplasmic binding protein."; RL BMC Struct. Biol. 13:18-18(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35125.1; -; Genomic_DNA. DR PIR; A72429; A72429. DR RefSeq; NP_227847.1; NC_000853.1. DR RefSeq; WP_010865032.1; NC_000853.1. DR PDB; 2O7I; X-ray; 1.50 A; A=22-606. DR PDB; 3I5O; X-ray; 1.50 A; A/B=22-606. DR PDB; 4JSD; X-ray; 2.05 A; A=24-605. DR PDB; 4JSO; X-ray; 2.07 A; A=24-605. DR PDBsum; 2O7I; -. DR PDBsum; 3I5O; -. DR PDBsum; 4JSD; -. DR PDBsum; 4JSO; -. DR ProteinModelPortal; Q9WXN8; -. DR SMR; Q9WXN8; 24-605. DR STRING; 243274.TM0031; -. DR TCDB; 3.A.1.5.16; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35125; AAD35125; TM_0031. DR GeneID; 896852; -. DR KEGG; tma:TM0031; -. DR PATRIC; 23934902; VBITheMar51294_0029. DR eggNOG; ENOG4107QMM; Bacteria. DR eggNOG; ENOG410XNRA; LUCA. DR InParanoid; Q9WXN8; -. DR KO; K02035; -. DR OMA; KNTQLIG; -. DR OrthoDB; EOG6QRW4B; -. DR BioCyc; TMAR243274:GC6P-31-MONOMER; -. DR EvolutionaryTrace; Q9WXN8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0042884; P:microcin transport; IBA:GO_Central. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2O7I, ECO:0000213|PDB:3I5O, KW ECO:0000213|PDB:4JSD, ECO:0000213|PDB:4JSO}; KW Calcium {ECO:0000213|PDB:4JSD, ECO:0000213|PDB:4JSO}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Metal-binding {ECO:0000213|PDB:4JSD, ECO:0000213|PDB:4JSO}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 606 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004335943. FT DOMAIN 73 465 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. FT METAL 56 56 Calcium. {ECO:0000213|PDB:4JSD, FT ECO:0000213|PDB:4JSO}. FT METAL 60 60 Calcium; via carbonyl oxygen. FT {ECO:0000213|PDB:4JSD, FT ECO:0000213|PDB:4JSO}. FT METAL 165 165 Calcium. {ECO:0000213|PDB:4JSD, FT ECO:0000213|PDB:4JSO}. SQ SEQUENCE 606 AA; 69942 MW; FC7217EC175A6082 CRC64; MGMRKSLVLL LALLVLSSLM AQVSLPREDT VYIGGALWGP ATTWNLYAPQ STWGTDQFMY LPAFQYDLGR DAWIPVIAER YEFVDDKTLR IYIRPEARWS DGVPITADDF VYALELTKEL GIGPGGGWDT YIEYVKAVDT KVVEFKAKEE NLNYFQFLSY SLGAQPMPKH VYERIRAQMN IKDWINDKPE EQVVSGPYKL YYYDPNIVVY QRVDDWWGKD IFGLPRPKYL AHVIYKDNPS ASLAFERGDI DWNGLFIPSV WELWEKKGLP VGTWYKKEPY FIPDGVGFVY VNNTKPGLSD PAVRKAIAYA IPYNEMLKKA YFGYGSQAHP SMVIDLFEPY KQYIDYELAK KTFGTEDGRI PFDLDMANKI LDEAGYKKGP DGVRVGPDGT KLGPYTISVP YGWTDWMMMC EMIAKNLRSI GIDVKTEFPD FSVWADRMTK GTFDLIISWS VGPSFDHPFN IYRFVLDKRL SKPVGEVTWA GDWERYDNDE VVELLDKAVS TLDPEVRKQA YFRIQQIIYR DMPSIPAFYT AHWYEYSTKY WINWPSEDNP AWFRPSPWHA DAWPTLFIIS KKSDPQPVPS WLGTVDEGGI EIPTAKIFED LQKATM // ID Q9X2C6_THEMA Unreviewed; 195 AA. AC Q9X2C6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36869.1}; GN OrderedLocusNames=TM_1806 {ECO:0000313|EMBL:AAD36869.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36869.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36869.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36869.1; -; Genomic_DNA. DR PIR; C72208; C72208. DR RefSeq; NP_229603.1; NC_000853.1. DR RefSeq; WP_010865407.1; NC_000853.1. DR STRING; 243274.TM1806; -. DR EnsemblBacteria; AAD36869; AAD36869; TM_1806. DR GeneID; 897433; -. DR KEGG; tma:TM1806; -. DR KEGG; tmi:THEMA_05160; -. DR PATRIC; 23938601; VBITheMar51294_1827. DR OMA; PAFQPIS; -. DR OrthoDB; EOG60KN3C; -. DR BioCyc; TMAR243274:GC6P-1857-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 195 AA; 21731 MW; FD14D96941CD9689 CRC64; MVCVVVGRFP IYVEEEFTSD EKKWEFVLSK IESIDPAVAS FVEEAPDGTM RVIGPFRARS GYALVISSPL SSLFHFLVLN VPRVLNAVVK PGRAYVEIYE KRDLFDSPGV FTLKVKGAKG FSLKQLKEDM KLFLGVEVEP AFQPVSLRNT KNGVIVTLKT LTPETTALVK LSRLCGTGES RKYGHGDVEI YRIVE // ID Q9X2E9_THEMA Unreviewed; 30 AA. AC Q9X2E9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36892.1}; GN OrderedLocusNames=TM_1829 {ECO:0000313|EMBL:AAD36892.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36892.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36892.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36892.1; -; Genomic_DNA. DR PIR; A72205; A72205. DR RefSeq; NP_229626.1; NC_000853.1. DR RefSeq; WP_010865412.1; NC_000853.1. DR STRING; 243274.TM1829; -. DR EnsemblBacteria; AAD36892; AAD36892; TM_1829. DR GeneID; 897820; -. DR KEGG; tma:TM1829; -. DR PATRIC; 23938645; VBITheMar51294_1849. DR BioCyc; TMAR243274:GC6P-1880-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 30 AA; 3362 MW; 874A30495C6A8222 CRC64; MEKTEYKRNA LGAGWNSRPA VKAREPSQEG // ID Q9WZ16_THEMA Unreviewed; 348 AA. AC Q9WZ16; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 93. DE RecName: Full=Threonine synthase {ECO:0000256|PIRNR:PIRNR038945}; DE EC=4.2.3.1 {ECO:0000256|PIRNR:PIRNR038945}; GN OrderedLocusNames=TM_0546 {ECO:0000313|EMBL:AAD35631.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35631.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35631.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L- CC phosphohomoserine and the beta-addition of water to produce L- CC threonine. {ECO:0000256|PIRNR:PIRNR038945}. CC -!- CATALYTIC ACTIVITY: O-phospho-L-homoserine + H(2)O = L-threonine + CC phosphate. {ECO:0000256|PIRNR:PIRNR038945}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|PIRNR:PIRNR038945}; CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 5/5. CC {ECO:0000256|PIRNR:PIRNR038945}. CC -!- SIMILARITY: Belongs to the threonine synthase family. CC {ECO:0000256|PIRNR:PIRNR038945}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35631.1; -; Genomic_DNA. DR PIR; G72364; G72364. DR RefSeq; NP_228356.1; NC_000853.1. DR RefSeq; WP_010865143.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ16; -. DR SMR; Q9WZ16; 1-332. DR STRING; 243274.TM0546; -. DR DNASU; 897600; -. DR EnsemblBacteria; AAD35631; AAD35631; TM_0546. DR GeneID; 897600; -. DR KEGG; tma:TM0546; -. DR KEGG; tmi:THEMA_01945; -. DR KEGG; tmw:THMA_0559; -. DR PATRIC; 23935999; VBITheMar51294_0554. DR eggNOG; ENOG4107R5I; Bacteria. DR eggNOG; COG0498; LUCA. DR KO; K01733; -. DR OMA; SKAIMCA; -. DR OrthoDB; EOG6HMX9M; -. DR BioCyc; TMAR243274:GC6P-570-MONOMER; -. DR UniPathway; UPA00050; UER00065. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0004795; F:threonine synthase activity; IBA:GO_Central. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS. DR InterPro; IPR004450; Thr_synthase-like. DR InterPro; IPR026260; Thr_Synthase_bac/arc. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF00291; PALP; 1. DR PIRSF; PIRSF038945; Thr_synthase; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR00260; thrC; 1. DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR038945}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Lyase {ECO:0000256|PIRNR:PIRNR038945}; KW Pyridoxal phosphate {ECO:0000256|PIRNR:PIRNR038945}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Threonine biosynthesis {ECO:0000256|PIRNR:PIRNR038945}. FT DOMAIN 23 316 PALP. {ECO:0000259|Pfam:PF00291}. SQ SEQUENCE 348 AA; 37762 MW; 8963F16DFFB9C77A CRC64; MKLGILEKYR RFLPVTDKTP MLSLNEGNTP LIPLVNMSRE LGINIYVKYE GSNPTGSFKD RGMVVAVAKA LEEGSKAIMC ASTGNTSASA AAYAARAGIK AIVLIPEGKI ALGKLAQAMI YGAVVLQVRG NFDKCLELVK EITSKYPITL VNSINPYRLE GQKTAAFEIV DELGDAPDYH FIPVGNAGNI SAYWMGYKEY YQHGFSTKLP KMMGFQAEGA APIVRGHPIE NPETVATAIR IGNPANWEKA VRARDESGGD IDMVSDEEIL RAQRLLAQKE GIFCEPASAA SIAGLLKKHR QGIFRGGEIV VCTLTGNGLK DPNIVISQLE PPRIIEGRVE EILEVLDI // ID Q9X1T5_THEMA Unreviewed; 120 AA. AC Q9X1T5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36666.1}; GN OrderedLocusNames=TM_1599 {ECO:0000313|EMBL:AAD36666.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36666.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36666.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36666.1; -; Genomic_DNA. DR PIR; C72234; C72234. DR RefSeq; NP_229399.1; NC_000853.1. DR RefSeq; WP_010865369.1; NC_000853.1. DR STRING; 243274.TM1599; -. DR EnsemblBacteria; AAD36666; AAD36666; TM_1599. DR GeneID; 897450; -. DR KEGG; tma:TM1599; -. DR KEGG; tmi:THEMA_06255; -. DR PATRIC; 23938172; VBITheMar51294_1618. DR OMA; YRIRCEY; -. DR OrthoDB; EOG6CK7S8; -. DR BioCyc; TMAR243274:GC6P-1645-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64 84 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 120 AA; 14025 MW; 5D8FAD83E77D0C92 CRC64; MKLLKDDRLN RILDGEEPIE GLPEELLRDY RVYREAITLY RIRCEYVPSE RLMRKILKKR RKKLVLSTVF AGIAVSLLLL SVVLDIFPVS PSRKVVQKQN PVVKELIDYI KTVEVVSDGW // ID Q9X0P0_THEMA Unreviewed; 129 AA. AC Q9X0P0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36232.1}; GN OrderedLocusNames=TM_1156 {ECO:0000313|EMBL:AAD36232.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36232.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36232.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36232.1; -; Genomic_DNA. DR PIR; B72287; B72287. DR RefSeq; NP_228962.1; NC_000853.1. DR RefSeq; WP_010865274.1; NC_000853.1. DR STRING; 243274.TM1156; -. DR EnsemblBacteria; AAD36232; AAD36232; TM_1156. DR GeneID; 898330; -. DR KEGG; tma:TM1156; -. DR PATRIC; 23937249; VBITheMar51294_1173. DR eggNOG; ENOG41067S9; Bacteria. DR eggNOG; COG1983; LUCA. DR InParanoid; Q9X0P0; -. DR OMA; WLIMPEE; -. DR OrthoDB; EOG6W9X4M; -. DR BioCyc; TMAR243274:GC6P-1185-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007168; Phageshock_PspC_N. DR Pfam; PF04024; PspC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 57 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 99 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 124 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 4 61 PspC. {ECO:0000259|Pfam:PF04024}. SQ SEQUENCE 129 AA; 14539 MW; 563FA22A939527E1 CRC64; MFMKQLRRSR KNRIIAGVCG GFAEYFGVDP TLVRLIWVLI TLAWGAGLLL YIIAWLIMPE EEGETESEKK PLQNTEGLKV LVGGLLIFLG IVFLVSAFFP IFFGVAWKVV LALLLVIFGV LLLLRRDEK // ID Q9WZB0_THEMA Unreviewed; 265 AA. AC Q9WZB0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35726.1}; GN OrderedLocusNames=TM_0642 {ECO:0000313|EMBL:AAD35726.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35726.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35726.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35726.1; -; Genomic_DNA. DR PIR; A72351; A72351. DR RefSeq; NP_228451.1; NC_000853.1. DR RefSeq; WP_010865173.1; NC_000853.1. DR STRING; 243274.TM0642; -. DR EnsemblBacteria; AAD35726; AAD35726; TM_0642. DR GeneID; 897746; -. DR KEGG; tma:TM0642; -. DR PATRIC; 23936198; VBITheMar51294_0652. DR eggNOG; ENOG4108MTC; Bacteria. DR eggNOG; ENOG410YMA0; LUCA. DR OrthoDB; EOG6PZX79; -. DR BioCyc; TMAR243274:GC6P-667-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 265 AA; 29629 MW; 10706D5EA1B4FBA9 CRC64; MTEDEWEKQS SFVPVNADPL SPYTEKVKTL AAHRLDFHIR ENLRLGVGEL TMIGGKYPDL FAVSPFSIWH NNYNEGYTNS MASFDFSWVP KKGFEVHGEF VLDDLVGTTE NESKPTAYAF NVGVRRALST GSLKGVLGVE YALATKFVYN TFLPYLKFNN RIVYLTNLPS SRTIVDYPVG FAFGPDAKLL NVSFDLFKEN VSLETDFFYL VKGPNTLYTE YPTAEEGETK TIFGASLRGK IGHVSFSLLF SGSEFLAGLG IEFGF // ID Q9WXU0_THEMA Unreviewed; 93 AA. AC Q9WXU0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35179.1}; GN OrderedLocusNames=TM_0085 {ECO:0000313|EMBL:AAD35179.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35179.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35179.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35179.1; -; Genomic_DNA. DR PIR; G72419; G72419. DR RefSeq; NP_227901.1; NC_000853.1. DR RefSeq; WP_010865046.1; NC_000853.1. DR STRING; 243274.TM0085; -. DR EnsemblBacteria; AAD35179; AAD35179; TM_0085. DR GeneID; 896912; -. DR KEGG; tma:TM0085; -. DR KEGG; tmi:THEMA_04380; -. DR PATRIC; 23935010; VBITheMar51294_0083. DR eggNOG; COG2747; LUCA. DR KO; K02398; -. DR OMA; INGPRDI; -. DR BioCyc; TMAR243274:GC6P-85-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro. DR InterPro; IPR007412; FlgM. DR InterPro; IPR031316; FlgM_C. DR Pfam; PF04316; FlgM; 1. DR SUPFAM; SSF101498; SSF101498; 1. DR TIGRFAMs; TIGR03824; FlgM_jcvi; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 45 89 FlgM. {ECO:0000259|Pfam:PF04316}. SQ SEQUENCE 93 AA; 10867 MW; D9E5023060C47C63 CRC64; MMIDRINGPR DINPIEGIKK PSVEKSKEKR KKESTDNVEL RHVEDVRKFA EEAKNISTVR EQLVEELKKA IESGNYFIDT ERLARKILEE LSE // ID Q9X1D3_THEMA Unreviewed; 35 AA. AC Q9X1D3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36484.1}; GN OrderedLocusNames=TM_1413 {ECO:0000313|EMBL:AAD36484.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36484.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36484.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36484.1; -; Genomic_DNA. DR PIR; F72258; F72258. DR RefSeq; NP_229214.1; NC_000853.1. DR RefSeq; WP_010865333.1; NZ_CP011107.1. DR EnsemblBacteria; AAD36484; AAD36484; TM_1413. DR GeneID; 898063; -. DR KEGG; tma:TM1413; -. DR KEGG; tmw:THMA_1441; -. DR PATRIC; 23937770; VBITheMar51294_1424. DR BioCyc; TMAR243274:GC6P-1450-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 35 AA; 3771 MW; AB05B5B5C1DB2259 CRC64; MVYGKREYGS SKNILLSECV CGINSPELNG VSIIP // ID Q9X154_THEMA Unreviewed; 144 AA. AC Q9X154; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36403.1}; GN OrderedLocusNames=TM_1331 {ECO:0000313|EMBL:AAD36403.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36403.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36403.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36403.1; -; Genomic_DNA. DR PIR; G72267; G72267. DR RefSeq; NP_229133.1; NC_000853.1. DR RefSeq; WP_010865316.1; NC_000853.1. DR STRING; 243274.TM1331; -. DR EnsemblBacteria; AAD36403; AAD36403; TM_1331. DR GeneID; 898151; -. DR KEGG; tma:TM1331; -. DR KEGG; tmi:THEMA_07690; -. DR eggNOG; ENOG4108E3M; Bacteria. DR eggNOG; ENOG41103K6; LUCA. DR OMA; IEEARFW; -. DR OrthoDB; EOG6N0HKR; -. DR BioCyc; TMAR243274:GC6P-1362-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:InterPro. DR InterPro; IPR003708; SecB. DR SUPFAM; SSF54611; SSF54611; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 144 AA; 16759 MW; 454DAD603039B678 CRC64; MMKQKNSIIP SRSFFRMLGY FIEEAKFQLK EVKGNFIDYQ LELEPEFGKI VHQKDYFSRS IVLGVYIRGR QGNVQVHDMY VRIKGKFEAN IEESSEDLFD KLCKYNGLMN LLIIVRSFVA TTTAQMGIHP VLIPMIDLTK VEVN // ID Q9X1V1_THEMA Unreviewed; 283 AA. AC Q9X1V1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=ATP synthase subunit a {ECO:0000256|RuleBase:RU000483}; GN OrderedLocusNames=TM_1616 {ECO:0000313|EMBL:AAD36683.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36683.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36683.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Key component of the proton channel; it plays a direct CC role in the translocation of protons across the membrane. CC {ECO:0000256|RuleBase:RU000483}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU000483}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000483}. CC -!- SIMILARITY: Belongs to the ATPase A chain family. CC {ECO:0000256|RuleBase:RU000483}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36683.1; -; Genomic_DNA. DR PIR; B72232; B72232. DR RefSeq; NP_229416.1; NC_000853.1. DR RefSeq; WP_010865370.1; NC_000853.1. DR ProteinModelPortal; Q9X1V1; -. DR STRING; 243274.TM1616; -. DR DNASU; 897933; -. DR EnsemblBacteria; AAD36683; AAD36683; TM_1616. DR GeneID; 897933; -. DR KEGG; tma:TM1616; -. DR KEGG; tmi:THEMA_06170; -. DR PATRIC; 23938206; VBITheMar51294_1635. DR eggNOG; ENOG4107VQ1; Bacteria. DR eggNOG; COG0356; LUCA. DR KO; K02108; -. DR OMA; TIMELIY; -. DR OrthoDB; EOG6K4054; -. DR BioCyc; TMAR243274:GC6P-1662-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.120.220; -; 1. DR HAMAP; MF_01393; ATP_synth_a_bact; 1. DR InterPro; IPR000568; ATPase_F0-cplx_asu. DR InterPro; IPR023011; ATPase_F0-cplx_asu_AS. DR PANTHER; PTHR11410; PTHR11410; 2. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR SUPFAM; SSF81336; SSF81336; 1. DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1. DR PROSITE; PS00449; ATPASE_A; 1. PE 3: Inferred from homology; KW CF(0) {ECO:0000256|RuleBase:RU000483}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrogen ion transport {ECO:0000256|RuleBase:RU000483}; KW Ion transport {ECO:0000256|RuleBase:RU000483}; KW Membrane {ECO:0000256|RuleBase:RU000483}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU000483}; KW Transport {ECO:0000256|RuleBase:RU000483}. SQ SEQUENCE 283 AA; 31770 MW; 77060CFFF5AE1C00 CRC64; MDGLKITFSK KEKIFLAVFI SLYVLVAVLN IQQLKRTPME EIFGGLGKRW IVDINGFRIN PMTIIVGTAI AIFLIVLAYR LRKFEMIPNR KQAFMESILE MFYEIVDESI PDKRFVKPTF VVATTLFLFI TISNIIGGAV PGVSVVADET GAVQKVVLFN DTWPAPTGDL NTNLTYAVMV LIISHAFAIK SKGFKEWLKS WFYPNPVMFP INLIGELAKP ISHSLRLFGN IGGGAILVYI LSYMTKYFFA PIIFWGFFGI FVGLVQAFVF SMLAVAYISS QLS // ID Q9WYH6_THEMA Unreviewed; 58 AA. AC Q9WYH6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35437.1}; GN OrderedLocusNames=TM_0341 {ECO:0000313|EMBL:AAD35437.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35437.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35437.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35437.1; -; Genomic_DNA. DR PIR; C72388; C72388. DR RefSeq; NP_228152.1; NC_000853.1. DR RefSeq; WP_010865100.1; NC_000853.1. DR STRING; 243274.TM0341; -. DR EnsemblBacteria; AAD35437; AAD35437; TM_0341. DR GeneID; 897297; -. DR KEGG; tma:TM0341; -. DR PATRIC; 23935561; VBITheMar51294_0345. DR OrthoDB; EOG6QP126; -. DR BioCyc; TMAR243274:GC6P-355-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 58 AA; 6238 MW; AFB0091EAB0B01C3 CRC64; MKGDLALIDA KESGKTPVVE GDIARISNFF VGGILKMISP FISNISVSSR KKKVEGEE // ID Q9WYJ3_THEMA Unreviewed; 304 AA. AC Q9WYJ3; G4FHS0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35445.1}; GN OrderedLocusNames=TM_0358 {ECO:0000313|EMBL:AAD35445.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35445.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35445.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains DAGKc domain. CC {ECO:0000256|SAAS:SAAS00382907}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35445.1; -; Genomic_DNA. DR PIR; F72386; F72386. DR RefSeq; NP_228169.1; NC_000853.1. DR RefSeq; WP_004083159.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYJ3; -. DR STRING; 243274.TM0358; -. DR EnsemblBacteria; AAD35445; AAD35445; TM_0358. DR GeneID; 897316; -. DR KEGG; tma:TM0358; -. DR KEGG; tmi:THEMA_02925; -. DR KEGG; tmw:THMA_0366; -. DR PATRIC; 23935597; VBITheMar51294_0363. DR eggNOG; ENOG410806K; Bacteria. DR eggNOG; COG1597; LUCA. DR OMA; KGTHITH; -. DR OrthoDB; EOG64XXPV; -. DR BioCyc; TMAR243274:GC6P-372-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR InterPro; IPR005218; Diacylglycerol/lipid_kinase. DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom. DR InterPro; IPR016064; NAD/diacylglycerol_kinase. DR Pfam; PF00781; DAGK_cat; 1. DR SMART; SM00046; DAGKc; 1. DR SUPFAM; SSF111331; SSF111331; 1. DR TIGRFAMs; TIGR00147; TIGR00147; 1. DR PROSITE; PS50146; DAGK; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00459942}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|SAAS:SAAS00459936}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00459942}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00459936}. FT DOMAIN 1 134 DAGKc. {ECO:0000259|PROSITE:PS50146}. SQ SEQUENCE 304 AA; 34249 MW; DFC84FAA61E24666 CRC64; MKVVFLICNP AAGGGRAGKI WNRVEDLLKK HGIDHKFAFT ERPGHAMEIS KKAFKEGYRR IAAFGGDGTV NEMVNGIFLN GYDLREVVFG WIPFGSGKDW ARTIGVPLEI EEAIKMLKDG KEFVQDLGVG EYEKASGEIE KRAFVNVAGL FFDGFVTYRT NLLKRKNRVS YFSRIFSSII EYDPPTARIQ IDEKVWEKRV FSMNVGICKY NGGGMNQLPH AVPDDGLLAV TVINDIGKLR ILANLHRVFN GKLLEHPGVE GYQAKKVVVE FQRDEPVEFD GESFWAKKIF FSIIPGVIRV LVKK // ID Q9WXQ1_THEMA Unreviewed; 211 AA. AC Q9WXQ1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35138.1}; GN OrderedLocusNames=TM_0044 {ECO:0000313|EMBL:AAD35138.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35138.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35138.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35138.1; -; Genomic_DNA. DR PIR; A72426; A72426. DR RefSeq; NP_227860.1; NC_000853.1. DR RefSeq; WP_010865035.1; NC_000853.1. DR STRING; 243274.TM0044; -. DR EnsemblBacteria; AAD35138; AAD35138; TM_0044. DR GeneID; 896868; -. DR KEGG; tma:TM0044; -. DR BioCyc; TMAR243274:GC6P-44-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 211 AA; 24195 MW; 3548AA648C4015C3 CRC64; MPPSFLWISS EVDLKVSSNG DCDHVVFLVD SHFNTCTESN YESFKVSCVA GTNTKDPTEF TKIELGHRPA GSTESPYDNS GFSVEFNGVF ENSKQIECVL TRSSINREKR SSISTKKISK TKPKTQLHIF CYRICEIETK IQVISGRSIG SCRCRRNNKI IIPKNADLQI LQRESESSHC HYREKNHKKL FHENSLPVMK FSVFNYNTQK W // ID Q9X1C5_THEMA Unreviewed; 471 AA. AC Q9X1C5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Lipopolysaccharide biosynthesis protein-related protein {ECO:0000313|EMBL:AAD36476.1}; GN OrderedLocusNames=TM_1405 {ECO:0000313|EMBL:AAD36476.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36476.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36476.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36476.1; -; Genomic_DNA. DR PIR; F72257; F72257. DR RefSeq; NP_229206.1; NC_000853.1. DR RefSeq; WP_010865330.1; NC_000853.1. DR ProteinModelPortal; Q9X1C5; -. DR STRING; 243274.TM1405; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR DNASU; 898071; -. DR EnsemblBacteria; AAD36476; AAD36476; TM_1405. DR GeneID; 898071; -. DR KEGG; tma:TM1405; -. DR eggNOG; ENOG4105DNM; Bacteria. DR eggNOG; COG0438; LUCA. DR InParanoid; Q9X1C5; -. DR OMA; SSWVNEM; -. DR OrthoDB; EOG6X10X6; -. DR BioCyc; TMAR243274:GC6P-1442-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR022622; DUF3492. DR InterPro; IPR001296; Glyco_trans_1. DR Pfam; PF11997; DUF3492; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 260 DUF3492. {ECO:0000259|Pfam:PF11997}. FT DOMAIN 281 441 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 471 AA; 53908 MW; CE7F53271AEF8D8C CRC64; MAPMKIGLIL EGTYPYVTGG VSNWVHTLLT NLPEFEFEIY HLKAVTEPQT IKYKIPENVT AVHELNIFGD FESDSSQKAN LESLERIVSQ LSIERDIRSI VSFAIDFIRE NAGKNVRKML KTKGFWNILL KIYEEFFSER GLTEFYWMIM NLFLPVVNVL QFVPNRCDLF HVPSTGYASL VGMNGKFVHD VPLVITEHGI YHKEREREII LSTWVPDAYK PMWIELFRII SMIAYRVSDA LTTLYRKNQI YQLELGADPE KMFIIPNGIN VEEYDLPPEK HEGFVVGFVG RVARIKDLKT AIRAISIVKE VVGEKLTFLI IGPVDAEDYL AECKRLVRVL RLEDTVEFLG PQNVKEYYPK FDLLLLSSVS EGQPLVILEA MAAGVPIVAT DVGACRDIIY DKDGQCGIVV PPKDHLSMSK AIIKLYEDKE LRDTFSKNAK KVVQKYRVET MIEKYRNLYL SLTSKKTVST V // ID Q9X1R1_THEMA Unreviewed; 346 AA. AC Q9X1R1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36642.1}; GN OrderedLocusNames=TM_1575 {ECO:0000313|EMBL:AAD36642.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36642.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36642.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36642.1; -; Genomic_DNA. DR PIR; H72237; H72237. DR RefSeq; NP_229375.1; NC_000853.1. DR RefSeq; WP_010865363.1; NC_000853.1. DR STRING; 243274.TM1575; -. DR EnsemblBacteria; AAD36642; AAD36642; TM_1575. DR GeneID; 897958; -. DR KEGG; tma:TM1575; -. DR PATRIC; 23938114; VBITheMar51294_1594. DR eggNOG; ENOG4106BTK; Bacteria. DR eggNOG; COG1520; LUCA. DR OMA; ADDFAVW; -. DR OrthoDB; EOG6CP3RV; -. DR BioCyc; TMAR243274:GC6P-1616-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 2.140.10.10; -; 1. DR InterPro; IPR027295; Quinoprotein_ADH-like_fam. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR SUPFAM; SSF50998; SSF50998; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 346 AA; 40247 MW; 3AC749B039EE1B3B CRC64; MDNFENLSTK DSFPEHFRRA VRGIFPDSQL PDEFFLVVYR DGKFERSLQP TATFAGRKAP VVIIPQWKEK HTLEIGNYRK VVDEEFYQIG GKMIYAGRDI FIEDVPGLYR NIDMVFLDGE KECIYRDGFL MMEEKILKIE EPVDVVDGIV ITRHRMGSKE IDDTILFRWN NFVLTASGFL VDIKGKWSWK VSNAPVEFSF QGDIFYVLDV CGFLRSYNLK TRQLLWEKKF EGAWGLDSSK DRVFLGAGDE VLVLNAQDGE TIERMEADDF AVWKGRLLVY KDGKVDGEDM EGFFIRNFGM PLFVSGKRVV MFGTEKKEFE EVEKVRLFDW GTVIKAGDEL WLIRRD // ID Q9X0W9_THEMA Unreviewed; 30 AA. AC Q9X0W9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36317.1}; GN OrderedLocusNames=TM_1242 {ECO:0000313|EMBL:AAD36317.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36317.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36317.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36317.1; -; Genomic_DNA. DR PIR; D72276; D72276. DR RefSeq; NP_229047.1; NC_000853.1. DR RefSeq; WP_010865289.1; NC_000853.1. DR STRING; 243274.TM1242; -. DR EnsemblBacteria; AAD36317; AAD36317; TM_1242. DR GeneID; 898241; -. DR KEGG; tma:TM1242; -. DR BioCyc; TMAR243274:GC6P-1273-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 30 AA; 3158 MW; F5519F304936D8B0 CRC64; MNENYIGGKH FEKNRKTGAL APVPGRGGGT // ID Q9WXV4_THEMA Unreviewed; 257 AA. AC Q9WXV4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35193.1}; GN OrderedLocusNames=TM_0099 {ECO:0000313|EMBL:AAD35193.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35193.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35193.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35193.1; -; Genomic_DNA. DR PIR; C72418; C72418. DR RefSeq; NP_227915.1; NC_000853.1. DR RefSeq; WP_010865051.1; NC_000853.1. DR STRING; 243274.TM0099; -. DR EnsemblBacteria; AAD35193; AAD35193; TM_0099. DR GeneID; 896926; -. DR KEGG; tma:TM0099; -. DR KEGG; tmi:THEMA_04310; -. DR PATRIC; 23935038; VBITheMar51294_0097. DR OMA; FSELRIW; -. DR OrthoDB; EOG6J74T9; -. DR BioCyc; TMAR243274:GC6P-99-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 257 AA; 29601 MW; 69E8627E9851851E CRC64; MEGMELIFEG KPLKSFCFSM VFNIGWRHEP PELRGSLLRT FDDLVGILKK ELPEYFDVSK HIDAEFSKLK VWGTSDEAES LLEAVHKVLA LPPQIFLEIG GGLIFSVAAG AMKSEVLKEL EKMKFPRPSK APKVHIRPRN FFKTFNLSRL ETIFLYSFLR ETAGEVFLEL SAIGDRIHYG KNFRLSPFHE ISKYKDRFKA SLAKQLETTE GTVDLLINLN IFKKEKVLIR DALEELENLD LLKKIDTIDK MFRRVSS // ID Q9X125_THEMA Unreviewed; 37 AA. AC Q9X125; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36373.1}; GN OrderedLocusNames=TM_1299 {ECO:0000313|EMBL:AAD36373.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36373.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36373.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36373.1; -; Genomic_DNA. DR PIR; E72269; E72269. DR RefSeq; NP_229103.1; NC_000853.1. DR RefSeq; WP_010865301.1; NC_000853.1. DR STRING; 243274.TM1299; -. DR EnsemblBacteria; AAD36373; AAD36373; TM_1299. DR GeneID; 898183; -. DR KEGG; tma:TM1299; -. DR BioCyc; TMAR243274:GC6P-1330-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 17 34 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 37 AA; 4251 MW; 6B0E73D8582D84DD CRC64; MVLSKVDDFS ILSLQNYYFY AILSHCCVTL GVKLHKT // ID Q9WZP6_THEMA Unreviewed; 262 AA. AC Q9WZP6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35871.1}; GN OrderedLocusNames=TM_0789 {ECO:0000313|EMBL:AAD35871.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35871.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35871.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35871.1; -; Genomic_DNA. DR PIR; F72333; F72333. DR RefSeq; NP_228598.1; NC_000853.1. DR RefSeq; WP_010865205.1; NC_000853.1. DR ProteinModelPortal; Q9WZP6; -. DR STRING; 243274.TM0789; -. DR EnsemblBacteria; AAD35871; AAD35871; TM_0789. DR GeneID; 898457; -. DR KEGG; tma:TM0789; -. DR PATRIC; 23936498; VBITheMar51294_0801. DR eggNOG; ENOG4105GC9; Bacteria. DR eggNOG; COG1082; LUCA. DR OMA; VVHFPNA; -. DR OrthoDB; EOG6D8B7X; -. DR BioCyc; TMAR243274:GC6P-816-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF01261; AP_endonuc_2; 1. DR SUPFAM; SSF51658; SSF51658; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 46 222 AP_endonuc_2. {ECO:0000259|Pfam:PF01261}. SQ SEQUENCE 262 AA; 30841 MW; EB0BEAF090793822 CRC64; MWTILCDKDS GGVLLRKGVS TSIIRSNPDL LEALPKAELY ELGFFKAEDL EKVLRFFHDK NFGIHAPFIY RYRYHHPNPT SLNEEEREDT FSVNKKCAEL ARKIGAEYMI IHFPNALQKE NWLSVYREVE REFSELAGVI SVRVENVYGN DHFHSAEDYR TFLENTGCKM CVDIGHLLLD AEVYGFSPIE FIEKLSDFVE EFHIYYADFE TYKKCHHAPW GESKEFLEVL EFIKDFDADF VLEPTPECEE GLEKLFEYWR DL // ID Q9X2G2_THEMA Unreviewed; 258 AA. AC Q9X2G2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=ROK family protein {ECO:0000313|EMBL:AAD36909.1}; GN OrderedLocusNames=TM_1847 {ECO:0000313|EMBL:AAD36909.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36909.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36909.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36909.1; -; Genomic_DNA. DR PIR; H72202; H72202. DR RefSeq; NP_229643.1; NC_000853.1. DR RefSeq; WP_010865418.1; NC_000853.1. DR ProteinModelPortal; Q9X2G2; -. DR STRING; 243274.TM1847; -. DR EnsemblBacteria; AAD36909; AAD36909; TM_1847. DR GeneID; 897811; -. DR KEGG; tma:TM1847; -. DR PATRIC; 23938683; VBITheMar51294_1868. DR eggNOG; ENOG411056T; LUCA. DR InParanoid; Q9X2G2; -. DR OMA; LTEINFI; -. DR OrthoDB; EOG6CGCDC; -. DR BioCyc; TMAR243274:GC6P-1898-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR000600; ROK. DR Pfam; PF00480; ROK; 1. DR PROSITE; PS01125; ROK; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 258 AA; 28966 MW; A7F07A3E6BC1C17E CRC64; MTEKVSRFPG VFPLIVIGVP GSVDKTHKKL AFAPNLNRWR DIDVEKYFKV FEVYLENDAN LAALAEMMRN KHFGDRKNIV YILVREGIGG GIIIEGKLYK GSFNAAGEIG HMKMYDRGPC FCGRVGCWEA NTSISHCVRQ YEKKKPLPGN TMYEKFETLC RIYEEDPLAK EVLDEFTGIL IDGIVNLVNI LSPEIVIVGG EGVFLPESVF EVIVSETRRQ VHPMDKEVSV EKGSLSNKEV VLEGTSILSS MMISERLV // ID Q9WXL9_THEMA Unreviewed; 31 AA. AC Q9WXL9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35098.1}; GN OrderedLocusNames=TM_0004 {ECO:0000313|EMBL:AAD35098.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35098.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35098.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35098.1; -; Genomic_DNA. DR PIR; F72429; F72429. DR RefSeq; NP_227820.1; NC_000853.1. DR RefSeq; WP_010865023.1; NC_000853.1. DR EnsemblBacteria; AAD35098; AAD35098; TM_0004. DR GeneID; 896812; -. DR KEGG; tma:TM0004; -. DR BioCyc; TMAR243274:GC6P-4-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 31 AA; 3827 MW; 692CE05C37AA1940 CRC64; MKDLYERFNN SLEVWKLVEL FGTSIRIHLF Q // ID Q9X0U8_THEMA Unreviewed; 282 AA. AC Q9X0U8; G4FEC5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD36296.1}; GN OrderedLocusNames=TM_1221 {ECO:0000313|EMBL:AAD36296.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36296.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36296.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36296.1; -; Genomic_DNA. DR PIR; C72282; C72282. DR RefSeq; NP_229026.1; NC_000853.1. DR RefSeq; WP_004080070.1; NZ_CP011107.1. DR STRING; 243274.TM1221; -. DR TCDB; 3.A.1.5.14; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36296; AAD36296; TM_1221. DR GeneID; 898263; -. DR KEGG; tma:TM1221; -. DR KEGG; tmi:THEMA_08225; -. DR KEGG; tmw:THMA_1247; -. DR PATRIC; 23937384; VBITheMar51294_1239. DR eggNOG; ENOG4105DG9; Bacteria. DR eggNOG; COG1173; LUCA. DR KO; K02034; -. DR OMA; FFAGYEG; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-1251-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 16 36 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 80 103 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 115 135 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 194 216 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 247 271 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 76 268 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 282 AA; 31306 MW; 036AA09AC6257258 CRC64; MTRKEFVHFF LKNKKVIFAI CVYAGLIILA LVGPYLSPYK DPLAFVGPGY QPPSKEHWLG TNTFGQDIFT QLVYGLRSSL FVGVLGGTLA TVIGLLIGFV AGYKGGWFDE LLMMFTNILM VIPTLALLII IAAYLPYRGV FIESIIIGLT AWPWTARAVR AQTLSLKTRE FVDLARITAR KPMKIIFGEI MPNMMSYVFM VFILQFGGAI LAATGLDFIG LGPTRGISLG IMMQQATLWN AIQLGMWWWA ITPGAVITLM VATLYVMNAG LDEVFNPKLR EM // ID Q9X0L2_THEMA Unreviewed; 164 AA. AC Q9X0L2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 110. DE RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145}; DE EC=1.16.3.2 {ECO:0000256|RuleBase:RU361145}; GN OrderedLocusNames=TM_1128 {ECO:0000313|EMBL:AAD36204.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36204.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36204.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1VLG} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH IRON. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of Ferritin (TM1128) from Thermotoga maritima at RT 2.00 A resolution."; RL Submitted (JUL-2004) to the PDB data bank. RN [3] {ECO:0000213|PDB:1Z4A} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS). RA Steinbacher S., Schiffmann S., Bacher A., Fischer M.; RT "Structure of T. maritima ferritin."; RL Submitted (MAR-2005) to the PDB data bank. CC -!- FUNCTION: Iron-storage protein. {ECO:0000256|RuleBase:RU361145}. CC -!- CATALYTIC ACTIVITY: 4 Fe(2+) + O(2) + 6 H(2)O = 4 (FeO(OH)) + 8 CC H(+). {ECO:0000256|RuleBase:RU361145}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361145}. CC -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily. CC {ECO:0000256|RuleBase:RU361145}. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC {ECO:0000256|RuleBase:RU003668}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36204.1; -; Genomic_DNA. DR PIR; E72293; E72293. DR RefSeq; NP_228934.1; NC_000853.1. DR RefSeq; WP_010865269.1; NC_000853.1. DR PDB; 1VLG; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-164. DR PDB; 1Z4A; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-164. DR PDBsum; 1VLG; -. DR PDBsum; 1Z4A; -. DR ProteinModelPortal; Q9X0L2; -. DR SMR; Q9X0L2; 1-164. DR STRING; 243274.TM1128; -. DR EnsemblBacteria; AAD36204; AAD36204; TM_1128. DR GeneID; 898636; -. DR KEGG; tma:TM1128; -. DR KEGG; tmi:THEMA_08705; -. DR PATRIC; 23937191; VBITheMar51294_1144. DR eggNOG; ENOG41090A1; Bacteria. DR eggNOG; COG1528; LUCA. DR KO; K02217; -. DR OMA; CEDKGFE; -. DR BioCyc; TMAR243274:GC6P-1157-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR001519; Ferritin. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR008331; Ferritin_DPS_dom. DR PANTHER; PTHR11431; PTHR11431; 1. DR Pfam; PF00210; Ferritin; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VLG, ECO:0000213|PDB:1Z4A}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|RuleBase:RU361145}; KW Iron {ECO:0000256|RuleBase:RU361145}; KW Iron storage {ECO:0000256|RuleBase:RU361145}; KW Metal-binding {ECO:0000213|PDB:1VLG, ECO:0000256|RuleBase:RU361145}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 147 Ferritin-like diiron. FT {ECO:0000259|PROSITE:PS50905}. FT METAL 19 19 Iron. {ECO:0000213|PDB:1VLG}. FT METAL 52 52 Iron. {ECO:0000213|PDB:1VLG}. FT METAL 55 55 Iron; via pros nitrogen. FT {ECO:0000213|PDB:1VLG}. SQ SEQUENCE 164 AA; 19379 MW; 1C239C9E3AD045BA CRC64; MMVISEKVRK ALNDQLNREI YSSYLYLSMA TYFDAEGFKG FAHWMKKQAQ EELTHAMKFY EYIYERGGRV ELEAIEKPPS NWNGIKDAFE AALKHEEFVT QSIYNILELA SEEKDHATVS FLKWFVDEQV EEEDQVREIL DLLEKANGQM SVIFQLDRYL GQRE // ID Q9WY29_THEMA Unreviewed; 113 AA. AC Q9WY29; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35278.1}; GN OrderedLocusNames=TM_0185 {ECO:0000313|EMBL:AAD35278.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35278.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35278.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35278.1; -; Genomic_DNA. DR PIR; D72408; D72408. DR RefSeq; NP_228000.1; NC_000853.1. DR RefSeq; WP_010865068.1; NC_000853.1. DR ProteinModelPortal; Q9WY29; -. DR STRING; 243274.TM0185; -. DR EnsemblBacteria; AAD35278; AAD35278; TM_0185. DR GeneID; 897033; -. DR KEGG; tma:TM0185; -. DR KEGG; tmi:THEMA_03850; -. DR PATRIC; 23935226; VBITheMar51294_0186. DR eggNOG; ENOG4105J98; Bacteria. DR eggNOG; COG3832; LUCA. DR OMA; WFTDGMK; -. DR OrthoDB; EOG6HQSPR; -. DR BioCyc; TMAR243274:GC6P-191-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR Gene3D; 3.30.530.20; -; 1. DR InterPro; IPR013538; Activator_of_Hsp90_ATPase. DR InterPro; IPR023393; START-like_dom. DR Pfam; PF08327; AHSA1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 113 AA; 13386 MW; 1117BB5A2FFDE7A4 CRC64; MKMELKEGGK IFFRWFRKTF GEEVTDEGII HRLEPPNLIE FSWNTYEDGF RSRVKMEFFP SSYNGTWVQV EDHTIVLNEE DMKIKLECAV GWGEMLTLAK IWIEYGISTL ENP // ID Q9WYQ1_THEMA Unreviewed; 283 AA. AC Q9WYQ1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 90. DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35505.1}; GN OrderedLocusNames=TM_0420 {ECO:0000313|EMBL:AAD35505.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35505.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35505.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35505.1; -; Genomic_DNA. DR PIR; D72378; D72378. DR RefSeq; NP_228230.1; NC_000853.1. DR RefSeq; WP_008191996.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYQ1; -. DR STRING; 243274.TM0420; -. DR TCDB; 3.A.1.1.38; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35505; AAD35505; TM_0420. DR GeneID; 897423; -. DR KEGG; tma:TM0420; -. DR KEGG; tmi:THEMA_02625; -. DR KEGG; tmw:THMA_0426; -. DR PATRIC; 23935723; VBITheMar51294_0425. DR eggNOG; ENOG410894D; Bacteria. DR eggNOG; COG0395; LUCA. DR HOGENOM; HOG000220526; -. DR KO; K17239; -. DR OMA; SFMAAYA; -. DR BioCyc; TMAR243274:GC6P-435-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 16 39 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 81 102 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 114 137 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 202 224 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 245 269 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 77 269 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 283 AA; 32441 MW; 093A6ED3F910F4F5 CRC64; MMKVTFWQKN SEKIRNLIII VILFLITSPI LIGYVWLVLR SFSEDLVNGF VPTKLTLKNW RFLWEEIKGY PNIWQTTLNT ALLALGVMGV EVAITSLGGY ALSRYDFPGR SSMMKFILAL HAFPAISLMT AVFYLLWTLK LLDTLWGVIL LKASLEVPWG TWIMKGFYDG IPWELEWAGL VDGYSRFQVW RRVLLPLVKP GIAVTAIFAF LSGWSEFVFV NTFIFSQNLW TLSKYVKGFI GDYRFADYGL VTAVGLFYMI PTIIFFFFVS KHMIKLTIGG VKG // ID Q9WZJ0_THEMA Unreviewed; 192 AA. AC Q9WZJ0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35833.1}; GN OrderedLocusNames=TM_0731 {ECO:0000313|EMBL:AAD35833.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35833.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35833.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35833.1; -; Genomic_DNA. DR PIR; F72338; F72338. DR RefSeq; NP_228540.1; NC_000853.1. DR RefSeq; WP_010865194.1; NC_000853.1. DR STRING; 243274.TM0731; -. DR EnsemblBacteria; AAD35833; AAD35833; TM_0731. DR GeneID; 898398; -. DR KEGG; tma:TM0731; -. DR PATRIC; 23936382; VBITheMar51294_0744. DR eggNOG; ENOG4105WPN; Bacteria. DR eggNOG; COG1636; LUCA. DR InParanoid; Q9WZJ0; -. DR KO; K09765; -. DR OMA; PNIHPYT; -. DR OrthoDB; EOG6S26FS; -. DR BioCyc; TMAR243274:GC6P-757-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR003828; DUF208. DR Pfam; PF02677; DUF208; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 192 AA; 22509 MW; 78F78856FDBB3122 CRC64; MGTVLIHVCC APDLLTTIFH VRDAEFFFYN PNIQPLSEYE KRREAVDKVA NHFSLNVRYG EYSTEEIRKW YTAVKDYKDL GEGSKRCERC ISFLLERTAQ EARKRGHESF STTLLASPRK NLPMIENIGK TIEEKYGVKF FFKNFRKGGA YQEGVRLSKE LGIYRQNYCG CVFSLLERRE KHAEISRKRG HM // ID Q9X107_THEMA Unreviewed; 322 AA. AC Q9X107; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36355.1}; GN OrderedLocusNames=TM_1280 {ECO:0000313|EMBL:AAD36355.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36355.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36355.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36355.1; -; Genomic_DNA. DR PIR; D72273; D72273. DR RefSeq; NP_229085.1; NC_000853.1. DR RefSeq; WP_010865295.1; NC_000853.1. DR ProteinModelPortal; Q9X107; -. DR STRING; 243274.TM1280; -. DR DNASU; 898203; -. DR EnsemblBacteria; AAD36355; AAD36355; TM_1280. DR GeneID; 898203; -. DR KEGG; tma:TM1280; -. DR PATRIC; 23937498; VBITheMar51294_1295. DR eggNOG; ENOG41080M4; Bacteria. DR eggNOG; COG2971; LUCA. DR InParanoid; Q9X107; -. DR OMA; DENFIAN; -. DR OrthoDB; EOG6QG8NX; -. DR BioCyc; TMAR243274:GC6P-1311-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR002731; ATPase_BadF. DR Pfam; PF01869; BcrAD_BadFG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 296 BcrAD_BadFG. {ECO:0000259|Pfam:PF01869}. SQ SEQUENCE 322 AA; 35928 MW; 4F9D8E9B34ABC856 CRC64; MKRLLFLGVD VGGTKTLAVL SDEQGNVLAI YKGKGANYQV VGKENAVRNL KDVIEAILDR AGKTRKEIDF AFFGYAGADF DYEMKIVREI LEKLGLEKFD FDNDGRIALR SGVFDDIGIM VSCGTGSISY ASDGRRVNRI GGLSFSLGER LGSHYIASLV TSAVMRAKDG RDDWTTLVDE VEKEIGPVEN LLRYDYEGGY TAELVKKVNQ ALFRCAEKGD AVSLRIFDEI VVEVKKIIDA HRKALNFTPP IKLILEGSFF KNAPSLLINM IESAIGREYE IVIPEHDPVI GAVLFAMERV GLRVTEDLYN RLVRNYLREV KK // ID Q9X2H7_THEMA Unreviewed; 176 AA. AC Q9X2H7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36925.1}; GN OrderedLocusNames=TM_1863 {ECO:0000313|EMBL:AAD36925.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36925.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36925.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36925.1; -; Genomic_DNA. DR PIR; H72201; H72201. DR RefSeq; NP_229659.1; NC_000853.1. DR RefSeq; WP_010865421.1; NC_000853.1. DR STRING; 243274.TM1863; -. DR EnsemblBacteria; AAD36925; AAD36925; TM_1863. DR GeneID; 897802; -. DR KEGG; tma:TM1863; -. DR PATRIC; 23938715; VBITheMar51294_1884. DR eggNOG; ENOG4105P8R; Bacteria. DR eggNOG; ENOG4111VIU; LUCA. DR InParanoid; Q9X2H7; -. DR OMA; DPGYIHH; -. DR OrthoDB; EOG68H86R; -. DR BioCyc; TMAR243274:GC6P-1914-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR025529; DUF4416. DR Pfam; PF14385; DUF4416; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 176 AA; 21311 MW; C50884A664CA47C6 CRC64; MKVPDMVNLV MFIFASHIDY WFNEVRPVLE GRFGPMDYIS DVLDFEKYTL YYSEEMGQGL KGRLVSFERL VHPFQLADIK RETNEIEKMF SIEGKRKVNM DPGYIHHTQF VLASTKHWGN RIYIGKGIYA EVTLVYVRGE FRHMEFTYPN YREEEYKKHL EKIRELYLKK RRKMMK // ID Q9WZG4_THEMA Unreviewed; 228 AA. AC Q9WZG4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35787.1}; GN OrderedLocusNames=TM_0705 {ECO:0000313|EMBL:AAD35787.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35787.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35787.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35787.1; -; Genomic_DNA. DR PIR; H72342; H72342. DR RefSeq; NP_228514.1; NC_000853.1. DR RefSeq; WP_010865188.1; NC_000853.1. DR ProteinModelPortal; Q9WZG4; -. DR STRING; 243274.TM0705; -. DR DNASU; 898372; -. DR EnsemblBacteria; AAD35787; AAD35787; TM_0705. DR GeneID; 898372; -. DR KEGG; tma:TM0705; -. DR PATRIC; 23936328; VBITheMar51294_0717. DR eggNOG; ENOG4105CQU; Bacteria. DR eggNOG; COG1136; LUCA. DR InParanoid; Q9WZG4; -. DR KO; K02003; -. DR OMA; QGMDKQA; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-731-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35787.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35787.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 228 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 228 AA; 25686 MW; E794DCDC88CC2781 CRC64; MKALIEVHNL WKEYNGKEKV TALKGINLRI NTGEFVVILG PSGSGKTTLL NCLSGVDRPT RGTVIIHGTD LYTLSEEERT RFRAENMGFV FQFFNLVPVL TAIENVELPL LILGVNRKEA RERAFEILRK VGLAHKCDRF PEELSGGEKQ RVAIARAIVH NPKVIWADEP TGALDNETGR MIIDLLMEMK ENSTLVVVTH DERIAEKADR VIRIRDGQIE QDICEKAL // ID Q9X1P1_THEMA Unreviewed; 211 AA. AC Q9X1P1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36621.1}; GN OrderedLocusNames=TM_1555 {ECO:0000313|EMBL:AAD36621.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36621.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36621.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36621.1; -; Genomic_DNA. DR PIR; F72239; F72239. DR RefSeq; NP_229355.1; NC_000853.1. DR RefSeq; WP_010865360.1; NC_000853.1. DR STRING; 243274.TM1555; -. DR EnsemblBacteria; AAD36621; AAD36621; TM_1555. DR GeneID; 897376; -. DR KEGG; tma:TM1555; -. DR PATRIC; 23938072; VBITheMar51294_1573. DR eggNOG; ENOG41084YX; Bacteria. DR eggNOG; COG4769; LUCA. DR InParanoid; Q9X1P1; -. DR KO; K00805; -. DR OMA; PIPYFRI; -. DR OrthoDB; EOG6DG306; -. DR BioCyc; TMAR243274:GC6P-1596-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR014535; Hpre_diP_synt_I. DR InterPro; IPR010898; Hpre_diP_synth_I. DR Pfam; PF07456; Hpre_diP_synt_I; 1. DR PIRSF; PIRSF027391; Hpre_diP_synt_I; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 88 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 100 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 129 152 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 159 179 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 211 AA; 23280 MW; B7285CF75E305A4D CRC64; MGWSRRDHHL CAKRGDNILR RKDRLRYRDL VRRITFLSVL TALSSTFYVL ENLLPFPVPF GRWGFSNSVV LMIASEIGFG DALIVASAKS ILGALFSGRF LSPSFLTGFF GAVSASLVES FLARFDFGYL SLSAMGSFVN NLVQLIVISF LVGSTKTFLL FPLMVILGLV SGTVNAFLAS RMGGIVFENY SRFFFAQKKA TDGVAGDRVR S // ID Q9X224_THEMA Unreviewed; 397 AA. AC Q9X224; G4FG85; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 109. DE SubName: Full=Aspartate aminotransferase {ECO:0000313|EMBL:AAD36765.1}; GN OrderedLocusNames=TM_1698 {ECO:0000313|EMBL:AAD36765.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36765.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36765.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:2GB3} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS). RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of Aspartate aminotransferase (tm1698) from RT Thermotoga maritima at 2.50 A resolution."; RL Submitted (MAR-2006) to the PDB data bank. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU000479}; CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|RuleBase:RU000479}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36765.1; -; Genomic_DNA. DR PIR; D72220; D72220. DR RefSeq; NP_229498.1; NC_000853.1. DR RefSeq; WP_004082214.1; NZ_CP011107.1. DR PDB; 2GB3; X-ray; 2.50 A; A/B/C/D/E/F=1-397. DR PDBsum; 2GB3; -. DR ProteinModelPortal; Q9X224; -. DR SMR; Q9X224; 1-392. DR STRING; 243274.TM1698; -. DR EnsemblBacteria; AAD36765; AAD36765; TM_1698. DR GeneID; 896815; -. DR KEGG; tma:TM1698; -. DR KEGG; tmi:THEMA_05750; -. DR KEGG; tmw:THMA_1740; -. DR PATRIC; 23938370; VBITheMar51294_1715. DR eggNOG; ENOG4105CHM; Bacteria. DR eggNOG; COG0436; LUCA. DR KO; K00812; -. DR OMA; AFYCIAQ; -. DR OrthoDB; EOG6RRKNS; -. DR BioCyc; TMAR243274:GC6P-1746-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2GB3}; KW Aminotransferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:AAD36765.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000479}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:AAD36765.1}. FT DOMAIN 36 381 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. SQ SEQUENCE 397 AA; 44918 MW; F49307EE068223DC CRC64; MDVFSDRVLL TEESPIRKLV PFAEMAKKRG VRIHHLNIGQ PDLKTPEVFF ERIYENKPEV VYYSHSAGIW ELREAFASYY KRRQRVDVKP ENVLVTNGGS EAILFSFAVI ANPGDEILVL EPFYANYNAF AKIAGVKLIP VTRRMEEGFA IPQNLESFIN ERTKGIVLSN PCNPTGVVYG KDEMRYLVEI AERHGLFLIV DEVYSEIVFR GEFASALSIE SDKVVVIDSV SKKFSACGAR VGCLITRNEE LISHAMKLAQ GRLAPPLLEQ IGSVGLLNLD DSFFDFVRET YRERVETVLK KLEEHGLKRF TKPSGAFYIT AELPVEDAEE FARWMLTDFN MDGETTMVAP LRGFYLTPGL GKKEIRIACV LEKDLLSRAI DVLMEGLKMF CSSRISC // ID Q9WXU7_THEMA Unreviewed; 297 AA. AC Q9WXU7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35186.1}; GN OrderedLocusNames=TM_0092 {ECO:0000313|EMBL:AAD35186.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35186.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35186.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35186.1; -; Genomic_DNA. DR PIR; F72420; F72420. DR RefSeq; NP_227908.1; NC_000853.1. DR RefSeq; WP_010865048.1; NC_000853.1. DR STRING; 243274.TM0092; -. DR EnsemblBacteria; AAD35186; AAD35186; TM_0092. DR GeneID; 896919; -. DR KEGG; tma:TM0092; -. DR KEGG; tmi:THEMA_04345; -. DR PATRIC; 23935024; VBITheMar51294_0090. DR eggNOG; ENOG4106E44; Bacteria. DR eggNOG; ENOG410XX5G; LUCA. DR OMA; IVNIPWD; -. DR OrthoDB; EOG6RRKQ8; -. DR BioCyc; TMAR243274:GC6P-92-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 297 AA; 33702 MW; 0C4CE1E086FCE441 CRC64; MKLLDHKLSL LEITDEEKSD EIILNLSRNV KKDLEDIVVA NVSMENVLVM NIKVPPTLNK QNAVEYATME ISRNLGILPE QLVVAPLDIR GGEGLFFVSK VDQVKSFVTD LMKKEFPETD VVIPDIVKYL EVFEFYFGKR LKGTSVLTVI SFLSDYYSIV VLENNHYRSL RLLFSMFWDY MDIVVENTGI QPKELIEGTV NVDLSFLQPY FGDFLIELDR EVKVSLDEVN LSRVNQFFYI VDPPIFSPVL SQSLEKFEGV ALKQGIVPSF KPGISLGTLG LMIRGGREIG KVKHLSV // ID Q9X0D8_THEMA Unreviewed; 334 AA. AC Q9X0D8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:AAD36125.1}; GN OrderedLocusNames=TM_1048 {ECO:0000313|EMBL:AAD36125.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36125.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36125.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1VHO} RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 2-334. RX PubMed=16021622; DOI=10.1002/prot.20541; RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., RA Bergseid M.G., Buchanan S.G., Buchanan M.D., Batiyenko Y., RA Christopher J.A., Emtage S., Eroshkina A., Feil I., Furlong E.B., RA Gajiwala K.S., Gao X., He D., Hendle J., Huber A., Hoda K., RA Kearins P., Kissinger C., Laubert B., Lewis H.A., Lin J., Loomis K., RA Lorimer D., Louie G., Maletic M., Marsh C.D., Miller I., Molinari J., RA Muller-Dieckmann H.J., Newman J.M., Noland B.W., Pagarigan B., RA Park F., Peat T.S., Post K.W., Radojicic S., Ramos A., Romero R., RA Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J., Winhoven J., RA Wright T.A., Wu L., Xu J., Harris T.J.; RT "Structural analysis of a set of proteins resulting from a bacterial RT genomics project."; RL Proteins 60:787-796(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36125.1; -; Genomic_DNA. DR PIR; B72301; B72301. DR RefSeq; NP_228854.1; NC_000853.1. DR RefSeq; WP_010865253.1; NC_000853.1. DR PDB; 1VHO; X-ray; 1.86 A; A=2-334. DR PDBsum; 1VHO; -. DR ProteinModelPortal; Q9X0D8; -. DR SMR; Q9X0D8; 3-333. DR STRING; 243274.TM1048; -. DR MEROPS; M42.007; -. DR DNASU; 898614; -. DR EnsemblBacteria; AAD36125; AAD36125; TM_1048. DR GeneID; 898614; -. DR KEGG; tma:TM1048; -. DR PATRIC; 23937025; VBITheMar51294_1061. DR eggNOG; ENOG4105CN9; Bacteria. DR eggNOG; COG1363; LUCA. DR InParanoid; Q9X0D8; -. DR KO; K01179; -. DR OMA; LKYMHTP; -. DR OrthoDB; EOG6V4GDH; -. DR BioCyc; TMAR243274:GC6P-1077-MONOMER; -. DR EvolutionaryTrace; Q9X0D8; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 2.40.30.40; -; 1. DR InterPro; IPR008007; Peptidase_M42. DR InterPro; IPR023367; Peptidase_M42_dom2. DR Pfam; PF05343; Peptidase_M42; 1. DR PIRSF; PIRSF001123; PepA_GA; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VHO}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT ACT_SITE 202 202 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR001123-1}. SQ SEQUENCE 334 AA; 36633 MW; 22496B0258CF4015 CRC64; MKMETGKLLM ELSNLDGPSG YETNVVSYIK SVIEPFVDEA KTTRHGSLIG YKKGKGIGKL AFFAHVDEIG FVVSKVEGQF ARLEPVGGVD PKVVYASKVR IYTKNGIERG VIGMLAPHLQ DSESRKKVLT YDEIFVDLSL CERDVRVGDI AVIDQTAFET NGKVVGKALD NRASCGVLVK VLEFLKRYDH PWDVYVVFSV QEETGCLGAL TGAYEINPDA AIVMDVTFAS EPPFSDHIEL GKGPVIGLGP VVDRNLVQKI IEIAKKHNVS LQEEAVGGRS GTETDFVQLV RNGVRTSLIS IPLKYMHTPV EMVDPRDVEE LARLLSLVAV ELEV // ID Q9X080_THEMA Unreviewed; 147 AA. AC Q9X080; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36064.1}; GN OrderedLocusNames=TM_0985 {ECO:0000313|EMBL:AAD36064.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36064.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36064.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36064.1; -; Genomic_DNA. DR PIR; F72310; F72310. DR RefSeq; NP_228793.1; NC_000853.1. DR RefSeq; WP_010865235.1; NC_000853.1. DR STRING; 243274.TM0985; -. DR EnsemblBacteria; AAD36064; AAD36064; TM_0985. DR GeneID; 898731; -. DR KEGG; tma:TM0985; -. DR PATRIC; 23936899; VBITheMar51294_0998. DR eggNOG; ENOG41076PD; Bacteria. DR eggNOG; ENOG410ZH8Z; LUCA. DR OMA; GGVYHEG; -. DR OrthoDB; EOG61VZ7H; -. DR BioCyc; TMAR243274:GC6P-1015-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 147 AA; 17503 MW; ABB98CAFB3F31E1A CRC64; MINLELGKDF LDRFTKVCEF LRVEPSLDVV VFECESLEEF HEITGMPYHT GGVYHEGVIY TQPLDVLRRK NSLEATILHE LLHHVLEMYF DLPRWMEEGV VLAVLGVKPE EVFGYHRDCL LRFMEKVRYE EIPDLVDRYR RSSVERR // ID Q9WY49_THEMA Unreviewed; 171 AA. AC Q9WY49; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000313|EMBL:AAD35298.1}; GN OrderedLocusNames=TM_0206 {ECO:0000313|EMBL:AAD35298.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35298.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35298.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35298.1; -; Genomic_DNA. DR PIR; H72405; H72405. DR RefSeq; NP_228021.1; NC_000853.1. DR RefSeq; WP_010865075.1; NC_000853.1. DR ProteinModelPortal; Q9WY49; -. DR STRING; 243274.TM0206; -. DR EnsemblBacteria; AAD35298; AAD35298; TM_0206. DR GeneID; 897077; -. DR KEGG; tma:TM0206; -. DR KEGG; tmi:THEMA_03695; -. DR PATRIC; 23935284; VBITheMar51294_0208. DR eggNOG; ENOG4108UGV; Bacteria. DR eggNOG; COG0634; LUCA. DR KO; K00760; -. DR OMA; TMDWMAV; -. DR BioCyc; TMAR243274:GC6P-219-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:InterPro. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR InterPro; IPR005904; Hxn_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01203; HGPRTase; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000313|EMBL:AAD35298.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35298.1}. FT DOMAIN 10 140 Pribosyltran. {ECO:0000259|Pfam:PF00156}. SQ SEQUENCE 171 AA; 20045 MW; 2FAC9427A691F655 CRC64; MMIKVLIDEE TLKKRIKELA REIEEYYLGK TDTIHAVCIL KGSIHFFSDL MLNIRKLNVK YSFIHVSSYQ GTSSTGKIRV KSWIDESIHD EYVLLVEDIV DTGLTLQHIV RYLKKYNPRD FRIVSLIEKT VHDHGIPLDF VGFRVDDKFL VGYGLDIDEK YRNLPYIGYV E // ID Q9WZK7_THEMA Unreviewed; 265 AA. AC Q9WZK7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35829.1}; GN OrderedLocusNames=TM_0748 {ECO:0000313|EMBL:AAD35829.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35829.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35829.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1O54} RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-265. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of SAM-dependent O-methyltransferase (TM0748) from RT Thermotoga maritima at 1.65 A resolution."; RL Submitted (AUG-2003) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35829.1; -; Genomic_DNA. DR PIR; G72340; G72340. DR RefSeq; NP_228557.1; NC_000853.1. DR RefSeq; WP_010865197.1; NC_000853.1. DR PDB; 1O54; X-ray; 1.65 A; A=2-265. DR PDBsum; 1O54; -. DR ProteinModelPortal; Q9WZK7; -. DR SMR; Q9WZK7; 1-263. DR STRING; 243274.TM0748; -. DR EnsemblBacteria; AAD35829; AAD35829; TM_0748. DR GeneID; 898415; -. DR KEGG; tma:TM0748; -. DR PATRIC; 23936416; VBITheMar51294_0761. DR eggNOG; ENOG41066UU; Bacteria. DR eggNOG; COG2519; LUCA. DR InParanoid; Q9WZK7; -. DR KO; K07442; -. DR OMA; RPDHRMI; -. DR OrthoDB; EOG68DD1D; -. DR BioCyc; TMAR243274:GC6P-774-MONOMER; -. DR EvolutionaryTrace; Q9WZK7; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IBA:GO_Central. DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR014816; tRNA_MeTrfase_Gcd14. DR Pfam; PF08704; GCD14; 1. DR PIRSF; PIRSF017269; GCD14; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51620; SAM_TRM61; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O54}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR017269-1}. FT BINDING 132 132 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR017269-1}. FT BINDING 160 160 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR017269-1}. FT BINDING 176 176 S-adenosyl-L-methionine. FT {ECO:0000256|PIRSR:PIRSR017269-1}. SQ SEQUENCE 265 AA; 30107 MW; 62000A230C801113 CRC64; MGKVADTLKP GDRVLLSFED ESEFLVDLEK DKKLHTHLGI IDLNEVFEKG PGEIIRTSAG KKGYILIPSL IDEIMNMKRR TQIVYPKDSS FIAMMLDVKE GDRIIDTGVG SGAMCAVLAR AVGSSGKVFA YEKREEFAKL AESNLTKWGL IERVTIKVRD ISEGFDEKDV DALFLDVPDP WNYIDKCWEA LKGGGRFATV CPTTNQVQET LKKLQELPFI RIEVWESLFR PYKPVPERLR PVDRMVAHTA YMIFATKVCR REETE // ID Q9X072_THEMA Unreviewed; 66 AA. AC Q9X072; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36056.1}; GN OrderedLocusNames=TM_0977 {ECO:0000313|EMBL:AAD36056.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36056.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36056.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36056.1; -; Genomic_DNA. DR PIR; F72309; F72309. DR RefSeq; NP_228785.1; NC_000853.1. DR RefSeq; WP_010865233.1; NC_000853.1. DR DNASU; 898723; -. DR EnsemblBacteria; AAD36056; AAD36056; TM_0977. DR GeneID; 898723; -. DR KEGG; tma:TM0977; -. DR PATRIC; 23936883; VBITheMar51294_0990. DR OMA; ISERNQK; -. DR OrthoDB; EOG625K6N; -. DR BioCyc; TMAR243274:GC6P-1007-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 45 64 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 66 AA; 7878 MW; E5C8893878D5910F CRC64; MRVLHLDRGF ERTLITLMVL PPPFIMPLFI SERNQKDMQL VLNTLYLHVL VTFVIFTLLF PILFNF // ID Q9X1S0_THEMA Unreviewed; 202 AA. AC Q9X1S0; G4FFX2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 111. DE SubName: Full=ComFC protein, putative {ECO:0000313|EMBL:AAD36651.1}; GN OrderedLocusNames=TM_1584 {ECO:0000313|EMBL:AAD36651.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36651.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36651.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36651.1; -; Genomic_DNA. DR PIR; H72235; H72235. DR RefSeq; NP_229384.1; NC_000853.1. DR RefSeq; WP_004082014.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1S0; -. DR STRING; 243274.TM1584; -. DR EnsemblBacteria; AAD36651; AAD36651; TM_1584. DR GeneID; 897700; -. DR KEGG; tma:TM1584; -. DR KEGG; tmi:THEMA_06360; -. DR KEGG; tmw:THMA_1619; -. DR PATRIC; 23938132; VBITheMar51294_1603. DR eggNOG; ENOG41084WK; Bacteria. DR eggNOG; COG1040; LUCA. DR KO; K02242; -. DR OMA; SAFPTCY; -. DR OrthoDB; EOG6716R8; -. DR BioCyc; TMAR243274:GC6P-1625-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU000395}. FT DOMAIN 116 199 Pribosyltran. {ECO:0000259|Pfam:PF00156}. SQ SEQUENCE 202 AA; 23576 MW; 6DD4CDC22B889EA1 CRC64; MLNYLFENNC LLCGKEVSPL RSLCENCEEK VLKNGPSFYR EVHRKYELFV YSDYTDEIER IIRLYKYHGE VSLSGTLVKL FLKLYSYFPR EANLITWVPS SLDSLEDRGF DHMRLLAKRI SKELGIPFDA VLENVSEGRQ VEKSKEERKR TGRFICKKDP PQNVILIDDV LTTGTSVRDC VETLFRNGVS KVFVYVLAKT RR // ID Q9X0Y5_THEMA Unreviewed; 319 AA. AC Q9X0Y5; G4FE90; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 108. DE SubName: Full=Sensor histidine kinase, PhoR-related {ECO:0000313|EMBL:AAD36332.1}; GN OrderedLocusNames=TM_1258 {ECO:0000313|EMBL:AAD36332.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36332.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36332.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains histidine kinase domain. CC {ECO:0000256|SAAS:SAAS00102782}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36332.1; -; Genomic_DNA. DR PIR; E72275; E72275. DR RefSeq; NP_229063.1; NC_000853.1. DR RefSeq; WP_004080004.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0Y5; -. DR STRING; 243274.TM1258; -. DR EnsemblBacteria; AAD36332; AAD36332; TM_1258. DR GeneID; 898225; -. DR KEGG; tma:TM1258; -. DR KEGG; tmi:THEMA_08045; -. DR KEGG; tmw:THMA_1283; -. DR PATRIC; 23937456; VBITheMar51294_1274. DR eggNOG; ENOG4108WDY; Bacteria. DR eggNOG; COG0642; LUCA. DR KO; K02484; -. DR OMA; MIFETEL; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1289-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00528924}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|SAAS:SAAS00529081, ECO:0000313|EMBL:AAD36332.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00528924}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|SAAS:SAAS00529081, KW ECO:0000313|EMBL:AAD36332.1}. FT DOMAIN 113 319 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. SQ SEQUENCE 319 AA; 36942 MW; 95F8E40E2DC3D67D CRC64; MRVIELEDLD HIREAIVILK GLEVEGANKP GEKLGFKKGK NLMSIFTCKE MDRFIRDVQE RKNFSLETNA YFFELHSKRF VSLRYLPKKS LLFVNDLTEE RTLSEAKLDF VTAVSHELFT PLSASKANVF LLKDIENDPE KLEILGKVER SLDRMETIIR QLKVLTMIQL RLYELKMEHI PVEEVVHMVL EELREKIESK KIKVNVFVDV ETIETDRFVF HTILKNLVSN AVKYSYPDSV VEISITGERL SVKDQGIGIK EEEKSRIFER FYRGSEALKM APGSGLGLSI VKHLCDTIGY RLEVNSQWLV GSEFIVHFK // ID Q9WXP2_THEMA Unreviewed; 485 AA. AC Q9WXP2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35129.1}; GN OrderedLocusNames=TM_0035 {ECO:0000313|EMBL:AAD35129.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35129.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35129.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35129.1; -; Genomic_DNA. DR PIR; H72424; H72424. DR RefSeq; NP_227851.1; NC_000853.1. DR RefSeq; WP_010865033.1; NC_000853.1. DR STRING; 243274.TM0035; -. DR EnsemblBacteria; AAD35129; AAD35129; TM_0035. DR GeneID; 896856; -. DR KEGG; tma:TM0035; -. DR PATRIC; 23934910; VBITheMar51294_0033. DR OMA; GQYLYMS; -. DR OrthoDB; EOG66B3V9; -. DR BioCyc; TMAR243274:GC6P-35-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 485 AA; 55612 MW; BFCDA610B50B1AB4 CRC64; MESPRNGSSR SFGPISWQQP SDWQETPPLA FNSTGVFKGV GDGQTLNQGI GVFFIYDAGV EEALVYGLSQ DASLVDQGET EWKGFKGRYY KFEGNNLSFN VQVFPLGMRD LAFWNFVAGE PADEDLKTLE KILSSIDLND RFKFSRWNSQ DGTLKIYQNG NHFEGSFGEK TLEGIVIENS IFGWWKKSDS TGSVGPSRFW DGAFSGKFVE GKLQLLFSSS EDPFYSLEGT TVTFENVSGK FESSTVEEVS VTESLLCRSV YENTPFATDT AFTPFDKRIV MWSATKPFEN SHIFKWEWYD PDGNLKETVY YIVAPTIETG YDYYDSVWGW MATDRFGEDA FGEWKVVVYA DGKKLDESSF KLVQEPEMKT IETETFKLNV PAYTYYQLSE GVHYFILDIA NLIFAEAHYE TEPLNGEVYK TPNYEVNFIE TSMPDYQTGQ NFIYWVVQFP EKDGQYLYMS FYAPEDDFKR LESLFERILN SVELK // ID Q9X0U2_THEMA Unreviewed; 177 AA. AC Q9X0U2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=NADH dehydrogenase, 30 kDa subunit, putative {ECO:0000313|EMBL:AAD36290.1}; GN OrderedLocusNames=TM_1215 {ECO:0000313|EMBL:AAD36290.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36290.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36290.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36290.1; -; Genomic_DNA. DR PIR; E72281; E72281. DR RefSeq; NP_229020.1; NC_000853.1. DR RefSeq; WP_010865281.1; NC_000853.1. DR ProteinModelPortal; Q9X0U2; -. DR STRING; 243274.TM1215; -. DR EnsemblBacteria; AAD36290; AAD36290; TM_1215. DR GeneID; 898269; -. DR KEGG; tma:TM1215; -. DR PATRIC; 23937372; VBITheMar51294_1233. DR eggNOG; ENOG4105JFU; Bacteria. DR eggNOG; COG0852; LUCA. DR InParanoid; Q9X0U2; -. DR KO; K00332; -. DR OMA; TPEGHLC; -. DR OrthoDB; EOG60PHFK; -. DR BioCyc; TMAR243274:GC6P-1245-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su. DR Pfam; PF00329; Complex1_30kDa; 1. DR ProDom; PD001581; NADH_UbQ_OxRdtase_30kDa_su; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 32 146 Complex1_30kDa. FT {ECO:0000259|Pfam:PF00329}. SQ SEQUENCE 177 AA; 20925 MW; 0BDAE9CC9C9BC088 CRC64; MCMTNSMSDA LKTLEVFRPE VEEIDEREVK LSVAPDRVIA VLETLKSLGY SHLSLMTCID WIEDSQFELV YILFSWKDGG KFIVTTRIDR NNPQFVTVKE IWPVARFYER EIHEFFGVKF SGNEDMKPLF LELWDDKPPL RKDFDPLEYS RRKFPGREYQ KDVIDEAKKI FRGEING // ID Q9WYU2_THEMA Unreviewed; 231 AA. AC Q9WYU2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35556.1}; GN OrderedLocusNames=TM_0471 {ECO:0000313|EMBL:AAD35556.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35556.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35556.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains GGDEF domain. CC {ECO:0000256|SAAS:SAAS00496774}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35556.1; -; Genomic_DNA. DR PIR; G72371; G72371. DR RefSeq; NP_228281.1; NC_000853.1. DR RefSeq; WP_010865128.1; NC_000853.1. DR STRING; 243274.TM0471; -. DR EnsemblBacteria; AAD35556; AAD35556; TM_0471. DR GeneID; 897503; -. DR KEGG; tma:TM0471; -. DR PATRIC; 23935839; VBITheMar51294_0478. DR eggNOG; ENOG4108E62; Bacteria. DR eggNOG; COG2199; LUCA. DR OMA; QVEDWME; -. DR OrthoDB; EOG6S52M1; -. DR BioCyc; TMAR243274:GC6P-491-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR SUPFAM; SSF55073; SSF55073; 1. DR PROSITE; PS50887; GGDEF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 131 231 GGDEF. {ECO:0000259|PROSITE:PS50887}. SQ SEQUENCE 231 AA; 27219 MW; C31BC3EA0D8CD8DB CRC64; MHVSPRTHRR FETAQILPGD GEMKVKIDLE DEKLRERIAS IVQEAGFFIN ESADVIITDD LKKQGRWVIL VSKNVPEKVP EGVLDVIDPR LPDFLLRRKF EMMKAYLIFP FGILSYLEDE FEKSKRYGFP LSVIYLFFED DGTARRVYEL LRELLRSSDR FDFLKRNEIM IVLPGTSKEG AERLLKRLKR KFLRLDWTKQ PMLEYGVAQV EDWMETVEDL LASLESSLRR L // ID Q9WZ18_THEMA Unreviewed; 584 AA. AC Q9WZ18; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 103. DE RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591}; DE EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591}; GN OrderedLocusNames=TM_0548 {ECO:0000313|EMBL:AAD35633.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35633.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35633.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2). CC {ECO:0000256|RuleBase:RU003591}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU003591}; CC Note=Binds 1 Mg(2+) ion per subunit. CC {ECO:0000256|RuleBase:RU003591}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|RuleBase:RU003591}; CC Note=Binds 1 thiamine pyrophosphate per subunit. CC {ECO:0000256|RuleBase:RU003591}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 1/4. CC {ECO:0000256|RuleBase:RU003591}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 1/4. {ECO:0000256|RuleBase:RU003591}. CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC {ECO:0000256|RuleBase:RU362132}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35633.1; -; Genomic_DNA. DR PIR; B72362; B72362. DR RefSeq; NP_228358.1; NC_000853.1. DR RefSeq; WP_010865145.1; NC_000853.1. DR ProteinModelPortal; Q9WZ18; -. DR STRING; 243274.TM0548; -. DR EnsemblBacteria; AAD35633; AAD35633; TM_0548. DR GeneID; 897602; -. DR KEGG; tma:TM0548; -. DR KEGG; tmi:THEMA_01935; -. DR PATRIC; 23936003; VBITheMar51294_0556. DR eggNOG; ENOG4105C7K; Bacteria. DR eggNOG; COG0028; LUCA. DR KO; K01652; -. DR OMA; HSWVVRD; -. DR OrthoDB; EOG6KT2NW; -. DR BioCyc; TMAR243274:GC6P-572-MONOMER; -. DR UniPathway; UPA00047; UER00055. DR UniPathway; UPA00049; UER00059. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.1220; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR012846; Acetolactate_synth_lsu. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR InterPro; IPR000399; TPP-bd_CS. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF00205; TPP_enzyme_M; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52467; SSF52467; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR TIGRFAMs; TIGR00118; acolac_lg; 1. DR PROSITE; PS00187; TPP_ENZYMES; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003591}; KW Branched-chain amino acid biosynthesis KW {ECO:0000256|RuleBase:RU003591}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Magnesium {ECO:0000256|RuleBase:RU003591}; KW Metal-binding {ECO:0000256|RuleBase:RU003591}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}; KW Transferase {ECO:0000256|RuleBase:RU003591}. FT DOMAIN 6 172 TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}. FT DOMAIN 197 331 TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}. FT DOMAIN 388 536 TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}. SQ SEQUENCE 584 AA; 64431 MW; B2F69C3D6A4F1205 CRC64; MVHVKMKGSK MLFEALLKEG VDTIFGIPGG AIINVYDELC NYEDKINFYL FRHEQGATHA ADGYARVTGK PGVVIVTSGP GATNTVTGIA TAYMDSIPIV VITGQVPTSF IGTDAFQEVD VTGITMPITK HNHLVTSIEE LPYAIKEMFY VATTGRPGPV LLDFPKDIQT AEGEFNYPDT VEIPGYKPTV KGHPKQIKKA VELLKESKRP VVIVGGGANL SGAMDLVNQF IDKFKVPAVS TLMGRGVNPS DEKLYYEGIG MHGTYYGNYA VANADLIIAL GVRFSDRILG NPRTFAKNAR IVHVDIDPAE IGKNVRVDVP IVGDLKSVLE EFLKYEIETD FSDWIEELQE IKKKYPLTYK RDGKLIKPQY VVEKVNEVFP DDTVVVADVG QNQMWVAQFY KFKHQRSFLC SGGLGTMGYA LPAGIGAKIG APDKEVVVFA GDGGFQMNIQ ELMTIKRYNL PVKIIVMDNK ALGMVRQWQQ LFFNCRYSAT ILSDNPDFAK IAEAVGIKAM RIEKPDQVDE AIEKLAKSKE PMLIHAVVDP AENVLPMVPP GGDVGTPLIE APYDETFVER VLKVIEESRR GDER // ID Q9WXL6_THEMA Unreviewed; 41 AA. AC Q9WXL6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35095.1}; GN OrderedLocusNames=TM_0001 {ECO:0000313|EMBL:AAD35095.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35095.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35095.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35095.1; -; Genomic_DNA. DR PIR; C72429; C72429. DR RefSeq; NP_227817.1; NC_000853.1. DR RefSeq; WP_010865020.1; NC_000853.1. DR EnsemblBacteria; AAD35095; AAD35095; TM_0001. DR GeneID; 897248; -. DR KEGG; tma:TM0001; -. DR PATRIC; 23934846; VBITheMar51294_0001. DR BioCyc; TMAR243274:GC6P-1-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 41 AA; 4633 MW; 08BE434E28F1FB56 CRC64; MVYGKEGYGR SKNILLSECV CGIISLELNG FQYFLRGMET L // ID Q9WY13_THEMA Unreviewed; 430 AA. AC Q9WY13; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 113. DE SubName: Full=Folylpolyglutamate synthase/dihydrofolate synthase {ECO:0000313|EMBL:AAD35259.1}; GN OrderedLocusNames=TM_0166 {ECO:0000313|EMBL:AAD35259.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35259.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35259.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1O5Z} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS). RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of Folylpolyglutamate synthase (TM0166) from RT Thermotoga maritima at 2.10 A resolution."; RL Submitted (OCT-2003) to the PDB data bank. CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family. CC {ECO:0000256|PIRNR:PIRNR001563}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35259.1; -; Genomic_DNA. DR PIR; D72411; D72411. DR RefSeq; NP_227981.1; NC_000853.1. DR RefSeq; WP_010865066.1; NC_000853.1. DR PDB; 1O5Z; X-ray; 2.10 A; A=1-430. DR PDBsum; 1O5Z; -. DR ProteinModelPortal; Q9WY13; -. DR SMR; Q9WY13; 1-430. DR STRING; 243274.TM0166; -. DR EnsemblBacteria; AAD35259; AAD35259; TM_0166. DR GeneID; 897005; -. DR KEGG; tma:TM0166; -. DR KEGG; tmi:THEMA_03970; -. DR PATRIC; 23935180; VBITheMar51294_0167. DR eggNOG; ENOG4105DPM; Bacteria. DR eggNOG; COG0285; LUCA. DR KO; K11754; -. DR OMA; IWIDVAH; -. DR OrthoDB; EOG6ZPSW2; -. DR BioCyc; TMAR243274:GC6P-167-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR InterPro; IPR001645; Folylpolyglutamate_synth. DR InterPro; IPR018109; Folylpolyglutamate_synth_CS. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR PANTHER; PTHR11136; PTHR11136; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR PIRSF; PIRSF001563; Folylpolyglu_synth; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01499; folC; 1. DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1. DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O5Z}; KW ATP-binding {ECO:0000256|PIRNR:PIRNR001563, KW ECO:0000256|SAAS:SAAS00431852}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Ligase {ECO:0000256|PIRNR:PIRNR001563}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563, KW ECO:0000256|SAAS:SAAS00431852}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 45 268 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 294 364 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. FT REGION 50 53 Sulfate 2 binding. FT {ECO:0000213|PDB:1O5Z}. FT REGION 292 295 Sulfate 2 binding. FT {ECO:0000213|PDB:1O5Z}. FT REGION 371 373 Sulfate 4 binding. FT {ECO:0000213|PDB:1O5Z}. FT REGION 408 410 Sulfate 3 binding. FT {ECO:0000213|PDB:1O5Z}. FT BINDING 47 47 Sulfate 1; via carbonyl oxygen. FT {ECO:0000213|PDB:1O5Z}. FT BINDING 147 147 Sulfate 1; via amide nitrogen. FT {ECO:0000213|PDB:1O5Z}. FT BINDING 185 185 Sulfate 1. {ECO:0000213|PDB:1O5Z}. FT BINDING 312 312 Sulfate 3. {ECO:0000213|PDB:1O5Z}. FT BINDING 334 334 Chloride. {ECO:0000213|PDB:1O5Z}. FT BINDING 358 358 Chloride. {ECO:0000213|PDB:1O5Z}. FT BINDING 368 368 Sulfate 3. {ECO:0000213|PDB:1O5Z}. FT BINDING 400 400 Chloride; via amide nitrogen. FT {ECO:0000213|PDB:1O5Z}. SQ SEQUENCE 430 AA; 48869 MW; 32B578EBFBD49A6C CRC64; MAYLEVLRYL YHKRPMGKVK PGLERISMLL SKLGNPHLEY KTIHIGGTNG KGSVANMVSN ILVSQGYRVG SYYSPHLSTF RERIRLNEEY ISEEDVVKIY ETMEPILNEL DKEEIFSPSF FEVVTAMAFL YFAEKNVDIA VLEVGLGGRL DATNVVFPLC STIVTVDRDH EKTLGYTIEQ IAWEKSGIIK ERVPLVTGER KREALKVMED VARKKSSRMY VIDKDFSVKV KSLKLHENRF DYCGENTFED LVLTMNGPHQ IENAGVALKT LEATGLPLSE KAIREGLKNA KNLGRFEILE KNGKMYILDG AHNPHGAESL VRSLKLYFNG EPLSLVIGIL DDKNREDILR KYTGIFERVI VTRVPSPRMK DMNSLVDMAK KFFKNVEVIE DPLEAIESTE RATVVTGSLF LVGYVREFLT TGKINEEWKL // ID Q9X1Z9_THEMA Unreviewed; 31 AA. AC Q9X1Z9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36738.1}; GN OrderedLocusNames=TM_1671 {ECO:0000313|EMBL:AAD36738.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36738.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36738.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36738.1; -; Genomic_DNA. DR PIR; E72225; E72225. DR RefSeq; NP_229471.1; NC_000853.1. DR RefSeq; WP_010865381.1; NC_000853.1. DR DNASU; 897904; -. DR EnsemblBacteria; AAD36738; AAD36738; TM_1671. DR GeneID; 897904; -. DR KEGG; tma:TM1671; -. DR BioCyc; TMAR243274:GC6P-1717-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 31 AA; 3434 MW; F1B39C57F02ACCBE CRC64; MPKGIPVFVL TGIFLFSSDS SKNTLLFQAK F // ID Q9X1T0_THEMA Unreviewed; 1206 AA. AC Q9X1T0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 100. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36661.1}; GN OrderedLocusNames=TM_1594 {ECO:0000313|EMBL:AAD36661.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36661.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36661.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains GGDEF domain. CC {ECO:0000256|SAAS:SAAS00496774}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36661.1; -; Genomic_DNA. DR PIR; F72233; F72233. DR RefSeq; NP_229394.1; NC_000853.1. DR RefSeq; WP_010865368.1; NC_000853.1. DR ProteinModelPortal; Q9X1T0; -. DR STRING; 243274.TM1594; -. DR EnsemblBacteria; AAD36661; AAD36661; TM_1594. DR GeneID; 897944; -. DR KEGG; tma:TM1594; -. DR PATRIC; 23938162; VBITheMar51294_1613. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR InParanoid; Q9X1T0; -. DR OMA; VLGQKFT; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1640-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF00990; GGDEF; 1. DR SMART; SM00267; GGDEF; 1. DR SUPFAM; SSF48452; SSF48452; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF55073; SSF55073; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR TIGRFAMs; TIGR00254; GGDEF; 1. DR PROSITE; PS50887; GGDEF; 1. DR PROSITE; PS50005; TPR; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 718 751 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. FT DOMAIN 1072 1200 GGDEF. {ECO:0000259|PROSITE:PS50887}. SQ SEQUENCE 1206 AA; 141661 MW; 53A67C364AE27D87 CRC64; MWKVRVKKFL RETYWGDEFL IEDDGEDQVL KIVRAPVDRS FFFNEYAKLK RLNLPNVLLP EKLKISDGKF LLFYPYYHNL APLENLSDQV AKQLLKLFLF LSKVGVTIPA LGMDDILVND GVFLIPALIS NIPDDVKGVV FSPERSSRAT EEVCRRFLKI HGIEPHLETR EPSFDSREIR IPYIHRKEEE LIKRDIEIAQ KFPFFILITG EQRVGKTKLA SVLVDGLREQ GYMVHQITSL EDLRVWYDAS DELDLLTKLD DGQKKVILID DLFEGSDLLS FLEEFSGLST ITKIIVLTTS TKAFQFFHKV YRLSPFTVEE TRIFLERAIG KISEDQVKLI HSLSKGLPGY MVELLKFFNK SNLRENIVGI FKPLLRELDS PEIRELSVLG QKFTGTELKV LEKITGKDYH DTLMSAYDSG VITTEEGLYR FALREFWKYY YNKLSENKKK NLHEKLFENL PDDLAIKHAL SLEDPRLKFF YVLRYVRKHF WDYEKTRSLI EYLRRLEEFF EKPYYSIESL KMKLIFRIDP LGVEKENFHF RRFKTLRNPD VESILQKDSL SYYDLYNLVV LSRFHIRAGK KAPQEILNTI KRELKEKNFS TRERLYLKAH LLYDLFSSTE DREALKEMMN IATSEGFLDL QVMGYRALGV LSRTRAMSNY YFHHSLELSR KIDPSLSIVD ESNLTWSLLY EGKITNFLVQ LERLRKQARL FEDMPILSYT YFLEGLYYIH KKDFQKAEEV FRTELELEEK HGIERRALRG LVMNYLFSGD VESAKSLLEK DEPEFDRFGF NFLKRLVLAK DDSELLKIWK ERLETPQKFF NEEIAYVFTE RLAKLDPEGF EEFLLELERE NVENSSNLTL ALVYETFYKF YSALGENFKA KRYLRRAIFV YNLIGLREVS VKPEVEEKTQ IEEKKAPFYL LLGFIETEKE FSDMMEFASA RLSEVIPYEV FSIRIIERTT KKVMEEYSTS PITPPMEKDF LEISPFRTVM SFHLDMKHDM IVGVETNLEC DEKTAWELVE TLEQFGNILT TILRERLYRD RSMKDPLTGV LSRWYFMERL EEEAYKSSRY KSPLSIIMCD ADDFKKINDQ FGHVAGDKTL GWLGRKMKSV LRKSDLVGRY GGEEFIIALP GTSLEEAKIV AEKLRKAVME DPENTYHITL SFGVAEYKNG EDPFETIKRA DEALYLAKIL GKNSVVTEKV LSRRSS // ID Q9X1D8_THEMA Unreviewed; 301 AA. AC Q9X1D8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Hydrogenase, putative {ECO:0000313|EMBL:AAD36491.1}; GN OrderedLocusNames=TM_1421 {ECO:0000313|EMBL:AAD36491.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36491.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36491.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36491.1; -; Genomic_DNA. DR PIR; B72256; B72256. DR RefSeq; NP_229221.1; NC_000853.1. DR RefSeq; WP_010865337.1; NC_000853.1. DR ProteinModelPortal; Q9X1D8; -. DR STRING; 243274.TM1421; -. DR EnsemblBacteria; AAD36491; AAD36491; TM_1421. DR GeneID; 898054; -. DR KEGG; tma:TM1421; -. DR PATRIC; 23937790; VBITheMar51294_1433. DR eggNOG; ENOG4107QXD; Bacteria. DR eggNOG; COG4624; LUCA. DR InParanoid; Q9X1D8; -. DR OMA; CANGSGV; -. DR OrthoDB; EOG67DPHW; -. DR BioCyc; TMAR243274:GC6P-1459-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central. DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GOC. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR009016; Fe_hydrogenase. DR InterPro; IPR004108; Fe_hydrogenase_lsu_C. DR Pfam; PF02906; Fe_hyd_lg_C; 1. DR Pfam; PF13187; Fer4_9; 1. DR SUPFAM; SSF53920; SSF53920; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 31 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 32 61 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 301 AA; 34056 MW; 21AC74D0C1109C98 CRC64; MAELIFSRET DCRYCYKCLR NCPVKAISFK SGKSTVLEEE CVFCGSCLDI CPQNARSYRK DVERFLSLSE PFLVSIAPSF FAYFENPLKV IGVLKEMGAV VVQETAVGAE IVSRRYEEVF EKHSGPFITT ACPVVVNLAE KHFPNVLKYF APVDSPLMTH AKFLKTRYGD FPIVFVGPCI AKKSESDLVD VALTFEELEE ILEEREGKEA LPDGPYPDRA RFYPTTDGIG YTVSVPWEKK LVVEGVENLM RVFSRIDEYK SVFIEASACY GSCLNGPVMK KKSNGKERLL EWQKKLPKEP K // ID Q9WY91_THEMA Unreviewed; 100 AA. AC Q9WY91; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=RnfB-related protein {ECO:0000313|EMBL:AAD35340.1}; GN OrderedLocusNames=TM_0249 {ECO:0000313|EMBL:AAD35340.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35340.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35340.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains 4Fe-4S domain. CC {ECO:0000256|SAAS:SAAS00508687}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35340.1; -; Genomic_DNA. DR PIR; B72399; B72399. DR RefSeq; NP_228063.1; NC_000853.1. DR RefSeq; WP_010865080.1; NC_000853.1. DR STRING; 243274.TM0249; -. DR EnsemblBacteria; AAD35340; AAD35340; TM_0249. DR GeneID; 897157; -. DR KEGG; tma:TM0249; -. DR PATRIC; 23935373; VBITheMar51294_0252. DR eggNOG; ENOG4108305; Bacteria. DR eggNOG; COG2878; LUCA. DR KO; K03616; -. DR OMA; EDPRVKM; -. DR OrthoDB; EOG60SCM3; -. DR BioCyc; TMAR243274:GC6P-262-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR InterPro; IPR007202; 4Fe-4S_dom. DR InterPro; IPR010207; Elect_transpt_cplx_RnfB/RsxB. DR Pfam; PF04060; FeS; 1. DR TIGRFAMs; TIGR01944; rnfB; 1. DR PROSITE; PS51656; 4FE4S; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 28 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 34 93 4Fe-4S. {ECO:0000259|PROSITE:PS51656}. SQ SEQUENCE 100 AA; 10934 MW; 8A1EAA89812AFF20 CRC64; MKELEVIYST LLLAVLGFGF GAFLAYSAQR FKVEEDPRVK MITEVLPGIN CGACGFAGCE AYAKAIVKGQ AETNRCLPGR PQGVEEKIKK ILEEYKNVSS // ID Q9X2D2_THEMA Unreviewed; 444 AA. AC Q9X2D2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36875.1}; GN OrderedLocusNames=TM_1812 {ECO:0000313|EMBL:AAD36875.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36875.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36875.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36875.1; -; Genomic_DNA. DR PIR; A72209; A72209. DR RefSeq; NP_229609.1; NC_000853.1. DR RefSeq; WP_010865408.1; NC_000853.1. DR STRING; 243274.TM1812; -. DR EnsemblBacteria; AAD36875; AAD36875; TM_1812. DR GeneID; 897375; -. DR KEGG; tma:TM1812; -. DR PATRIC; 23938613; VBITheMar51294_1833. DR eggNOG; ENOG41084D9; Bacteria. DR eggNOG; ENOG410ZXPM; LUCA. DR InParanoid; Q9X2D2; -. DR OMA; TECEDLT; -. DR OrthoDB; EOG6GBM95; -. DR BioCyc; TMAR243274:GC6P-1863-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR019016; CRISPR-assoc_DxTHG_prot. DR InterPro; IPR013383; CRISPR-assoc_prot_DxTHG_CS. DR Pfam; PF09455; Cas_DxTHG; 1. DR TIGRFAMs; TIGR02549; CRISPR_DxTHG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 444 AA; 50905 MW; 3E7A715527C184E5 CRC64; MNFLVRNLVE NLEEGDRVIL DVTHSFRSIP LMASVVALYL KEAKDVNVSV VYGKYNKETK VTECEDLTPL TKATSWIYAV RLFKEYGYAK ELADLIKKRN EEIYRRSQSS KKPKLLGSMS QKLQDLSSSI RLGSIVAIRK NLTNFFNFID RNKARIREET EVFVPEIAAL LDGIEKRYRV IHVKSENFEL SEKELESEKE LLDFYLQTGD LGMALRLARE YLINVYLMSG GEKSDFLDRN VRESVSISTF GYDTILQARN HVAHFGFNKL QLPSLKKIED HLKVLVQTPP EQLLESARKT QRNRKRALLT PLGTTKGALY TVLKKISPDL LLVITSKQGK AILSEILEKA EFKGEFRVIL LEDPFMGVSE IDRVVSEIKE HLSDVDEVIV NLTGGTTFLT YVIERAKNQI RYGRKVKTIL AVDKRTYEEQ KQNPFVVGEI LELD // ID Q9WZI5_THEMA Unreviewed; 499 AA. AC Q9WZI5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=TldD protein {ECO:0000313|EMBL:AAD35808.1}; GN OrderedLocusNames=TM_0726 {ECO:0000313|EMBL:AAD35808.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35808.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35808.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35808.1; -; Genomic_DNA. DR PIR; D72342; D72342. DR RefSeq; NP_228535.1; NC_000853.1. DR RefSeq; WP_010865192.1; NC_000853.1. DR STRING; 243274.TM0726; -. DR EnsemblBacteria; AAD35808; AAD35808; TM_0726. DR GeneID; 898393; -. DR KEGG; tma:TM0726; -. DR PATRIC; 23936372; VBITheMar51294_0739. DR eggNOG; ENOG4105D1U; Bacteria. DR eggNOG; COG0312; LUCA. DR InParanoid; Q9WZI5; -. DR KO; K03568; -. DR OMA; ENGNLQY; -. DR OrthoDB; EOG65J4ZF; -. DR BioCyc; TMAR243274:GC6P-752-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR InterPro; IPR025502; TldD. DR InterPro; IPR002510; TldD/PmbA. DR Pfam; PF01523; PmbA_TldD; 1. DR PIRSF; PIRSF004919; TldD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 499 AA; 54090 MW; 1818EF3CEF342AC3 CRC64; MLSTSHRSYS TPVEGVEIVS TPNLGSSIMV KKKGGITVLN ESVIRDVLSA VLKSGGDFAE LFFERKYENR YELKDGKIEQ ATSGEIVGVG IRGFLGTKAV YAYTNDLSRE NLINVAKKVG EALGETKVED LTFNFNRTKR KERHVVLIPP AQVEKTDKVS VMKKAYYAAK NYSELIKQVV VWYWDYDQEI LVANSEGTWA EDRRVRTRLM INAVAEKDGV LERGFYGPGA GMGFEFFDRI DVEEAAKKAA RIAARMVEAE PAPAGKMTVV IANGFGGVIF HEAVGHGLEA TSVAKGASVF AGKLGQKVAA ECVSAVDDAT IPNGWGSANV DDEGTPTQRT LLIDKGVLVG YLVDKLGERR MGMKSTGSGR RQDYTFPPTS RMSNTFILPG DYHPEEIIAA TEYGLYAKTM GGGSVNPATG EFNFAVSEAY LIEKGRITKP VRGATLIGKG HEIIQKIDMV GNDLARDQGM CGSFSGSVPA DVGQPTIRVK EIVVGGRNK // ID Q9WZV0_THEMA Unreviewed; 132 AA. AC Q9WZV0; G4FCX8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Cytidine/deoxycytidine deaminase {ECO:0000313|EMBL:AAD35928.1}; GN OrderedLocusNames=TM_0846 {ECO:0000313|EMBL:AAD35928.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35928.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35928.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35928.1; -; Genomic_DNA. DR PIR; G72326; G72326. DR RefSeq; NP_228655.1; NC_000853.1. DR RefSeq; WP_004080780.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZV0; -. DR STRING; 243274.TM0846; -. DR EnsemblBacteria; AAD35928; AAD35928; TM_0846. DR GeneID; 898517; -. DR KEGG; tma:TM0846; -. DR KEGG; tmi:THEMA_00410; -. DR KEGG; tmw:THMA_0867; -. DR PATRIC; 23936618; VBITheMar51294_0859. DR eggNOG; ENOG4105KG3; Bacteria. DR eggNOG; COG0295; LUCA. DR KO; K01489; -. DR OMA; KLVKMAL; -. DR OrthoDB; EOG6XDH25; -. DR BioCyc; TMAR243274:GC6P-875-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0009972; P:cytidine deamination; IBA:GO_Central. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn-bd. DR InterPro; IPR006262; Cyt_deam_tetra. DR InterPro; IPR016193; Cytidine_deaminase-like. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR TIGRFAMs; TIGR01354; cyt_deam_tetra; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 128 CMP/dCMP-type deaminase. FT {ECO:0000259|PROSITE:PS51747}. SQ SEQUENCE 132 AA; 14379 MW; D3DCBB02EC43CB4F CRC64; MVNPEKLVKM ALEARKKAYA KYSGFRVGAA LLTKSGKIYT GVNVENSSYG LTVCAERVAV FKAVSEGERE FVAIAIASDS PDKTAPCGAC RQVLYEFSDD LDVIMADRDG NFEIVKLKDL LPRGFRLGGG EY // ID Q9WYL0_THEMA Unreviewed; 32 AA. AC Q9WYL0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35464.1}; GN OrderedLocusNames=TM_0377 {ECO:0000313|EMBL:AAD35464.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35464.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35464.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35464.1; -; Genomic_DNA. DR PIR; C72383; C72383. DR RefSeq; NP_228188.1; NC_000853.1. DR RefSeq; WP_010865106.1; NC_000853.1. DR EnsemblBacteria; AAD35464; AAD35464; TM_0377. DR GeneID; 897349; -. DR KEGG; tma:TM0377; -. DR BioCyc; TMAR243274:GC6P-391-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 32 AA; 3367 MW; E063EF511C874227 CRC64; MVYGKGGYGS SKNILLSDCV CGIISLELNG FQ // ID Q9X0W7_THEMA Unreviewed; 357 AA. AC Q9X0W7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36315.1}; GN OrderedLocusNames=TM_1240 {ECO:0000313|EMBL:AAD36315.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36315.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36315.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36315.1; -; Genomic_DNA. DR PIR; A72280; A72280. DR RefSeq; NP_229045.1; NC_000853.1. DR RefSeq; WP_010865288.1; NC_000853.1. DR ProteinModelPortal; Q9X0W7; -. DR STRING; 243274.TM1240; -. DR EnsemblBacteria; AAD36315; AAD36315; TM_1240. DR GeneID; 898244; -. DR KEGG; tma:TM1240; -. DR PATRIC; 23937420; VBITheMar51294_1257. DR eggNOG; ENOG4105C3G; Bacteria. DR eggNOG; COG0012; LUCA. DR InParanoid; Q9X0W7; -. DR KO; K06942; -. DR OMA; CTIEPNI; -. DR OrthoDB; EOG6NSGJC; -. DR BioCyc; TMAR243274:GC6P-1270-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR Gene3D; 1.10.150.300; -; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR004396; ATPase_YchF/OLA1. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR013029; DUF933. DR InterPro; IPR031167; G_OBG. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR012676; TGS-like. DR InterPro; IPR023192; TGS-like_dom. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF06071; YchF-GTPase_C; 1. DR PIRSF; PIRSF006641; CHP00092; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR TIGRFAMs; TIGR00092; TIGR00092; 1. DR PROSITE; PS51710; G_OBG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 250 OBG-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51710}. SQ SEQUENCE 357 AA; 41000 MW; 44CCCD2BEB9A83B4 CRC64; MGIVGLPNAG KSSFFNFLTD NSVPAESFPF CTIEPNVGIL VVPDERIEIL AKNEGSKKVV HPFVEVVDIA GLVKGASKGE GLGNQFLDHI SKVDVIAHVV RLFEDGRVSH PYQNVDPKRD IEIVETELIL KDLETVQKRL EKRMKVARTG DKEAKREVEL LQNLREFLSQ GKKASKFPRH DRFEEEVIES LFLLTDKPQI LVFNVDELDE EKRKLIEEIV KEKDEEYIII NVKLEEELKF LPEEEAEVFR REYNLFGDKR KEFFEKVLKL LNLIRFLTAT QNEARSWTIK KGSTAYEAAG LIHSDIQKGF IKVEVIPFER YVEFGSLKKA REAGAVETHG KDYIVREGDV IHFLFRA // ID Q9X2B9_THEMA Unreviewed; 730 AA. AC Q9X2B9; G4FGI7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 105. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36862.1}; GN OrderedLocusNames=TM_1799 {ECO:0000313|EMBL:AAD36862.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36862.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36862.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36862.1; -; Genomic_DNA. DR PIR; D72210; D72210. DR RefSeq; NP_229596.1; NC_000853.1. DR RefSeq; WP_004082346.1; NC_000853.1. DR ProteinModelPortal; Q9X2B9; -. DR STRING; 243274.TM1799; -. DR EnsemblBacteria; AAD36862; AAD36862; TM_1799. DR GeneID; 897835; -. DR KEGG; tma:TM1799; -. DR KEGG; tmi:THEMA_05195; -. DR PATRIC; 23938587; VBITheMar51294_1820. DR eggNOG; ENOG4105DKM; Bacteria. DR eggNOG; COG1203; LUCA. DR KO; K07012; -. DR OMA; NQSAGRC; -. DR OrthoDB; EOG6CK7HW; -. DR BioCyc; TMAR243274:GC6P-1850-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR006483; CRISPR-assoc_Cas3_HD. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR006474; Helicase_Cas3_CRISPR-ass_core. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01587; cas3_core; 1. DR TIGRFAMs; TIGR01596; cas3_HD; 1. DR PROSITE; PS51643; HD_CAS3; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU004294}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004294}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 14 200 HD Cas3-type. FT {ECO:0000259|PROSITE:PS51643}. FT DOMAIN 246 425 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 427 623 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. SQ SEQUENCE 730 AA; 84742 MW; 460BCC984D0EEA12 CRC64; MEGGRAEHSV DVMKSHPDRR LIDHLEGVKR RSLEKFRSLD LSWEELFGYD ENVLEEFVSL LSESHDVGKS TIYFQKHLSG ERVERSLSAH ALFSAVAFFH RSKNLPDKLR IFGFEIIRRH HGDFRNFLDI EIDEKVLEKQ FSAIPEDFLR RYDLHDLKLS ETIERIKRSI SKFSILGKKD LSDYFLIHLF MSILVSSDRE DVVFKSEPLP SLPSYEKEKI LSYREKLGRK NQIDSLRWKF QEEILSFKPE RGKIYSITAP TGIGKTIANL LFASHLADED TIVIYALPFI NIIEQTVDKI KEIFETESPF FVLPFHHLAN PAYEEPDKYE DLLMNLWHSR VVVTTFVSLL ESLITFRKIP FFYKFPKAVL ILDEVQAIPH EYWTPVEKTV EFLSKMGTTV LLSTATKPAL LKEALEVVSN KNVYFTALNR TVLKVEKEMS FEEYKEFVRE TLKDGKRTLI ITNTIREAEE IYDVVEGMGK TCFLSSRVIP KHRLEIVSKI NEYDLCVSTQ VVEAGVDISF ERVIRDIAPV DSIVQAAGRC NRHFELEKGE VIVVPVRNER KNTLFSSYVY GSFLTETSMN VLKNHKFLEE SEFFMLVEDF FSYVKTYGNP DKKGIGKALE NLNFKKIGEF SLIEPEPTVP FIVLVDEEAQ RVFEEFAEIF SGKRSRENFS LVKSLFRELS PYIVSARIKR DLPFPHTIAG MMVIHRNVLD KWYHPVKGLR VEGSDEVIII // ID Q9X212_THEMA Unreviewed; 395 AA. AC Q9X212; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36753.1}; GN OrderedLocusNames=TM_1686 {ECO:0000313|EMBL:AAD36753.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36753.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36753.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36753.1; -; Genomic_DNA. DR PIR; H72222; H72222. DR RefSeq; NP_229486.1; NC_000853.1. DR RefSeq; WP_010865382.1; NC_000853.1. DR ProteinModelPortal; Q9X212; -. DR STRING; 243274.TM1686; -. DR EnsemblBacteria; AAD36753; AAD36753; TM_1686. DR GeneID; 897320; -. DR KEGG; tma:TM1686; -. DR PATRIC; 23938346; VBITheMar51294_1703. DR eggNOG; ENOG41080D2; Bacteria. DR eggNOG; COG1376; LUCA. DR InParanoid; Q9X212; -. DR OMA; GEYISPR; -. DR OrthoDB; EOG64V2GW; -. DR BioCyc; TMAR243274:GC6P-1734-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR Gene3D; 3.10.350.10; -; 1. DR InterPro; IPR005490; LD_TPept_cat_dom. DR InterPro; IPR018392; LysM_dom. DR Pfam; PF01476; LysM; 1. DR Pfam; PF03734; YkuD; 1. DR SMART; SM00257; LysM; 1. DR SUPFAM; SSF54106; SSF54106; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 211 255 LysM. {ECO:0000259|SMART:SM00257}. SQ SEQUENCE 395 AA; 45235 MW; 56693E8811125EFD CRC64; MKMTRFVWLA VFLMLFQTLL ADHLLELKSV SEDHVTLSVK KLYEGEITTF LLYSPAGFVF PEKVKNSDYT FEVDFEGPFF PIVEGVNSFG KRMYRVAPQV LRVPLEKPET RVISDIKNGE VLVYVFIQSP EGVVPVSLNL EGKRFRFFNL EGKWICVFKS FLEDGAHELE ITFNGPYGYT FSLKKEIYVI KRVAVPMRGE DGAFDYTVFA EHVVKRGETL WSIANQYGVR VGDIVLINRL EDPDRIVAGQ VLKIGRVYFR ENPVTIVVNL FSSKLALYYD GVLLKVYPVA LGRSDATPPG RYWVLRKEID PALYWFGEYI SPRTPLNGLG TRYLQLSDPT YAIHGTSKPW EIGKRISHGC IRMFNRDVEE IDAFAGVGTE VVVVKEDKEF PERIY // ID Q9X0H4_THEMA Unreviewed; 495 AA. AC Q9X0H4; G4FEQ8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=TRK system potassium uptake protein TrkH {ECO:0000313|EMBL:AAD36165.1}; GN OrderedLocusNames=TM_1089 {ECO:0000313|EMBL:AAD36165.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36165.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36165.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36165.1; -; Genomic_DNA. DR PIR; H72297; H72297. DR RefSeq; NP_228895.1; NC_000853.1. DR RefSeq; WP_004080375.1; NZ_CP011107.1. DR STRING; 243274.TM1089; -. DR TCDB; 2.A.38.1.4; the k(+) transporter (trk) family. DR EnsemblBacteria; AAD36165; AAD36165; TM_1089. DR GeneID; 898677; -. DR KEGG; tma:TM1089; -. DR KEGG; tmi:THEMA_08905; -. DR KEGG; tmw:THMA_1112; -. DR PATRIC; 23937109; VBITheMar51294_1103. DR eggNOG; ENOG4105D37; Bacteria. DR eggNOG; COG0168; LUCA. DR KO; K03498; -. DR OMA; FHMESSD; -. DR OrthoDB; EOG63589N; -. DR BioCyc; TMAR243274:GC6P-1118-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0022820; F:potassium ion symporter activity; IEA:InterPro. DR InterPro; IPR003445; Cat_transpt. DR InterPro; IPR004772; TrkH. DR Pfam; PF02386; TrkH; 2. DR TIGRFAMs; TIGR00933; 2a38; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 35 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 41 60 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 72 98 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 142 165 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 208 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 240 259 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 300 318 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 324 344 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 400 423 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 454 477 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 495 AA; 54747 MW; BDCEB62C5844E6AD CRC64; MTSTKYRLKV IFWYVGQLLI WFPAILLLPT IFVIFYPEEW IYIESFLVPS IISFASGVVL KKVSKLNETR VVGYQEGAVI VVTTWCAAVV LSALPFVIEG LLNFHQAVFE ATSGWTTTGL TMFPDVESLP HVFLVWRSVM QFIGGAGFAV IMLATLIGPL GASLYSSEGR VDNILPNVTH STKVIMVIYV AYAAAGMFFL HMAGMPWFDA FNHSLTALAT GGFSVKNASI GYYGSVSIEV ITIVLMLLGG TGFGIHYTLW KGNFKAFVKN GEPWIMGSTI VIASLFLLRP AEKVFHEKAL RYVVFQVVSA ITGTGFSNAD LVPWVTLFPI GVYLLTVIMM LGGMMDSTAG GLKQFRVFVT LKLIYRSIIN FMGPRRKVEK IIVWKGENRK TIDDGIIKDM FVFFGVYALT YLVGTLILMS YGYDPLVSMF EFSSAMNGVG LSVGLTSPNL PVGVIWTMTV GMFLGRLEFL VVFYAIVRII RDVKILLEER GGVNS // ID Q9X164_THEMA Unreviewed; 69 AA. AC Q9X164; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36414.1}; GN OrderedLocusNames=TM_1342 {ECO:0000313|EMBL:AAD36414.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36414.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36414.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36414.1; -; Genomic_DNA. DR PIR; F72266; F72266. DR RefSeq; NP_229144.1; NC_000853.1. DR RefSeq; WP_010865322.1; NC_000853.1. DR STRING; 243274.TM1342; -. DR EnsemblBacteria; AAD36414; AAD36414; TM_1342. DR GeneID; 898140; -. DR KEGG; tma:TM1342; -. DR PATRIC; 23937615; VBITheMar51294_1353. DR BioCyc; TMAR243274:GC6P-1373-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 15 35 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 68 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 69 AA; 8071 MW; 87FF33A95F49E238 CRC64; MFWTKFLHVA SPEGFFGVAF VLMTTISGFI HIVVWRQSGN MVFTFIPHFL LNLGPLFWTG YSIVPYLWR // ID Q9WZ54_THEMA Unreviewed; 360 AA. AC Q9WZ54; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Lipopolysaccharide biosynthesis protein BplA {ECO:0000313|EMBL:AAD35670.1}; GN OrderedLocusNames=TM_0585 {ECO:0000313|EMBL:AAD35670.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35670.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35670.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35670.1; -; Genomic_DNA. DR PIR; B72359; B72359. DR RefSeq; NP_228395.1; NC_000853.1. DR RefSeq; WP_008192388.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZ54; -. DR STRING; 243274.TM0585; -. DR EnsemblBacteria; AAD35670; AAD35670; TM_0585. DR GeneID; 897655; -. DR KEGG; tma:TM0585; -. DR KEGG; tmi:THEMA_01740; -. DR KEGG; tmw:THMA_0600; -. DR PATRIC; 23936081; VBITheMar51294_0594. DR eggNOG; ENOG4105CIB; Bacteria. DR eggNOG; COG0673; LUCA. DR OMA; PVKFPFE; -. DR OrthoDB; EOG69PQ1M; -. DR BioCyc; TMAR243274:GC6P-610-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000683; Oxidoreductase_N. DR InterPro; IPR004104; OxRdtase_C. DR Pfam; PF01408; GFO_IDH_MocA; 1. DR Pfam; PF02894; GFO_IDH_MocA_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 127 GFO_IDH_MocA. {ECO:0000259|Pfam:PF01408}. FT DOMAIN 141 240 GFO_IDH_MocA_C. FT {ECO:0000259|Pfam:PF02894}. SQ SEQUENCE 360 AA; 41023 MW; 3B17BCD4A94A6EC6 CRC64; MKLRIALVGC GRIGQKKHVP ALIETQDLFE TVAVCDLVEE RANRAAEHFE KSGLRRPETM TNYRELLKRE DVDVISIATE SGKHYQITME ALEAGKHVLV EKPMALSTKH MNEMVELSKQ KNLKLGVFFQ NRFNPPVQEV RKKLDSGAFG KIFYASVAVR WNRNEDYYKQ ASWRGTWEMD GGVLMNQSTH AIDLLQWFLG GEIEEIYGHI ANTNHPYIEA EDEGFAIVKF KGGKTGLIEA TSNVFPRNLE ETLAIFGEKG TVVIGGIAVN RILTWRFEGE EGHPFMNLPD PDTVYGDSHK YVYRDFYEAV TNDRKPYISG EDGKKAVEIV LGIYRSFLEG RPVKYPFDFS TEEMKGVKLR // ID Q9WZ67_THEMA Unreviewed; 277 AA. AC Q9WZ67; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 87. DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35683.1}; GN OrderedLocusNames=TM_0598 {ECO:0000313|EMBL:AAD35683.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35683.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35683.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35683.1; -; Genomic_DNA. DR PIR; G72357; G72357. DR RefSeq; NP_228408.1; NC_000853.1. DR RefSeq; WP_010865157.1; NC_000853.1. DR ProteinModelPortal; Q9WZ67; -. DR STRING; 243274.TM0598; -. DR EnsemblBacteria; AAD35683; AAD35683; TM_0598. DR GeneID; 897674; -. DR KEGG; tma:TM0598; -. DR PATRIC; 23936111; VBITheMar51294_0609. DR eggNOG; ENOG4105EX2; Bacteria. DR eggNOG; COG0395; LUCA. DR InParanoid; Q9WZ67; -. DR KO; K02026; -. DR OMA; LANYRFR; -. DR OrthoDB; EOG693GR8; -. DR BioCyc; TMAR243274:GC6P-623-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 73 97 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 109 130 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 142 159 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 196 217 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 244 263 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 74 263 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 277 AA; 31340 MW; 6186FAA329FF29B5 CRC64; MSSWKIVDAP DFVKEVRVKG GEVIEILLEG VPSVFLSDET IDSVKLKFSF SEVLANIFQN YVDAWNAAPF PRYYFNTFFV ATTTTLLEVV TASLAAYAFS WMVFPGRDFI FGLFLATMMI PGEVLLVPNF ITISKLGWID TYYALIIPWI VSVFAIFLLR QHFLTIPREL FDAAKIDGCS HWRFLWQMVV PLSKPAVITS ALLKFVGSWN AFLWVLIVTN SEKYRTLPVG LQAFSSDVGT QYNLLMAAAT FSILPVVILF IFTQKYFIQG IARTGLK // ID Q9X2A8_THEMA Unreviewed; 248 AA. AC Q9X2A8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36851.1}; GN OrderedLocusNames=TM_1788 {ECO:0000313|EMBL:AAD36851.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36851.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36851.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:4URG, ECO:0000213|PDB:4URQ, ECO:0000213|PDB:4URS} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 90-248 IN COMPLEX WITH RP CYCLIC DIGUANOSINE MONOPHOSPHATE. RX PubMed=25360685; DOI=10.1371/JOURNAL.PONE.0110912; RA Deepthi A., Liew C.W., Liang Z.X., Swaminathan K., Lescar J.; RT "Structure of a diguanylate cyclase from Thermotoga maritima: insights RT into activation, feedback inhibition and thermostability."; RL PLoS ONE 9:e110912-e110912(2014). CC -!- SIMILARITY: Contains GGDEF domain. CC {ECO:0000256|SAAS:SAAS00496774}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36851.1; -; Genomic_DNA. DR PIR; G72211; G72211. DR RefSeq; NP_229585.1; NC_000853.1. DR RefSeq; WP_010865403.1; NC_000853.1. DR PDB; 4URG; X-ray; 1.90 A; A/B=90-248. DR PDB; 4URQ; X-ray; 2.50 A; U/V/W/X/Y/Z=91-248. DR PDB; 4URS; X-ray; 2.27 A; A/B=82-248. DR PDBsum; 4URG; -. DR PDBsum; 4URQ; -. DR PDBsum; 4URS; -. DR ProteinModelPortal; Q9X2A8; -. DR STRING; 243274.TM1788; -. DR EnsemblBacteria; AAD36851; AAD36851; TM_1788. DR GeneID; 897742; -. DR KEGG; tma:TM1788; -. DR PATRIC; 23938563; VBITheMar51294_1808. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR InParanoid; Q9X2A8; -. DR OMA; ELEYMAY; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; TMAR243274:GC6P-1839-MONOMER; -. DR BRENDA; 2.7.7.65; 6331. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR Pfam; PF00990; GGDEF; 1. DR SMART; SM00267; GGDEF; 1. DR SUPFAM; SSF55073; SSF55073; 1. DR TIGRFAMs; TIGR00254; GGDEF; 1. DR PROSITE; PS50887; GGDEF; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4URG, ECO:0000213|PDB:4URQ, KW ECO:0000213|PDB:4URS}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000213|PDB:4URS}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 118 248 GGDEF. {ECO:0000259|PROSITE:PS50887}. FT NP_BIND 158 161 Cyclic diguanosine monophosphate. FT {ECO:0000213|PDB:4URS}. FT NP_BIND 176 177 Cyclic diguanosine monophosphate. FT {ECO:0000213|PDB:4URS}. FT BINDING 115 115 Cyclic diguanosine monophosphate. FT {ECO:0000213|PDB:4URS}. FT BINDING 182 182 Cyclic diguanosine monophosphate. FT {ECO:0000213|PDB:4URS}. FT BINDING 189 189 Cyclic diguanosine monophosphate. FT {ECO:0000213|PDB:4URS}. SQ SEQUENCE 248 AA; 28615 MW; AD9ABB38997C505C CRC64; MKVSGGEVPP FFKEGFFFTS EELTHLINVC SSTSAIISVL KDSKYRRSLV LYLKRPLSKD ALLLIQTLLT TLEREDLSFG VKELEYMAYH DPLTGLPNRR YFFELGNRYL DLAKREGKKV FVLFVDLAGF KAINDTYGHL SGDEVLKTVS KRILDRVRRS DVVARYGGDE FTILLYDMKE EYLKSLLERI LSTFREPVRV ENKHLSVTPN IGVARFPEDG ENLEELLKVA DMRMYKAKEM KVPYFSLS // ID Q9X1D2_THEMA Unreviewed; 47 AA. AC Q9X1D2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36483.1}; GN OrderedLocusNames=TM_1412 {ECO:0000313|EMBL:AAD36483.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36483.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36483.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36483.1; -; Genomic_DNA. DR PIR; E72258; E72258. DR RefSeq; NP_229213.1; NC_000853.1. DR RefSeq; WP_010865332.1; NC_000853.1. DR EnsemblBacteria; AAD36483; AAD36483; TM_1412. DR GeneID; 898064; -. DR KEGG; tma:TM1412; -. DR BioCyc; TMAR243274:GC6P-1449-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 47 AA; 5438 MW; 776C75B7B97866BA CRC64; METHLLNSVV CYKLGFNNSL EVWKLFFGFP IAGITRCFNT SLDVRKK // ID Q9WYJ6_THEMA Unreviewed; 113 AA. AC Q9WYJ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35448.1}; GN OrderedLocusNames=TM_0361 {ECO:0000313|EMBL:AAD35448.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35448.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35448.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35448.1; -; Genomic_DNA. DR PIR; A72387; A72387. DR RefSeq; NP_228172.1; NC_000853.1. DR RefSeq; WP_010865101.1; NC_000853.1. DR STRING; 243274.TM0361; -. DR EnsemblBacteria; AAD35448; AAD35448; TM_0361. DR GeneID; 897319; -. DR KEGG; tma:TM0361; -. DR KEGG; tmi:THEMA_02910; -. DR PATRIC; 23935603; VBITheMar51294_0366. DR OMA; DIVWITA; -. DR OrthoDB; EOG69GZRM; -. DR BioCyc; TMAR243274:GC6P-375-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 28 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 60 91 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 113 AA; 13649 MW; 21E4EEC1AB2211F8 CRC64; MHGGDIVWIT ALVVLGFTLY SFYTWAFLVR HRKIISYIER EILELEEREK LFRREVVSGN DFVKEKYEKI LKLLEKARED YNFEVEKFNR KLKSPLYFIP AKLFGEVPLE KKD // ID Q9WYB9_THEMA Unreviewed; 254 AA. AC Q9WYB9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Sugar isomerase {ECO:0000313|EMBL:AAD35371.1}; GN OrderedLocusNames=TM_0283 {ECO:0000313|EMBL:AAD35371.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35371.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35371.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35371.1; -; Genomic_DNA. DR PIR; A72396; A72396. DR RefSeq; NP_228095.1; NC_000853.1. DR RefSeq; WP_010865088.1; NC_000853.1. DR ProteinModelPortal; Q9WYB9; -. DR STRING; 243274.TM0283; -. DR EnsemblBacteria; AAD35371; AAD35371; TM_0283. DR GeneID; 897201; -. DR KEGG; tma:TM0283; -. DR PATRIC; 23935445; VBITheMar51294_0288. DR eggNOG; ENOG4105CR5; Bacteria. DR eggNOG; COG0235; LUCA. DR InParanoid; Q9WYB9; -. DR KO; K03080; -. DR OMA; QNHGVFT; -. DR OrthoDB; EOG6358F1; -. DR BioCyc; TMAR243274:GC6P-296-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. DR Gene3D; 3.40.225.10; -; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; SSF53639; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Isomerase {ECO:0000313|EMBL:AAD35371.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 49 224 Aldolase_II. {ECO:0000259|SMART:SM01007}. SQ SEQUENCE 254 AA; 28183 MW; FCDB944C570159FF CRC64; MRSTDRLLFI DFLLKFENKN GTVIPCCVDN FDCTFTHKGG KSMYEKERKE LYNAHLLLEK YGLVAYTSGN VSVRIGDHVL IKPSGVPYTE LKPEDFVVVD LEGNVIEGEK KPSVDTATHL YLYKHLDWAK SVIHTHSTFA MVWAILEKSI PVLCTAHADV FGEEIPLTEY APVGSEAIGK AVVKVIGKSG AVLLRKHGVM IVGTSVDDAV KKAIFLEEVA KAAYFATLAG KPTPLPPDEV DHLYNQYHTK YGQK // ID Q9WZ58_THEMA Unreviewed; 196 AA. AC Q9WZ58; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35674.1}; GN OrderedLocusNames=TM_0589 {ECO:0000313|EMBL:AAD35674.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35674.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35674.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35674.1; -; Genomic_DNA. DR PIR; F72356; F72356. DR RefSeq; NP_228399.1; NC_000853.1. DR RefSeq; WP_010865155.1; NC_000853.1. DR EnsemblBacteria; AAD35674; AAD35674; TM_0589. DR GeneID; 897661; -. DR KEGG; tma:TM0589; -. DR BioCyc; TMAR243274:GC6P-614-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 196 AA; 21589 MW; 9FAF3052460762A0 CRC64; MLPQGVKDQK YDQNENIPVS WNCEESDQNH NKQKRNGSPA EGKAQKGGKE TQNVLEDVVP EDAEKGKNID HSTTPMTITL SGTSRVTFSR KYSSSRPATV PMNRYSLKAT FHFSLSKYTF QPVTSMSSIT ESLGTRSPLT TPTTDSRSFS TLTFSTKSSE NTLITFEIGP FSTTIPRNLF SSGSRTMAPS SASPRM // ID Q9X153_THEMA Unreviewed; 111 AA. AC Q9X153; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=LacI family transcriptional regulator, putative {ECO:0000313|EMBL:AAD36402.1}; GN OrderedLocusNames=TM_1330 {ECO:0000313|EMBL:AAD36402.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36402.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36402.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36402.1; -; Genomic_DNA. DR PIR; F72267; F72267. DR RefSeq; NP_229132.1; NC_000853.1. DR RefSeq; WP_010865315.1; NC_000853.1. DR ProteinModelPortal; Q9X153; -. DR STRING; 243274.TM1330; -. DR EnsemblBacteria; AAD36402; AAD36402; TM_1330. DR GeneID; 898152; -. DR KEGG; tma:TM1330; -. DR PATRIC; 23937597; VBITheMar51294_1344. DR eggNOG; ENOG4108IMY; Bacteria. DR eggNOG; COG1396; LUCA. DR InParanoid; Q9X153; -. DR OMA; PEYKFRE; -. DR OrthoDB; EOG6K13P3; -. DR BioCyc; TMAR243274:GC6P-1361-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 23 81 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 111 AA; 12202 MW; F2B3C53E6062A8BF CRC64; MGFHHSEEEK VFIEVMSQIG GQLLAYRKMH NLTQKDLAKK LGVSQSMVSK IETGEKNISI RVLAKIVAAL GGKIKISLGL LPEEENKSPR YGFGVSEEII TSFEAQRSVA A // ID Q9X0L1_THEMA Unreviewed; 178 AA. AC Q9X0L1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36203.1}; GN OrderedLocusNames=TM_1127 {ECO:0000313|EMBL:AAD36203.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36203.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36203.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36203.1; -; Genomic_DNA. DR PIR; D72293; D72293. DR RefSeq; NP_228933.1; NC_000853.1. DR RefSeq; WP_010865268.1; NZ_CP011107.1. DR STRING; 243274.TM1127; -. DR EnsemblBacteria; AAD36203; AAD36203; TM_1127. DR GeneID; 898637; -. DR KEGG; tma:TM1127; -. DR KEGG; tmi:THEMA_08710; -. DR KEGG; tmw:THMA_1150; -. DR PATRIC; 23937189; VBITheMar51294_1143. DR OMA; NYTYTIT; -. DR OrthoDB; EOG6D2KV8; -. DR BioCyc; TMAR243274:GC6P-1156-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR012902; N_methyl_site. DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 41 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 178 AA; 19894 MW; F6665DA03B4F4C0D CRC64; MPHFSVNNQN GGDTMRNGFT IVELLITIAV LLIGILLVLG FTARTIVATV QSFTTIELAD DLLKAAMEIR KEILKAGPRA DQIYPENPEK ISFLVNVPFG GEKYYSRNYT YTIAFEKPDI KLYIFQEDSN STDTRILVTD ISTCTFLAGT GTVSFVIGKE KHNIERTYFM SVALPNLK // ID Q9WXQ2_THEMA Unreviewed; 74 AA. AC Q9WXQ2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35139.1}; GN OrderedLocusNames=TM_0045 {ECO:0000313|EMBL:AAD35139.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35139.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35139.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35139.1; -; Genomic_DNA. DR PIR; B72426; B72426. DR RefSeq; NP_227861.1; NC_000853.1. DR RefSeq; WP_010865036.1; NC_000853.1. DR STRING; 243274.TM0045; -. DR EnsemblBacteria; AAD35139; AAD35139; TM_0045. DR GeneID; 896869; -. DR KEGG; tma:TM0045; -. DR PATRIC; 23934930; VBITheMar51294_0043. DR eggNOG; ENOG4106EH6; Bacteria. DR eggNOG; ENOG410XXGP; LUCA. DR OMA; MWMDKEK; -. DR OrthoDB; EOG6DRPPD; -. DR BioCyc; TMAR243274:GC6P-45-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 74 AA; 8521 MW; B6198394BFCA7981 CRC64; MWMDKEKYVK GIEKALQKIA VRELKIVDIS EIWIETALPK DLIIEILKEG KLNIPSGIET IKDGRDVIWK RSGS // ID Q9WZF1_THEMA Unreviewed; 189 AA. AC Q9WZF1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35767.1}; GN OrderedLocusNames=TM_0685 {ECO:0000313|EMBL:AAD35767.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35767.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35767.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35767.1; -; Genomic_DNA. DR PIR; B72348; B72348. DR RefSeq; NP_228494.1; NC_000853.1. DR RefSeq; WP_010865186.1; NC_000853.1. DR ProteinModelPortal; Q9WZF1; -. DR STRING; 243274.TM0685; -. DR CAZy; GH23; Glycoside Hydrolase Family 23. DR EnsemblBacteria; AAD35767; AAD35767; TM_0685. DR GeneID; 898352; -. DR KEGG; tma:TM0685; -. DR PATRIC; 23936288; VBITheMar51294_0697. DR eggNOG; ENOG4105SXY; Bacteria. DR eggNOG; COG0741; LUCA. DR InParanoid; Q9WZF1; -. DR OMA; ELGMMQI; -. DR OrthoDB; EOG6JTCB0; -. DR BioCyc; TMAR243274:GC6P-711-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR008258; Transglycosylase_SLT_dom_1. DR Pfam; PF01464; SLT; 1. DR SUPFAM; SSF53955; SSF53955; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 68 175 SLT. {ECO:0000259|Pfam:PF01464}. SQ SEQUENCE 189 AA; 22156 MW; B532A5D367073425 CRC64; MKKITILILV LMVIPVFLST VPSENNISFR EINSIAVKEW FKELVRSRRA SYKLKSDEEF LEDLWKTINN VAKETNFDPI LIISVIDVES DFRNVVGLYG ELGMMQIKKE TAEMVANLYG LEIPESGWTE LVWNYRLNIK YGAHYLKYLF DKFNNLRLAL EYYNGGNSRK SYAQKILETY EEFKKELGI // ID Q9X261_THEMA Unreviewed; 303 AA. AC Q9X261; G4FGC5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36804.1}; GN OrderedLocusNames=TM_1739 {ECO:0000313|EMBL:AAD36804.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36804.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36804.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1ZUP} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS). RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of hypothetical protein (tm1739) from Thermotoga RT maritima at 2.20 A resolution."; RL Submitted (MAY-2005) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36804.1; -; Genomic_DNA. DR PIR; B72218; B72218. DR RefSeq; NP_229537.1; NC_000853.1. DR RefSeq; WP_004082261.1; NZ_CP011107.1. DR PDB; 1ZUP; X-ray; 2.20 A; A/B=1-303. DR PDBsum; 1ZUP; -. DR ProteinModelPortal; Q9X261; -. DR SMR; Q9X261; 1-301. DR STRING; 243274.TM1739; -. DR EnsemblBacteria; AAD36804; AAD36804; TM_1739. DR GeneID; 897869; -. DR KEGG; tma:TM1739; -. DR KEGG; tmi:THEMA_05540; -. DR KEGG; tmw:THMA_1781; -. DR PATRIC; 23938454; VBITheMar51294_1757. DR eggNOG; ENOG4108E6K; Bacteria. DR eggNOG; COG2380; LUCA. DR KO; K09785; -. DR OMA; ISECLTI; -. DR OrthoDB; EOG6PP9JS; -. DR BioCyc; TMAR243274:GC6P-1787-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR InterPro; IPR018977; NurA_domain. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF09376; NurA; 1. DR SMART; SM00933; NurA; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1ZUP}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 43 285 NurA. {ECO:0000259|SMART:SM00933}. SQ SEQUENCE 303 AA; 34880 MW; DFB8AD83EB308EFA CRC64; MQVRIERAER IESELEEHVG DQTFVEESRF LEEDEQREGE ILDQIIFVDG KRRSFVRITT DEGITGIFAE LCVGAVIWDR EGGTKTLFSP DKPPVKERVL GFSQSFQEEG YEEVGGILFK VVKEGKDAMQ SIDLYMRSLE IEEVRKHMDK NILIVKDGPA ARELPFEENV GPIGLVKNIG VTELSKEDFK KLRFLKKGKR SKMFVSSRET PLKKVGAYVK LIDGEGIRGL VRLETYVKDD NQIPYIRKVF DDLAKTLPHL TADLPIPRLP ENILPIQFLE ENLSYYLTDK NYMNTRLFAY IGR // ID Q9X2F8_THEMA Unreviewed; 220 AA. AC Q9X2F8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36904.1}; GN OrderedLocusNames=TM_1842 {ECO:0000313|EMBL:AAD36904.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36904.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36904.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36904.1; -; Genomic_DNA. DR PIR; E72204; E72204. DR RefSeq; NP_229638.1; NC_000853.1. DR RefSeq; WP_010865417.1; NC_000853.1. DR STRING; 243274.TM1842; -. DR DNASU; 897193; -. DR EnsemblBacteria; AAD36904; AAD36904; TM_1842. DR GeneID; 897193; -. DR KEGG; tma:TM1842; -. DR KEGG; tmi:THEMA_04995; -. DR PATRIC; 23938673; VBITheMar51294_1863. DR eggNOG; ENOG4106FRM; Bacteria. DR eggNOG; ENOG410Y820; LUCA. DR OMA; SASIPIW; -. DR OrthoDB; EOG6VMTJ4; -. DR BioCyc; TMAR243274:GC6P-1893-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 220 AA; 24479 MW; BB117629332B9D29 CRC64; MISLKKIIPA LLLITFLSGC MTLLNIKLPD GVYVIGDFSN GVPSSEYKMA LQGDFYTLEL PSSVLSFEND IAWYQVVVVE NGKPVKTTSE IPLWKQLVGA TVTIYATPNL MENDTAKGVG DSEKETPPWY CAGDFNNWTL EEMTYQDGKF VLNTGRTVSS GETIQYKIAR NTDWTPYEEQ FDGTSYEAGY GKNATFTADK DGTFVIEFDP KTSTLQAYVE // ID Q9X133_THEMA Unreviewed; 127 AA. AC Q9X133; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36381.1}; GN OrderedLocusNames=TM_1307 {ECO:0000313|EMBL:AAD36381.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36381.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36381.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36381.1; -; Genomic_DNA. DR PIR; E72270; E72270. DR RefSeq; NP_229111.1; NC_000853.1. DR RefSeq; WP_010865303.1; NC_000853.1. DR STRING; 243274.TM1307; -. DR EnsemblBacteria; AAD36381; AAD36381; TM_1307. DR GeneID; 898175; -. DR KEGG; tma:TM1307; -. DR OrthoDB; EOG67HJSJ; -. DR BioCyc; TMAR243274:GC6P-1338-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 78 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 127 AA; 14537 MW; 411A0C2F74E802C1 CRC64; MRLLRHFWIS YKGVSLWLNW KAYAAEKIIN PIFRLLFYST LLAYGYKTLH DARAFIIANI MALSSISVFK GLGIIFFLRA RSGIVDFLRC FAFIEIQSNA KKDAFSHNRC TGHGDSGTGC FILLFKT // ID Q9WY44_THEMA Unreviewed; 608 AA. AC Q9WY44; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 112. DE SubName: Full=NADP-reducing hydrogenase, subunit D, putative {ECO:0000313|EMBL:AAD35293.1}; GN OrderedLocusNames=TM_0201 {ECO:0000313|EMBL:AAD35293.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35293.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35293.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35293.1; -; Genomic_DNA. DR PIR; C72405; C72405. DR RefSeq; NP_228016.1; NC_000853.1. DR RefSeq; WP_010865073.1; NC_000853.1. DR ProteinModelPortal; Q9WY44; -. DR STRING; 243274.TM0201; -. DR EnsemblBacteria; AAD35293; AAD35293; TM_0201. DR GeneID; 897071; -. DR KEGG; tma:TM0201; -. DR PATRIC; 23935274; VBITheMar51294_0203. DR eggNOG; COG1034; LUCA. DR eggNOG; COG4624; LUCA. DR InParanoid; Q9WY44; -. DR KO; K00336; -. DR OMA; DMPVYET; -. DR OrthoDB; EOG6CVV7G; -. DR BioCyc; TMAR243274:GC6P-214-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central. DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 4.10.260.20; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR009016; Fe_hydrogenase. DR InterPro; IPR004108; Fe_hydrogenase_lsu_C. DR InterPro; IPR003149; Fe_hydrogenase_ssu. DR InterPro; IPR013352; Fe_hydrogenase_subset. DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. DR Pfam; PF02906; Fe_hyd_lg_C; 1. DR Pfam; PF02256; Fe_hyd_SSU; 1. DR Pfam; PF13187; Fer4_9; 1. DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1. DR SMART; SM00902; Fe_hyd_SSU; 1. DR SMART; SM00929; NADH-G_4Fe-4S_3; 1. DR SUPFAM; SSF53920; SSF53920; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR02512; FeFe_hydrog_A; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 28 107 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. FT DOMAIN 165 195 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 208 237 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 608 AA; 67652 MW; 8C90822E35F905A6 CRC64; MRRFFKNNLR NLSQNGETNS VRRCFALADV TVVINGRTLT VPDNLTVIEA CEKAGIEIPA LCHHPRLGES IGACRVCVVE VEGARNLQPA CVTKVRDGMV IKTSSDRVKT ARKFNLALLL SEHPNDCMTC EANGRCEFQD LIYKYDVEPI FGYGTKEGLV DRSSPAIVRD LSKCIKCQRC VRACSELQGM HIYSMVERGH RTYPGTPFDM PVYETDCIGC GQCAAFCPTG AIVENSAVKV VLEELEKKEK ILVVQTAPSV RVAIGEEFGY APGTISTGQM VAALRRLGFD YVFDTNFGAD LTIMEEGSEF LERLEKGDLE DLPMFTSCCP GWVNLVEKVY PELRTRLSSA KSPQGMLSAM VKTYFAEKLG VKPEDIFHVS IMPCTAKKDE ALRKQLMVNG VPAVDVVLTT RELGKLIRMK KIPFANLPEE EYDAPLGIST GAAALFGVTG GVMEAALRTA YELKTGKALP KIVFEEVRGL KGVREAEIDL DGKKIRIAVV HGTANVRNLV EKILRREVKY HFVEVMACPG GCIGGGGQPY SRDPEILRKR AEAIYTIDER MTLRKSHENP AIKKLYEEYL EHPLSHKAHE LLHTYYEDRS RKKRLAVK // ID Q9X1V2_THEMA Unreviewed; 116 AA. AC Q9X1V2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36684.1}; GN OrderedLocusNames=TM_1617 {ECO:0000313|EMBL:AAD36684.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36684.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36684.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36684.1; -; Genomic_DNA. DR PIR; C72232; C72232. DR RefSeq; NP_229417.1; NC_000853.1. DR RefSeq; WP_010865371.1; NZ_CP011107.1. DR STRING; 243274.TM1617; -. DR EnsemblBacteria; AAD36684; AAD36684; TM_1617. DR GeneID; 897671; -. DR KEGG; tma:TM1617; -. DR KEGG; tmi:THEMA_06165; -. DR KEGG; tmw:THMA_1657; -. DR PATRIC; 23938208; VBITheMar51294_1636. DR eggNOG; ENOG4106EJI; Bacteria. DR eggNOG; ENOG410Y6WE; LUCA. DR OMA; VEAFIFS; -. DR OrthoDB; EOG6130DC; -. DR BioCyc; TMAR243274:GC6P-1663-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005598; ATPase_I. DR Pfam; PF03899; ATP-synt_I; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 91 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 116 AA; 12819 MW; A17F2207AEF84E45 CRC64; MIKVKRLTKK MAVTIMIMGM VEALVFGLIS GFEKSWSPLL GSAGAVLNLF SLKNDIEKMA SRGTTKGWVF GYLGRYTFSA ALLLLGGLVS FETLLGVFFG LMNLKIVSFI AWRWTD // ID Q9X1S3_THEMA Unreviewed; 131 AA. AC Q9X1S3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36654.1}; GN OrderedLocusNames=TM_1587 {ECO:0000313|EMBL:AAD36654.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36654.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36654.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36654.1; -; Genomic_DNA. DR PIR; C72236; C72236. DR RefSeq; NP_229387.1; NC_000853.1. DR RefSeq; WP_010865366.1; NC_000853.1. DR STRING; 243274.TM1587; -. DR EnsemblBacteria; AAD36654; AAD36654; TM_1587. DR GeneID; 897952; -. DR KEGG; tma:TM1587; -. DR KEGG; tmi:THEMA_06345; -. DR PATRIC; 23938138; VBITheMar51294_1606. DR eggNOG; ENOG410629M; Bacteria. DR eggNOG; ENOG4112DCW; LUCA. DR OMA; DFPEELY; -. DR OrthoDB; EOG6PKFFM; -. DR BioCyc; TMAR243274:GC6P-1628-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 131 AA; 14900 MW; 342916981EBD36BD CRC64; MSDVRKSLAF LIVSVLLSIS FGDFLYLVPL SVDFPEELYE STGTRSFLVK YFTLFEDEFQ KGIVFSGWIF SPSDQATTTV EVKLEGKGEQ HSFFVEAIRE GFYLVIPPHL LVFPKDLKVF IGKYEVGGEP R // ID Q9WZD7_THEMA Unreviewed; 204 AA. AC Q9WZD7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35751.1}; GN OrderedLocusNames=TM_0669 {ECO:0000313|EMBL:AAD35751.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35751.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35751.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35751.1; -; Genomic_DNA. DR PIR; B72350; B72350. DR RefSeq; NP_228478.1; NC_000853.1. DR RefSeq; WP_010865180.1; NC_000853.1. DR STRING; 243274.TM0669; -. DR EnsemblBacteria; AAD35751; AAD35751; TM_0669. DR GeneID; 897784; -. DR KEGG; tma:TM0669; -. DR PATRIC; 23936252; VBITheMar51294_0679. DR eggNOG; ENOG4108TD1; Bacteria. DR eggNOG; ENOG4111GN0; LUCA. DR OMA; RIISVAQ; -. DR OrthoDB; EOG6091CJ; -. DR BioCyc; TMAR243274:GC6P-694-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 204 AA; 22301 MW; 70E6E755455D9E01 CRC64; MGGIWMSSAK TLEEVISKIS GVISAKVIEE DGQPREIHVI ADPSRNPKQI VRDIETVALA SLGMKIDRRI ISVAQLSQGR FPSSQTYEIT SIEVKNLDRK KQVKVTIHNP LEDEDMVGES AGPGTSTNLP RLVGEAVIEA FNPDCPVSVD DVQKVFLAGR EFVLVHLTIQ DEDRERTEVG VAPLEGDFLK SVATATLKVV KDLT // ID Q9WZK4_THEMA Unreviewed; 142 AA. AC Q9WZK4; G4FD78; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35826.1}; GN OrderedLocusNames=TM_0745 {ECO:0000313|EMBL:AAD35826.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35826.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35826.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35826.1; -; Genomic_DNA. DR PIR; D72340; D72340. DR RefSeq; NP_228554.1; NC_000853.1. DR RefSeq; WP_004080973.1; NC_000853.1. DR STRING; 243274.TM0745; -. DR EnsemblBacteria; AAD35826; AAD35826; TM_0745. DR GeneID; 898412; -. DR KEGG; tma:TM0745; -. DR PATRIC; 23936410; VBITheMar51294_0758. DR OMA; GFWNDIA; -. DR OrthoDB; EOG62G5R8; -. DR BioCyc; TMAR243274:GC6P-771-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 15 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 44 66 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 86 111 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 118 137 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 142 AA; 16658 MW; A6B2A4712364E170 CRC64; MMLNLINLDD SGKKYSFLVP ILVFFVNTVV FWNDIAMVYN SLRILLKIFE DFFLFFLYSL SISGLYKTIT NRAPAEMMWA LSPYVFLPLL SAFLDVRISL LILFFASLFL FRKLELKNLI LISLVRASAL CLFIWKISSW MR // ID Q9X0V6_THEMA Unreviewed; 482 AA. AC Q9X0V6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36304.1}; GN OrderedLocusNames=TM_1229 {ECO:0000313|EMBL:AAD36304.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36304.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36304.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36304.1; -; Genomic_DNA. DR PIR; F72278; F72278. DR RefSeq; NP_229034.1; NC_000853.1. DR RefSeq; WP_010865284.1; NC_000853.1. DR ProteinModelPortal; Q9X0V6; -. DR STRING; 243274.TM1229; -. DR CAZy; GT81; Glycosyltransferase Family 81. DR EnsemblBacteria; AAD36304; AAD36304; TM_1229. DR GeneID; 898255; -. DR KEGG; tma:TM1229; -. DR PATRIC; 23937400; VBITheMar51294_1247. DR eggNOG; ENOG4106J7S; Bacteria. DR eggNOG; COG0463; LUCA. DR OMA; IPSYNNA; -. DR OrthoDB; EOG613072; -. DR BioCyc; TMAR243274:GC6P-1259-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IBA:GO_Central. DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central. DR GO; GO:0019348; P:dolichol metabolic process; IBA:GO_Central. DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 107 232 Glyco_trans_2-like. FT {ECO:0000259|Pfam:PF00535}. SQ SEQUENCE 482 AA; 54820 MW; A08EE5C8C3D70AE0 CRC64; MGESASGSDR SQKARGAFRV RSLQIRYKTS RPEIRQSWRS MLQRERPCKG GREDFEKGRR GNFSSPLRSV SLQGDCRTQL RSGKEALQFR ETRRHTEQGG ITMKVVVGIP SYNNAETISH VARTAAQGIV DFFDGDGMIV NSDGGSADGT RERFMETDTF GLPKESFVYE GLPGKGSAMR AIMEFALKQD AEAVVFLDAD LRSVKPWWVE RLAGPVLKGE ADYVTPFYLR HRFDGTITNN VCFPMTAVLY GKKVRQPIGG DFGVGRKLLE IYLGKPKEIW NTDVARFGID IWMTTTAINE SGRVVQAALG TKVHDVKDPG KHLKGMFLQV VGTLFELVIT YENVWKEIWK IEDVPIYGET PQEEVPSMSI DIGNLKKLAR ETLEEVEYID RGILSEVKES GTLSLSSWVD TLYRSAVQYR KTRDKKVVEN LLPFYFARTA RFAEEVKSLS DEEAERYVYE QLDVFLEKKH SLREEWKVED KR // ID Q9WYP0_THEMA Unreviewed; 271 AA. AC Q9WYP0; G4FHW8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35494.1}; GN OrderedLocusNames=TM_0409 {ECO:0000313|EMBL:AAD35494.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35494.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35494.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35494.1; -; Genomic_DNA. DR PIR; G72380; G72380. DR RefSeq; NP_228219.1; NC_000853.1. DR RefSeq; WP_004083253.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYP0; -. DR STRING; 243274.TM0409; -. DR DNASU; 897408; -. DR EnsemblBacteria; AAD35494; AAD35494; TM_0409. DR GeneID; 897408; -. DR KEGG; tma:TM0409; -. DR KEGG; tmi:THEMA_02680; -. DR KEGG; tmw:THMA_0415; -. DR PATRIC; 23935701; VBITheMar51294_0414. DR eggNOG; ENOG4105DR5; Bacteria. DR eggNOG; COG0739; LUCA. DR OMA; AFNDEKF; -. DR OrthoDB; EOG62NX36; -. DR BioCyc; TMAR243274:GC6P-424-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.10.350.10; -; 2. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR018392; LysM_dom. DR InterPro; IPR016047; Peptidase_M23. DR Pfam; PF01476; LysM; 2. DR Pfam; PF01551; Peptidase_M23; 1. DR SMART; SM00257; LysM; 2. DR SUPFAM; SSF51261; SSF51261; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 25 69 LysM. {ECO:0000259|SMART:SM00257}. FT DOMAIN 75 118 LysM. {ECO:0000259|SMART:SM00257}. SQ SEQUENCE 271 AA; 30291 MW; AAD687B67CF8B470 CRC64; MKRGFFLLFL VVFFVYGFSS YFLIHYKVQK NDTLYSISLN FGISPSLLLD WNPGLDPHSL RVGQEIVIPQ PPGYLYTVKK GDTLDAIAKR FFTTATFIKE ANQLKSYTIY AGQKLFIPES IIGKAFNDEK FFIWPVYGVI SSGFGWRIHP ITGKYSFHSG VDISAPEGTP IFAAESGVVE FAGKNGGYGL MIKIKSASYE HIYGHLSQID VYEGQYVKKG QIIGRVGNTG LSTGPHLHFE VRVNQKAVNP INYLPNQIWV LKKELIGTGG E // ID Q9X134_THEMA Unreviewed; 31 AA. AC Q9X134; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36382.1}; GN OrderedLocusNames=TM_1308 {ECO:0000313|EMBL:AAD36382.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36382.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36382.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36382.1; -; Genomic_DNA. DR PIR; F72270; F72270. DR RefSeq; NP_229112.1; NC_000853.1. DR RefSeq; WP_010865304.1; NC_000853.1. DR STRING; 243274.TM1308; -. DR EnsemblBacteria; AAD36382; AAD36382; TM_1308. DR GeneID; 898174; -. DR KEGG; tma:TM1308; -. DR BioCyc; TMAR243274:GC6P-1339-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 31 AA; 3410 MW; A9985C8D8D44D50D CRC64; MAALGLLTRD INMLLGVAEM MVFILSVQVF L // ID Q9X140_THEMA Unreviewed; 535 AA. AC Q9X140; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36388.1}; GN OrderedLocusNames=TM_1314 {ECO:0000313|EMBL:AAD36388.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36388.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36388.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36388.1; -; Genomic_DNA. DR PIR; B72268; B72268. DR RefSeq; NP_229118.1; NC_000853.1. DR RefSeq; WP_010865307.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X140; -. DR STRING; 243274.TM1314; -. DR EnsemblBacteria; AAD36388; AAD36388; TM_1314. DR GeneID; 898168; -. DR KEGG; tma:TM1314; -. DR KEGG; tmi:THEMA_07775; -. DR KEGG; tmw:THMA_1338; -. DR PATRIC; 23937564; VBITheMar51294_1328. DR eggNOG; ENOG4108E48; Bacteria. DR eggNOG; ENOG41103JN; LUCA. DR OMA; FFDAPRF; -. DR OrthoDB; EOG6VXF5P; -. DR BioCyc; TMAR243274:GC6P-1345-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 285 341 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 535 AA; 63068 MW; 4E31E862848E90C2 CRC64; MKSHQLLKAP FQHGFLFSRP LVMYCFKTCH DSAWKHYIRF LKYRHEKLYE EALSEIDNAI KVCNSIAFRY FLLSEKLTVL GYMGKHEEGI KLYSHLRGRM RNVSPNLRSI FIGNLLNYCS MYLHNAFECL GRIKPEAHHL EKSSYAFILI GKARYMARTG NVKEAIESYE KALKILQEIP HPSGIIACLN DMAWYTKEKD PEKAKDMAEE ALYWNGYFFD APRFYALDTL FEVQRTTSDP AIVETARLIE IASEGLKDSA SDLLKKDQRL FLRLNNSLYR NTKSLQRFLR RNTTSIKHLS EITGVARNRL SDILNGKTQK IRGETLRKIA KAFEKSNILS FPPPLLSEWV KLRIEENFSA ALREIKTKRL EERQILFLST YTALIDRKFL SRKERLKKAY TLLEDIESFA DFMAKDHRTM EFVVSMVKAH PFVEGRKEAV KRALARMKRK RLERFVLRYI EMKESDRKLL DRFLRNYGRY DGVRFGIRLK GPEVVREFAK KYSLKVQPLF AAFWCEEDGR VRRRLERVLK HMVLN // ID Q9X090_THEMA Unreviewed; 38 AA. AC Q9X090; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36077.1}; GN OrderedLocusNames=TM_0995 {ECO:0000313|EMBL:AAD36077.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36077.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36077.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36077.1; -; Genomic_DNA. DR PIR; E72306; E72306. DR RefSeq; NP_228803.1; NC_000853.1. DR RefSeq; WP_010865237.1; NC_000853.1. DR STRING; 243274.TM0995; -. DR EnsemblBacteria; AAD36077; AAD36077; TM_0995. DR GeneID; 897103; -. DR KEGG; tma:TM0995; -. DR KEGG; tmi:THEMA_09375; -. DR PATRIC; 23936921; VBITheMar51294_1009. DR OrthoDB; EOG63C13R; -. DR BioCyc; TMAR243274:GC6P-1025-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 38 AA; 4189 MW; 68C76290B4C3C33D CRC64; MMSEIEENSS KKLSMSYDDK KAAFSGGFVV NRVLSQAC // ID Q9X098_THEMA Unreviewed; 278 AA. AC Q9X098; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Transposase-related protein {ECO:0000313|EMBL:AAD36085.1}; GN OrderedLocusNames=TM_1003 {ECO:0000313|EMBL:AAD36085.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36085.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36085.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36085.1; -; Genomic_DNA. DR PIR; E72307; E72307. DR RefSeq; NP_228811.1; NC_000853.1. DR RefSeq; WP_010865240.1; NC_000853.1. DR STRING; 243274.TM1003; -. DR EnsemblBacteria; AAD36085; AAD36085; TM_1003. DR GeneID; 898711; -. DR KEGG; tma:TM1003; -. DR KEGG; tmi:THEMA_09340; -. DR PATRIC; 23936935; VBITheMar51294_1016. DR eggNOG; ENOG4108QGC; Bacteria. DR eggNOG; COG0675; LUCA. DR KO; K07496; -. DR OMA; ERFVCQN; -. DR OrthoDB; EOG65F8QJ; -. DR BioCyc; TMAR243274:GC6P-1033-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR001959; Transposase_2. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR Pfam; PF01385; OrfB_IS605; 1. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 50 145 OrfB_IS605. {ECO:0000259|Pfam:PF01385}. FT DOMAIN 180 251 OrfB_Zn_ribbon. FT {ECO:0000259|Pfam:PF07282}. SQ SEQUENCE 278 AA; 32019 MW; A37BDC2009207110 CRC64; MARFSTLQGR IKWIPMKGWS KHFEYLKSGK IGDPILTYDK SSKTFFLLVP VTLEVQEHQP KEILGVDVGE RHIAAATSTK GTRYLIDLPE EFKQRKQHYQ RLRSELMSKG TRSAKRKLAR ISRREKRFTE NVLHIIAKKL ITSHPGARFV LEDLTQIRAN RITYRGKDKE ARRQSEQWPF ASLQQKIEYK AKLYYGVQSE KVDPSYTSQT CPRCGHVSKE NRPDHGERFV CQNCGYEEHA DIVGAINIAL RVLVKDQQGN LEKLLGADVS RPDAPRLG // ID Q9X2B4_THEMA Unreviewed; 815 AA. AC Q9X2B4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36857.1}; GN OrderedLocusNames=TM_1794 {ECO:0000313|EMBL:AAD36857.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36857.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36857.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36857.1; -; Genomic_DNA. DR PIR; G72209; G72209. DR RefSeq; NP_229591.1; NC_000853.1. DR RefSeq; WP_010865405.1; NC_000853.1. DR STRING; 243274.TM1794; -. DR DNASU; 896966; -. DR EnsemblBacteria; AAD36857; AAD36857; TM_1794. DR GeneID; 896966; -. DR KEGG; tma:TM1794; -. DR KEGG; tmi:THEMA_05220; -. DR PATRIC; 23938577; VBITheMar51294_1815. DR eggNOG; ENOG4105XC4; Bacteria. DR eggNOG; COG1353; LUCA. DR KO; K19076; -. DR OMA; PVITHPT; -. DR OrthoDB; EOG6Z9B30; -. DR BioCyc; TMAR243274:GC6P-1845-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR024615; CRISPR-assoc_Crm2_N. DR InterPro; IPR013407; CRISPR-assoc_prot_Crm2. DR InterPro; IPR000160; GGDEF_dom. DR Pfam; PF12469; DUF3692; 1. DR TIGRFAMs; TIGR02577; cas_TM1794_Cmr2; 1. DR PROSITE; PS50887; GGDEF; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 535 692 GGDEF. {ECO:0000259|PROSITE:PS50887}. FT COILED 113 140 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 815 AA; 93495 MW; 21E06C30E67898A3 CRC64; MDQKTRRKRN PGGIIVSKRE EFWKSKITAL LHDPLVKAFD VKNHENIAGE ILKTLGIKKT RGEEDRLASA MDRFPIPYEK DAKKQIHVSF DETLFVHPFS GEGLPEVKSF FQNQKVEEMK SRLINALTKL KEKNDTYEKL FHSIWWNLPY ILEGSQFLPA DTRIANHSII DHLDVTSALK GCVEGKQVKA SLVAVAIGPV QEVIAQARKV KDLWAGSYLL SYLIYGAIEV VGKKYGFDSI ISPYLRGNYF VKETLESMGV DLEDLCPVPP RREVASLPNL FVAIVPSSDE EILKECEEAI RNRWKTIVDE TKEKLSKSEF LFNEHSFDYQ SSLFPDIQTS KVSFDEPERI VETVRNLFTG SGIEDFKEVL KKVSEHAGYK ENPGTFYRYL HRLLTSKLAA RKMARLFPGY EEDVYPDHFT DADDFGAGVR ACAVFKDKDI EKDIEKEDRL GTLNTVKRFL PEILNIRIKF DSTTDVARNN QANKEIEDPE KFKNGYIAVL LMDGDRMGDW MLGENAPFLE KVINPKVIEM FQETDDLKYA WEKLKEFKTI QPAYHRGVSR TLGIFSQLVG KIVDRHNGML VYSGGDDVLA LLPADSVLEC ANDIRKFFSG HLEYEIEIES GSDVERFRSE NGVLYHNDKP FAPLMGRAAT MSAGIAIVHH KFPLQVALKI AREAEKRAKN VYGRNAFCVT QVKRSGQMIF AGSTWEIEEE DVVKRSLKIL EEMKNYNVSH RSLYKLLSPD FSLYEDKMEK FVEFTLRRSI HSEKSKNEFI GNFKNFLSRL LAYYKNTKKS SFDEAMREAL ELLIMVYSMK RGESQ // ID Q9WY01_THEMA Unreviewed; 76 AA. AC Q9WY01; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35247.1}; GN OrderedLocusNames=TM_0154 {ECO:0000313|EMBL:AAD35247.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35247.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35247.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35247.1; -; Genomic_DNA. DR PIR; H72412; H72412. DR RefSeq; NP_227969.1; NC_000853.1. DR RefSeq; WP_010865062.1; NC_000853.1. DR EnsemblBacteria; AAD35247; AAD35247; TM_0154. DR GeneID; 896990; -. DR KEGG; tma:TM0154; -. DR BioCyc; TMAR243274:GC6P-155-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 76 AA; 9303 MW; 79F0C2D0D907082B CRC64; MKTRISSSRV RFSRYYLRIR ESLISIPSRK NQFRFIRKNR FALQASFRSF TENSLTLSFM LLRRSPMKQS RTFLIF // ID Q9WZU4_THEMA Unreviewed; 214 AA. AC Q9WZU4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35922.1}; GN OrderedLocusNames=TM_0840 {ECO:0000313|EMBL:AAD35922.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35922.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35922.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35922.1; -; Genomic_DNA. DR PIR; A72326; A72326. DR RefSeq; NP_228649.1; NC_000853.1. DR RefSeq; WP_010865213.1; NC_000853.1. DR STRING; 243274.TM0840; -. DR EnsemblBacteria; AAD35922; AAD35922; TM_0840. DR GeneID; 898511; -. DR KEGG; tma:TM0840; -. DR PATRIC; 23936606; VBITheMar51294_0853. DR OMA; IYDVDVW; -. DR OrthoDB; EOG64FKF2; -. DR BioCyc; TMAR243274:GC6P-869-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 214 AA; 24905 MW; C5FCBFEEC8D9C405 CRC64; MKKMKRFFPF LGLILLILTA CLPPIEERHE FIIEVVGNAY LDDVMDWYQP SYGDYLVQAH PVIVLYYPDE SYAYYERATF YEQYNDFVAA AGVIVDTADL KNDLGRIWNS YYPIYDVDVW WQADREEWQA RVKGLTRDVN ITTFFVVTFN GRDNYCEVVD IKDEGEIYLD NNGVYHLGPL SGVDGFAAFV QENPSRLTLE SNTKILGAEV RWIK // ID Q9X1Z6_THEMA Unreviewed; 163 AA. AC Q9X1Z6; G4FG57; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36735.1}; GN OrderedLocusNames=TM_1668 {ECO:0000313|EMBL:AAD36735.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36735.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36735.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36735.1; -; Genomic_DNA. DR PIR; B72225; B72225. DR RefSeq; NP_229468.1; NC_000853.1. DR RefSeq; WP_004082186.1; NZ_CP011107.1. DR STRING; 243274.TM1668; -. DR EnsemblBacteria; AAD36735; AAD36735; TM_1668. DR GeneID; 897126; -. DR KEGG; tma:TM1668; -. DR KEGG; tmi:THEMA_05905; -. DR KEGG; tmw:THMA_1709; -. DR PATRIC; 23938310; VBITheMar51294_1687. DR eggNOG; ENOG4108371; Bacteria. DR eggNOG; COG1430; LUCA. DR KO; K09005; -. DR OMA; LMYRKSI; -. DR OrthoDB; EOG6XHC8T; -. DR BioCyc; TMAR243274:GC6P-1714-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003795; DUF192. DR Pfam; PF02643; DUF192; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 14 32 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 163 AA; 18672 MW; E5A3AED220DA398C CRC64; MWGLRPLFLR LQKFLLPLLI TIGIIVVVVV SGQSDRVKFP KGRIVITDGE KSLKLDVEIA NTPALRSIGL MYRKSIPDDF GMLFVFEEDT CSGFWMKNTY VPLEIAFIDK NGVIFSIQEM EPCKEEPCKI YYAPGPFRYA LEVKKGFFER HRFGVGSRVS IEK // ID Q9WZ82_THEMA Unreviewed; 123 AA. AC Q9WZ82; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35698.1}; GN OrderedLocusNames=TM_0613 {ECO:0000313|EMBL:AAD35698.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35698.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35698.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1O3U} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=14997578; DOI=10.1002/prot.10631; RA Erlandsen H., Canaves J.M., Elsliger M.A., von Delft F., Brinen L.S., RA Dai X., Deacon A.M., Floyd R., Godzik A., Grittini C., Grzechnik S.K., RA Jaroszewski L., Klock H.E., Koesema E., Kovarik J.S., Kreusch A., RA Kuhn P., Lesley S.A., McMullan D., McPhillips T.M., Miller M.D., RA Morse A., Moy K., Ouyang J., Page R., Robb A., Quijano K., RA Schwarzenbacher R., Spraggon G., Stevens R.C., van den Bedem H., RA Velasquez J., Vincent J., Wang X., West B., Wolf G., Hodgson K.O., RA Wooley J., Wilson I.A.; RT "Crystal structure of an HEPN domain protein (TM0613) from Thermotoga RT maritima at 1.75 A resolution."; RL Proteins 54:806-809(2004). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35698.1; -; Genomic_DNA. DR PIR; A72356; A72356. DR RefSeq; NP_228423.1; NC_000853.1. DR RefSeq; WP_010865163.1; NC_000853.1. DR PDB; 1O3U; X-ray; 1.75 A; A=1-123. DR PDBsum; 1O3U; -. DR ProteinModelPortal; Q9WZ82; -. DR SMR; Q9WZ82; 1-123. DR STRING; 243274.TM0613; -. DR EnsemblBacteria; AAD35698; AAD35698; TM_0613. DR GeneID; 897696; -. DR KEGG; tma:TM0613; -. DR PATRIC; 23936139; VBITheMar51294_0623. DR eggNOG; ENOG4108ZMG; Bacteria. DR eggNOG; COG2250; LUCA. DR InParanoid; Q9WZ82; -. DR OMA; EAWGHSV; -. DR OrthoDB; EOG6PKFFJ; -. DR BioCyc; TMAR243274:GC6P-638-MONOMER; -. DR EvolutionaryTrace; Q9WZ82; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR007842; HEPN_dom. DR Pfam; PF05168; HEPN; 1. DR SMART; SM00748; HEPN; 1. DR PROSITE; PS50910; HEPN; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1O3U}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 112 HEPN. {ECO:0000259|PROSITE:PS50910}. FT DISULFID 24 79 {ECO:0000213|PDB:1O3U}. SQ SEQUENCE 123 AA; 14095 MW; B41BF12531D40635 CRC64; MDAAKDDLEH AKHDLEHGFY NWACFSSQQA AEKAVKAVFQ RMGAQAWGYS VPDFLGELSS RFEIPEELMD HALELDKACI PTRYPDALPS GSPRNRYSRI EAERLVNYAE KIIRFCEDLL SRI // ID Q9X0C0_THEMA Unreviewed; 200 AA. AC Q9X0C0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 112. DE SubName: Full=Transcriptional regulator, TetR family {ECO:0000313|EMBL:AAD36107.1}; GN OrderedLocusNames=TM_1030 {ECO:0000313|EMBL:AAD36107.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36107.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36107.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:2ID6} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). RA Koclega K.D., Chruszcz M., Minor W.; RT "Crystal structure of transcriptional regulator (tm1030) at 1.75A RT resolution."; RL Submitted (SEP-2006) to the PDB data bank. RN [3] {ECO:0000213|PDB:2IEK} RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS). RA Koclega K.D., Chruszcz M., Minor W.; RT "New crystal form of transcriptional regulator tm1030 from Thermotoga RT maritima."; RL Submitted (SEP-2006) to the PDB data bank. RN [4] {ECO:0000213|PDB:1Z77} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS). RX PubMed=17588774; DOI=10.1016/j.jsb.2007.04.012; RA Koclega K.D., Chruszcz M., Zimmerman M.D., Cymborowski M., RA Evdokimova E., Minor W.; RT "Crystal structure of a transcriptional regulator TM1030 from RT Thermotoga maritima solved by an unusual MAD experiment."; RL J. Struct. Biol. 159:424-432(2007). RN [5] {ECO:0000213|PDB:1ZKG} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS). RX PubMed=17444523; DOI=10.1002/prot.21436; RA Premkumar L., Rife C.L., Sri Krishna S., McMullan D., Miller M.D., RA Abdubek P., Ambing E., Astakhova T., Axelrod H.L., Canaves J.M., RA Carlton D., Chiu H.J., Clayton T., DiDonato M., Duan L., RA Elsliger M.A., Feuerhelm J., Floyd R., Grzechnik S.K., Hale J., RA Hampton E., Han G.W., Haugen J., Jaroszewski L., Jin K.K., Klock H.E., RA Knuth M.W., Koesema E., Kovarik J.S., Kreusch A., Levin I., RA McPhillips T.M., Morse A.T., Nigoghossian E., Okach L., Oommachen S., RA Paulsen J., Quijano K., Reyes R., Rezezadeh F., Rodionov D., RA Schwarzenbacher R., Spraggon G., van den Bedem H., White A., Wolf G., RA Xu Q., Hodgson K.O., Wooley J., Deacon A.M., Godzik A., Lesley S.A., RA Wilson I.A.; RT "Crystal structure of TM1030 from Thermotoga maritima at 2.3 A RT resolution reveals molecular details of its transcription repressor RT function."; RL Proteins 68:418-424(2007). RN [6] {ECO:0000213|PDB:3IH2, ECO:0000213|PDB:3IH3, ECO:0000213|PDB:3IH4} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS). RX PubMed=20161694; DOI=10.1021/cg900971h; RA Koclega K.D., Chruszcz M., Zimmerman M.D., Bujacz G., Minor W.; RT "'Hot' macromolecular crystals."; RL Cryst. Growth Des. 10:580-580(2009). RN [7] {ECO:0000213|PDB:4I6Z} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS). RA Koclega K.D., Chruszcz M., Cooper D.R., Petkowski J.J., Tkaczuk K.L., RA Joachimiak A., Minor W.; RT "Crystal structure of the transcriptional regulator TM1030 with 24bp RT DNA oligonucleotide."; RL Submitted (NOV-2012) to the PDB data bank. RN [8] {ECO:0000213|PDB:4I76} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS). RA Koclega K.D., Chruszcz M., Cooper D.R., Petkowski J.J., Tkaczuk K.L., RA Joachimiak A., Minor W.; RT "Crystal structure of transcriptional regulator TM1030 with octanol."; RL Submitted (NOV-2012) to the PDB data bank. CC -!- SIMILARITY: Contains 1 HTH tetR-type DNA-binding domain. CC {ECO:0000256|RuleBase:RU000710}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36107.1; -; Genomic_DNA. DR PIR; E72303; E72303. DR RefSeq; NP_228836.1; NC_000853.1. DR RefSeq; WP_010865247.1; NC_000853.1. DR PDB; 1Z77; X-ray; 2.00 A; A=1-200. DR PDB; 1ZKG; X-ray; 2.30 A; A/B=1-200. DR PDB; 2ID6; X-ray; 1.75 A; A=1-200. DR PDB; 2IEK; X-ray; 1.83 A; A=1-200. DR PDB; 3IH2; X-ray; 2.30 A; A=1-200. DR PDB; 3IH3; X-ray; 2.35 A; A=1-200. DR PDB; 3IH4; X-ray; 2.30 A; A=1-200. DR PDB; 4I6Z; X-ray; 3.20 A; A/B=1-200. DR PDB; 4I76; X-ray; 2.10 A; A/B=1-200. DR PDBsum; 1Z77; -. DR PDBsum; 1ZKG; -. DR PDBsum; 2ID6; -. DR PDBsum; 2IEK; -. DR PDBsum; 3IH2; -. DR PDBsum; 3IH3; -. DR PDBsum; 3IH4; -. DR PDBsum; 4I6Z; -. DR PDBsum; 4I76; -. DR ProteinModelPortal; Q9X0C0; -. DR SMR; Q9X0C0; 1-200. DR STRING; 243274.TM1030; -. DR EnsemblBacteria; AAD36107; AAD36107; TM_1030. DR GeneID; 897092; -. DR KEGG; tma:TM1030; -. DR KEGG; tmi:THEMA_09210; -. DR PATRIC; 23936989; VBITheMar51294_1043. DR eggNOG; ENOG4105Z3X; Bacteria. DR eggNOG; COG1309; LUCA. DR OMA; ALKFLMW; -. DR OrthoDB; EOG6ZH2G9; -. DR BioCyc; TMAR243274:GC6P-1059-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 2. DR Gene3D; 1.10.357.10; -; 1. DR InterPro; IPR023772; DNA-bd_HTH_TetR-type_CS. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001647; HTH_TetR. DR InterPro; IPR015893; Tet_transcr_reg_TetR-like_C. DR InterPro; IPR011075; Tet_transcr_reg_TetR-rel_C. DR Pfam; PF00440; TetR_N; 1. DR PRINTS; PR00455; HTHTETR. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF48498; SSF48498; 1. DR PROSITE; PS01081; HTH_TETR_1; 1. DR PROSITE; PS50977; HTH_TETR_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1Z77, ECO:0000213|PDB:1ZKG, KW ECO:0000213|PDB:2ID6, ECO:0000213|PDB:2IEK}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00483316}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00482171}; KW Transcription regulation {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00482171}. FT DOMAIN 2 62 HTH tetR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50977}. SQ SEQUENCE 200 AA; 23801 MW; CBF79565CB2D4273 CRC64; MLSKRDAILK AAVEVFGKKG YDRATTDEIA EKAGVAKGLI FHYFKNKEEL YYQAYMSVTE KLQKEFENFL MKNRNRDIFD FMERWIEKKL EYSASHPEEA DFLITLVSVD EGLRKRILLD LEKSQRVFFD FVREKLKDLD LAEDVTEEIA LKFLMWFFSG FEEVYLRTYQ GKPELLKRDM NTLVEEVKVM LRILKKGMTK // ID Q9WYZ4_THEMA Unreviewed; 254 AA. AC Q9WYZ4; G4FDU7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35609.1}; GN OrderedLocusNames=TM_0524 {ECO:0000313|EMBL:AAD35609.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35609.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35609.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35609.1; -; Genomic_DNA. DR PIR; B72366; B72366. DR RefSeq; NP_228334.1; NC_000853.1. DR RefSeq; WP_004081397.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYZ4; -. DR STRING; 243274.TM0524; -. DR EnsemblBacteria; AAD35609; AAD35609; TM_0524. DR GeneID; 897576; -. DR KEGG; tma:TM0524; -. DR KEGG; tmi:THEMA_02055; -. DR KEGG; tmw:THMA_0537; -. DR PATRIC; 23935955; VBITheMar51294_0532. DR eggNOG; ENOG4107W76; Bacteria. DR eggNOG; COG0500; LUCA. DR OMA; FHPNTAM; -. DR OrthoDB; EOG6FZ4G2; -. DR BioCyc; TMAR243274:GC6P-548-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR007536; 16SrRNA_methylTrfase_J. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF04445; SAM_MT; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 254 AA; 29611 MW; 0A238AEE58A6DFAC CRC64; MKNFVVTTSH KPDREQVMKA KELAEKLGTI YVSRRRLKEF KVDFYYVVEK NRISIKWPGG EFFFHPSSAI LRMRNIRSGQ KDYLIESLQP EGNEIVLDTT FGLGSEAILM AAFLPEGKVI GLEGSIHIYT IVKYGMENFE TDIRWLKDAL KRIELYHANF KEYIRSQPDN SFDVVYCDPM FENPVYESSA MNPLRPFAVY DTVNEEDIEE MLRIAKKKVI LKSHVKDSLF KRIRVDELKG SRKSGVLYGV IYKR // ID Q9X029_THEMA Unreviewed; 135 AA. AC Q9X029; G4FF59; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36012.1}; GN OrderedLocusNames=TM_0931 {ECO:0000313|EMBL:AAD36012.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36012.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36012.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36012.1; -; Genomic_DNA. DR PIR; C72315; C72315. DR RefSeq; NP_228739.1; NC_000853.1. DR RefSeq; WP_004080631.1; NZ_CP011107.1. DR STRING; 243274.TM0931; -. DR EnsemblBacteria; AAD36012; AAD36012; TM_0931. DR GeneID; 898605; -. DR KEGG; tma:TM0931; -. DR KEGG; tmi:THEMA_09695; -. DR KEGG; tmw:THMA_0953; -. DR PATRIC; 23936793; VBITheMar51294_0945. DR OMA; SHKTVSG; -. DR OrthoDB; EOG6Q8J45; -. DR BioCyc; TMAR243274:GC6P-961-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 135 AA; 15852 MW; 8DE9881D1576D108 CRC64; MLGIVLTAVV IFIVFILSLI EKRKKVDVET VCRTVKRYYE GRRYQISHKT VSGCEVFLIK KGLRKIIICV GSVNFDVVKE ILYMAYTNRT RDIRVAYSSI TKESLEAFER MRRNSKIHKT KVKVHDLYHF ESVVF // ID Q9X000_THEMA Unreviewed; 76 AA. AC Q9X000; G4FCS7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35979.1}; GN OrderedLocusNames=TM_0898 {ECO:0000313|EMBL:AAD35979.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35979.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35979.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35979.1; -; Genomic_DNA. DR PIR; A72318; A72318. DR RefSeq; NP_228706.1; NC_000853.1. DR RefSeq; WP_004080673.1; NZ_CP011107.1. DR STRING; 243274.TM0898; -. DR EnsemblBacteria; AAD35979; AAD35979; TM_0898. DR GeneID; 898572; -. DR KEGG; tma:TM0898; -. DR KEGG; tmi:THEMA_00145; -. DR KEGG; tmw:THMA_0920; -. DR PATRIC; 23936727; VBITheMar51294_0912. DR eggNOG; ENOG4106H6B; Bacteria. DR eggNOG; ENOG410Y6J8; LUCA. DR OMA; CITDERI; -. DR OrthoDB; EOG6N6872; -. DR BioCyc; TMAR243274:GC6P-928-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 76 AA; 9223 MW; 8DE41A23000778B5 CRC64; MKPEIREIVR AMEEDSRIKV IVTQILKMSA EEREQFKKKV MYYFMDRNSE VDTEAFKFFK TVLENVEELS KLIEQK // ID Q9X096_THEMA Unreviewed; 103 AA. AC Q9X096; G4FEZ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36083.1}; GN OrderedLocusNames=TM_1001 {ECO:0000313|EMBL:AAD36083.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36083.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36083.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36083.1; -; Genomic_DNA. DR PIR; C72307; C72307. DR RefSeq; NP_228809.1; NC_000853.1. DR RefSeq; WP_004080550.1; NC_000853.1. DR ProteinModelPortal; Q9X096; -. DR STRING; 243274.TM1001; -. DR EnsemblBacteria; AAD36083; AAD36083; TM_1001. DR GeneID; 897252; -. DR KEGG; tma:TM1001; -. DR KEGG; tmi:THEMA_09350; -. DR PATRIC; 23936931; VBITheMar51294_1014. DR eggNOG; ENOG41069W3; Bacteria. DR eggNOG; ENOG411278Q; LUCA. DR KO; K07076; -. DR OMA; RESICDI; -. DR OrthoDB; EOG6CP42N; -. DR BioCyc; TMAR243274:GC6P-1031-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 89 NTP_transf_2. {ECO:0000259|Pfam:PF01909}. SQ SEQUENCE 103 AA; 12087 MW; 794FF14F602D76A9 CRC64; MEILQILSEF KKRVSEKFGE VEVVLFGSCA RGSTREESDI DVFVILDRDV DIKVKESIYD IAYEFNLNYD IVLDVSVYSK KEWDRYRKIL PFIVNVEKEG IIV // ID Q9WZI8_THEMA Unreviewed; 751 AA. AC Q9WZI8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=(P)ppGpp synthetase {ECO:0000313|EMBL:AAD35811.1}; GN OrderedLocusNames=TM_0729 {ECO:0000313|EMBL:AAD35811.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35811.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35811.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5-' CC diphosphate) is a mediator of the stringent response that CC coordinates a variety of cellular activities in response to CC changes in nutritional abundance. {ECO:0000256|RuleBase:RU003847}. CC -!- SIMILARITY: Belongs to the relA/spoT family. CC {ECO:0000256|RuleBase:RU003847}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35811.1; -; Genomic_DNA. DR PIR; D72338; D72338. DR RefSeq; NP_228538.1; NC_000853.1. DR RefSeq; WP_010865193.1; NC_000853.1. DR ProteinModelPortal; Q9WZI8; -. DR STRING; 243274.TM0729; -. DR EnsemblBacteria; AAD35811; AAD35811; TM_0729. DR GeneID; 898396; -. DR KEGG; tma:TM0729; -. DR PATRIC; 23936378; VBITheMar51294_0742. DR eggNOG; ENOG4105CWR; Bacteria. DR eggNOG; COG0317; LUCA. DR InParanoid; Q9WZI8; -. DR KO; K00951; -. DR OMA; TREIYAP; -. DR OrthoDB; EOG6SV551; -. DR BioCyc; TMAR243274:GC6P-755-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005618; C:cell wall; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008728; F:GTP diphosphokinase activity; IBA:GO_Central. DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IBA:GO_Central. DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IBA:GO_Central. DR GO; GO:0042594; P:response to starvation; IBA:GO_Central. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR004811; RelA/Spo_fam. DR InterPro; IPR007685; RelA_SpoT. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR Pfam; PF13291; ACT_4; 1. DR Pfam; PF13328; HD_4; 1. DR Pfam; PF04607; RelA_SpoT; 1. DR Pfam; PF02824; TGS; 1. DR SMART; SM00471; HDc; 1. DR SMART; SM00954; RelA_SpoT; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR TIGRFAMs; TIGR00691; spoT_relA; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 89 206 HDc. {ECO:0000259|SMART:SM00471}. FT DOMAIN 289 399 RelA_SpoT. {ECO:0000259|SMART:SM00954}. SQ SEQUENCE 751 AA; 86975 MW; E58B868E28BF404C CRC64; MCGNAHPRLM TAHDRIRLML LSRVIIFSTE GEFGGEIVIN RTEIETEAKV VIRELESLKK KSFTREEKKL LIKAYEFARI VHEGQKRFSG EPFITHPVEV TKILAGLGVD VTTLVAALLH DVVEDGENVS LDQIKKEFGP EVARIVDGVT KVSNINAPIG RDQDSRKKIE TIQKMFFAMA EDMRVIFVKL ADRLHNMRTI HYVQDPEKKR YKAYETLEIY APLAHKLGIY SIKSELEDLA FKVLYPEEYY KIKELVAEKR KEREKRTNEY ISLLKSALEE HKIKAIVEGR YKHYYSIWRK MKEKGKKFEE IYDLIALRVI VKDVTTCYTV LGIVHNIWKP LPGRFKDYIA APKSNGYRSL HTTVITGYGE PLEIQIRDEE MHREAEYGLI AHWIYKERPD VKTAKEWIER LLDWRKELAQ GFTEFEDIKK ELQMDEVFVF TPKGDILHLP KGSTPIDFAY AIHTEIGHHY SGAKVNGKIV PIDYQLKNGD VVEIIVNKNS PGPSVDWLKY AKTHSARAKI RRFLKEKLAP ELVERGKEVL RKICRKLGKS FEEVMQTEGI KRYLNTYQEK DFFMRIGEGS ITTQDLIEAI LGKKIVVKKR STKKKTRIQN LVKVDGIDSI EFHIAKCCHP IMGDPIVAVV SRRGMTIHRR DCRNLKNMSQ DRIFPAEWNL ETSEMFDAHI RVVLNSEKNL PSLIDRITNL GAEFVAMKTL KSEEPLVVQI HIKISNTVEL TGLLDRLRSY RYVLDAERVV Q // ID Q9X2E4_THEMA Unreviewed; 271 AA. AC Q9X2E4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36887.1}; GN OrderedLocusNames=TM_1824 {ECO:0000313|EMBL:AAD36887.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36887.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36887.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36887.1; -; Genomic_DNA. DR PIR; C72207; C72207. DR RefSeq; NP_229621.1; NC_000853.1. DR RefSeq; WP_010865411.1; NC_000853.1. DR ProteinModelPortal; Q9X2E4; -. DR STRING; 243274.TM1824; -. DR EnsemblBacteria; AAD36887; AAD36887; TM_1824. DR GeneID; 897515; -. DR KEGG; tma:TM1824; -. DR KEGG; tmi:THEMA_05075; -. DR PATRIC; 23938635; VBITheMar51294_1844. DR eggNOG; ENOG4106R4T; Bacteria. DR eggNOG; ENOG410YI9U; LUCA. DR OMA; VHNAGRH; -. DR OrthoDB; EOG6FRCTN; -. DR BioCyc; TMAR243274:GC6P-1875-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR002495; Glyco_trans_8. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF01501; Glyco_transf_8; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 271 AA; 31419 MW; 56AC2A0B60A550E2 CRC64; MFLNLIATAG NDRIRDFLVN DWYRSLKENV DLSKTDVLVI NYGLTGLPKE VINFPAVERS GLINNTRFIN LAIFLENHPE YDQILFCDGG DIIFQSDISH LFEEHRDAFR AVVEQLSPPI DLVVKEEDLV NGKEIKSFLS NKKLFNVGVI IAPREGFLEL ARTMERRLKN INVWGGDTVI GNYVIYKNPH VELPSKYNFI PSTAREKFYV KDSKFYLENG ELIPIVHNAG RYRFLRPVKD FGYGPGKNRV NKFNIWMFRM LFSVSNFLKM K // ID Q9WYE5_THEMA Unreviewed; 660 AA. AC Q9WYE5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein {ECO:0000313|EMBL:AAD35397.1}; GN OrderedLocusNames=TM_0309 {ECO:0000313|EMBL:AAD35397.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35397.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35397.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35397.1; -; Genomic_DNA. DR PIR; D72391; D72391. DR RefSeq; NP_228121.1; NC_000853.1. DR RefSeq; WP_010865091.1; NC_000853.1. DR ProteinModelPortal; Q9WYE5; -. DR STRING; 243274.TM0309; -. DR DNASU; 897245; -. DR EnsemblBacteria; AAD35397; AAD35397; TM_0309. DR GeneID; 897245; -. DR KEGG; tma:TM0309; -. DR KEGG; tmi:THEMA_03180; -. DR PATRIC; 23935497; VBITheMar51294_0314. DR eggNOG; ENOG4105EN8; Bacteria. DR eggNOG; ENOG410XRAT; LUCA. DR KO; K02035; -. DR OMA; WDILENG; -. DR OrthoDB; EOG6PP9H6; -. DR BioCyc; TMAR243274:GC6P-322-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GOC. DR InterPro; IPR023765; SBP_5_CS. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PROSITE; PS01040; SBP_BACTERIAL_5; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 114 514 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. SQ SEQUENCE 660 AA; 76532 MW; B5816BAB133C0E94 CRC64; MFMRKVFVFL LVSLFIVIGL SWSVYATPED YYKATGKRIE KFNEAPMLAE LVKQGKLPPV EQRLPKEPLV VVPEESVGQY GGTWRRVWKG PSDRWGIPRI NQASLVFWDK NGEKFVPGVA KSWDILENGK VYVFYLREGM KWSDGHPYTS EDILFWVDDI LGNDELTPAK PAWYRLLDRV EAPDPYTVKF VFKQPYALFL LQVANRGFTG SPKHFLKQFH PNYTPMEEIE KKMVEGVHNT WVDLFNDKSD FLESLDLPVL TPWKPVTDPT EQFYILERNP YFWAVDIEGN QLPYIDRIRH EYVQSSEVIM LKAISGEIDM QWRHIGLLGP GPGVLPLLLE NAKSGGYRVL RWKTDNGSVS MVMLNISDPP DPVLGEVFRD VRFRQALSLA INREEINEIL FNGLAEPRQA SFVSGSPYYD PEWEKAYAEY DPDRANKLLD EMGLKWDSRH EYRLLPDGRP LRFTIQVTGQ THVDVWTMVK EYWKQIGVRV EIENLERSLY DSRLSAHDFD AQAWVMDRAS QPLVDPLWII PGSTEYASAW YIGWADWAGS YLEGEESLKE YLQQEDAIVP PEGIKETLEK LLDVWKEIQN TSDPEKIKEL MKEVTKIHRE NLWMIGTVGE DISPAIVKNN FKNVPEELVT ATPFFSPWNA MPIQFYIEQK // ID Q9X0A0_THEMA Unreviewed; 299 AA. AC Q9X0A0; G4FEZ1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 107. DE SubName: Full=Transcriptional regulator, putative {ECO:0000313|EMBL:AAD36087.1}; GN OrderedLocusNames=TM_1005 {ECO:0000313|EMBL:AAD36087.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36087.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36087.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains HTH araC/xylS-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00503533}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36087.1; -; Genomic_DNA. DR PIR; G72307; G72307. DR RefSeq; NP_228813.1; NC_000853.1. DR RefSeq; WP_004080540.1; NC_000853.1. DR ProteinModelPortal; Q9X0A0; -. DR STRING; 243274.TM1005; -. DR DNASU; 896843; -. DR EnsemblBacteria; AAD36087; AAD36087; TM_1005. DR GeneID; 896843; -. DR KEGG; tma:TM1005; -. DR KEGG; tmi:THEMA_09325; -. DR PATRIC; 23936941; VBITheMar51294_1019. DR eggNOG; ENOG4105CF7; Bacteria. DR eggNOG; ENOG410XRKV; LUCA. DR OMA; HHFRSMT; -. DR OrthoDB; EOG625JZ9; -. DR BioCyc; TMAR243274:GC6P-1035-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 2. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR018060; HTH_AraC. DR InterPro; IPR018062; HTH_AraC-typ_CS. DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type. DR InterPro; IPR009594; Tscrpt_reg_HTH_AraC_N. DR Pfam; PF06719; AraC_N; 1. DR Pfam; PF12833; HTH_18; 1. DR PRINTS; PR00032; HTHARAC. DR SMART; SM00342; HTH_ARAC; 1. DR SUPFAM; SSF46689; SSF46689; 2. DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1. DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW DNA-binding {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503812}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transcription {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503758}; KW Transcription regulation {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503758}. FT DOMAIN 191 288 HTH araC/xylS-type DNA-binding. FT {ECO:0000259|PROSITE:PS01124}. SQ SEQUENCE 299 AA; 34360 MW; 25451262F0776020 CRC64; MDEFDYVRRK LIERILHLTE KQPVVRPLPG LTVGRRESPT EPSTYILPPS ICIAVQGAKR VLIGEEYYVY DVENFLLNSF DVPVVAQVIE ASKEKPYIGM TWEIDMEILM EIVVEQKLNT RPITSSRGTS LGKVTHQLLD AFRRMLELLD EPEHISALLP VIKKEIIYRL LVSEQGPRLI QIALSGKNDV ITALNYLKEH FNESVNMKRL AEMVGMSVST FYQNFKILTG MTPLQYQKKL RLCEARKLLM AGSDVTTAAY QVGYESLSQF SREYKRFFGV SPSQDAKKLK EEPYTRILY // ID Q9WZA5_THEMA Unreviewed; 41 AA. AC Q9WZA5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35721.1}; GN OrderedLocusNames=TM_0637 {ECO:0000313|EMBL:AAD35721.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35721.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35721.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35721.1; -; Genomic_DNA. DR PIR; D72350; D72350. DR RefSeq; NP_228446.1; NC_000853.1. DR RefSeq; WP_010865171.1; NC_000853.1. DR STRING; 243274.TM0637; -. DR EnsemblBacteria; AAD35721; AAD35721; TM_0637. DR GeneID; 897734; -. DR KEGG; tma:TM0637; -. DR PATRIC; 23936187; VBITheMar51294_0647. DR OrthoDB; EOG61GGG8; -. DR BioCyc; TMAR243274:GC6P-662-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR012454; DUF1659. DR Pfam; PF07872; DUF1659; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 41 AA; 4652 MW; E0EB5CA597EDF3BC CRC64; MEKALRIVWA TGEVDENGNP VTRRQTISVS PNATDRILRT R // ID Q9WYM2_THEMA Unreviewed; 31 AA. AC Q9WYM2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35476.1}; GN OrderedLocusNames=TM_0391 {ECO:0000313|EMBL:AAD35476.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35476.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35476.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35476.1; -; Genomic_DNA. DR PIR; H72381; H72381. DR RefSeq; NP_228201.1; NC_000853.1. DR RefSeq; WP_010865111.1; NC_000853.1. DR EnsemblBacteria; AAD35476; AAD35476; TM_0391. DR GeneID; 897373; -. DR KEGG; tma:TM0391; -. DR BioCyc; TMAR243274:GC6P-405-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 31 AA; 3798 MW; F1D57EBE3838D551 CRC64; MRKMGKENRF HTSKELLKPV EFKRNYTTNT L // ID Q9X1D9_THEMA Unreviewed; 230 AA. AC Q9X1D9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=RnfB-related protein {ECO:0000313|EMBL:AAD36492.1}; GN OrderedLocusNames=TM_1422 {ECO:0000313|EMBL:AAD36492.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36492.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36492.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains 4Fe-4S domain. CC {ECO:0000256|SAAS:SAAS00508687}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36492.1; -; Genomic_DNA. DR PIR; C72256; C72256. DR RefSeq; NP_229222.1; NC_000853.1. DR RefSeq; WP_010865338.1; NC_000853.1. DR STRING; 243274.TM1422; -. DR EnsemblBacteria; AAD36492; AAD36492; TM_1422. DR GeneID; 898053; -. DR KEGG; tma:TM1422; -. DR PATRIC; 23937792; VBITheMar51294_1434. DR eggNOG; COG2000; LUCA. DR KO; K06939; -. DR OrthoDB; EOG6GJBZM; -. DR BioCyc; TMAR243274:GC6P-1460-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR InterPro; IPR007202; 4Fe-4S_dom. DR Pfam; PF04060; FeS; 1. DR PROSITE; PS51656; 4FE4S; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 35 97 4Fe-4S. {ECO:0000259|PROSITE:PS51656}. SQ SEQUENCE 230 AA; 26375 MW; 67E4BC457302AAE9 CRC64; MAEETPKRTE VNHLKIDTFR SYRNKSRNVE VPEEEIKKVL VSIGKDDPSK ELNCGACGYD SCREKARAVV LGKAEKEMCF VYLLDLVKSS SYRVVEESPN AVFVLKDEKV IYRNRVAGEL IQNYPEILER AKGSVGETLT IEGKRFFFVK EFSLEDGEEV IMLVDITQEK LKDEELDKVK RETLRKVEEM LNKQMRIAQE IAGILGESIA ETKSSFMELK MFMEGENADL // ID Q9WZH0_THEMA Unreviewed; 407 AA. AC Q9WZH0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35793.1}; GN OrderedLocusNames=TM_0711 {ECO:0000313|EMBL:AAD35793.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35793.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35793.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35793.1; -; Genomic_DNA. DR PIR; F72343; F72343. DR RefSeq; NP_228520.1; NC_000853.1. DR RefSeq; WP_010865190.1; NC_000853.1. DR ProteinModelPortal; Q9WZH0; -. DR STRING; 243274.TM0711; -. DR EnsemblBacteria; AAD35793; AAD35793; TM_0711. DR GeneID; 898378; -. DR KEGG; tma:TM0711; -. DR KEGG; tmi:THEMA_01110; -. DR PATRIC; 23936340; VBITheMar51294_0723. DR eggNOG; ENOG4106439; Bacteria. DR eggNOG; ENOG4112APM; LUCA. DR OMA; QDKADTC; -. DR OrthoDB; EOG6SJJMS; -. DR BioCyc; TMAR243274:GC6P-737-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR001119; SLH_dom. DR Pfam; PF00395; SLH; 1. DR PROSITE; PS51272; SLH; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 384 405 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 20 83 SLH (S-layer homology). FT {ECO:0000259|PROSITE:PS51272}. FT COILED 126 153 {ECO:0000256|SAM:Coils}. FT COILED 172 220 {ECO:0000256|SAM:Coils}. FT COILED 242 269 {ECO:0000256|SAM:Coils}. FT COILED 302 378 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 407 AA; 45615 MW; F92774DDF139B69D CRC64; MKSLRKILVL GLVVISILLL SQNIKDLEPD SPFFEAVNYV VKAGIMELDD KGNFRGALLV TRYDVAQYIY RLVMRFELEK LKEKLPLLDE LDIVKAATIA LDERTSNLEK NYNSLNSRVD SAVLEITSAA SEVSELKTKI DSLEEAFNNL SLAFTSFKQE TAGIDSEILR RIDVVEKNLK KLEESSKQNT SRLTLLEKNL ENVSKEMTSL KEAVTQISSD TRSLLTWKQD AGEDILMLKG RTGSLSEELN QLRKELDSLS SDVVNLKNEM NQKVSVVSSR VSAQEEKVSD LEKSILQITA KFQMLESSVE NLKSDLENLN KRFSGLEESV AEDQQNRTTM ESEIQDLKKQ VSDLSKKIER LSSDLTALSQ RVEEKEKSSL QMDISTLMVI GAGALALLLG IILLAGR // ID Q9X0P4_THEMA Unreviewed; 446 AA. AC Q9X0P4; G4FEI5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 95. DE RecName: Full=Magnesium transporter MgtE {ECO:0000256|RuleBase:RU362011}; GN OrderedLocusNames=TM_1161 {ECO:0000313|EMBL:AAD36237.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36237.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36237.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Acts as a magnesium transporter. CC {ECO:0000256|RuleBase:RU362011}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362011}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU362011}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU362011}. CC -!- SIMILARITY: Belongs to the SLC41A transporter family. CC {ECO:0000256|RuleBase:RU362011}. CC -!- SIMILARITY: Contains 2 CBS domains. CC {ECO:0000256|RuleBase:RU362011}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|RuleBase:RU362011}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36237.1; -; Genomic_DNA. DR PIR; G72287; G72287. DR RefSeq; NP_228967.1; NC_000853.1. DR RefSeq; WP_004080209.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X0P4; -. DR STRING; 243274.TM1161; -. DR EnsemblBacteria; AAD36237; AAD36237; TM_1161. DR GeneID; 898325; -. DR KEGG; tma:TM1161; -. DR KEGG; tmi:THEMA_08530; -. DR KEGG; tmw:THMA_1186; -. DR PATRIC; 23937259; VBITheMar51294_1178. DR eggNOG; ENOG4105CJW; Bacteria. DR eggNOG; COG2239; LUCA. DR KO; K06213; -. DR OMA; RAIQRYD; -. DR OrthoDB; EOG60GRRN; -. DR BioCyc; TMAR243274:GC6P-1190-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015693; P:magnesium ion transport; IEA:InterPro. DR Gene3D; 1.10.357.20; -; 1. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR006668; Mg_transptr_MgtE_intracell_dom. DR InterPro; IPR006669; MgtE_transporter. DR InterPro; IPR006667; SLC41_membr_dom. DR Pfam; PF00571; CBS; 2. DR Pfam; PF01769; MgtE; 1. DR Pfam; PF03448; MgtE_N; 1. DR SMART; SM00116; CBS; 2. DR SMART; SM00924; MgtE_N; 1. DR TIGRFAMs; TIGR00400; mgtE; 1. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU362011}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Magnesium {ECO:0000256|RuleBase:RU362011}; KW Membrane {ECO:0000256|RuleBase:RU362011}; KW Metal-binding {ECO:0000256|RuleBase:RU362011}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU362011}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362011}; KW Transport {ECO:0000256|RuleBase:RU362011}. FT TRANSMEM 309 336 Helical. {ECO:0000256|RuleBase:RU362011}. FT TRANSMEM 357 378 Helical. {ECO:0000256|RuleBase:RU362011}. FT TRANSMEM 384 406 Helical. {ECO:0000256|RuleBase:RU362011}. FT TRANSMEM 418 440 Helical. {ECO:0000256|RuleBase:RU362011}. FT DOMAIN 135 197 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 199 255 CBS. {ECO:0000259|PROSITE:PS51371}. SQ SEQUENCE 446 AA; 50662 MW; 6A2986EE021A1D46 CRC64; MKIKVEIDLQ ELIEKGDFKT LKRVLEQQDP ADVKEMIEKL PPDLKVVVFR LLPKDKAAEV FSELEPDDQL ELIKLFREER LKEIFESMDP DDRVELLEEM PANVVKKLLS YLPPQEREEL LYILNYPEDS AARLATTEYV ELFEDMTVRE ALEKVRKEGK KKENIYSLMV IDRTRKLKGT VELRDLIVAD PDQKVSEIMN KDPVFVHAID DQELAAELMK KYDLIILPVV DSEERLIGVI TFDDLVDVIE EEATEDIQKM ASMSATYTSY FHTPAWKLIL KRSPWLVVLL LLESVNGNII SSYEKFLASI PIIAAFIPTM IGSAGNTGAQ ISALMIRGFT LNEISLKDWW KVLLRESLIG STLGLILAGV LYLRAFLISS DPTLNFAVAT ALLVLILYAN IMGALLPFIA RIFKIDPAFM AGPLLTTIVD VTGIMIYFYV VHSFLS // ID Q9WY36_THEMA Unreviewed; 263 AA. AC Q9WY36; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35285.1}; GN OrderedLocusNames=TM_0193 {ECO:0000313|EMBL:AAD35285.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35285.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35285.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35285.1; -; Genomic_DNA. DR PIR; A72407; A72407. DR RefSeq; NP_228008.1; NC_000853.1. DR RefSeq; WP_010865070.1; NC_000853.1. DR STRING; 243274.TM0193; -. DR EnsemblBacteria; AAD35285; AAD35285; TM_0193. DR GeneID; 897052; -. DR KEGG; tma:TM0193; -. DR PATRIC; 23935254; VBITheMar51294_0195. DR eggNOG; ENOG4105C4B; Bacteria. DR eggNOG; COG0390; LUCA. DR InParanoid; Q9WY36; -. DR KO; K02069; -. DR OMA; QYQIAIM; -. DR OrthoDB; EOG64BQ6B; -. DR BioCyc; TMAR243274:GC6P-204-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015075; F:ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central. DR GO; GO:0034220; P:ion transmembrane transport; IBA:GOC. DR InterPro; IPR005226; UPF0014_fam. DR PANTHER; PTHR30028:SF0; PTHR30028:SF0; 1. DR Pfam; PF03649; UPF0014; 1. DR TIGRFAMs; TIGR00245; TIGR00245; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 152 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 191 209 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 229 251 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 263 AA; 29176 MW; 9F4BCF45401AF218 CRC64; MMGPVDIGLI QLLSAYIFVV VLMLILRIRR IPREKEVLVA SIRMTFQLVM AGFVLSYILD HPSPLYTILA VLVMEIFAIY NVYKRARLSL PARVKKRLEL FIAISVSTGT LLSLVYFLYV VVRISPWFDP RYVIPLAGMI IGNSMTGVSL GVKTLSESIT IQKDIVEAAL MLGARPKDAV RMFSDRAFDS AILPTLNSMI GMGIVFLPGM MTGQILSGAS PITAIKYQIA IMLGILGEVT ISVSVFLYLG YKAFFNRENQ LIV // ID Q9WXS1_THEMA Unreviewed; 205 AA. AC Q9WXS1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase {ECO:0000313|EMBL:AAD35160.1}; GN OrderedLocusNames=TM_0066 {ECO:0000313|EMBL:AAD35160.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35160.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35160.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1VLW} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), AND DISULFIDE BONDS. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of 2-dehydro-3-deoxyphosphogluconate aldolase/4- RT hydroxy-2-oxoglutarate aldolase (TM0066) from Thermotoga maritima at RT 2.30 A resolution."; RL Submitted (AUG-2004) to the PDB data bank. RN [3] {ECO:0000213|PDB:1WA3} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH PYRUVATE, AND RP DISULFIDE BONDS. RX PubMed=16403639; DOI=10.1016/j.bmc.2005.12.022; RA Fullerton S.W., Griffiths J.S., Merkel A.B., Cheriyan M., Wymer N.J., RA Hutchins M.J., Fierke C.A., Toone E.J., Naismith J.H.; RT "Mechanism of the Class I KDPG aldolase."; RL Bioorg. Med. Chem. 14:3002-3010(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35160.1; -; Genomic_DNA. DR PIR; F72422; F72422. DR RefSeq; NP_227882.1; NC_000853.1. DR RefSeq; WP_010865041.1; NC_000853.1. DR PDB; 1VLW; X-ray; 2.30 A; A/B/C=1-205. DR PDB; 1WA3; X-ray; 1.90 A; A/B/C/D/E/F=1-205. DR PDBsum; 1VLW; -. DR PDBsum; 1WA3; -. DR ProteinModelPortal; Q9WXS1; -. DR SMR; Q9WXS1; 1-204. DR STRING; 243274.TM0066; -. DR EnsemblBacteria; AAD35160; AAD35160; TM_0066. DR GeneID; 896890; -. DR KEGG; tma:TM0066; -. DR KEGG; tmi:THEMA_04475; -. DR PATRIC; 23934972; VBITheMar51294_0064. DR eggNOG; ENOG4108UHU; Bacteria. DR eggNOG; COG0800; LUCA. DR KO; K01625; -. DR OMA; GQVIVMP; -. DR OrthoDB; EOG6K9QNZ; -. DR BioCyc; MetaCyc:MONOMER-4906; -. DR BioCyc; TMAR243274:GC6P-66-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR000887; Aldlse_KDPG_KHG. DR InterPro; IPR013785; Aldolase_TIM. DR Pfam; PF01081; Aldolase; 1. DR TIGRFAMs; TIGR01182; eda; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VLW, ECO:0000213|PDB:1WA3}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Pyruvate {ECO:0000213|PDB:1WA3}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT BINDING 129 129 Pyruvate (covalent). FT {ECO:0000213|PDB:1WA3}. FT DISULFID 165 203 {ECO:0000213|PDB:1VLW, FT ECO:0000213|PDB:1WA3}. SQ SEQUENCE 205 AA; 22236 MW; 1ACBCF04B6B3EFA0 CRC64; MKMEELFKKH KIVAVLRANS VEEAKEKALA VFEGGVHLIE ITFTVPDADT VIKELSFLKE KGAIIGAGTV TSVEQCRKAV ESGAEFIVSP HLDEEISQFC KEKGVFYMPG VMTPTELVKA MKLGHTILKL FPGEVVGPQF VKAMKGPFPN VKFVPTGGVN LDNVCEWFKA GVLAVGVGSA LVKGTPDEVR EKAKAFVEKI RGCTE // ID Q9X257_THEMA Unreviewed; 1074 AA. AC Q9X257; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36800.1}; GN OrderedLocusNames=TM_1735 {ECO:0000313|EMBL:AAD36800.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36800.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36800.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36800.1; -; Genomic_DNA. DR PIR; F72217; F72217. DR RefSeq; NP_229533.1; NC_000853.1. DR RefSeq; WP_010865391.1; NC_000853.1. DR STRING; 243274.TM1735; -. DR EnsemblBacteria; AAD36800; AAD36800; TM_1735. DR GeneID; 897871; -. DR KEGG; tma:TM1735; -. DR PATRIC; 23938446; VBITheMar51294_1753. DR eggNOG; ENOG4107SKD; Bacteria. DR eggNOG; COG0795; LUCA. DR OMA; NDWYLFD; -. DR OrthoDB; EOG60KN1F; -. DR BioCyc; TMAR243274:GC6P-1783-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005495; LptG/LptF_permease. DR Pfam; PF03739; YjgP_YjgQ; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 46 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 91 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 112 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 287 307 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 314 333 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 353 374 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 381 400 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 1074 AA; 123510 MW; 5E80FCFFC79CE870 CRC64; MNSFSSKNPE GCSLKVLIKY LLKLSVVPFL IGLGGFIVFV SLEILYQLSD LIVRHRVGIE KLFLMLYYYL PYFVAMGVPV GVLLAIFWTF SRLSEERELM AIQVHGISQK NLIVPFLILG ALLSIAVFFL SDQIVPEYQS KAEEAMSKYV LKKPEVFVVE NVISKIGDDQ YFYVEKYDER TSTMWNVVIF RYGHEETIVT AKRVQKKGND WYLFDGNYYT VDKDGFLKLD VHFSEMKLDI TEDIEKLLRV GKTPKEMTGK ELKEKIEFFK KVGVKPSPWV VELHSRYANS LTPIVIVLVG VPLSLLFQLR SKSWGVIFTF VLVVLYQGSG AWLSAMGKEN LLNPVLAPWI PNIVFTIVGT LLFILLDTFF AYRITEFLSR LFFVAFIFTV SSLFSSQVVI VSDRMEKFPE EMVFHGSVEI AYKDMTVQAS EATIQLTEEG KAKKLEASGG VIYRKADTIL MGEHLIFYLE NEKSVLTHIR GSTVLEIEKE KKKIYLSGED LTSEGSRTIV DMGSISTCSE TPPHYKLKAR YIEIKENDYL LAKDVVFYLL EIPLFYQPIF FTSLSDKPQP FSVEVGVGNN PHLKTSYNVS YPSGLLYFST KSVLSGGLSK ELNWNHKMGS WSLNLDYKES TSHSVLVKIF DSKNTFLFSQ KNEERIHQFE RKEKILNGSL NVVLRKESDG EDSYILPRVT VKKVSVKTGV GTFSVDSFNH ETRIEDQEKR NSGSVSLSFR SVPFLLFQSV SVSTTGKYLF ENQNLDERTS YLKTDSIWDF QNLSLGKFLV LDDKIYAGVY RSNEDGYRVG NLFTTTLRVP LGPFSFESYY KLFTVSGENL RKFSQNESKN EVDLKVSFSY ENFKSSLETT YDFLEKEFSD PYLKTSYSFK TGDITHTVDS TTRFVLDEIS RSYTTWNFQQ RMGAFLNRFY FTYYYREPHV KYVEDQMRIY GKNFLFMENP RITTYTKLSV DPFELDEFWI RGTFKKGEST HSLKMSYSSD NLEFSYQTKN GDPALEISFS LKDWNVEKFS LSVEKALHCL GTKISTSFGR NFTLESFSIL FFIRDFPNSG IGFDTEEGIG LNVF // ID Q9X2A0_THEMA Unreviewed; 144 AA. AC Q9X2A0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36842.1}; GN OrderedLocusNames=TM_1779 {ECO:0000313|EMBL:AAD36842.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36842.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36842.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36842.1; -; Genomic_DNA. DR PIR; B72214; B72214. DR RefSeq; NP_229576.1; NC_000853.1. DR RefSeq; WP_010865401.1; NC_000853.1. DR STRING; 243274.TM1779; -. DR EnsemblBacteria; AAD36842; AAD36842; TM_1779. DR GeneID; 896986; -. DR KEGG; tma:TM1779; -. DR BioCyc; TMAR243274:GC6P-1828-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 144 AA; 16586 MW; C00F283CA685A15A CRC64; MKNRDLKSPG LSLAERVGFE PTGGFWPPHA LQACALDPSA TSPLHTRKIL YTQSFPCSSF HFSSFFFILK YFHTPTAKTK SAKMERIFVI IDFSPHIYYF TISRKGLSIL TEIVFSVIDI HKHENNMWIS SFTKLKITVK KHFI // ID Q9X0E4_THEMA Unreviewed; 236 AA. AC Q9X0E4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 112. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36131.1}; GN OrderedLocusNames=TM_1054 {ECO:0000313|EMBL:AAD36131.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36131.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36131.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36131.1; -; Genomic_DNA. DR PIR; H72301; H72301. DR RefSeq; NP_228860.1; NC_000853.1. DR RefSeq; WP_008193421.1; NC_000853.1. DR ProteinModelPortal; Q9X0E4; -. DR STRING; 243274.TM1054; -. DR EnsemblBacteria; AAD36131; AAD36131; TM_1054. DR GeneID; 897279; -. DR KEGG; tma:TM1054; -. DR KEGG; tmi:THEMA_09090; -. DR PATRIC; 23937037; VBITheMar51294_1067. DR eggNOG; ENOG4108IUZ; Bacteria. DR eggNOG; COG1137; LUCA. DR KO; K06861; -. DR OMA; MTLELKQ; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; TMAR243274:GC6P-1083-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR032823; BCA_ABC_TP_C. DR InterPro; IPR030921; LPS_export_LptB. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF12399; BCA_ABC_TP_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR04406; LPS_export_lptB; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD36131.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD36131.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 236 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 236 AA; 27139 MW; 861A4B75E8F2A7CA CRC64; MDVLRCENLK KRFGRRYVVN GVNLEFHRGE IVGLLGPNGA GKTTIFNMIL GVVVPTSGKI IFRDVDITKF PVYRRARLGI TYLQQETSIF GGLTVRENID LVLRFHEKDK EKRERKIEEL LHEFHLKHLE NQPASFLSGG EKRKLELARM MCLNPAFILL DEPFSGIDPK TVKEIQKMTL ELKQKNFGIV ITDHNVDELV EIADRIYVIY KGEILAEGSP ERILEDETVR EVYLGT // ID Q9X160_THEMA Unreviewed; 44 AA. AC Q9X160; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36410.1}; GN OrderedLocusNames=TM_1338 {ECO:0000313|EMBL:AAD36410.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36410.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36410.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36410.1; -; Genomic_DNA. DR PIR; B72266; B72266. DR RefSeq; NP_229140.1; NC_000853.1. DR RefSeq; WP_010865318.1; NZ_CP011107.1. DR EnsemblBacteria; AAD36410; AAD36410; TM_1338. DR GeneID; 898144; -. DR KEGG; tma:TM1338; -. DR KEGG; tmi:THEMA_07655; -. DR KEGG; tmw:THMA_1362; -. DR OrthoDB; EOG6M0TG7; -. DR BioCyc; TMAR243274:GC6P-1369-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 44 AA; 5165 MW; 12D480D827F9EEAD CRC64; MVVLYHKAPD MQNLLTSNLK AKNSLKASFP FCLNKKIIFH QYRI // ID Q9WZ17_THEMA Unreviewed; 739 AA. AC Q9WZ17; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Aspartokinase II {ECO:0000313|EMBL:AAD35632.1}; GN OrderedLocusNames=TM_0547 {ECO:0000313|EMBL:AAD35632.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35632.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35632.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35632.1; -; Genomic_DNA. DR PIR; H72364; H72364. DR RefSeq; NP_228357.1; NC_000853.1. DR RefSeq; WP_010865144.1; NC_000853.1. DR ProteinModelPortal; Q9WZ17; -. DR STRING; 243274.TM0547; -. DR DNASU; 897601; -. DR EnsemblBacteria; AAD35632; AAD35632; TM_0547. DR GeneID; 897601; -. DR KEGG; tma:TM0547; -. DR PATRIC; 23936001; VBITheMar51294_0555. DR eggNOG; ENOG4105CFH; Bacteria. DR eggNOG; COG0460; LUCA. DR eggNOG; COG0527; LUCA. DR InParanoid; Q9WZ17; -. DR KO; K12524; -. DR OMA; KTIDENP; -. DR OrthoDB; EOG6NSGHC; -. DR BioCyc; TMAR243274:GC6P-571-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004072; F:aspartate kinase activity; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro. DR Gene3D; 3.40.1160.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd. DR InterPro; IPR005260; Asp_kin_monofn. DR InterPro; IPR001341; Asp_kinase_dom. DR InterPro; IPR027795; GATS-like_ACT_dom. DR InterPro; IPR001342; HDH_cat. DR InterPro; IPR019811; HDH_CS. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF13840; ACT_7; 1. DR Pfam; PF00742; Homoserine_dh; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR00656; asp_kin_monofn; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS01042; HOMOSER_DHGENASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000313|EMBL:AAD35632.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35632.1}. FT DOMAIN 600 681 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 739 AA; 81435 MW; E33C5D940976F949 CRC64; MRTYRSFKMF TNSSQGVRKV RVGIAGLGTV GGSIYRILKE RGNEIEKRIG EKFIISKVIN RSPQKYELLG VPKEEIAFDF DDLILNSDVV VEAIGGTDVA VDLVRRALEL GRIVVTPNKN LISEYGNEFS EYIKKRKLFF EASVGGGIPI ISLLQDYLIF QKVTRIRGIM NGTTNYILTE MSKGRHFEEV LKEAQELGYA EADPTNDIEG YDVAYKVSVL AGVVTGRFPG INSVQFEGIT RIDPEYLKEI VRSGKKLKLI GELDFSTNRY EVRLREVTPE DPFFNVDGVD NAIEVSTDLA GDFLLKGRGA GGYPTASAVI ADLFRVAKYK VLGGAEKFSV VVMKFGGAAI SDVEKLEKVA EKIIKRKKSG VKPVVVLSAM GDTTDHLIEL AKTIDENPDP RELDLLLSTG EIQSVALMSI ALRKRGYKAI SFTGNQLKII TDKRYGSARI IDINTDIISR YLKQDFIPVV AGFQGITETG DITTLGRGGS DLTAIALAYS LGADLCELYK DVDGVYTADP RIVKDARVIK ELSWEEMIEL SRHGAQVLQA RAAEFARKYG VKVLIKNAHK ETRGTLIWEG TKVENPIVRA VTFEDGMAKV VLKDVPDKPG VAARIMRTLS QMGVNIDMII QGMKSGEYNT VAFIVPESQL GKLDIDLLKT RSEAKEIIIE KGLAKVSIVG VNLTSTPEIS ATLFETLANE GINIDMISAS SSRISVIIDG KYVEDAVKAI HSRFELDRE // ID Q9WZN5_THEMA Unreviewed; 200 AA. AC Q9WZN5; G4FD45; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35860.1}; GN OrderedLocusNames=TM_0778 {ECO:0000313|EMBL:AAD35860.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35860.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35860.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35860.1; -; Genomic_DNA. DR PIR; C72332; C72332. DR RefSeq; NP_228587.1; NC_000853.1. DR RefSeq; WP_004080910.1; NZ_CP011107.1. DR STRING; 243274.TM0778; -. DR EnsemblBacteria; AAD35860; AAD35860; TM_0778. DR GeneID; 898446; -. DR KEGG; tma:TM0778; -. DR KEGG; tmw:THMA_0797; -. DR PATRIC; 23936478; VBITheMar51294_0791. DR InParanoid; Q9WZN5; -. DR OMA; INMKILF; -. DR OrthoDB; EOG6384JF; -. DR BioCyc; TMAR243274:GC6P-805-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 200 AA; 22166 MW; EB13030D26030090 CRC64; MINMKILFLL FLVTASLLLM MGTSCESRVQ VPVPLPKVDV EMPKVDLGFK VVEPTGTEDF FEDFEAYGQG QVAPFGPWKV LGKAPHVEEG VQAGKTIGKV LKVIIDRGVF TPGEWTNFIL ECNLKREGSA EGRVYFRLSE DGKKSFYVIF SECGISLHKF AGSIDMKIAE NSSFKLSDRT PTTQAIPLQG DRFVVVLIIL // ID Q9X0C3_THEMA Unreviewed; 336 AA. AC Q9X0C3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 87. DE SubName: Full=Mannose-1-phosphate guanylyltransferase {ECO:0000313|EMBL:AAD36110.1}; GN OrderedLocusNames=TM_1033 {ECO:0000313|EMBL:AAD36110.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36110.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36110.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:2X5S, ECO:0000213|PDB:2X5Z, ECO:0000213|PDB:2X60} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH GTP. RX PubMed=20573954; DOI=10.1074/jbc.M109.095182; RA Pelissier M.C., Lesley S.A., Kuhn P., Bourne Y.; RT "Structural insights into the catalytic mechanism of bacterial RT guanosine-diphospho-D-mannose pyrophosphorylase and its regulation by RT divalent ions."; RL J. Biol. Chem. 285:27468-27476(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36110.1; -; Genomic_DNA. DR PIR; H72303; H72303. DR RefSeq; NP_228839.1; NC_000853.1. DR RefSeq; WP_010865249.1; NC_000853.1. DR PDB; 2X5S; X-ray; 2.35 A; A/B=1-336. DR PDB; 2X5Z; X-ray; 2.70 A; A/B=1-336. DR PDB; 2X60; X-ray; 2.80 A; A/B=1-336. DR PDB; 2X65; X-ray; 2.10 A; A/B=1-336. DR PDBsum; 2X5S; -. DR PDBsum; 2X5Z; -. DR PDBsum; 2X60; -. DR PDBsum; 2X65; -. DR ProteinModelPortal; Q9X0C3; -. DR STRING; 243274.TM1033; -. DR EnsemblBacteria; AAD36110; AAD36110; TM_1033. DR GeneID; 897249; -. DR KEGG; tma:TM1033; -. DR PATRIC; 23936995; VBITheMar51294_1046. DR eggNOG; ENOG4105CJT; Bacteria. DR eggNOG; COG0836; LUCA. DR InParanoid; Q9X0C3; -. DR KO; K00971; -. DR OMA; SHHHRAE; -. DR BioCyc; TMAR243274:GC6P-1062-MONOMER; -. DR BRENDA; 2.7.7.13; 6331. DR EvolutionaryTrace; Q9X0C3; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2X5S, ECO:0000213|PDB:2X5Z, KW ECO:0000213|PDB:2X60, ECO:0000213|PDB:2X65}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW GTP-binding {ECO:0000213|PDB:2X60}; KW Nucleotide-binding {ECO:0000213|PDB:2X60}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAD36110.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD36110.1}. FT DOMAIN 3 272 NTP_transferase. FT {ECO:0000259|Pfam:PF00483}. FT NP_BIND 7 14 GTP. {ECO:0000213|PDB:2X60}. FT NP_BIND 84 85 GTP. {ECO:0000213|PDB:2X60}. FT NP_BIND 108 109 GTP. {ECO:0000213|PDB:2X60}. FT BINDING 25 25 GTP. {ECO:0000213|PDB:2X60}. FT BINDING 56 56 GTP; via carbonyl oxygen. FT {ECO:0000213|PDB:2X60}. FT BINDING 80 80 GTP. {ECO:0000213|PDB:2X60}. SQ SEQUENCE 336 AA; 38617 MW; 4F67576BCC113527 CRC64; MMKALILAGG SGERFWPLST PETPKQFLKL FGNKSLMRWT FERVLEEMDP KDVIVVTHKD YVERTKKELP ELPDENIIAE PMKKNTAPAC FIGTKLADDD EPVLVLPADH RIPDTKKFWK TVKKALDALE KYDGLFTFGI VPTRPETGYG YIEIGEELEE GVHKVAQFRE KPDLETAKKF VESGRFLWNS GMFLWKAREF IEEVKVCEPS IYENLKDVDP RNFEELKKAY EKVPSISVDY AVMEKSKKVR VVKADFEWSD VGNWSSVREI EGYTEESDEV ILVDSDRVFV KTHNKPIAVV GLSDVIVIDT PNGILICKEE YAQKVREVVK KLFRTS // ID Q9WYS4_THEMA Unreviewed; 476 AA. AC Q9WYS4; G4FE27; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 100. DE SubName: Full=Gluconate kinase {ECO:0000313|EMBL:AAD35528.1}; GN OrderedLocusNames=TM_0443 {ECO:0000313|EMBL:AAD35528.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35528.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35528.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the FGGY kinase family. CC {ECO:0000256|RuleBase:RU003733}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35528.1; -; Genomic_DNA. DR PIR; F72377; F72377. DR RefSeq; NP_228253.1; NC_000853.1. DR RefSeq; WP_004081523.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WYS4; -. DR STRING; 243274.TM0443; -. DR EnsemblBacteria; AAD35528; AAD35528; TM_0443. DR GeneID; 897458; -. DR KEGG; tma:TM0443; -. DR KEGG; tmi:THEMA_02510; -. DR KEGG; tmw:THMA_0449; -. DR PATRIC; 23935771; VBITheMar51294_0449. DR eggNOG; ENOG4105CMG; Bacteria. DR eggNOG; COG1070; LUCA. DR KO; K00851; -. DR OMA; YIRISRK; -. DR OrthoDB; EOG63FW13; -. DR BioCyc; TMAR243274:GC6P-458-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000256|SAAS:SAAS00430777, KW ECO:0000313|EMBL:AAD35528.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU003733, KW ECO:0000256|SAAS:SAAS00430777, ECO:0000313|EMBL:AAD35528.1}. FT DOMAIN 1 231 FGGY_N. {ECO:0000259|Pfam:PF00370}. FT DOMAIN 240 424 FGGY_C. {ECO:0000259|Pfam:PF02782}. SQ SEQUENCE 476 AA; 54153 MW; 0B1EBA8B58526A5A CRC64; MIAAIDIGTE SARLMFKSNG EWKVLKKSYR IFFPSPEAAE QDPNEIFSAV FDLLKQVPNE DEVLYVGMSS VFHSIIGLDE NLNPVTPLLN WADRRSFREK EELEKKYGVR FFYEKTACPL HPMYWPSKIL WMKKNSNAKK FCSIKAYIVN KMTREFVEEL SLASGTGMMN IHSLEWDGEI LEITGVRKED LPEIKSPYTQ LRVKDEIAKE LGFKKVYLVL GGGDGVMTNV GVNVMDPDSA TVTIGTSGAF RVVMDRPVID REGISTWCYL IDEENYVLGG AINNGGIVLM WLRDIMKFKD YNDIIEEAKE SPAGANGLVF LPFLNGERAP HWRERYRGVL VGLTSSHRRS DIARAALEGI CFRIKDIHNA VKRVGSVDPN RIVATGGFTS SPYWVQLLSD VLGKDIIVTN VENPSAFGAY VMALKSLGED VEGFIEKEVR VERVFHPDSE RNAVYERLYN DYKFLYEKLV DYYYKE // ID Q9X1F2_THEMA Unreviewed; 218 AA. AC Q9X1F2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36508.1}; GN OrderedLocusNames=TM_1439 {ECO:0000313|EMBL:AAD36508.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36508.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36508.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36508.1; -; Genomic_DNA. DR PIR; C72255; C72255. DR RefSeq; NP_229238.1; NC_000853.1. DR RefSeq; WP_010865343.1; NC_000853.1. DR STRING; 243274.TM1439; -. DR DNASU; 898036; -. DR EnsemblBacteria; AAD36508; AAD36508; TM_1439. DR GeneID; 898036; -. DR KEGG; tma:TM1439; -. DR PATRIC; 23937828; VBITheMar51294_1452. DR eggNOG; ENOG4105F70; Bacteria. DR eggNOG; COG3330; LUCA. DR KO; K09942; -. DR OMA; SSRERWY; -. DR OrthoDB; EOG6KDKQT; -. DR BioCyc; TMAR243274:GC6P-1477-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR032585; DUF4912. DR Pfam; PF16258; DUF4912; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 218 AA; 25047 MW; 6685516D276C1744 CRC64; MKKKEVIKLI KEHVESAFST TDSSSGVSTT VQRREEKDLN LPRTYDKNKL VLMPVNPYVV FAYWDFDQRT RELMKQKARE GKAVIRLYDV TFIMFNGTNA HRTFEHRLDE LTLDAGNFYF NVPMPRADYL SEMGYLDDEG KFVSVLRSNV TRTPAASPSA SSRERWYDLK NKKRTVVLSE GSLIKPVEKI RGVTSPGFPS GQGMMAQGIM WEIFRSGR // ID Q9WZF0_THEMA Unreviewed; 157 AA. AC Q9WZF0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35766.1}; GN OrderedLocusNames=TM_0684 {ECO:0000313|EMBL:AAD35766.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35766.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35766.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35766.1; -; Genomic_DNA. DR PIR; A72348; A72348. DR RefSeq; NP_228493.1; NC_000853.1. DR RefSeq; WP_008192645.1; NZ_CP011107.1. DR STRING; 243274.TM0684; -. DR DNASU; 898351; -. DR EnsemblBacteria; AAD35766; AAD35766; TM_0684. DR GeneID; 898351; -. DR KEGG; tma:TM0684; -. DR KEGG; tmi:THEMA_01245; -. DR KEGG; tmw:THMA_0699; -. DR PATRIC; 23936286; VBITheMar51294_0696. DR eggNOG; ENOG4106BRF; Bacteria. DR eggNOG; COG1838; LUCA. DR OMA; NILSARD; -. DR OrthoDB; EOG6SZ1JN; -. DR BioCyc; TMAR243274:GC6P-710-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 157 AA; 18339 MW; 5F51F5B53F9C0BDE CRC64; MIFLIVLKYP VSLNVIRKLK TGDVVYYTGK IVVMDRSVVD ILEKYERYEG TKLYDLTGEI VVLGTFRKNK LQFQEMTEEL LERLFLLGVN GVILERVRPF SATKRFSRVL FEPLEEIRGT RRVIYKTPDS KKLEELEVEK LVLRVVQDSS GKVYSKV // ID Q9X0U4_THEMA Unreviewed; 618 AA. AC Q9X0U4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 114. DE SubName: Full=Glutamate synthase, beta subunit {ECO:0000313|EMBL:AAD36292.1}; GN OrderedLocusNames=TM_1217 {ECO:0000313|EMBL:AAD36292.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36292.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36292.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36292.1; -; Genomic_DNA. DR PIR; G72281; G72281. DR RefSeq; NP_229022.1; NC_000853.1. DR RefSeq; WP_010865282.1; NC_000853.1. DR ProteinModelPortal; Q9X0U4; -. DR STRING; 243274.TM1217; -. DR DNASU; 898267; -. DR EnsemblBacteria; AAD36292; AAD36292; TM_1217. DR GeneID; 898267; -. DR KEGG; tma:TM1217; -. DR PATRIC; 23937376; VBITheMar51294_1235. DR eggNOG; ENOG4107QZ5; Bacteria. DR eggNOG; COG0493; LUCA. DR eggNOG; COG1143; LUCA. DR InParanoid; Q9X0U4; -. DR KO; K00266; -. DR OMA; HGPDIIH; -. DR OrthoDB; EOG6XSZQF; -. DR BioCyc; TMAR243274:GC6P-1247-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 2. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR028261; DPD_II. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2. DR Pfam; PF14691; Fer4_20; 1. DR Pfam; PF12838; Fer4_7; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00469; PNDRDTASEII. DR SUPFAM; SSF46548; SSF46548; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 46 76 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 88 117 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 191 222 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 618 AA; 69570 MW; E710C5CC9B8D81A9 CRC64; MRKMAVQKLP EKDFFAPLKA WKFLVRKPVT IEVPNKIRRE ASERYRGFHV NDWGKCIGCG TCAKICPTDA ITMVEVPDLT QEDGKLPQRP VIDYGRCSFC ALCVDICTTG SLKMTREYIH ISEDPEDFIF MPTDKGLNAK KGLYEFGKAP LGWVRDENSE LLDLERIEMP VEPPEVRIKS FIEIVKGYSR EQAMQEAARC VECGVCTYTC PEHMDIPQYI KSVYEDNLEE GLRWLYRTNP LSMVCGRVCT HRCETACSVG VRGEPVAIQW LKRYIVDSIP LERYGEILDI KPERKGKSVG IIGSGPAGLA AAYFLATMGY DVTIYESESK PGGVMRYGIP KYRLPDEALD KDIAFIEALG VKILLNTRVV QDVSFEDVRK RHDVVFLATG FGLGRSTGVP GTDHPDVKQA LPLLKMIRDY LRGDGPKPPV PERLVVIGGG NVAMDISRSM ARLQFMEYGR VNVQVLSLEG CFEDMPADME EIEEALEEGI VINPGWGPME VVIENDRIKG VKFKKCVSVF DGEGRFNPQF DEKEQIFVEA DMVVEAIGQA PDYSYLPEEI RSKLEFFRGR IKTNEYNQTS VEWLFAGGDI VHGPDIIHGI ADGYAAAKGI DMYLRKEK // ID Q9X2B5_THEMA Unreviewed; 442 AA. AC Q9X2B5; G4FGI3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36858.1}; GN OrderedLocusNames=TM_1795 {ECO:0000313|EMBL:AAD36858.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36858.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36858.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36858.1; -; Genomic_DNA. DR PIR; H72209; H72209. DR RefSeq; NP_229592.1; NC_000853.1. DR RefSeq; WP_004082342.1; NZ_CP011107.1. DR STRING; 243274.TM1795; -. DR EnsemblBacteria; AAD36858; AAD36858; TM_1795. DR GeneID; 897837; -. DR KEGG; tma:TM1795; -. DR KEGG; tmi:THEMA_05215; -. DR KEGG; tmw:THMA_1841; -. DR PATRIC; 23938579; VBITheMar51294_1816. DR eggNOG; ENOG4105QHQ; Bacteria. DR eggNOG; COG1367; LUCA. DR KO; K07061; -. DR OMA; RFWFRAI; -. DR OrthoDB; EOG6DZDZS; -. DR BioCyc; TMAR243274:GC6P-1846-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR007522; CRISPR-assoc_prot_TM1795. DR InterPro; IPR005537; RAMP_III_fam. DR Pfam; PF03787; RAMPs; 1. DR TIGRFAMs; TIGR01894; cas_TM1795_cmr1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 442 AA; 50208 MW; 62F0B3C023ADB916 CRC64; MASSSEGVSV LEIECKVVTP MFSRGAAEPK WENGNRVYPF ELRPQSIKGV LRFWFRAIAP TVIDIYSLEG LENLSKKEKE RWEKEKYKGL KYLEGLIFGS QERKSSFSLE VKVEGESQAL GKYMNNRFSF TDDRLKDTKY ALYGLYDKSG IYEYLQEGKN FIIILQTAND SIKGIILSLL KLVSTFSGFG AKTRKGFGEF EIVDPKLTRN DYNLVISECQ EHIREFVNHH NSSSKVKIKL GRTNFNGIPD FPCFCDYKIF EITKFSGNSP LEVLREVFKV GRNFKGWYPS LKQKMRFSEG DCVKDLVEAL EGLLKGRKTE KKIEIPTAVV GLPIQYQNLG RGEIRRLKVI VSSSLRGLGI DDIDGRKASP LFLSVHEGER GKWKLVVLLM RSRVTNDGEL ITEVKGGKTP SSGIKTIVKE EKDYKNLLEW IKKLGGKEIQ GG // ID Q9WYV7_THEMA Unreviewed; 104 AA. AC Q9WYV7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35572.1}; GN OrderedLocusNames=TM_0487 {ECO:0000313|EMBL:AAD35572.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35572.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35572.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1UWD, ECO:0000213|PDB:1WCJ} RP STRUCTURE BY NMR OF 2-104. RX PubMed=16199668; DOI=10.1110/ps.051755805; RA Almeida M.S., Herrmann T., Peti W., Wilson I.A., Wuthrich K.; RT "NMR structure of the conserved hypothetical protein TM0487 from RT Thermotoga maritima: implications for 216 homologous DUF59 proteins."; RL Protein Sci. 14:2880-2886(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35572.1; -; Genomic_DNA. DR PIR; F72369; F72369. DR RefSeq; NP_228297.1; NC_000853.1. DR RefSeq; WP_010865131.1; NC_000853.1. DR PDB; 1UWD; NMR; -; A=2-104. DR PDB; 1WCJ; NMR; -; A=2-104. DR PDBsum; 1UWD; -. DR PDBsum; 1WCJ; -. DR ProteinModelPortal; Q9WYV7; -. DR SMR; Q9WYV7; 3-104. DR STRING; 243274.TM0487; -. DR EnsemblBacteria; AAD35572; AAD35572; TM_0487. DR GeneID; 897527; -. DR KEGG; tma:TM0487; -. DR PATRIC; 23935879; VBITheMar51294_0494. DR eggNOG; ENOG4105VG1; Bacteria. DR eggNOG; COG2151; LUCA. DR InParanoid; Q9WYV7; -. DR OMA; EVKILMT; -. DR OrthoDB; EOG62RSJQ; -. DR BioCyc; TMAR243274:GC6P-511-MONOMER; -. DR EvolutionaryTrace; Q9WYV7; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR002744; DUF59. DR Pfam; PF01883; DUF59; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1UWD, ECO:0000213|PDB:1WCJ}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 9 82 DUF59. {ECO:0000259|Pfam:PF01883}. SQ SEQUENCE 104 AA; 11639 MW; 6736BA22791B98D3 CRC64; MPMSKKVTKE DVLNALKNVI DFELGLDVVS LGLVYDIQID DQNNVKVLMT MTTPMCPLAG MILSDAEEAI KKIEGVNNVE VELTFDPPWT PERMSPELRE KFGV // ID Q9X0T5_THEMA Unreviewed; 70 AA. AC Q9X0T5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36283.1}; GN OrderedLocusNames=TM_1208 {ECO:0000313|EMBL:AAD36283.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36283.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36283.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36283.1; -; Genomic_DNA. DR PIR; F72280; F72280. DR RefSeq; NP_229013.1; NC_000853.1. DR RefSeq; WP_010865280.1; NC_000853.1. DR STRING; 243274.TM1208; -. DR DNASU; 898276; -. DR EnsemblBacteria; AAD36283; AAD36283; TM_1208. DR GeneID; 898276; -. DR KEGG; tma:TM1208; -. DR PATRIC; 23937358; VBITheMar51294_1226. DR eggNOG; ENOG41069KK; Bacteria. DR eggNOG; COG1563; LUCA. DR InParanoid; Q9X0T5; -. DR KO; K05566; -. DR OMA; FIFAIKR; -. DR OrthoDB; EOG6GJC0Z; -. DR BioCyc; TMAR243274:GC6P-1238-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR025383; DUF4040. DR Pfam; PF13244; DUF4040; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 15 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 62 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 65 DUF4040. {ECO:0000259|Pfam:PF13244}. SQ SEQUENCE 70 AA; 7523 MW; D5DAE416BCCB3F51 CRC64; MMLIAAFFAV EARKILDSVI AFSSLSLLSV FLFIIMKAPD VAITEASVGA GLTTAVLLIT LFKMGKDDER // ID Q9X0J5_THEMA Unreviewed; 265 AA. AC Q9X0J5; G4FEN7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36187.1}; GN OrderedLocusNames=TM_1111 {ECO:0000313|EMBL:AAD36187.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36187.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36187.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36187.1; -; Genomic_DNA. DR PIR; A72296; A72296. DR RefSeq; NP_228917.1; NC_000853.1. DR RefSeq; WP_004080315.1; NC_000853.1. DR STRING; 243274.TM1111; -. DR EnsemblBacteria; AAD36187; AAD36187; TM_1111. DR GeneID; 898654; -. DR KEGG; tma:TM1111; -. DR PATRIC; 23937155; VBITheMar51294_1126. DR OMA; CEPGQAR; -. DR OrthoDB; EOG66B3ZP; -. DR BioCyc; TMAR243274:GC6P-1140-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 150 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 265 AA; 28846 MW; C0EC286466739DE8 CRC64; MEGFRAGQKA LQPLLNLKPS GKCCRILMHH ARRGAGGPLY PKSAVRGAEF PPEALRVGKR RDSGAMKTGS HATEPCEPGQ AREGAAISRC FRVPWGSPVG AFRSCTPRSG EVDGGCVVHF SSGYSLVETL ALMFCICTVV MIGLLSLSLA MKTRARLVYD IDLLTDEFYA VDFMKHEYEV KAAASPSVSV TSNSLSFNAS YDKKSGTISY LVMFKDGLYK IVRFGLSGEG NNYLIETKKE IHFSQEGKVF SVMIGDTIYD LGISE // ID Q9X0M8_THEMA Unreviewed; 146 AA. AC Q9X0M8; G4FEK4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36220.1}; GN OrderedLocusNames=TM_1144 {ECO:0000313|EMBL:AAD36220.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36220.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36220.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36220.1; -; Genomic_DNA. DR PIR; D72291; D72291. DR RefSeq; NP_228950.1; NC_000853.1. DR RefSeq; WP_004080240.1; NZ_CP011107.1. DR STRING; 243274.TM1144; -. DR EnsemblBacteria; AAD36220; AAD36220; TM_1144. DR GeneID; 898620; -. DR KEGG; tma:TM1144; -. DR KEGG; tmi:THEMA_08625; -. DR KEGG; tmw:THMA_1167; -. DR PATRIC; 23937223; VBITheMar51294_1160. DR BioCyc; TMAR243274:GC6P-1173-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 146 AA; 17263 MW; 70D0D05BC940971E CRC64; MKVFCEKTMD IMFLFLITFE FNEERGTLFV SRYNSLHKLD VKLFPLDHDK ARLEIVEVPI TTQQKWWNPT IGILELKGRK RNIIISNTSN EEIVFILSGV RDMEVDRREI SRIETPEGSY EGFITGKIRI AGVPHFVFKI EERRDR // ID Q9WYX7_THEMA Unreviewed; 65 AA. AC Q9WYX7; G4FDW4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35592.1}; GN OrderedLocusNames=TM_0507 {ECO:0000313|EMBL:AAD35592.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35592.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35592.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35592.1; -; Genomic_DNA. DR PIR; A72368; A72368. DR RefSeq; NP_228317.1; NC_000853.1. DR RefSeq; WP_004081433.1; NZ_CP011107.1. DR STRING; 243274.TM0507; -. DR EnsemblBacteria; AAD35592; AAD35592; TM_0507. DR GeneID; 897551; -. DR KEGG; tma:TM0507; -. DR KEGG; tmi:THEMA_02140; -. DR KEGG; tmw:THMA_0519; -. DR PATRIC; 23935919; VBITheMar51294_0514. DR OrthoDB; EOG66B46T; -. DR BioCyc; TMAR243274:GC6P-531-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 28 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 65 AA; 7547 MW; C996C957F166C364 CRC64; MEIKGALGPL YFFSFCGMMK ISIVPFRYGN LLRKRSKNSF ELIQYFLRGL KKEGAFAPSF GFIKR // ID Q9X040_THEMA Unreviewed; 386 AA. AC Q9X040; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36023.1}; GN OrderedLocusNames=TM_0942 {ECO:0000313|EMBL:AAD36023.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36023.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36023.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36023.1; -; Genomic_DNA. DR PIR; A72313; A72313. DR RefSeq; NP_228750.1; NC_000853.1. DR RefSeq; WP_010865222.1; NC_000853.1. DR STRING; 243274.TM0942; -. DR EnsemblBacteria; AAD36023; AAD36023; TM_0942. DR GeneID; 898679; -. DR KEGG; tma:TM0942; -. DR KEGG; tmi:THEMA_09640; -. DR PATRIC; 23936815; VBITheMar51294_0956. DR eggNOG; ENOG41083RP; Bacteria. DR eggNOG; ENOG410ZX3N; LUCA. DR OMA; VEVLWIR; -. DR OrthoDB; EOG6GBM9C; -. DR BioCyc; TMAR243274:GC6P-972-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 187 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 237 257 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 266 282 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 358 379 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 386 AA; 45094 MW; C8FEA3CA584E13FE CRC64; MEFSFLFDDM IDGKRVVLFD LSSRKDLPPE AEIVILKGEP LFWEPQELAE KLKGKWLGIV EFDPSYDFAR KVALLKKDGL FFRVHTVKPE EIEKLNLDEE ALFHRYKRAV LERSVEVLWI RDIDEKELLV QRLSSYFKGK VVPFPAPPES EPPFPKWIFL IPPILMITSL NPLLLSVVFV LPFSREWFVS LLFVSGTLAA YFVPKKKWLK VLSFLLLSIS LSLSLSDLYH LNGILDFRGV KLSLVLLPGL LFLSGLWKNR RNWKKYLPLL FLAIPVGFYY LMRSGNSGWV LEVERKFRDW LESVLMVRPR FKEIVCYPFF WLEGFREYDF LRESFGSVAL VSMFNTFCHV KTPLVVSIYR SALGLAIGYA VFLFLKVFLN RFLTSK // ID Q9X122_THEMA Unreviewed; 223 AA. AC Q9X122; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 104. DE SubName: Full=Ribonuclease H-related protein {ECO:0000313|EMBL:AAD36370.1}; GN OrderedLocusNames=TM_1296 {ECO:0000313|EMBL:AAD36370.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36370.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36370.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36370.1; -; Genomic_DNA. DR PIR; B72269; B72269. DR RefSeq; NP_229100.1; NC_000853.1. DR RefSeq; WP_010865300.1; NC_000853.1. DR ProteinModelPortal; Q9X122; -. DR SMR; Q9X122; 6-50. DR STRING; 243274.TM1296; -. DR EnsemblBacteria; AAD36370; AAD36370; TM_1296. DR GeneID; 898187; -. DR KEGG; tma:TM1296; -. DR KEGG; tmi:THEMA_07855; -. DR PATRIC; 23937532; VBITheMar51294_1312. DR eggNOG; ENOG4108Z2I; Bacteria. DR eggNOG; COG3341; LUCA. DR KO; K03469; -. DR OMA; GIEKWCT; -. DR OrthoDB; EOG62C9C9; -. DR BioCyc; TMAR243274:GC6P-1327-MONOMER; -. DR BRENDA; 3.1.26.4; 6331. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IBA:GO_Central. DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GOC. DR Gene3D; 3.30.420.10; -; 1. DR Gene3D; 3.40.970.10; -; 1. DR InterPro; IPR009027; Ribosomal_L9/RNase_H1_N. DR InterPro; IPR011320; RNase_H1_N. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR002156; RNaseH_domain. DR Pfam; PF01693; Cauli_VI; 1. DR Pfam; PF00075; RNase_H; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR SUPFAM; SSF55658; SSF55658; 1. DR PROSITE; PS50879; RNASE_H; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 62 197 RNase H. {ECO:0000259|PROSITE:PS50879}. SQ SEQUENCE 223 AA; 25950 MW; E7843A9717FE2725 CRC64; MKLAKKYYAV RKGRVPGIYK TWKEAEEQVK GFPGAEYKSF ERLEDAKAYM EGKNECICPE LDTETMIAYV DGSYDEVCGS GIVLCYRGKK EEYYFWTNIE EFKDSRNITG EIMAALFAMD YALKKGARKL VLRYDLEGLE KWATEEYRTN KLVTKVYRHY YRKFCQMGLK VVFEKIKSHS GNFCNDEADS LAKKASKKES NVEWMPEDFE SIIRTLTKKG GCL // ID Q9WYY6_THEMA Unreviewed; 305 AA. AC Q9WYY6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Clostripain-related protein {ECO:0000313|EMBL:AAD35601.1}; GN OrderedLocusNames=TM_0516 {ECO:0000313|EMBL:AAD35601.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35601.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35601.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35601.1; -; Genomic_DNA. DR PIR; B72365; B72365. DR RefSeq; NP_228326.1; NC_000853.1. DR RefSeq; WP_010865140.1; NC_000853.1. DR STRING; 243274.TM0516; -. DR DNASU; 897561; -. DR EnsemblBacteria; AAD35601; AAD35601; TM_0516. DR GeneID; 897561; -. DR KEGG; tma:TM0516; -. DR KEGG; tmi:THEMA_02095; -. DR PATRIC; 23935937; VBITheMar51294_0523. DR OMA; TFEILWE; -. DR OrthoDB; EOG6PGK59; -. DR BioCyc; TMAR243274:GC6P-540-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR005077; Peptidase_C11. DR Pfam; PF03415; Peptidase_C11; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 305 AA; 34978 MW; C93C39120B8E1E40 CRC64; MGNPSWINVF ALVDYRSSSD TLYRVEEGLI PLETFDEINS GDPVVLSSFL NAYRGEDLSL LVIWNHGDWW RGESQKQVKG VAYDFVNLDF FTIKEIKSVL RDSPVTVLGF DACLMGTFEI LWELKDCARY VVVSSKEAPG NGWDYSVLRY SKDLSSLLSN IVKRYGEIYG TEYSLSVWDT SKLDEIMLWL DRVAQYMIEN NLSPWEFEVE RRTAGGSTTE LVELGSFAKS LQNSSDVVLR EYGEGLYSAI VSARVYGTPD NYTDLTIYLP QNMKNPEYWD DFVALSDFTS ESSWDDLIEH WRDKN // ID Q9WXL7_THEMA Unreviewed; 41 AA. AC Q9WXL7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35096.1}; GN OrderedLocusNames=TM_0002 {ECO:0000313|EMBL:AAD35096.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35096.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35096.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35096.1; -; Genomic_DNA. DR PIR; D72429; D72429. DR RefSeq; NP_227818.1; NC_000853.1. DR RefSeq; WP_010865021.1; NC_000853.1. DR EnsemblBacteria; AAD35096; AAD35096; TM_0002. DR GeneID; 896810; -. DR KEGG; tma:TM0002; -. DR PATRIC; 23934848; VBITheMar51294_0002. DR BioCyc; TMAR243274:GC6P-2-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 41 AA; 4822 MW; 53B3BB177C1FBDF4 CRC64; MSPEDWKRLI CFHTSKEVLK QTLDDAQQNI SDSVSIPLRK Y // ID Q9X1A6_THEMA Unreviewed; 69 AA. AC Q9X1A6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36456.1}; GN OrderedLocusNames=TM_1386 {ECO:0000313|EMBL:AAD36456.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36456.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36456.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36456.1; -; Genomic_DNA. DR PIR; C72262; C72262. DR RefSeq; NP_229187.1; NC_000853.1. DR RefSeq; WP_010865329.1; NC_000853.1. DR STRING; 243274.TM1386; -. DR EnsemblBacteria; AAD36456; AAD36456; TM_1386. DR GeneID; 898092; -. DR KEGG; tma:TM1386; -. DR KEGG; tmi:THEMA_07395; -. DR PATRIC; 23937714; VBITheMar51294_1398. DR OMA; FFIEGGP; -. DR OrthoDB; EOG6MWNG0; -. DR BioCyc; TMAR243274:GC6P-1421-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 69 AA; 8037 MW; AE7243AA781F36CF CRC64; MREGEKVFFI EGGPLGEEGT YIIVSDDPTV EERIAKVIEE LNTTSVIFLA EDEYERFKNE LEKKAKRIW // ID Q9X161_THEMA Unreviewed; 137 AA. AC Q9X161; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36411.1}; GN OrderedLocusNames=TM_1339 {ECO:0000313|EMBL:AAD36411.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36411.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36411.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36411.1; -; Genomic_DNA. DR PIR; C72266; C72266. DR RefSeq; NP_229141.1; NC_000853.1. DR RefSeq; WP_010865319.1; NC_000853.1. DR STRING; 243274.TM1339; -. DR EnsemblBacteria; AAD36411; AAD36411; TM_1339. DR GeneID; 898143; -. DR KEGG; tma:TM1339; -. DR KEGG; tmi:THEMA_07650; -. DR PATRIC; 23937609; VBITheMar51294_1350. DR OMA; PPIVRCL; -. DR OrthoDB; EOG6H1Q2G; -. DR BioCyc; TMAR243274:GC6P-1370-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 137 AA; 15868 MW; 1A58E1A348B123C1 CRC64; MRRPPIVRCL FFLNDTIVLE LEKTRVISER SNEEVIVVIR KTVKGTDGRE YTFVAKEGTF EKLTGLGTTI RGHIPGTDSP FYGILEDGEE GLRAWIMTFR VVNRVPIDSE TEEELVRLFL PLVERRRIDR SILLYVE // ID Q9WXX5_THEMA Unreviewed; 368 AA. AC Q9WXX5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35215.1}; GN OrderedLocusNames=TM_0121 {ECO:0000313|EMBL:AAD35215.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35215.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35215.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35215.1; -; Genomic_DNA. DR PIR; A72415; A72415. DR RefSeq; NP_227937.1; NC_000853.1. DR RefSeq; WP_010865056.1; NC_000853.1. DR ProteinModelPortal; Q9WXX5; -. DR STRING; 243274.TM0121; -. DR EnsemblBacteria; AAD35215; AAD35215; TM_0121. DR GeneID; 896948; -. DR KEGG; tma:TM0121; -. DR PATRIC; 23935082; VBITheMar51294_0119. DR eggNOG; ENOG4105CK3; Bacteria. DR eggNOG; COG1509; LUCA. DR InParanoid; Q9WXX5; -. DR OMA; KRVRYVM; -. DR OrthoDB; EOG635879; -. DR BioCyc; TMAR243274:GC6P-121-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004911; DUF160; 1. DR TIGRFAMs; TIGR00238; TIGR00238; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|PIRSR:PIRSR004911-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|PIRSR:PIRSR004911-1}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR004911-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR004911-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 100 250 Radical_SAM. {ECO:0000259|Pfam:PF04055}. FT METAL 101 101 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004911-1}. FT METAL 105 105 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004911-1}. FT METAL 108 108 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|PIRSR:PIRSR004911-1}. SQ SEQUENCE 368 AA; 42937 MW; 5AA86EEA2665CF59 CRC64; MIRLKVKYYT SITQVEQLSP EERERLKRVE EKYRFRANSY YLSLIDWSDP DDPIRKIIVP EEDELEEWGT LDASNEKSYT VAKGLQHKYP DTALFLVNDV CGGFCRFCFR KRLFINVGAE VIRDITPQLD YIRTHKEITN VLLTGGDPLL LSTEKLEKIV SSLREIDHVQ IIRIGSKIPA FNPYRIIDDP DLLKMIRKYS TKEKKIYVMT QFNHPRELTR EAIEAVNLLK DAGAVLCNQT PLLRGINDDP EVLGELLDRL SFVGVTPYYV FQNRPVSGNR KFAVPIEEGY EIFTKAISNI SGVAKRVRYV MSHRTGKIEI AALTKDFIVF KYHRAHDEKN RRKVMVYKRN PQALWFDDYS ELLEEYTV // ID Q9WXM6_THEMA Unreviewed; 128 AA. AC Q9WXM6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=NADP-reducing hydrogenase, subunit B {ECO:0000313|EMBL:AAD35105.1}; GN OrderedLocusNames=TM_0011 {ECO:0000313|EMBL:AAD35105.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35105.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35105.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35105.1; -; Genomic_DNA. DR PIR; E72430; E72430. DR RefSeq; NP_227827.1; NC_000853.1. DR RefSeq; WP_010865025.1; NC_000853.1. DR ProteinModelPortal; Q9WXM6; -. DR STRING; 243274.TM0011; -. DR EnsemblBacteria; AAD35105; AAD35105; TM_0011. DR GeneID; 896820; -. DR KEGG; tma:TM0011; -. DR PATRIC; 23934862; VBITheMar51294_0009. DR eggNOG; ENOG4105M1A; Bacteria. DR eggNOG; COG3411; LUCA. DR InParanoid; Q9WXM6; -. DR KO; K17992; -. DR OMA; CEVEPTI; -. DR OrthoDB; EOG65N1BV; -. DR BioCyc; TMAR243274:GC6P-11-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IBA:GO_Central. DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR012336; Thioredoxin-like_fold. DR SUPFAM; SSF52833; SSF52833; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 128 AA; 14035 MW; 1BE59291B45B0AE7 CRC64; MRMAKVKSLE ELMKIKEQAL KDLQLRGETG KRGKITVAMG TCGIAAGAKE TLKAIVEALN EYNINDIAVV QSGCMGLCEV EPTVEVRLEG QEPVIYGRVT PENAKRIVKM HILEGRVVED LVVKRGEA // ID Q9WXT9_THEMA Unreviewed; 116 AA. AC Q9WXT9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35178.1}; GN OrderedLocusNames=TM_0084 {ECO:0000313|EMBL:AAD35178.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35178.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35178.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35178.1; -; Genomic_DNA. DR PIR; F72419; F72419. DR RefSeq; NP_227900.1; NC_000853.1. DR RefSeq; WP_010865045.1; NC_000853.1. DR STRING; 243274.TM0084; -. DR EnsemblBacteria; AAD35178; AAD35178; TM_0084. DR GeneID; 896911; -. DR KEGG; tma:TM0084; -. DR PATRIC; 23935008; VBITheMar51294_0082. DR OMA; ETCNERL; -. DR OrthoDB; EOG6VTK3M; -. DR BioCyc; TMAR243274:GC6P-84-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro. DR Gene3D; 1.20.58.300; -; 1. DR InterPro; IPR007809; FlgN-like. DR Pfam; PF05130; FlgN; 1. DR SUPFAM; SSF140566; SSF140566; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 2 33 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 116 AA; 13759 MW; 570868DD97B243CB CRC64; MREELKRVLT EKIRLMENMR NLLEEELEAI INKDFERLES ILPRIEELSV SMETCNERLK SSLESHGNGT KLIDLLEIYK DDEEMLSELR SFFETLNKLV FEIEKLKQAI GFHLNS // ID Q9X0Z4_THEMA Unreviewed; 473 AA. AC Q9X0Z4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 83. DE SubName: Full=ThiH protein, putative {ECO:0000313|EMBL:AAD36342.1}; GN OrderedLocusNames=TM_1267 {ECO:0000313|EMBL:AAD36342.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36342.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36342.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36342.1; -; Genomic_DNA. DR PIR; B72274; B72274. DR RefSeq; NP_229072.1; NC_000853.1. DR RefSeq; WP_010865292.1; NC_000853.1. DR ProteinModelPortal; Q9X0Z4; -. DR STRING; 243274.TM1267; -. DR DNASU; 898216; -. DR EnsemblBacteria; AAD36342; AAD36342; TM_1267. DR GeneID; 898216; -. DR KEGG; tma:TM1267; -. DR PATRIC; 23937474; VBITheMar51294_1283. DR eggNOG; ENOG4105D41; Bacteria. DR eggNOG; COG1060; LUCA. DR InParanoid; Q9X0Z4; -. DR KO; K03150; -. DR OMA; CTPNALF; -. DR OrthoDB; EOG63JR5B; -. DR BioCyc; TMAR243274:GC6P-1298-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR010722; BATS_dom. DR InterPro; IPR024007; FeFe-hyd_mat_HydG. DR InterPro; IPR007197; rSAM. DR Pfam; PF06968; BATS; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00876; BATS; 1. DR TIGRFAMs; TIGR03955; rSAM_HydG; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00448030}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|SAAS:SAAS00448030}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00448030}; KW Metal-binding {ECO:0000256|SAAS:SAAS00448030}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00448054}. FT DOMAIN 276 385 BATS. {ECO:0000259|SMART:SM00876}. SQ SEQUENCE 473 AA; 54751 MW; 5512C79E0ED3B4CD CRC64; MCMYVFVKER VESRSFIPEE KIFELLEKTK NPDPARVREI IQKSLDKNRL EPEETATLLN VEDPELLEEI FEAARTLKER IYGNRIVLFA PLYIGNDCIN DCVYCGFRVS NKVVERRTLT EEQLKEEVKA LVSQGHKRLI VVYGEHPNYS PEFIARTIDI VYNTKYGNGE IRRVNVNAAP QTIEGYKIIK SVGIGTFQIF QETYHRETYL KLHPRGPKSN YNWRLYGLDR AMMAGIDDVG IGALFGLYDW KFEVMGLLYH TIHLEERFGV GPHTISFPRI KPAINTPYSQ KPEHVVSDED FKKLVAIIRL SVPYTGMILT AREPAKLRDE VIKLGVSQID AGSRIGIGAY SHKEDDEDRK RQFTLEDPRP LDQVMRSLLK EGFVPSFCTA CYRAGRTGEH FMEFAIPGFV KNFCTPNALF TLQEYLCDYA TEETRKVGEE VIERELQKMN PKIRERVREG LEKIKRGERD VRF // ID Q9X085_THEMA Unreviewed; 967 AA. AC Q9X085; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 106. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36069.1}; GN OrderedLocusNames=TM_0990 {ECO:0000313|EMBL:AAD36069.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36069.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36069.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36069.1; -; Genomic_DNA. DR PIR; D72308; D72308. DR RefSeq; NP_228798.1; NC_000853.1. DR RefSeq; WP_010865236.1; NC_000853.1. DR ProteinModelPortal; Q9X085; -. DR STRING; 243274.TM0990; -. DR EnsemblBacteria; AAD36069; AAD36069; TM_0990. DR GeneID; 897043; -. DR KEGG; tma:TM0990; -. DR KEGG; tmi:THEMA_09400; -. DR PATRIC; 23936909; VBITheMar51294_1003. DR eggNOG; ENOG4105BZK; Bacteria. DR eggNOG; COG0553; LUCA. DR OMA; INYEAPW; -. DR OrthoDB; EOG65N16D; -. DR BioCyc; TMAR243274:GC6P-1020-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR024975; DUF3883. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000330; SNF2_N. DR Pfam; PF13020; DUF3883; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00176; SNF2_N; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU004294}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004294}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 167 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 352 513 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. SQ SEQUENCE 967 AA; 111853 MW; 5B71A64912B775AC CRC64; MLSRPVRILI ADEIGLGKTI QALAIARYLE LQGEAKKILI LVPKILREQW KQEIRRLGGK PVVITNGSEV ERKLLRKATF NNAAEYFVVS IDLAKSQNHS EKFSAIDWDL LIVDEVHNVT YNTQRYNFLK SLIEKSKEDL NIVFLSATPH RGNPKDYIER LRLLDPTLTA DWNALDSEKF YRRTHGVLVF RRTKKVVNDL EKREIFKKCD FNAVIVDITE EEKRFFEELD EVLFEMVKDV HMNSPVALLA VLLRKRAASS YESALKTINN IIKNQYSGAS GEDVLEDQIK QIFGLGYDEM ELEENSEIDD LISSIINSVA KRYPLDKGQI NALEKILKIG KAIGKNDSKL KTLAEVLAYH LKKNEKVIVF TEFKDTLEYL RNNLPTLLEQ EGIHLSEEKD ISVLHGGMKS EEIEKQVEKF ANDGKLLIST DVASEGLNLQ VANILINYEI PWSPIKLEQR VGRIWRLNQT KETIAYTLLL NHEADLQILE SLYQKILNIT DAVGTGPNVG KPVFGTRTLS GNFEYRLENV QDEETSDSPV SEFELMLSAI KRRNLDEQTK RIISTLKSLR TKIEEVVPLN TCNEIQEELN SVLLPDDMES EIVFEKLKKY ISVFENSFIN SIGSYLFKIL TDRIHEPLLN EKCLKIAVKN ESKEYRLFQV EVIDRGRKIY EYPVLIEIGG NVSPQLYRGT SLLEKLADVF SKEWFVIEWA NPKEKMDIQT AKLIDRSAKD LQSIMDKHTD YDIKLNESLM KTDSLFRRLN TRSSEILRVE GLSDREFSVF KLLHPSILEI LGLSLDSIEL PPSDYEKWME RSFVPLEDIL ESERKAMEIV MDIEKKRLIE KYGESSDWKV EDVSLKEHYD IKVSEPEGEK YIEVKGHKPL WLSAELTAAE HRFANDNRDR YWIYIVSNLG GKKPVILKIF SPFDDEKRKI YLVHENKDID ITEIFGSTIK TKQRYVISLG QKIYRRR // ID Q9X259_THEMA Unreviewed; 299 AA. AC Q9X259; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|PIRNR:PIRNR000477}; DE EC=2.4.2.1 {ECO:0000256|PIRNR:PIRNR000477}; DE AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|PIRNR:PIRNR000477}; GN OrderedLocusNames=TM_1737 {ECO:0000313|EMBL:AAD36802.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36802.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36802.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: The purine nucleoside phosphorylases catalyze the CC phosphorolytic breakdown of the N-glycosidic bond in the beta- CC (deoxy)ribonucleoside molecules, with the formation of the CC corresponding free purine bases and pentose-1-phosphate. CC {ECO:0000256|PIRNR:PIRNR000477}. CC -!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine + CC alpha-D-ribose 1-phosphate. {ECO:0000256|PIRNR:PIRNR000477}. CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage. CC {ECO:0000256|PIRNR:PIRNR000477}. CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. CC {ECO:0000256|PIRNR:PIRNR000477}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36802.1; -; Genomic_DNA. DR PIR; H72217; H72217. DR RefSeq; NP_229535.1; NC_000853.1. DR RefSeq; WP_010865392.1; NC_000853.1. DR ProteinModelPortal; Q9X259; -. DR STRING; 243274.TM1737; -. DR EnsemblBacteria; AAD36802; AAD36802; TM_1737. DR GeneID; 897870; -. DR KEGG; tma:TM1737; -. DR PATRIC; 23938450; VBITheMar51294_1755. DR eggNOG; ENOG4107QSW; Bacteria. DR eggNOG; COG0005; LUCA. DR InParanoid; Q9X259; -. DR KO; K03783; -. DR OMA; TDECFPD; -. DR OrthoDB; EOG6423M2; -. DR BioCyc; TMAR243274:GC6P-1785-MONOMER; -. DR UniPathway; UPA00606; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IBA:GO_Central. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0043101; P:purine-containing compound salvage; IBA:GO_Central. DR Gene3D; 3.40.50.1580; -; 1. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR001369; PNP/MTAP. DR InterPro; IPR011270; Pur_Nuc_Pase_Ino/Guo-sp. DR InterPro; IPR011268; Purine_phosphorylase. DR PANTHER; PTHR11904; PTHR11904; 1. DR PANTHER; PTHR11904:SF9; PTHR11904:SF9; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR PIRSF; PIRSF000477; PurNPase; 1. DR SUPFAM; SSF53167; SSF53167; 1. DR TIGRFAMs; TIGR01700; PNPH; 1. DR TIGRFAMs; TIGR01697; PNPH-PUNA-XAPA; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000477}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|PIRNR:PIRNR000477}. FT DOMAIN 48 296 PNP_UDP_1. {ECO:0000259|Pfam:PF01048}. SQ SEQUENCE 299 AA; 33372 MW; 94FDE0C022C1C9B1 CRC64; MKSMWCIHDR IFLKKTREVF DVDIKAYKER VEKAVEYLKG QIDETPEIAI ILGSGLSVIA DEVEKEGTSK KIPYSEIPGF PISTAPGHKG ELIFGKLFGK NVMLMNGRFH YYEGYSMKEV TFPIRVMQLL GVEILIVTNA AGGLNPDFEV GRPMIITDHI NFMGDNPLIG PNVDEWGPRF PDMSEPYDKE LIELAYNSAR ELGIPVYQGV YVAVTGPCFE TPAELRMLRK FGADAVGMST VPEVIVARHG QIRVLGISAI TDRAVPEDLK PLTAEEVLEV AEKTGRKIAQ IIFEVVRKL // ID Q9WYN8_THEMA Unreviewed; 160 AA. AC Q9WYN8; G4FHW6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Diacylglycerol kinase, putative {ECO:0000313|EMBL:AAD35492.1}; GN OrderedLocusNames=TM_0407 {ECO:0000313|EMBL:AAD35492.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35492.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35492.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35492.1; -; Genomic_DNA. DR PIR; E72380; E72380. DR RefSeq; NP_228217.1; NC_000853.1. DR RefSeq; WP_004083250.1; NZ_CP011107.1. DR STRING; 243274.TM0407; -. DR EnsemblBacteria; AAD35492; AAD35492; TM_0407. DR GeneID; 897406; -. DR KEGG; tma:TM0407; -. DR KEGG; tmw:THMA_0413; -. DR PATRIC; 23935697; VBITheMar51294_0412. DR eggNOG; ENOG4107YR5; Bacteria. DR eggNOG; COG0818; LUCA. DR InParanoid; Q9WYN8; -. DR KO; K00901; -. DR OMA; IWIFFAV; -. DR OrthoDB; EOG6JB19C; -. DR BioCyc; TMAR243274:GC6P-422-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004143; F:diacylglycerol kinase activity; IEA:InterPro. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro. DR InterPro; IPR000829; Diacylglycerol_kinase_prok. DR Pfam; PF01219; DAGK_prokar; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000313|EMBL:AAD35492.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35492.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 31 48 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 94 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 125 144 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 160 AA; 18266 MW; ACF70E91BF105D01 CRC64; MQRDSNNILK SFKNAFEGIE NALKLERNLK IHFFIGIVVA IFSLFLPLSA NDLLWIYFAI FSVIGAELLN TVVEKFLDLF FKEYSESVKL VKDIAAGVVL WYSLFSVVVG ILILGKALFS WEPSFAKFFV SGVLIFFPVI SFSMRRYRND RQGDKSTGSR // ID Q9X2I0_THEMA Unreviewed; 457 AA. AC Q9X2I0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Membrane bound protein LytR, putative {ECO:0000313|EMBL:AAD36928.1}; GN OrderedLocusNames=TM_1866 {ECO:0000313|EMBL:AAD36928.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36928.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36928.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36928.1; -; Genomic_DNA. DR PIR; C72202; C72202. DR RefSeq; NP_229662.1; NC_000853.1. DR RefSeq; WP_010865422.1; NC_000853.1. DR ProteinModelPortal; Q9X2I0; -. DR STRING; 243274.TM1866; -. DR EnsemblBacteria; AAD36928; AAD36928; TM_1866. DR GeneID; 897369; -. DR KEGG; tma:TM1866; -. DR PATRIC; 23938721; VBITheMar51294_1887. DR eggNOG; ENOG41082EE; Bacteria. DR eggNOG; COG1316; LUCA. DR InParanoid; Q9X2I0; -. DR OMA; RIERQKD; -. DR OrthoDB; EOG68WR71; -. DR BioCyc; TMAR243274:GC6P-1917-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR004474; LytR_CpsA_psr. DR Pfam; PF03816; LytR_cpsA_psr; 1. DR TIGRFAMs; TIGR00350; lytR_cpsA_psr; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 85 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 117 259 LytR_cpsA_psr. FT {ECO:0000259|Pfam:PF03816}. SQ SEQUENCE 457 AA; 52507 MW; C76B8D4BF2C824EA CRC64; MRSRASPSAL FLSTSIRTIS LAKPFIRSAK AVLEPTLPSP TIPIFIRITS PVIEYSQGDI VLKKIFLSLS ISLAFFLIIS SFFLLDKMVS YLFKGEVKNP YVFLVLGKDK EIEHTVRTDV IVVGVLDWKK GNLSFVSIPR DLMIEGKKIN AIYNTYGMEK LFQIIESLLG QKPDSYVIFN YEAFKILVDE LGPIEVIPNE VMFYEDLSQN LVIDFKPGVP YKLNGEQLLA YIRYRKDSMG DLARIERQKD VLKKLLSKAL SRNPLEISVL YKKISPYIET DIGLPEILTL FSKLKNSVRV SFSTLPYNVD SDGSIFVDEK RLVSFKENLI GSSVQEKYRV NFLVVNTSSL VSRVFEANLR GVWKDRVGFE PDRVVWEDVG ISQKFEGDHV FIGEPEKEDY ILEILRKAHP SRHFTVHRFD RPEDYTMYYT ILESLAKNRI YPDFPVSALI LIDDFRE // ID Q9X225_THEMA Unreviewed; 558 AA. AC Q9X225; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36766.1}; GN OrderedLocusNames=TM_1699 {ECO:0000313|EMBL:AAD36766.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36766.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36766.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36766.1; -; Genomic_DNA. DR PIR; E72220; E72220. DR RefSeq; NP_229499.1; NC_000853.1. DR RefSeq; WP_010865384.1; NC_000853.1. DR ProteinModelPortal; Q9X225; -. DR STRING; 243274.TM1699; -. DR EnsemblBacteria; AAD36766; AAD36766; TM_1699. DR GeneID; 897889; -. DR KEGG; tma:TM1699; -. DR PATRIC; 23938372; VBITheMar51294_1716. DR eggNOG; ENOG4105DW3; Bacteria. DR eggNOG; COG3437; LUCA. DR InParanoid; Q9X225; -. DR OMA; SKHRIER; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1747-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR029016; GAF_dom-like. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR SUPFAM; SSF55781; SSF55781; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 61 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 390 525 HDc. {ECO:0000259|SMART:SM00471}. FT COILED 66 111 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 558 AA; 64553 MW; 1CF587C0DE245CA4 CRC64; MFIKYRRRLL KVTEKMEKLI NLLEISLVVL LSSFSFLEIL KGNLLSLAYP CLVFAVFLSL FRRRWYRNLK NEMNEKSEEM SAMNQELTAL NQQLTAVNQE LEASYESLQI LSTQLARIME TMGEMDLEVD PVPTLERIFY DVKKLVEPLS GLELKNSQRS IVVGEFTENL LYKEAGKTSA KIFVSRELEK DEELFLNSVL NFSLFLLNAH DSYLEVMRNR DTLSRMISSL EEVLDVSRRA ELIEKTLHYL KDMFPGIVLS SVSLLEDGKI KTFFLKNGQI EVVNLKRGIV VKAFETKRDL FVNDVRDFPE FYDVTNGRTR SAAAIFFEYE NTPLVLEIEK DSEITEYELS SLKMMARILA IFFSRLSLYR KLRKTFFQTI EAFSYAVELK DPYTSGHSLR VADYSQEIAR RKGLPDQVVE RIRIAAVLHD IGKIGVKGAI LNKTSKLTKE EYEEVKKHPE LGEKLISKIE DFSDIAKIVR HHHEWYSGQG YPDGLRGEEI PLESRIIAVA DAFDAMTSDR PYRKAMDRKT ALEILRRNEG PQWDPEILKI ALDYFSGL // ID Q9X0B1_THEMA Unreviewed; 426 AA. AC Q9X0B1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36096.1}; GN OrderedLocusNames=TM_1019 {ECO:0000313|EMBL:AAD36096.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36096.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36096.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36096.1; -; Genomic_DNA. DR PIR; C72306; C72306. DR RefSeq; NP_228825.1; NC_000853.1. DR RefSeq; WP_010865244.1; NC_000853.1. DR STRING; 243274.TM1019; -. DR EnsemblBacteria; AAD36096; AAD36096; TM_1019. DR GeneID; 897676; -. DR KEGG; tma:TM1019; -. DR PATRIC; 23936967; VBITheMar51294_1032. DR BioCyc; TMAR243274:GC6P-1048-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 426 AA; 51304 MW; B245565C11E77744 CRC64; MKTSQLIRKI QEKIDEAMSR LNDLESMEIK TEEYLDTFLA LVNNTYKKAE IYNTLVDQWN LLMKQGDEIK RSIEEFKPEY VHHLTEMMKY DGINLLYLRE NEHLRAIGID EIAARTFQEF LKEEELAERS EAFNQAVRKT REQIQQYHMF HYYVSLTDNE LKVDENYRLA GNYYRYSIDF FDKNFPYKSI GISRKLENVP ELLEKFFRLR EKLEGEDPEG DRVRKTLERL YSLSSFDTVE EFNAIIDEWT DLYEAYKQED PFKTNVLSYS YINKDGRTVQ KTYPTYDFLR WLSQRNRKNQ EYILNNYLRR ITDDPTREGY EIRDPSVVLE NRLVEATIKA LPNYKSGIMS EIDSLKKMSR MKRKRKEEEI QKKIMTDPFA AVGAKVPEEI KYWLLRRLDV THPDLYEEWN RITSELQAYL EEVVKQ // ID Q9WZ63_THEMA Unreviewed; 461 AA. AC Q9WZ63; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35679.1}; GN OrderedLocusNames=TM_0594 {ECO:0000313|EMBL:AAD35679.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35679.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35679.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35679.1; -; Genomic_DNA. DR PIR; C72357; C72357. DR RefSeq; NP_228404.1; NC_000853.1. DR RefSeq; WP_010865156.1; NC_000853.1. DR STRING; 243274.TM0594; -. DR DNASU; 897669; -. DR EnsemblBacteria; AAD35679; AAD35679; TM_0594. DR GeneID; 897669; -. DR KEGG; tma:TM0594; -. DR PATRIC; 23936103; VBITheMar51294_0605. DR eggNOG; ENOG4105C7N; Bacteria. DR eggNOG; COG2252; LUCA. DR InParanoid; Q9WZ63; -. DR KO; K06901; -. DR OMA; MVDFFDT; -. DR OrthoDB; EOG6DNT97; -. DR BioCyc; TMAR243274:GC6P-619-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR029940; AzgA. DR InterPro; IPR026033; Pur_Permease_PbuG-like. DR InterPro; IPR006043; Xant/urac/vitC. DR PANTHER; PTHR11119; PTHR11119; 1. DR PANTHER; PTHR11119:SF9; PTHR11119:SF9; 1. DR Pfam; PF00860; Xan_ur_permease; 1. DR PIRSF; PIRSF005353; PbuG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 63 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 104 124 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 148 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 160 184 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 196 215 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 222 241 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 348 367 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 373 390 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 402 431 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 443 459 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 461 AA; 48876 MW; A5190694F3486497 CRC64; MRKSKQSTGS RDPLKFFISE VSCVFRLKEN GTNVKTEIFA GIATFLTMAY IVFVNPSILV QAVGVDASSP LYQQFFGAFM VATILGSATA TLVMAFFANY PFALAPGMGL NAYFTYTVCL GMGIDWRVAL AAVFVEGLIF IGLTLVGFRK FVAGIIPESI KVAISAGIGF FIAFIGLRSA GIVVSNPATS VTLGDLTNPG VLVTVVGLLV IVALYHRKIP GAVMIGILVA TLVGAIPGIG VTKYQGIVGP VPDISPTFMK LDFSGFLSLD FWIVVLTFFF VDFFDTLGTI TGLAQSAGFM KNGELPRANR AFLADAIGTS VGALFGTSTV TTYIESGAGI AEGGRTGLTA LVVALCMLAM LFFAPLAQTV PGYATAPALI FVGALMIGNL GRVKWDDITE ALPAFITVIT MPLTYSIANG IALGIISYAL VKLFSGKSKE VHWFTWILAL AFALWLLFIK H // ID Q9X1G8_THEMA Unreviewed; 94 AA. AC Q9X1G8; G4FFJ2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36525.1}; GN OrderedLocusNames=TM_1457 {ECO:0000313|EMBL:AAD36525.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36525.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36525.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1S12} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=16242963; DOI=10.1016/j.jsb.2005.08.008; RA Shin D.H., Lou Y., Jancarik J., Yokota H., Kim R., Kim S.H.; RT "Crystal structure of TM1457 from Thermotoga maritima."; RL J. Struct. Biol. 152:113-117(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36525.1; -; Genomic_DNA. DR PIR; B72251; B72251. DR RefSeq; NP_229256.1; NC_000853.1. DR RefSeq; WP_004081744.1; NZ_CP011107.1. DR PDB; 1S12; X-ray; 2.00 A; A/B/C/D=1-94. DR PDBsum; 1S12; -. DR ProteinModelPortal; Q9X1G8; -. DR SMR; Q9X1G8; 1-94. DR STRING; 243274.TM1457; -. DR EnsemblBacteria; AAD36525; AAD36525; TM_1457. DR GeneID; 898019; -. DR KEGG; tma:TM1457; -. DR KEGG; tmi:THEMA_07030; -. DR KEGG; tmw:THMA_1487; -. DR PATRIC; 23937866; VBITheMar51294_1471. DR OMA; KLEPCEV; -. DR OrthoDB; EOG64V2GR; -. DR BioCyc; TMAR243274:GC6P-1495-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR007422; Peptidase_C108. DR Pfam; PF04327; Peptidase_C108; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1S12}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DISULFID 62 62 Interchain. {ECO:0000213|PDB:1S12}. SQ SEQUENCE 94 AA; 10540 MW; 6E35DD4A6013204B CRC64; MIKVTVTNSF FEVTGHAPDK TLCASVSLLT QHVANFLKAE KKAKIKKESG YLKVKFEELE NCEVKVLAAM VRSLKELEQK FPSQIRVEVI DNGS // ID Q9WXQ0_THEMA Unreviewed; 581 AA. AC Q9WXQ0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 116. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35137.1}; GN OrderedLocusNames=TM_0043 {ECO:0000313|EMBL:AAD35137.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35137.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35137.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35137.1; -; Genomic_DNA. DR PIR; H72425; H72425. DR RefSeq; NP_227859.1; NC_000853.1. DR RefSeq; WP_010865034.1; NC_000853.1. DR ProteinModelPortal; Q9WXQ0; -. DR STRING; 243274.TM0043; -. DR EnsemblBacteria; AAD35137; AAD35137; TM_0043. DR GeneID; 896867; -. DR KEGG; tma:TM0043; -. DR KEGG; tmi:THEMA_04585; -. DR PATRIC; 23934926; VBITheMar51294_0041. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K06148; -. DR OMA; FASRAHY; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; TMAR243274:GC6P-43-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35137.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35137.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 16 36 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 125 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 137 160 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 166 187 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 244 267 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 21 309 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 342 576 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 581 AA; 66325 MW; 55719E0DCA5D0A05 CRC64; MILSPEKFLL RYAKKYWYLF LVGTVLSLIL TVMEILPPRL MKTAIDKFLV ESTLSSFERL NGIVITAFII LGIRVLSFLV GFASSYVTGY AGSRIVLLMR KDVFSHVISL PYSFFTGIPS GVVTTRIVND TQNIQEFFSS VVTSVIMDVL LLGAVVVSLV QLSRELFGHV YYLLPLIVIS ILLFRYFDRR AYRKVRTNLA RLNAFLAEHI AGINVTKILN LEKHKEREFS TVATEYYRSL MEQLYVFGVF RPLMDFLYFL GVSLVLWYGA RYIANKTLGF GSLYAFVSYL DMFFRPLRDL SEKYDIIQNS MASSEKILNL LKEEPEVIGN PNGPNKISKG RVRFENVWFS YDGKNWVLKD INLDFQPGKL YAIVGETGGG KSTLMSLING LYIPQKGNIF IDEIPLLEYN LKLVRKQIAA VPQDVLLFSG TILDNIRLFD ESIPEERVLE ALKRVHALDI IERLPGGVYY EIVERGTTLS AGERQLIALA RAVLFDAKIF ILDEATSNVD VITETKIQEA LEELSKDRTV IMIAHRLSTV KDVDEIVVVH NGRIVEKGNH YELLEKRGFY YNLYKIQFEN A // ID Q9WZE7_THEMA Unreviewed; 269 AA. AC Q9WZE7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Dehydrase-related protein {ECO:0000313|EMBL:AAD35763.1}; GN OrderedLocusNames=TM_0681 {ECO:0000313|EMBL:AAD35763.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35763.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35763.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35763.1; -; Genomic_DNA. DR PIR; F72347; F72347. DR RefSeq; NP_228490.1; NC_000853.1. DR RefSeq; WP_010865184.1; NC_000853.1. DR ProteinModelPortal; Q9WZE7; -. DR STRING; 243274.TM0681; -. DR EnsemblBacteria; AAD35763; AAD35763; TM_0681. DR GeneID; 898348; -. DR KEGG; tma:TM0681; -. DR KEGG; tmi:THEMA_01260; -. DR PATRIC; 23936280; VBITheMar51294_0693. DR eggNOG; ENOG41087K8; Bacteria. DR eggNOG; COG0491; LUCA. DR OMA; VGCLCAE; -. DR OrthoDB; EOG6PP9MH; -. DR BioCyc; TMAR243274:GC6P-707-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 40 213 Lactamase_B. {ECO:0000259|SMART:SM00849}. SQ SEQUENCE 269 AA; 30736 MW; 2977E1E04CAA85C2 CRC64; MPRKTTSLCR RILLENYTTR GEKMITNLSD RVFVIGTGTS ANSVLVCGKK FCVLFDSTLF PEKARKIKEF AAEILGKEIA VVFNTHYHPD HTFGNEVFDR IISHSLTRKS LEEMDEEYIR KIGVEVSLKF PDETFSEREN YRFGDIVVEA VHLGGHTPDS SIFVLKNEKI VICGDLLTTG IHAEIVTDSD LFGWIEALSE IEKIRADYFV PGHGKVGTIE DVRNMKDYIS KVLRFREGSV KHSELLEDPN FINREHPELL TWGLENIIR // ID Q9WZH7_THEMA Unreviewed; 152 AA. AC Q9WZH7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Purine-binding chemotaxis protein {ECO:0000313|EMBL:AAD35800.1}; GN OrderedLocusNames=TM_0718 {ECO:0000313|EMBL:AAD35800.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35800.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35800.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35800.1; -; Genomic_DNA. DR PIR; D72341; D72341. DR RefSeq; NP_228527.1; NC_000853.1. DR RefSeq; WP_010865191.1; NC_000853.1. DR ProteinModelPortal; Q9WZH7; -. DR STRING; 243274.TM0718; -. DR DNASU; 898385; -. DR EnsemblBacteria; AAD35800; AAD35800; TM_0718. DR GeneID; 898385; -. DR KEGG; tma:TM0718; -. DR PATRIC; 23936356; VBITheMar51294_0731. DR eggNOG; ENOG4108RD3; Bacteria. DR eggNOG; COG0835; LUCA. DR InParanoid; Q9WZH7; -. DR KO; K03408; -. DR OMA; MEKITLI; -. DR OrthoDB; EOG60CWQ7; -. DR BioCyc; TMAR243274:GC6P-744-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro. DR GO; GO:0006935; P:chemotaxis; IEA:InterPro. DR InterPro; IPR002545; CheW. DR Pfam; PF01584; CheW; 1. DR SMART; SM00260; CheW; 1. DR SUPFAM; SSF50341; SSF50341; 1. DR PROSITE; PS50851; CHEW; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 144 CheW-like. {ECO:0000259|PROSITE:PS50851}. SQ SEQUENCE 152 AA; 17066 MW; 37E4CC5E9EA2DCE1 CRC64; MKMELKVVTF KLGNQVFGVD IMKVESIVEV EKIVPVPETA EYIEGVMNLR GKIIPVVNLR KKFKMPDMED KKRAKIIVSM VKNTLIGFLV DDVSEVLTLT ESDIEQPPQN LAGKGKNYIL GLAKVRDDIV IILNIEEVLT SEELVEISNI NV // ID Q9X0F0_THEMA Unreviewed; 436 AA. AC Q9X0F0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36144.1}; GN OrderedLocusNames=TM_1060 {ECO:0000313|EMBL:AAD36144.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36144.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36144.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36144.1; -; Genomic_DNA. DR PIR; G72299; G72299. DR RefSeq; NP_228866.1; NC_000853.1. DR RefSeq; WP_010865256.1; NC_000853.1. DR ProteinModelPortal; Q9X0F0; -. DR STRING; 243274.TM1060; -. DR DNASU; 898503; -. DR EnsemblBacteria; AAD36144; AAD36144; TM_1060. DR GeneID; 898503; -. DR KEGG; tma:TM1060; -. DR KEGG; tmi:THEMA_09060; -. DR PATRIC; 23937049; VBITheMar51294_1073. DR eggNOG; ENOG4108CTN; Bacteria. DR eggNOG; ENOG410YZDA; LUCA. DR OMA; WRIPGLL; -. DR OrthoDB; EOG69WFGP; -. DR BioCyc; TMAR243274:GC6P-1089-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 9 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 161 180 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 212 231 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 243 263 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 275 293 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 299 324 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 336 359 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 365 384 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 436 AA; 48996 MW; 91F514D474FCF804 CRC64; MNISIIEGAL AVLINQFFGG AYLTGYFLWM GASSFFIGLF GSIPFLANTL QLLTLSFSHR LKSRKQIIVP LMWTARTSIL LFAVFPAIKH GLLLAYLLYF YIQIAGALSA PLWQSWMSDL VPKDMIGSYF GFRNLIHGAV QIPAMFLAGA ILDSLGENWK GFGTLFLIAG SLGALNGYFL KIQYEPPYKP REASVSITKA VKFLLKEEHF KNFLFGFAFW NFAIGVGTVY INVMLLKEVE FSYLQISVLN AVGMFIGTLF QPFWGKLGDR YGFQYFLKVC LWIHAIVILL WTLTPRSFLY VFFLQIIIGI FVTAGTSQLV FYTLMYTAPS SLKTEAFSVF NSLSNLSLFA GSLVASVLVA SLENISLPFG ISAIRLTMFI SFFLRASAAY IISRMDLGTP QKVDSLIQAV KESFFSGTVP WIRERLNTLN IFRRKR // ID Q9WXM7_THEMA Unreviewed; 176 AA. AC Q9WXM7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE SubName: Full=NADP-reducing hydrogenase, subunit A {ECO:0000313|EMBL:AAD35106.1}; GN OrderedLocusNames=TM_0012 {ECO:0000313|EMBL:AAD35106.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35106.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35106.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000256|PIRSR:PIRSR000216-1}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|PIRSR:PIRSR000216-1}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35106.1; -; Genomic_DNA. DR PIR; F72430; F72430. DR RefSeq; NP_227828.1; NC_000853.1. DR RefSeq; WP_010865026.1; NC_000853.1. DR ProteinModelPortal; Q9WXM7; -. DR STRING; 243274.TM0012; -. DR EnsemblBacteria; AAD35106; AAD35106; TM_0012. DR GeneID; 896823; -. DR KEGG; tma:TM0012; -. DR PATRIC; 23934864; VBITheMar51294_0010. DR eggNOG; ENOG410902H; Bacteria. DR eggNOG; COG1905; LUCA. DR InParanoid; Q9WXM7; -. DR KO; K00334; -. DR OMA; LRPVYCL; -. DR OrthoDB; EOG689HX9; -. DR BioCyc; TMAR243274:GC6P-12-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central. DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR002023; NuoE-like. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS01099; COMPLEX1_24K; 1. PE 4: Predicted; KW 2Fe-2S {ECO:0000256|PIRSR:PIRSR000216-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|PIRSR:PIRSR000216-1}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR000216-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000216-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT METAL 98 98 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. FT METAL 103 103 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. FT METAL 139 139 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. FT METAL 143 143 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. SQ SEQUENCE 176 AA; 19958 MW; 54EB9ADE69B65895 CRC64; MKKFPINSDQ EVAVLVKSKE ELFKELENFI EENGYEGKKD ALIQVLHKAQ ELFGYLPADV LEYISDKLDV PLSKVYGVVT FYNFFSTKPK GKHQIKVCLG TACYVKGADR IFERFLEELK VNPDEPTSDG MFSVHGVRCL GACSMAPVVM VDEDDFYGRV TPDMVPQIIS KYKREG // ID Q9WYM1_THEMA Unreviewed; 174 AA. AC Q9WYM1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35475.1}; GN OrderedLocusNames=TM_0390 {ECO:0000313|EMBL:AAD35475.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35475.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35475.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35475.1; -; Genomic_DNA. DR PIR; G72381; G72381. DR RefSeq; NP_228200.1; NC_000853.1. DR RefSeq; WP_010865110.1; NC_000853.1. DR EnsemblBacteria; AAD35475; AAD35475; TM_0390. DR GeneID; 897371; -. DR KEGG; tma:TM0390; -. DR BioCyc; TMAR243274:GC6P-404-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 174 AA; 20568 MW; CE4EB47ED7A5512B CRC64; METQTRKHSE QKHNSFNNSL EVWKLCFSYP DFVFVSCFNN SLEVWKPGKT LTYDSATNGF NNSLEVWKHS SEALFKAEFR RFNNSLEVWK HHRARRRTLL LPGFNNSLEV WKLIDFKYDS SHYSGFNNSL EVWKPFVLEL PDACDCTCFN NSLEVWKPHH RGDSLIRCRV SIIP // ID Q9X0B2_THEMA Unreviewed; 608 AA. AC Q9X0B2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36097.1}; GN OrderedLocusNames=TM_1020 {ECO:0000313|EMBL:AAD36097.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36097.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36097.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36097.1; -; Genomic_DNA. DR PIR; D72306; D72306. DR RefSeq; NP_228826.1; NC_000853.1. DR RefSeq; WP_010865245.1; NC_000853.1. DR STRING; 243274.TM1020; -. DR EnsemblBacteria; AAD36097; AAD36097; TM_1020. DR GeneID; 897212; -. DR KEGG; tma:TM1020; -. DR PATRIC; 23936969; VBITheMar51294_1033. DR OrthoDB; EOG67DPG8; -. DR BioCyc; TMAR243274:GC6P-1049-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 608 AA; 71172 MW; F539E738E058120B CRC64; MFRFVILPLL LVASLFFAQL TTYQEVRNDF GMAKDFASLL EIPAEEYSFF VSGASNFLDV LDVSEGISHL KEGNYDKAFE NFSKVGVSQI VNLIPYVNTM LTVLSFSQPF WDRVEKYVFD QRIKEYSQKF VSLKMKELEE ILEEDPLAFK GEDFKRWLET DDSIEVRDFL EDIFVNEGMK HGLYNVGNKV LNERDFASKP WYEKLKKLYL NFSYKAYTVD EVKHFWITQW RRELFKRGAE YVLKRKKEAL NYFLSESTVN ITLKINSPEV FVLTVPELNL SAQVQKEHKI SSSLEDMKSR QITIVLKDLK GNTVYTKVLD EKDLFSRYDP WLSDKKSTYY VKTINIIPTY KRKIVKNLRV QLPEEVKSAT VTIKTQKTDL HVENSPSFSL SDLVLTLDEE IRVEAEIIDS ATETHLMVYE TFVPSSGEIM LDEPKVSKIQ FESEEEYSAY LKELKKEFLE NVDDPNAVKV LRKKLEEAFY AFHANPLARS SFEVIAYSRK FIGDEYRLTD EELLFENLDD EFSSLNQKFQ ETDSEWGKIS YNARNLEHIS SRTLDKGAVI PAYYRYVVQA KEDLPEPERN RRNEKQPGRN SEQILGNFRA SRRTQKEC // ID Q9X0I8_THEMA Unreviewed; 110 AA. AC Q9X0I8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 82. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36180.1}; GN OrderedLocusNames=TM_1104 {ECO:0000313|EMBL:AAD36180.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36180.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36180.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36180.1; -; Genomic_DNA. DR PIR; B72295; B72295. DR RefSeq; NP_228910.1; NC_000853.1. DR RefSeq; WP_010865264.1; NC_000853.1. DR STRING; 243274.TM1104; -. DR EnsemblBacteria; AAD36180; AAD36180; TM_1104. DR GeneID; 898661; -. DR KEGG; tma:TM1104; -. DR KEGG; tmi:THEMA_08825; -. DR PATRIC; 23937141; VBITheMar51294_1119. DR eggNOG; ENOG4105G3Y; Bacteria. DR eggNOG; COG1006; LUCA. DR KO; K05567; -. DR OMA; SMDVMST; -. DR OrthoDB; EOG6CK7RD; -. DR BioCyc; TMAR243274:GC6P-1133-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K. DR Pfam; PF00420; Oxidored_q2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 67 91 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 110 AA; 11779 MW; 4779CAECB0392ACD CRC64; MAERLTLLLV LIGLLGVLIN RDLIKKIISL DIMGTGVVSF FVLISRRQGE AVPIPFQQNS ADPVPQALII TSIVIGFATV ALLVTTASVI ASKYSSVSSD RLDREGGKKE // ID Q9WZT2_THEMA Unreviewed; 323 AA. AC Q9WZT2; G4FCZ9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 96. DE SubName: Full=AstB/chuR-related protein {ECO:0000313|EMBL:AAD35907.1}; GN OrderedLocusNames=TM_0825 {ECO:0000313|EMBL:AAD35907.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35907.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35907.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35907.1; -; Genomic_DNA. DR PIR; E72327; E72327. DR RefSeq; NP_228634.1; NC_000853.1. DR RefSeq; WP_004080828.1; NZ_CP011107.1. DR ProteinModelPortal; Q9WZT2; -. DR STRING; 243274.TM0825; -. DR DNASU; 898495; -. DR EnsemblBacteria; AAD35907; AAD35907; TM_0825. DR GeneID; 898495; -. DR KEGG; tma:TM0825; -. DR KEGG; tmi:THEMA_00515; -. DR KEGG; tmw:THMA_0846; -. DR PATRIC; 23936574; VBITheMar51294_0837. DR eggNOG; ENOG4105EZY; Bacteria. DR eggNOG; COG0535; LUCA. DR OMA; MINTNGS; -. DR OrthoDB; EOG6RNQBW; -. DR BioCyc; TMAR243274:GC6P-854-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF13186; SPASM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|SAAS:SAAS00421379}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|SAAS:SAAS00421379}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00421379}; KW Metal-binding {ECO:0000256|SAAS:SAAS00421379}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00421341}. FT DOMAIN 6 207 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 323 AA; 36895 MW; E5BEE23AE6B9809F CRC64; MRNPPFIVEY ELTLRCNFRC KHCYCEAGKP HLEELSFEEI KELILDMKEL GTWALDIVGG EPLLHPQILD ILAFGKEVGQ RLMINTNGSL ATKEMVQKIK KANPDVLIGV SLEGPDPETN DFVRGTGNFK RAVQGIKNFV DEGFQVTILN VINKRNWRKF EDMVKLALEL GVNALYVDRF IPVGRGMIHA RELDMNPEEW RVAIKHVLGV IENYKNHLTF YVEESISGKP CSAGITHASV LADGTVVPCG HFRYRKEFYM GNVREKKFSE IWHEYTPIPS PASCQQCPIL NECGGGCKAY YLLREHEKDE AICFLNKERY NIK // ID Q9X1E6_THEMA Unreviewed; 479 AA. AC Q9X1E6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36502.1}; GN OrderedLocusNames=TM_1432 {ECO:0000313|EMBL:AAD36502.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36502.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36502.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36502.1; -; Genomic_DNA. DR PIR; E72254; E72254. DR RefSeq; NP_229232.1; NC_000853.1. DR RefSeq; WP_010865341.1; NC_000853.1. DR ProteinModelPortal; Q9X1E6; -. DR STRING; 243274.TM1432; -. DR EnsemblBacteria; AAD36502; AAD36502; TM_1432. DR GeneID; 898043; -. DR KEGG; tma:TM1432; -. DR PATRIC; 23937812; VBITheMar51294_1444. DR eggNOG; ENOG4105D5U; Bacteria. DR eggNOG; COG0579; LUCA. DR InParanoid; Q9X1E6; -. DR KO; K00111; -. DR OMA; CELVSEY; -. DR OrthoDB; EOG6X9MHV; -. DR BioCyc; TMAR243274:GC6P-1470-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF01266; DAO; 1. DR Pfam; PF04324; Fer2_BFD; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 3 354 DAO. {ECO:0000259|Pfam:PF01266}. FT DOMAIN 402 454 Fer2_BFD. {ECO:0000259|Pfam:PF04324}. SQ SEQUENCE 479 AA; 53629 MW; 17CDF55B052D6A35 CRC64; MKAVVIGGGV FGSLIARELT KYDLEVTLIE KNLDVGWGVT KANSAVVHAG YDDPPESVRA QFCASGNAMY EDLSKELDFD FKRIGSFVVA FNDEELKELE RLLKQGEENG VPGLTILERD EVLSMEPNLN PEVKYALYAP TAGITEPWMV AIAAVENAVQ NGLKLVLGES VVGFEKVNGR VRKVHTSRGE YEADIVINCA GLHADEIAKL AGAEYVPLHP RKGEYILLDK KLQGLVKRVI FPTPTKISKG ILVLPTVDGG ILLGPTAEDL PEEMKDRPIT TREGLEKVRE FTRRLVPSLD FSLVVKTFSG LRPESPQKDF FIKVSETVKN FVNVMATRSP GLTAAPAVAK YVVEELIQEK MRIPLEKKKD FKPERKRIVH YSELPLEEWR REIERDPRAG RLVCFCNEVT EKEIVEAIRR GARTLNGVKF RTRAMFGRCQ GGFCMARILK ILERELGVDM SEIKMKSENS WVVNGKVRE // ID Q9WYM7_THEMA Unreviewed; 152 AA. AC Q9WYM7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 89. DE SubName: Full=Iron-sulfur cluster-binding protein {ECO:0000313|EMBL:AAD35481.1}; GN OrderedLocusNames=TM_0396 {ECO:0000313|EMBL:AAD35481.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35481.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35481.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35481.1; -; Genomic_DNA. DR PIR; E72382; E72382. DR RefSeq; NP_228206.1; NC_000853.1. DR RefSeq; WP_010865112.1; NC_000853.1. DR ProteinModelPortal; Q9WYM7; -. DR STRING; 243274.TM0396; -. DR EnsemblBacteria; AAD35481; AAD35481; TM_0396. DR GeneID; 897388; -. DR KEGG; tma:TM0396; -. DR PATRIC; 23935673; VBITheMar51294_0401. DR eggNOG; ENOG4108E2D; Bacteria. DR eggNOG; COG1142; LUCA. DR InParanoid; Q9WYM7; -. DR KO; K00196; -. DR OMA; MACAECE; -. DR OrthoDB; EOG6XSZQF; -. DR BioCyc; TMAR243274:GC6P-410-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GOC. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF13247; Fer4_11; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 6 35 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 54 86 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 88 117 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 152 AA; 16905 MW; B2564D10B8451EE0 CRC64; MVIAVRRILI REEYCMGCKL CEINCVAAQV GTGNLIKVYR YVPELPEPNV IVEEHDYVTF ALQCRNCDDP SCLKACMTGA MHRDPKTGAI RVNQEKCVGC WMCVMACPFG VIRRNTKEKK VASKCDLCAD RGTPGCVEGC PNEALVLVEV RE // ID Q9X0J3_THEMA Unreviewed; 240 AA. AC Q9X0J3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 74. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36185.1}; GN OrderedLocusNames=TM_1109 {ECO:0000313|EMBL:AAD36185.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36185.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36185.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36185.1; -; Genomic_DNA. DR PIR; G72295; G72295. DR RefSeq; NP_228915.1; NC_000853.1. DR RefSeq; WP_010865265.1; NC_000853.1. DR ProteinModelPortal; Q9X0J3; -. DR STRING; 243274.TM1109; -. DR DNASU; 898656; -. DR EnsemblBacteria; AAD36185; AAD36185; TM_1109. DR GeneID; 898656; -. DR KEGG; tma:TM1109; -. DR PATRIC; 23937151; VBITheMar51294_1124. DR eggNOG; ENOG410661Q; Bacteria. DR eggNOG; ENOG41123BK; LUCA. DR KO; K07242; -. DR OMA; RDGSYHI; -. DR OrthoDB; EOG6F55FT; -. DR BioCyc; TMAR243274:GC6P-1138-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR025383; DUF4040. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR Pfam; PF13244; DUF4040; 1. DR Pfam; PF00497; SBP_bac_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 44 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 68 87 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 26 89 DUF4040. {ECO:0000259|Pfam:PF13244}. FT DOMAIN 110 158 PBPb. {ECO:0000259|Pfam:PF00497}. SQ SEQUENCE 240 AA; 27806 MW; FCCC716FFF330ED2 CRC64; MGAFRFTRYS AHVHGGIVLI ENLVLILMVS VSLYTIFTPI RLNAVIGRTA LSVLAVLLYT LFSSPDVAIA EALLGALLTT LVYLIALKSR DRVKIGFTSV RLLFEKLGEA FMGFEYELLK RFCEKYDYRS EFVEFSSLED LLEALNDGKV DVACGGVFSE DKKGYLETKI FYLEDEKLDL LRYTERVYRG ERLNHVLHRD GSYHILFADE ELRMRFREFL RTEREFVEEL KKKYFGEEIG // ID Q9WYH3_THEMA Unreviewed; 35 AA. AC Q9WYH3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35425.1}; GN OrderedLocusNames=TM_0338 {ECO:0000313|EMBL:AAD35425.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35425.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35425.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35425.1; -; Genomic_DNA. DR PIR; H72387; H72387. DR RefSeq; NP_228149.1; NC_000853.1. DR RefSeq; WP_010865098.1; NZ_CP011107.1. DR STRING; 243274.TM0338; -. DR EnsemblBacteria; AAD35425; AAD35425; TM_0338. DR GeneID; 897294; -. DR KEGG; tma:TM0338; -. DR KEGG; tmi:THEMA_03025; -. DR KEGG; tmw:THMA_0346; -. DR OrthoDB; EOG6BGPBB; -. DR BioCyc; TMAR243274:GC6P-352-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 35 AA; 4173 MW; 0AB654CEBC6C8646 CRC64; MRIILKKEVR KMFVLIPVDV LIAIHSEKIG QKRNR // ID Q9WZA9_THEMA Unreviewed; 217 AA. AC Q9WZA9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35725.1}; GN OrderedLocusNames=TM_0641 {ECO:0000313|EMBL:AAD35725.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35725.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35725.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35725.1; -; Genomic_DNA. DR PIR; H72350; H72350. DR RefSeq; NP_228450.1; NC_000853.1. DR RefSeq; WP_010865172.1; NC_000853.1. DR STRING; 243274.TM0641; -. DR DNASU; 897744; -. DR EnsemblBacteria; AAD35725; AAD35725; TM_0641. DR GeneID; 897744; -. DR KEGG; tma:TM0641; -. DR PATRIC; 23936196; VBITheMar51294_0651. DR BioCyc; TMAR243274:GC6P-666-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 217 AA; 24783 MW; E433E958191255EC CRC64; MKLSRSAGEK MRWPVFLFVM LSCVLFSEPL VTQMSPQFVY ESLESKEALP GVLPVPSGEK GNGISFRVSP FFYSGNFEGK TKTGWFVLSD PPWENFYLYE NTPPLFSVIL EGNVGDLSFY TEIPFNNNYN YFYKESLNNI PPLWKEIASP DSNFPYTAYG VYDGDSFYAV IGRSKIRWGS SEFPVAISDV SPISITSRFL QKERSSTRSI LYRSTRF // ID Q9X0E7_THEMA Unreviewed; 363 AA. AC Q9X0E7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Potassium channel, putative {ECO:0000313|EMBL:AAD36134.1}; GN OrderedLocusNames=TM_1057 {ECO:0000313|EMBL:AAD36134.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36134.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36134.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36134.1; -; Genomic_DNA. DR PIR; C72302; C72302. DR RefSeq; NP_228863.1; NC_000853.1. DR RefSeq; WP_010865254.1; NC_000853.1. DR ProteinModelPortal; Q9X0E7; -. DR STRING; 243274.TM1057; -. DR EnsemblBacteria; AAD36134; AAD36134; TM_1057. DR GeneID; 898305; -. DR KEGG; tma:TM1057; -. DR PATRIC; 23937043; VBITheMar51294_1070. DR eggNOG; ENOG4107Y6M; Bacteria. DR eggNOG; COG1226; LUCA. DR InParanoid; Q9X0E7; -. DR KO; K10716; -. DR OMA; GIHIAKG; -. DR OrthoDB; EOG654P17; -. DR BioCyc; TMAR243274:GC6P-1086-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro. DR Gene3D; 3.30.70.1450; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR013099; K_chnl_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006037; RCK_C. DR InterPro; IPR003148; RCK_N. DR Pfam; PF07885; Ion_trans_2; 1. DR Pfam; PF02080; TrkA_C; 1. DR Pfam; PF02254; TrkA_N; 1. DR SUPFAM; SSF116726; SSF116726; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS51202; RCK_C; 1. DR PROSITE; PS51201; RCK_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Ion channel {ECO:0000313|EMBL:AAD36134.1}; KW Ion transport {ECO:0000313|EMBL:AAD36134.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000313|EMBL:AAD36134.1}. FT TRANSMEM 36 57 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 87 107 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 138 262 RCK N-terminal. FT {ECO:0000259|PROSITE:PS51201}. FT DOMAIN 278 362 RCK C-terminal. FT {ECO:0000259|PROSITE:PS51202}. SQ SEQUENCE 363 AA; 40459 MW; 0D4DF93BD28ECE9E CRC64; MPEILINYKT NREDYKRQSK YCNICMRRYK SVKKNVIILA LMIVFVFVFG TVAFHLIEGW NLFDSFFFTL ITVSTVGYSI PENLSQAGKV IASILISAGV TIVLYGFTSV TSMIVEGHIG EYFKSRRMRK MIDRLKDHFI VVGAGRTGRH TTLEIMKAKK PFVVIDQSEE AIARLKDFLG EEFPYVVGDA TEEEILMKAG VERARSLVVT LPDDAKSTFV VLTAKSLNPN LEIVSRVSDM KALSKLVYAG ADKVIATSEL AGVRLAQMAL NPTTISFLDI LSFGEESFRI EEVVIPPESP VANKTLGEIN LAKRAGTIVI AIRRGGEVIF NPTGDTKILP EDRLMVVGKS DHFEKLHRLI EEG // ID Q9X2C5_THEMA Unreviewed; 272 AA. AC Q9X2C5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36868.1}; GN OrderedLocusNames=TM_1805 {ECO:0000313|EMBL:AAD36868.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36868.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36868.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36868.1; -; Genomic_DNA. DR PIR; B72208; B72208. DR RefSeq; NP_229602.1; NC_000853.1. DR RefSeq; WP_010865406.1; NC_000853.1. DR STRING; 243274.TM1805; -. DR EnsemblBacteria; AAD36868; AAD36868; TM_1805. DR GeneID; 897832; -. DR KEGG; tma:TM1805; -. DR KEGG; tmi:THEMA_05165; -. DR PATRIC; 23938599; VBITheMar51294_1826. DR OMA; KAYYCGL; -. DR BioCyc; TMAR243274:GC6P-1856-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 272 AA; 31893 MW; 12757A18238EB681 CRC64; MMFGYIKPLK CELKVKEYEE FRGYYCGVCK ALKKYSIIPR FLLTYEAASL GLLLSSLNNS DLKRKKELCI FTLKKVDFYS SSEIDEVARV FTALLREKLK DNYIDRKNPV YLFASAFLKK DPEISSLFEN FYEMEKKEQD FKILAEEQGK IVGTILSKMV KEETQRKILY YLGLSLGKWL YIVDALDDFE KDKRKNVFNP LVKKYNGDLE KARSELRPHL KKCIDEMWKA YDLLDIKRNK TILDNIVYLG IPFITENVLV GKTCNLNHST IL // ID Q9S5X7_THEMA Unreviewed; 164 AA. AC Q9S5X7; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Fe-hydrogenase, subunit gamma {ECO:0000313|EMBL:AAD36494.1}; GN OrderedLocusNames=TM_1424 {ECO:0000313|EMBL:AAD36494.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36494.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36494.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000256|PIRSR:PIRSR000216-1}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|PIRSR:PIRSR000216-1}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36494.1; -; Genomic_DNA. DR PIR; E72256; E72256. DR RefSeq; NP_229224.1; NC_000853.1. DR RefSeq; WP_010865339.1; NC_000853.1. DR ProteinModelPortal; Q9S5X7; -. DR STRING; 243274.TM1424; -. DR EnsemblBacteria; AAD36494; AAD36494; TM_1424. DR GeneID; 898051; -. DR KEGG; tma:TM1424; -. DR PATRIC; 23937796; VBITheMar51294_1436. DR eggNOG; ENOG410902H; Bacteria. DR eggNOG; COG1905; LUCA. DR InParanoid; Q9S5X7; -. DR KO; K17999; -. DR OMA; VIRVCRG; -. DR OrthoDB; EOG689HX9; -. DR BioCyc; TMAR243274:GC6P-1462-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central. DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR002023; NuoE-like. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS01099; COMPLEX1_24K; 1. PE 4: Predicted; KW 2Fe-2S {ECO:0000256|PIRSR:PIRSR000216-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Iron {ECO:0000256|PIRSR:PIRSR000216-1}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR000216-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000216-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT METAL 81 81 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. FT METAL 86 86 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. FT METAL 122 122 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. FT METAL 126 126 Iron-sulfur (2Fe-2S). FT {ECO:0000256|PIRSR:PIRSR000216-1}. SQ SEQUENCE 164 AA; 18324 MW; 7385B6BD26B3832A CRC64; MLALERHFEK VEEILKKYGY KRENLIKILL EIQEIYRYLP EDVINYVSTA MGIPPAKIYG VATFYAQFSL KPKGKYTIMV CDGTACHMAG SPEVLKAIEE ETGLTPGNVT EDLMFSLDQV GCLGACALAP VMVINGEVYG NLTADKVKEI LRKIKEKERE SANV // ID Q9WZQ0_THEMA Unreviewed; 260 AA. AC Q9WZQ0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 104. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD35875.1}; GN OrderedLocusNames=TM_0793 {ECO:0000313|EMBL:AAD35875.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35875.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35875.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35875.1; -; Genomic_DNA. DR PIR; B72334; B72334. DR RefSeq; NP_228602.1; NC_000853.1. DR RefSeq; WP_010865206.1; NC_000853.1. DR ProteinModelPortal; Q9WZQ0; -. DR STRING; 243274.TM0793; -. DR EnsemblBacteria; AAD35875; AAD35875; TM_0793. DR GeneID; 898461; -. DR KEGG; tma:TM0793; -. DR PATRIC; 23936506; VBITheMar51294_0805. DR eggNOG; ENOG4105CJ1; Bacteria. DR eggNOG; COG1131; LUCA. DR InParanoid; Q9WZQ0; -. DR KO; K01990; -. DR OMA; CESAAKT; -. DR OrthoDB; EOG65J54C; -. DR BioCyc; TMAR243274:GC6P-820-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35875.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD35875.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 12 241 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 260 AA; 29253 MW; 06DDBB9AEDD3D9F8 CRC64; MDSERRELIS LIVARGLTRK FGDFTAVDHI DLSVRPGEIY GFLGPNGAGK TTTIKMLTGV LKPTEGEVEI LGMKMSTHEI EIKKSIGVIP DEPKIYSHLT GKEFLDFIIE IYDLKEEEID KRIAELCEAF KVDYLGKRVG EMSHGMKQKL MLVSVFMRKP KVIFLDEPTV GLDAKSARIL KLLLRKYADE GAAIFLTTHI LEIAEKMCDR IGIINKGRLI AEGTMEELRK LAGQKEASLE DLFLQLTAEG EEIEEIIKEL // ID Q9X0S0_THEMA Unreviewed; 374 AA. AC Q9X0S0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36263.1}; GN OrderedLocusNames=TM_1188 {ECO:0000313|EMBL:AAD36263.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36263.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36263.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36263.1; -; Genomic_DNA. DR PIR; B72285; B72285. DR RefSeq; NP_228993.1; NC_000853.1. DR RefSeq; WP_010865278.1; NC_000853.1. DR STRING; 243274.TM1188; -. DR EnsemblBacteria; AAD36263; AAD36263; TM_1188. DR GeneID; 898297; -. DR KEGG; tma:TM1188; -. DR PATRIC; 23937316; VBITheMar51294_1206. DR OMA; AFMEILL; -. DR OrthoDB; EOG6SFP7F; -. DR BioCyc; TMAR243274:GC6P-1217-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro. DR InterPro; IPR002656; Acyl_transf_3. DR Pfam; PF01757; Acyl_transf_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 60 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 84 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 176 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 183 203 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248 266 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 278 297 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 309 329 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 341 359 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 39 355 Acyl_transf_3. FT {ECO:0000259|Pfam:PF01757}. SQ SEQUENCE 374 AA; 43805 MW; 889D7ADFF40F485A CRC64; MKGESFASTK NRTRYSRAKC LFFKFFTPFD TILAEVGQLE SLRGLLILFV LTGHAIVGVY RDLTFLVPLL RFVSPSVFVF VYLFGYSQGR VKKNPLKILQ KASSFFHFYL FWASLSFLAY VLLDGEYTNV WVTKRVFSVD DSILKKYLIT IFSFTGSWQY YFVLVVMILL LISIFIKDPR KILPFSFAGA VVNSSFVSFW FLTKNRLLPP IEGALITYLN PVHWLFPFLM GYKDAVERKK REPRKLSLFL YVFLFAIGSL EYWNAYGKFH TLLGVDQFSL TGVLLGIYSI EVFTWLAEKV NLPFLKRMGR YSFLLFMIHM PFQWMFYVFL DSFVDLPEWC WVIIMVMFSL IFMEILLKLS RILPKPVRKI VIGA // ID Q9WY39_THEMA Unreviewed; 156 AA. AC Q9WY39; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 76. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35288.1}; GN OrderedLocusNames=TM_0196 {ECO:0000313|EMBL:AAD35288.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35288.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35288.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35288.1; -; Genomic_DNA. DR PIR; D72407; D72407. DR RefSeq; NP_228011.1; NC_000853.1. DR RefSeq; WP_010865071.1; NC_000853.1. DR ProteinModelPortal; Q9WY39; -. DR SMR; Q9WY39; 3-150. DR EnsemblBacteria; AAD35288; AAD35288; TM_0196. DR GeneID; 897066; -. DR KEGG; tma:TM0196; -. DR PATRIC; 23935262; VBITheMar51294_0197. DR eggNOG; ENOG4108SM2; Bacteria. DR eggNOG; COG1839; LUCA. DR InParanoid; Q9WY39; -. DR KO; K09129; -. DR OMA; IAFCEAS; -. DR OrthoDB; EOG6BPDGX; -. DR BioCyc; TMAR243274:GC6P-209-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.40.1520.10; -; 1. DR InterPro; IPR007153; Adenosine_kinase. DR Pfam; PF04008; Adenosine_kin; 1. DR SUPFAM; SSF103165; SSF103165; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 156 AA; 17334 MW; FC613AD2321FEB3C CRC64; MDVSIPENAN IILGHSHFIK TVEDLYEVMV TTNPNLKFGI AFNEASGPCL IRYEGNDEEL VNQAIETAKK IGAGHTFVIY IRGGYPINIL NQIKNVQEVC RIYTATANPL QVIVGITSQG RAVLGVVDGY SPKGVEGEED KRKRHAFLRE ITKYKK // ID Q9X0G0_THEMA Unreviewed; 383 AA. AC Q9X0G0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Sugar isomerase {ECO:0000313|EMBL:AAD36148.1}; GN OrderedLocusNames=TM_1071 {ECO:0000313|EMBL:AAD36148.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36148.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36148.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: L-rhamnopyranose = L-rhamnulose. CC {ECO:0000256|SAAS:SAAS00064888}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00064880}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36148.1; -; Genomic_DNA. DR PIR; A72299; A72299. DR RefSeq; NP_228877.1; NC_000853.1. DR RefSeq; WP_010865259.1; NC_000853.1. DR ProteinModelPortal; Q9X0G0; -. DR STRING; 243274.TM1071; -. DR EnsemblBacteria; AAD36148; AAD36148; TM_1071. DR GeneID; 897104; -. DR KEGG; tma:TM1071; -. DR KEGG; tmi:THEMA_09005; -. DR PATRIC; 23937071; VBITheMar51294_1084. DR eggNOG; ENOG4105C9F; Bacteria. DR eggNOG; COG4952; LUCA. DR KO; K01820; -. DR OMA; MIDQSHN; -. DR OrthoDB; EOG62C9B4; -. DR BioCyc; TMAR243274:GC6P-1100-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008740; F:L-rhamnose isomerase activity; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0019324; P:L-lyxose metabolic process; IBA:GO_Central. DR GO; GO:0019301; P:rhamnose catabolic process; IBA:GO_Central. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR013457; Rhamnose_iso-rel. DR InterPro; IPR009308; Rhamnose_isomerase. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF06134; RhaA; 1. DR SUPFAM; SSF51658; SSF51658; 1. DR TIGRFAMs; TIGR02635; RhaI_grampos; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00448652}; KW Isomerase {ECO:0000256|SAAS:SAAS00448650, KW ECO:0000313|EMBL:AAD36148.1}; KW Manganese {ECO:0000256|SAAS:SAAS00448655}; KW Metal-binding {ECO:0000256|SAAS:SAAS00448649}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Rhamnose metabolism {ECO:0000256|SAAS:SAAS00448653}. SQ SEQUENCE 383 AA; 44732 MW; 9AD3E7CEFDA95752 CRC64; MINMERIFKE LDELKFELPS WAFSDAGTRF AVFHEEGAAR NVFERIEDAA LVHRLTGCCP SVALHIPWDK VENWEELREF AEEKGLKIGA INPNLFQDPD YKYGSLTNPS EKIRKKAIAH VMECVDIAEK TGSKVISLWL ADGTDYPGQD DFRSRKKRLE ESLRYIYENM PADMYLLIEY KFFEPAFYHT DIPDWGMSYL LSEKLGERAL VLVDLGHHPQ GTNIEYIVAT LLSEKKLGGF HLNNRKYADD DLTIASINPY EVFLIFKEIV FAKRDPELSD SAKKVVLMFD QAHITKPKIL AMIQSVLIAQ ELFTKALLID ENRLREAQKN YDVVEAEEIL LDAFRTDVRP ILREYRRQKG LPEDPLRVFR EEDYMEKRRR ERR // ID Q9WXZ1_THEMA Unreviewed; 118 AA. AC Q9WXZ1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35237.1}; GN OrderedLocusNames=TM_0144 {ECO:0000313|EMBL:AAD35237.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35237.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35237.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35237.1; -; Genomic_DNA. DR PIR; F72411; F72411. DR RefSeq; NP_227959.1; NC_000853.1. DR RefSeq; WP_010865060.1; NC_000853.1. DR STRING; 243274.TM0144; -. DR EnsemblBacteria; AAD35237; AAD35237; TM_0144. DR GeneID; 896974; -. DR KEGG; tma:TM0144; -. DR PATRIC; 23935132; VBITheMar51294_0143. DR eggNOG; ENOG41085GH; Bacteria. DR eggNOG; COG2331; LUCA. DR InParanoid; Q9WXZ1; -. DR OMA; CERGHIF; -. DR OrthoDB; EOG60KN7T; -. DR BioCyc; TMAR243274:GC6P-144-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR013429; Regulatory_FmdB_Zinc_ribbon. DR Pfam; PF09723; Zn-ribbon_8; 1. DR SMART; SM00834; CxxC_CXXC_SSSS; 1. DR TIGRFAMs; TIGR02605; CxxC_CxxC_SSSS; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 44 84 CxxC_CXXC_SSSS. FT {ECO:0000259|SMART:SM00834}. SQ SEQUENCE 118 AA; 13086 MW; 9E9B93386893618C CRC64; MDRGVAQVAS APALGAGGRW FKSSRPDHFF IEVDKALLKE VKDMPIYRYV CEECGYETTV MHGINESPEV ICEECGAKMK RTIGRVGIIF KGSGFYITDS RKSEKKKEAA SASSEKKD // ID Q9X269_THEMA Unreviewed; 341 AA. AC Q9X269; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 87. DE SubName: Full=Oligopeptide ABC transporter, permease protein {ECO:0000313|EMBL:AAD36812.1}; GN OrderedLocusNames=TM_1747 {ECO:0000313|EMBL:AAD36812.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36812.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36812.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36812.1; -; Genomic_DNA. DR PIR; F72215; F72215. DR RefSeq; NP_229545.1; NC_000853.1. DR RefSeq; WP_010865393.1; NC_000853.1. DR STRING; 243274.TM1747; -. DR TCDB; 3.A.1.5.15; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36812; AAD36812; TM_1747. DR GeneID; 897865; -. DR KEGG; tma:TM1747; -. DR PATRIC; 23938470; VBITheMar51294_1765. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR InParanoid; Q9X269; -. DR KO; K02033; -. DR OMA; TACYLLL; -. DR OrthoDB; EOG66F098; -. DR BioCyc; TMAR243274:GC6P-1795-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015421; F:oligopeptide-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0042937; F:tripeptide transporter activity; IBA:GO_Central. DR GO; GO:0035672; P:oligopeptide transmembrane transport; IBA:GO_Central. DR GO; GO:0042939; P:tripeptide transport; IBA:GOC. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 32 53 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 134 157 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 169 197 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 209 227 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 264 284 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 314 334 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 130 327 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 341 AA; 37977 MW; 2ECFFF333B0FF8B0 CRC64; MNSEPWDFPG LLLNMSNGVV DMRFLKFLLK RLLTIAISMV VVIVITYVLM WLAPGNFFEL QRVRDAIARV TTPDDPAYQA TLKGFEERYG LNNPLWKQIL MYLKGAVVFK FGPSFSDPAR NIEDLIKEKF PITFTLALSS ILFALVVGVP LGILAALKKN TWIDYTAMTV SVIGVAIPSY VVAVFLILIF SIYLGWLPTS GWEGIRTKIL PTIALALGPL ASVARFTRVS LLDTLNQDFI RTAYAKGGDD RTVIMKHALR PSMIPLVTIV GPQMAYLMVG TVWVENIFRI PGLGQLFANA AVTRDYPLLV TSTFILALTV MIMNLIVDVL YAILDPRIKL D // ID Q9X2B1_THEMA Unreviewed; 244 AA. AC Q9X2B1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36854.1}; GN OrderedLocusNames=TM_1791 {ECO:0000313|EMBL:AAD36854.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36854.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36854.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36854.1; -; Genomic_DNA. DR PIR; D72209; D72209. DR RefSeq; NP_229588.1; NC_000853.1. DR RefSeq; WP_010865404.1; NC_000853.1. DR STRING; 243274.TM1791; -. DR EnsemblBacteria; AAD36854; AAD36854; TM_1791. DR GeneID; 897839; -. DR KEGG; tma:TM1791; -. DR PATRIC; 23938569; VBITheMar51294_1811. DR eggNOG; ENOG41083A9; Bacteria. DR eggNOG; COG1604; LUCA. DR InParanoid; Q9X2B1; -. DR KO; K19142; -. DR OMA; YESLAHI; -. DR OrthoDB; EOG6JQH2G; -. DR BioCyc; TMAR243274:GC6P-1842-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR010172; CRISPR-assoc_prot_TM1791. DR InterPro; IPR005537; RAMP_III_fam. DR Pfam; PF03787; RAMPs; 1. DR TIGRFAMs; TIGR01898; cas_TM1791_cmr6; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 244 AA; 27927 MW; 72F4899110593179 CRC64; MVKRMKLPES KNLSLYWEKY SFLLLEGSNS KDKEIVSKIF QTVEKLQSDF GKISSILKER REQLIKKRKP FINLKMRVKG KLLLGAGNPS SIEVGITLSR NYGLPIIPGT AVKGAFASFL FEFERDKYES LAHIFGDTER EGDLIFLDAI PVSDLKFSLD IVNPHFQPYY MKEKLPPNDW YDPVPIKYLV VSSGVFWFTV LESRSGVIGN SEKELIKQRF VEMLKAYGLG AKTSYGYGRF EEPS // ID Q9X141_THEMA Unreviewed; 57 AA. AC Q9X141; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36389.1}; GN OrderedLocusNames=TM_1315 {ECO:0000313|EMBL:AAD36389.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36389.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36389.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36389.1; -; Genomic_DNA. DR PIR; C72268; C72268. DR RefSeq; NP_229119.1; NC_000853.1. DR RefSeq; WP_010865308.1; NZ_CP011107.1. DR STRING; 243274.TM1315; -. DR EnsemblBacteria; AAD36389; AAD36389; TM_1315. DR GeneID; 898167; -. DR KEGG; tma:TM1315; -. DR KEGG; tmi:THEMA_07770; -. DR KEGG; tmw:THMA_1339; -. DR PATRIC; 23937566; VBITheMar51294_1329. DR eggNOG; ENOG4108E69; Bacteria. DR eggNOG; ENOG41103HT; LUCA. DR OrthoDB; EOG6S52S9; -. DR BioCyc; TMAR243274:GC6P-1346-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 57 AA; 6570 MW; AE55C94551F6E342 CRC64; MKIVRRIILT IVILLSLLYT LVFPSPSDDY QTTVRKKTVV HTFLIEKLHS EDLTVGN // ID Q9WY86_THEMA Unreviewed; 451 AA. AC Q9WY86; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 114. DE RecName: Full=Electron transport complex subunit C {ECO:0000256|HAMAP-Rule:MF_00461}; GN OrderedLocusNames=TM_0244 {ECO:0000313|EMBL:AAD35335.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35335.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35335.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000256|HAMAP-Rule:MF_00461}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00461}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00461}; CC -!- SUBUNIT: Composed of six subunits. {ECO:0000256|HAMAP- CC Rule:MF_00461}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00461}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00461}. CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. CC RnfC subfamily. {ECO:0000256|HAMAP-Rule:MF_00461}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000256|HAMAP-Rule:MF_00461}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35335.1; -; Genomic_DNA. DR PIR; E72398; E72398. DR RefSeq; NP_228058.1; NC_000853.1. DR RefSeq; WP_010865079.1; NC_000853.1. DR ProteinModelPortal; Q9WY86; -. DR STRING; 243274.TM0244; -. DR DNASU; 897146; -. DR EnsemblBacteria; AAD35335; AAD35335; TM_0244. DR GeneID; 897146; -. DR KEGG; tma:TM0244; -. DR PATRIC; 23935363; VBITheMar51294_0247. DR eggNOG; ENOG4107QTR; Bacteria. DR eggNOG; COG4656; LUCA. DR InParanoid; Q9WY86; -. DR KO; K03615; -. DR OMA; FGGPMMG; -. DR OrthoDB; EOG6W45RX; -. DR BioCyc; TMAR243274:GC6P-257-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IBA:GO_Central. DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central. DR HAMAP; MF_00461; RsxC_RnfC; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR010208; Elect_transpt_RnfC/RsxC. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR011538; Nuo51_FMN-bd. DR InterPro; IPR026902; RnfC_N. DR InterPro; IPR019554; Soluble_ligand-bd. DR Pfam; PF01512; Complex1_51K; 1. DR Pfam; PF13237; Fer4_10; 1. DR Pfam; PF13375; RnfC_N; 1. DR Pfam; PF10531; SLBB; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR TIGRFAMs; TIGR01945; rnfC; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00461, KW ECO:0000256|SAAS:SAAS00445598}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00461}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00461}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00461}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00461, ECO:0000256|SAAS:SAAS00445598}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00461, KW ECO:0000256|SAAS:SAAS00445598}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00461}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00461, KW ECO:0000256|SAAS:SAAS00445598}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_00461}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00461}. FT DOMAIN 366 397 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 366 397 4Fe-4S ferredoxin-type 1. FT {ECO:0000256|HAMAP-Rule:MF_00461}. FT DOMAIN 405 436 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. FT DOMAIN 405 436 4Fe-4S ferredoxin-type 2. FT {ECO:0000256|HAMAP-Rule:MF_00461}. FT METAL 377 377 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00461}. FT METAL 380 380 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00461}. FT METAL 383 383 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00461}. FT METAL 387 387 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00461}. FT METAL 416 416 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00461}. FT METAL 419 419 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00461}. FT METAL 422 422 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00461}. FT METAL 426 426 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00461}. SQ SEQUENCE 451 AA; 49515 MW; 7B2D7272CFC6E418 CRC64; MKAQEVPSTT FTGGETVLTF KGGVHPPELK EWSKDKPIER APLPQKVFVF LSNHAGNPAK PVVSPGDEVK TGQVIGEPEG FISAYLHSPV TGRVLEIKKI LHPILGKPIE AIVIERTSDD EWVHIETGDF ERMSKEEILE IIKKAGIVGL GGAMFPTHVK LSPPPEKKVD TLIVNGAECE PVLTIDHRLM LERAEDILQG ILIMMKVLGV QKAVVGVESN KMDAYHNLKK VFKGYPVDVA LLRTKYPQGA EKQLIYAITG RMVPRGGLPM DVGVVVQNVG TCVAVKEAVV DGKPLVERGM TVSGDAVKNQ KNLIVRIGTP VKDVIDYCGG IDENTERVIL GGPMMGISIT NLDIPVMKGT SGITAFLPKK SRPQKPCIRC SECVQVCPMN LQPYLLYLLS TKRKYDEAVE NGLMDCIECG SCTYTCPSKI EHVRYIKLAK TVYRATRRGR R // ID Q9WZ91_THEMA Unreviewed; 79 AA. AC Q9WZ91; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35707.1}; GN OrderedLocusNames=TM_0623 {ECO:0000313|EMBL:AAD35707.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35707.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35707.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35707.1; -; Genomic_DNA. DR PIR; F72354; F72354. DR RefSeq; NP_228432.1; NC_000853.1. DR RefSeq; WP_010865168.1; NZ_CP011107.1. DR STRING; 243274.TM0623; -. DR DNASU; 897710; -. DR EnsemblBacteria; AAD35707; AAD35707; TM_0623. DR GeneID; 897710; -. DR KEGG; tma:TM0623; -. DR KEGG; tmi:THEMA_01545; -. DR KEGG; tmw:THMA_0639; -. DR PATRIC; 23936159; VBITheMar51294_0633. DR OMA; TLSECVE; -. DR OrthoDB; EOG6XM7MW; -. DR BioCyc; TMAR243274:GC6P-648-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 79 AA; 8667 MW; 4C257745E17F8AB7 CRC64; MTAGSSRDDK IVPCGSPAAG GVEKLVTDLA GFSDRSKFEV SVLNVIQDTY WPEEEMLTET SIKVYTTDMT LSECVETER // ID Q9WYW1_THEMA Unreviewed; 204 AA. AC Q9WYW1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35576.1}; GN OrderedLocusNames=TM_0491 {ECO:0000313|EMBL:AAD35576.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35576.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35576.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35576.1; -; Genomic_DNA. DR PIR; B72370; B72370. DR RefSeq; NP_228301.1; NC_000853.1. DR RefSeq; WP_010865134.1; NC_000853.1. DR STRING; 243274.TM0491; -. DR EnsemblBacteria; AAD35576; AAD35576; TM_0491. DR GeneID; 897532; -. DR KEGG; tma:TM0491; -. DR KEGG; tmi:THEMA_02215; -. DR PATRIC; 23935887; VBITheMar51294_0498. DR eggNOG; ENOG4105TB5; Bacteria. DR eggNOG; ENOG411212U; LUCA. DR OMA; PTERENN; -. DR OrthoDB; EOG6BS8QZ; -. DR BioCyc; TMAR243274:GC6P-515-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032604; DUF4897. DR Pfam; PF16238; DUF4897; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 9 29 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 204 AA; 23110 MW; D70CA83DD5C1886E CRC64; MKRLSSRTIY ILLIIMVVFM LVEFLFFFLG GRAPFEIVYY RSTMEYDYSG NATFTTSAKL YFKDEKKKEE YKINYASASK EELNKYFSQI SKEVGREIVP LDYNVRVEDT GGMLEVTETT LLRGAAQVKG DVLDTSMGSL TMNVAGETEI VVKLPEDAAV ISVTPTPSER ENNTLIWRPD SSMVFPKVIF KRVNENEGIP GSSQ // ID Q9X163_THEMA Unreviewed; 157 AA. AC Q9X163; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36413.1}; GN OrderedLocusNames=TM_1341 {ECO:0000313|EMBL:AAD36413.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36413.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36413.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36413.1; -; Genomic_DNA. DR PIR; E72266; E72266. DR RefSeq; NP_229143.1; NC_000853.1. DR RefSeq; WP_010865321.1; NC_000853.1. DR STRING; 243274.TM1341; -. DR EnsemblBacteria; AAD36413; AAD36413; TM_1341. DR GeneID; 898141; -. DR KEGG; tma:TM1341; -. DR PATRIC; 23937613; VBITheMar51294_1352. DR OrthoDB; EOG6TXQVD; -. DR BioCyc; TMAR243274:GC6P-1372-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 57 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 77 93 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 129 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 157 AA; 18070 MW; 0ADD73B282D79874 CRC64; MSGVKTYDPT SWRPKHLDLL LSAVIAFSLP AVAGWLYDLS GVLIPMLIYY SLAWGLVKLR RGVVGYGTPF PKKPPKWFYV NVLVILTALF FAYQARIRVE EVDRFGVLLT ALLWAPVNAS TEQILWLYLF DSWDLYPEKP RLRYRLQAWC SSPPSWG // ID Q9X1W7_THEMA Unreviewed; 161 AA. AC Q9X1W7; G4FG21; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36699.1}; GN OrderedLocusNames=TM_1632 {ECO:0000313|EMBL:AAD36699.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36699.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36699.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36699.1; -; Genomic_DNA. DR PIR; H72229; H72229. DR RefSeq; NP_229432.1; NC_000853.1. DR RefSeq; WP_004082108.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1W7; -. DR STRING; 243274.TM1632; -. DR EnsemblBacteria; AAD36699; AAD36699; TM_1632. DR GeneID; 897925; -. DR KEGG; tma:TM1632; -. DR KEGG; tmi:THEMA_06085; -. DR KEGG; tmw:THMA_1673; -. DR PATRIC; 23938238; VBITheMar51294_1651. DR eggNOG; ENOG410800R; Bacteria. DR eggNOG; COG0802; LUCA. DR KO; K06925; -. DR OMA; TEFMRGI; -. DR OrthoDB; EOG6GBMHT; -. DR BioCyc; TMAR243274:GC6P-1678-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003442; T6A_TsaE. DR Pfam; PF02367; TsaE; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00150; T6A_YjeE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 161 AA; 18628 MW; D11CA2B8D5FA1A5A CRC64; MRHLRFENLT EEQLKRLAKI LTENLKGGEV VILSGNLGAG KTTFVKGMIR AIGLDEKMVK SPTFTLMNVY PGLKTIYHLD LYRLQDTDFL SLDVEDILED EDGIMVVEWG DLFDGFWPED SIKVKIEIAD ESHRNVEILI PEEVNFLVEK IERYRKELQN T // ID Q9X1D5_THEMA Unreviewed; 245 AA. AC Q9X1D5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 108. DE SubName: Full=ABC transporter, ATP-binding protein {ECO:0000313|EMBL:AAD36488.1}; GN OrderedLocusNames=TM_1417 {ECO:0000313|EMBL:AAD36488.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36488.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36488.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000256|RuleBase:RU363033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36488.1; -; Genomic_DNA. DR PIR; G72255; G72255. DR RefSeq; NP_229218.1; NC_000853.1. DR RefSeq; WP_010865335.1; NC_000853.1. DR ProteinModelPortal; Q9X1D5; -. DR STRING; 243274.TM1417; -. DR EnsemblBacteria; AAD36488; AAD36488; TM_1417. DR GeneID; 898058; -. DR KEGG; tma:TM1417; -. DR PATRIC; 23937780; VBITheMar51294_1428. DR eggNOG; ENOG4108NYS; Bacteria. DR eggNOG; COG0396; LUCA. DR InParanoid; Q9X1D5; -. DR KO; K09013; -. DR OMA; PARYDGI; -. DR OrthoDB; EOG6J74ZM; -. DR BioCyc; TMAR243274:GC6P-1455-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD36488.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAD36488.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4 235 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 245 AA; 27518 MW; 236D0529967721E9 CRC64; MNVLELIDVW YEVEGKAILK GINARFEKQR VYSILGTNGA GKSTLAYLIM GLEGYRPTRG KILLDGEDIT DLSVTERAKR GITLMWQEPA RFTGIKIRDY LTLGGRRKVS KEELERVLEL VGLNPALYLE RNVDEKLSGG ERKRVELASI LLMKPRYTIL DEPDSGIDIM SLEMIEKVLS ELVSAGGSVI LVTHREEIAL ESDYAFLICH GSILKEGNPS EIVQFYKNSC DRCDHPNEPS GEMIV // ID Q9X071_THEMA Unreviewed; 33 AA. AC Q9X071; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36055.1}; GN OrderedLocusNames=TM_0976 {ECO:0000313|EMBL:AAD36055.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36055.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36055.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36055.1; -; Genomic_DNA. DR PIR; E72309; E72309. DR RefSeq; NP_228784.1; NC_000853.1. DR RefSeq; WP_010865232.1; NC_000853.1. DR EnsemblBacteria; AAD36055; AAD36055; TM_0976. DR GeneID; 898722; -. DR KEGG; tma:TM0976; -. DR BioCyc; TMAR243274:GC6P-1006-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 33 AA; 4133 MW; 66B2AC49A5911F7B CRC64; MRWLKPQYHL QKEMNVIQYS GRVRFKKIVE GLR // ID Q9X130_THEMA Unreviewed; 271 AA. AC Q9X130; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 84. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36378.1}; GN OrderedLocusNames=TM_1304 {ECO:0000313|EMBL:AAD36378.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36378.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36378.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36378.1; -; Genomic_DNA. DR PIR; B72270; B72270. DR RefSeq; NP_229108.1; NC_000853.1. DR RefSeq; WP_010865302.1; NC_000853.1. DR STRING; 243274.TM1304; -. DR DNASU; 898178; -. DR EnsemblBacteria; AAD36378; AAD36378; TM_1304. DR GeneID; 898178; -. DR KEGG; tma:TM1304; -. DR KEGG; tmi:THEMA_07820; -. DR PATRIC; 23937548; VBITheMar51294_1320. DR eggNOG; ENOG4106AT1; Bacteria. DR eggNOG; COG0842; LUCA. DR KO; K01992; -. DR OMA; YWILASS; -. DR OrthoDB; EOG6ZPSXG; -. DR BioCyc; TMAR243274:GC6P-1335-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR InterPro; IPR000412; ABC_2_transport. DR PIRSF; PIRSF006648; DrrB; 1. DR PROSITE; PS51012; ABC_TM2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 25 45 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 88 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 151 174 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 180 200 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 238 259 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 271 AA; 30512 MW; 8DE8E6054E1BD9E0 CRC64; MGIMVRSLYL AKASFLSAKR YRIDWYGAFL TPLLTIMPVV LLYYFGTESG LVRFFYGATN TKNIIGYLLL GAAYWNYVEV LWGSVFALRY YMRIGQLEEL FIMPVSSIGY ILSWSVFGLV KVTVESVPII VLAVLLNLMT FNLVEFALAA GVVILSIIAS FGLVFLFFGI TLRFKEGDEL VSLLGNAAPL IGGMFFPVNV LPKVLEYLAY AFPFTWGLDL TRYFLMKTNT LLDLKKEFII LIVLSLLYLA FGTISFKVLQ TKGRKNGLQG F // ID Q9X0F7_THEMA Unreviewed; 655 AA. AC Q9X0F7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein {ECO:0000313|EMBL:AAD36142.1}; GN OrderedLocusNames=TM_1067 {ECO:0000313|EMBL:AAD36142.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36142.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36142.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36142.1; -; Genomic_DNA. DR PIR; F72300; F72300. DR RefSeq; NP_228873.1; NC_000853.1. DR RefSeq; WP_010865258.1; NC_000853.1. DR ProteinModelPortal; Q9X0F7; -. DR STRING; 243274.TM1067; -. DR TCDB; 3.A.1.5.12; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD36142; AAD36142; TM_1067. DR GeneID; 897643; -. DR KEGG; tma:TM1067; -. DR PATRIC; 23937063; VBITheMar51294_1080. DR InParanoid; Q9X0F7; -. DR KO; K02035; -. DR OMA; FRYQAYE; -. DR BioCyc; TMAR243274:GC6P-1096-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GOC. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 124 533 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. SQ SEQUENCE 655 AA; 75929 MW; C9DB6D821E1818FC CRC64; MMFRKVLWSL LVVIFTAQIL AIGLNEIVPG EYYNLTDYER LTGKKITKFN ESPMLKEMVE KGLLPPVEER LPKNPVVVTP YESIGKYGGT WNRAWYGLSD EWNAGRICYE FMVISDKAGK SLLPDVLESL EVSKDGREYT MRIRRGLKWS DGEPVTTKDV EFWYHDILLN ESLTPSIPSV FQPGGKVFKL EIVDDYTFKV IFEEPYPLFP FALAGDGGRA GIEFVVPSHY IKKFHPKYIG LEQAEKIAKE NGYSSWYQFV SDKCLQTNSW LVNPDLPILF PWKLSKESSE RALILERNPY YFKVDPEGNQ LPYIDRIIFH YVENQQMLLM KAISGEIDMQ GRHLTVADYS ILAANREKGG YKLILARQAV GSADTLMINQ NYTDDPVIGE ILRDPRFRQA ISLAVNREEI WQLVYQGLGE PRQASFVKGV KYYDPEWEKA FAEYNPERAN QLLDEMGLKW NPSRTYRLRP DGKKLEIVIE YTTPSQTREK TMEMVKSYLE KVGISVILKP IDRSLYVTRL EAGQLQIGVW EFDRNIDPVG DPAHILGSQW APLTWQWYNS GKKTGMPPEE GTDMWKLYEI WDQIVKEVAP EKRDELMKEI INLHKKNIWM VGFVGALPQP IVVKENFKNV PQGLLWDFPL IRSPKNFRPE QFYFE // ID Q9X152_THEMA Unreviewed; 80 AA. AC Q9X152; G4FI04; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36401.1}; GN OrderedLocusNames=TM_1329 {ECO:0000313|EMBL:AAD36401.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36401.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36401.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36401.1; -; Genomic_DNA. DR PIR; E72267; E72267. DR RefSeq; NP_229131.1; NC_000853.1. DR RefSeq; WP_004083342.1; NZ_CP011107.1. DR STRING; 243274.TM1329; -. DR EnsemblBacteria; AAD36401; AAD36401; TM_1329. DR GeneID; 898153; -. DR KEGG; tma:TM1329; -. DR KEGG; tmi:THEMA_07700; -. DR KEGG; tmw:THMA_1353; -. DR PATRIC; 23937595; VBITheMar51294_1343. DR eggNOG; ENOG4108E5N; Bacteria. DR eggNOG; ENOG41103IB; LUCA. DR OMA; IRIIFSF; -. DR OrthoDB; EOG6QP14R; -. DR BioCyc; TMAR243274:GC6P-1360-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 80 AA; 9643 MW; 4082A42120D3ABBE CRC64; MKKEIITLDE FQKEFEELIK RYVPRRRRDK LISKYESLIN TLAIEGEKVL VQPYFEKLKG IGDVNLYALR LEKKNPKRTM // ID Q9WYB5_THEMA Unreviewed; 281 AA. AC Q9WYB5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 89. DE SubName: Full=Sugar ABC transporter, permease protein {ECO:0000313|EMBL:AAD35367.1}; GN OrderedLocusNames=TM_0279 {ECO:0000313|EMBL:AAD35367.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35367.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35367.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000256|RuleBase:RU363032}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000256|RuleBase:RU363032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35367.1; -; Genomic_DNA. DR PIR; E72395; E72395. DR RefSeq; NP_228091.1; NC_000853.1. DR RefSeq; WP_010865087.1; NC_000853.1. DR ProteinModelPortal; Q9WYB5; -. DR STRING; 243274.TM0279; -. DR EnsemblBacteria; AAD35367; AAD35367; TM_0279. DR GeneID; 897196; -. DR KEGG; tma:TM0279; -. DR PATRIC; 23935437; VBITheMar51294_0284. DR eggNOG; ENOG4105DRW; Bacteria. DR eggNOG; COG0395; LUCA. DR InParanoid; Q9WYB5; -. DR KO; K02026; -. DR OMA; FFLEVPG; -. DR OrthoDB; EOG60PHFH; -. DR BioCyc; TMAR243274:GC6P-292-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Transport {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 12 33 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 83 105 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 117 137 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 143 169 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 190 212 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 247 269 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 79 269 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 281 AA; 31304 MW; 0AABA07FD54B76EB CRC64; MMKKILTIVR YILIAICLIF FLFPVYWLVI TAFKPSDEWF TMPPRFFPTK PTLANFFGAK ETEVFGGTTG SIENIFPYLR NSIVVGVSVA LIGTVISALA AYAIARYRVG GPFLAEWIIS IRMLPPIVSA VPLYVIFTKL RLINTWWALI LSHLVIVVPL GVWLLISFFR EIPREIDEAA YVDGATPFQA FFYVVLPLSA PGLAAVAVLS LIQSWGEFLL ALVLTNDARA QTLPIFLGRY ITGWRVAWGP LSAAGIVTML PVVVFALVAQ RYLIRGLTSE R // ID Q9WY02_THEMA Unreviewed; 353 AA. AC Q9WY02; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Chorismate mutase/prephenate dehydratase {ECO:0000313|EMBL:AAD35248.1}; GN OrderedLocusNames=TM_0155 {ECO:0000313|EMBL:AAD35248.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35248.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35248.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35248.1; -; Genomic_DNA. DR PIR; A72410; A72410. DR RefSeq; NP_227970.1; NC_000853.1. DR RefSeq; WP_010865063.1; NC_000853.1. DR ProteinModelPortal; Q9WY02; -. DR STRING; 243274.TM0155; -. DR EnsemblBacteria; AAD35248; AAD35248; TM_0155. DR GeneID; 896991; -. DR KEGG; tma:TM0155; -. DR PATRIC; 23935152; VBITheMar51294_0153. DR eggNOG; ENOG4105CQC; Bacteria. DR eggNOG; COG0077; LUCA. DR eggNOG; COG1605; LUCA. DR InParanoid; Q9WY02; -. DR KO; K14170; -. DR OMA; ILAMGEM; -. DR OrthoDB; EOG6WHNT1; -. DR BioCyc; TMAR243274:GC6P-156-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro. DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro. DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro. DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.59.10; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR008242; Chor_mutase/pphenate_deHydtase. DR InterPro; IPR002701; Chorismate_mutase. DR InterPro; IPR020822; Chorismate_mutase_type_II. DR InterPro; IPR001086; Preph_deHydtase. DR Pfam; PF01842; ACT; 1. DR Pfam; PF01817; CM_2; 1. DR Pfam; PF00800; PDT; 1. DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1. DR SMART; SM00830; CM_2; 1. DR SUPFAM; SSF48600; SSF48600; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS51168; CHORISMATE_MUT_2; 1. DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 80 Chorismate mutase. FT {ECO:0000259|PROSITE:PS51168}. FT DOMAIN 85 260 Prephenate dehydratase. FT {ECO:0000259|PROSITE:PS51171}. FT DOMAIN 271 353 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 353 AA; 40665 MW; CA2DFE6588CFBA5E CRC64; MRHKIRLIDF ILLRFIEERM KVARDVAKEK KKTDSPIVIR DIEEQKIKEI LDRTDLNPVR MRRIFEEIMK LAKEEEYRLL GISKTVAVLG PMGSFSDEMA MKLIGSRIPL KYCSTTDEII EMVEKGEVDY GIVPIENSTY GTVIPVLDAL LNHEVEVFGE AKLEIHHCLV AKKKLDLKEI KRIYSHPQAI SQSLGFINTY LSHAEIRYTS STSDAVNLLD DESAAIMSES AAKMYGLLIL RRSIQDLKEK NITRFYIIRR KTGKMEGKYT SLFFGVQDRP GSLKAVLDIF ASRGINLRKL ESRPARTFLG DYVFFVEVEA PLKEEDIRDL ERVTAFYKII GVFDEVEELD VFK // ID Q9WYH5_THEMA Unreviewed; 94 AA. AC Q9WYH5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35427.1}; GN OrderedLocusNames=TM_0340 {ECO:0000313|EMBL:AAD35427.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35427.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35427.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35427.1; -; Genomic_DNA. DR PIR; B72388; B72388. DR RefSeq; NP_228151.1; NC_000853.1. DR RefSeq; WP_010865099.1; NC_000853.1. DR STRING; 243274.TM0340; -. DR EnsemblBacteria; AAD35427; AAD35427; TM_0340. DR GeneID; 897296; -. DR KEGG; tma:TM0340; -. DR PATRIC; 23935559; VBITheMar51294_0344. DR OrthoDB; EOG6QP126; -. DR BioCyc; TMAR243274:GC6P-354-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 94 AA; 10682 MW; 5F4A35D05A9AAA7C CRC64; MSDEIRKILE AVARGEISPE EGEMLIKAMQ EKEREENGSK DDFSEREGDY ILDEDEMVEE DLVLSKKKAI IRGKIKGDLA LINCETFFSG EVGR // ID Q9WYG3_THEMA Unreviewed; 329 AA. AC Q9WYG3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 97. DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026}; DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362026}; GN OrderedLocusNames=TM_0328 {ECO:0000313|EMBL:AAD35415.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35415.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35415.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC {ECO:0000256|RuleBase:RU362026}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35415.1; -; Genomic_DNA. DR PIR; B72390; B72390. DR RefSeq; NP_228139.1; NC_000853.1. DR RefSeq; WP_010865095.1; NC_000853.1. DR ProteinModelPortal; Q9WYG3; -. DR STRING; 243274.TM0328; -. DR REBASE; 3927; M.TmaI. DR DNASU; 897275; -. DR EnsemblBacteria; AAD35415; AAD35415; TM_0328. DR GeneID; 897275; -. DR KEGG; tma:TM0328; -. DR PATRIC; 23935537; VBITheMar51294_0333. DR eggNOG; ENOG4107SSB; Bacteria. DR eggNOG; COG0863; LUCA. DR InParanoid; Q9WYG3; -. DR KO; K00571; -. DR OMA; IGFLMRG; -. DR OrthoDB; EOG6MSS08; -. DR BioCyc; TMAR243274:GC6P-342-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR017985; MeTrfase_CN4_CS. DR InterPro; IPR001091; RM_Methylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00093; N4_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Methyltransferase {ECO:0000313|EMBL:AAD35415.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35415.1}. FT DOMAIN 95 313 N6_N4_Mtase. {ECO:0000259|Pfam:PF01555}. SQ SEQUENCE 329 AA; 37569 MW; B1A41222CB7E82BA CRC64; MWVRVPPPAP FSIFLSPGDD IVKRRKSTRT SSFGVKGRES HDSSPFYSRA IYSNFSLPKP SEEDLIENPL PENLLDKVIE GDAREVLKKI PDCSIHLMVT SPPYNVGKEY DEDMTLDEYL EFIEEIMKEV YRVLVWGGRA CFNVANLGRK PYIPLHAYLI HLFEKIGFLI RGEIIWDKGE AVSGSSTAWG SWMSPVNPVL RDQHEYIIVM SKGDLKRRKP SDREAKSTIT REEFLEFTRS VWKFPPESAK RVGHPAPFPE ELPYRCIQLY TFKGDVVLDP FAGVGTTCVA AVKTGRHFVG IEINPEYVKK AEERVKDILS KPTLFEDHC // ID Q9X1P0_THEMA Unreviewed; 106 AA. AC Q9X1P0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36620.1}; GN OrderedLocusNames=TM_1554 {ECO:0000313|EMBL:AAD36620.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36620.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36620.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36620.1; -; Genomic_DNA. DR PIR; E72239; E72239. DR RefSeq; NP_229354.1; NC_000853.1. DR RefSeq; WP_010865359.1; NC_000853.1. DR ProteinModelPortal; Q9X1P0; -. DR STRING; 243274.TM1554; -. DR EnsemblBacteria; AAD36620; AAD36620; TM_1554. DR GeneID; 897969; -. DR KEGG; tma:TM1554; -. DR PATRIC; 23938070; VBITheMar51294_1572. DR eggNOG; ENOG4108609; Bacteria. DR eggNOG; COG5341; LUCA. DR InParanoid; Q9X1P0; -. DR OMA; NTGWVEN; -. DR OrthoDB; EOG6NSGP6; -. DR BioCyc; TMAR243274:GC6P-1595-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 2.60.320.10; -; 1. DR InterPro; IPR024045; NusG_dom2. DR Pfam; PF07009; NusG_II; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 5 97 NusG_II. {ECO:0000259|Pfam:PF07009}. SQ SEQUENCE 106 AA; 11958 MW; 260BBE6B757B3E03 CRC64; MLIILIFVVL IFSILASEKK GSKVVVQGRD FRKILSKPGT YDITENGRFL MKVEFDGNRV RVVESTCPLK LCVKTGWVGP GGTIICVPNE VIIFFEEKTD YDTVTW // ID Q9X121_THEMA Unreviewed; 218 AA. AC Q9X121; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36369.1}; GN OrderedLocusNames=TM_1295 {ECO:0000313|EMBL:AAD36369.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36369.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36369.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36369.1; -; Genomic_DNA. DR PIR; F72272; F72272. DR RefSeq; NP_229099.1; NC_000853.1. DR RefSeq; WP_010865299.1; NC_000853.1. DR ProteinModelPortal; Q9X121; -. DR STRING; 243274.TM1295; -. DR EnsemblBacteria; AAD36369; AAD36369; TM_1295. DR GeneID; 898188; -. DR KEGG; tma:TM1295; -. DR PATRIC; 23937530; VBITheMar51294_1311. DR eggNOG; ENOG4108GYP; Bacteria. DR eggNOG; COG0491; LUCA. DR InParanoid; Q9X121; -. DR OMA; KDEYRAT; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; TMAR243274:GC6P-1326-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 23 185 Lactamase_B. {ECO:0000259|SMART:SM00849}. SQ SEQUENCE 218 AA; 24832 MW; F350491EEC1A8BBF CRC64; MRKDEYRATL LEPNVWHIAD YRGDSMYLVV GEEKALLVDT GMGEGDLKGF VRSITEKPVE VVLTHAHWDH IMQANQFEKV YLNHRDFQII ELFKINVNYE NFLNVKEGDR FDLGGRTLEV IEVPGHTPGS IVLLDRENRL LFSGDSVGAG HTWMHLPGCL PLREYLKSLK KLKETDSFEK IYHGHLTGTQ LKPFGPDYLD DLIKAVEGVI DGSLRGEP // ID Q9WYZ9_THEMA Unreviewed; 63 AA. AC Q9WYZ9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Heavy metal binding protein {ECO:0000313|EMBL:AAD35614.1}; GN OrderedLocusNames=TM_0529 {ECO:0000313|EMBL:AAD35614.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35614.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35614.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35614.1; -; Genomic_DNA. DR PIR; G72366; G72366. DR RefSeq; NP_228339.1; NC_000853.1. DR RefSeq; WP_010865142.1; NC_000853.1. DR ProteinModelPortal; Q9WYZ9; -. DR STRING; 243274.TM0529; -. DR DNASU; 897581; -. DR EnsemblBacteria; AAD35614; AAD35614; TM_0529. DR GeneID; 897581; -. DR KEGG; tma:TM0529; -. DR PATRIC; 23935965; VBITheMar51294_0537. DR eggNOG; COG2608; LUCA. DR OMA; FKVDYEM; -. DR OrthoDB; EOG696C26; -. DR BioCyc; TMAR243274:GC6P-553-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR InterPro; IPR006121; HMA_dom. DR Pfam; PF00403; HMA; 1. DR SUPFAM; SSF55008; SSF55008; 1. DR PROSITE; PS50846; HMA_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 1 63 HMA. {ECO:0000259|PROSITE:PS50846}. SQ SEQUENCE 63 AA; 7088 MW; 820B4A4576B85A8D CRC64; MLKGAKTEED YKRVKEAIEK LDGVFKVDYE MAAEVVGVDY DDEKVSKEQI KSAVDSLGYT LIV // ID Q9X146_THEMA Unreviewed; 536 AA. AC Q9X146; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36394.1}; GN OrderedLocusNames=TM_1322 {ECO:0000313|EMBL:AAD36394.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36394.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36394.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36394.1; -; Genomic_DNA. DR PIR; H72268; H72268. DR RefSeq; NP_229124.1; NC_000853.1. DR RefSeq; WP_010865310.1; NC_000853.1. DR STRING; 243274.TM1322; -. DR EnsemblBacteria; AAD36394; AAD36394; TM_1322. DR GeneID; 898160; -. DR KEGG; tma:TM1322; -. DR PATRIC; 23937581; VBITheMar51294_1336. DR eggNOG; ENOG41090JT; Bacteria. DR eggNOG; ENOG4111TFJ; LUCA. DR InParanoid; Q9X146; -. DR OMA; NDETNEY; -. DR OrthoDB; EOG6KWXTC; -. DR BioCyc; TMAR243274:GC6P-1353-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 536 AA; 62609 MW; 14E72C45B2D70535 CRC64; MKMKGIESLK EIFKYGAFSL PVANYLLCEG NIPGDCKRIL DVLKLAWKGN FKEAIRRADK AVENSRSETA KYFLLANKLA FLKYTGKTDV NLYRYLKRNL PKMSKSIRDT VIVTLINFEA SGIKPLRKVR VWKNDYRKST LSFLYLSLAR READSGRLSE AVHDYIQAYR LSREVPHPTC IVSSLNDLAW DIREKHPKLA HALSQGAVFW LGYYREEPGN LFGALDTLFV VEKDMDSPSI HSTAHIIVSL PVPEDYLSLL KKAKKFVLDY TGSTYPNTSQ LRRYVEKVAW KGKTLSSKGI SDILKGKTKM IRADTIRKLL TSGVDTGAPF PVWNEWIKME IERKYRESSE KLKELPFHQR QILFLTTYMA LLDREFLSRK EKLKKAYTLL EDIESFADFM AKDHRTMEFV VSMVKAHPFV EGRKEAVKRA LARMKRKRLE RFVLRYIEMK ESDRKLLDRF LRNYGRYDGV RFGIRLKGPE VVREFAKKYS LKVQPLFAAF WCEEDGRVRR RLERVLKHMV LYNLIEIAIL FVMVEK // ID Q9WYE8_THEMA Unreviewed; 328 AA. AC Q9WYE8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35400.1}; GN OrderedLocusNames=TM_0312 {ECO:0000313|EMBL:AAD35400.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35400.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35400.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1ZH8} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH NADP. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of Oxidoreductase (TM0312) from Thermotoga maritima RT at 2.50 A resolution."; RL Submitted (APR-2005) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35400.1; -; Genomic_DNA. DR PIR; G72391; G72391. DR RefSeq; NP_228124.1; NC_000853.1. DR RefSeq; WP_010865093.1; NC_000853.1. DR PDB; 1ZH8; X-ray; 2.50 A; A/B=1-328. DR PDBsum; 1ZH8; -. DR ProteinModelPortal; Q9WYE8; -. DR SMR; Q9WYE8; 4-328. DR STRING; 243274.TM0312; -. DR EnsemblBacteria; AAD35400; AAD35400; TM_0312. DR GeneID; 897250; -. DR KEGG; tma:TM0312; -. DR PATRIC; 23935503; VBITheMar51294_0317. DR eggNOG; ENOG4107T86; Bacteria. DR eggNOG; COG0673; LUCA. DR InParanoid; Q9WYE8; -. DR OMA; RMLVGCE; -. DR OrthoDB; EOG69GZJ7; -. DR BioCyc; TMAR243274:GC6P-325-MONOMER; -. DR EvolutionaryTrace; Q9WYE8; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000683; Oxidoreductase_N. DR InterPro; IPR004104; OxRdtase_C. DR Pfam; PF01408; GFO_IDH_MocA; 1. DR Pfam; PF02894; GFO_IDH_MocA_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1ZH8}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW NADP {ECO:0000213|PDB:1ZH8}; KW Nucleotide-binding {ECO:0000213|PDB:1ZH8}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 126 GFO_IDH_MocA. {ECO:0000259|Pfam:PF01408}. FT DOMAIN 140 201 GFO_IDH_MocA_C. FT {ECO:0000259|Pfam:PF02894}. FT NP_BIND 14 17 NADP. {ECO:0000213|PDB:1ZH8}. FT NP_BIND 40 45 NADP. {ECO:0000213|PDB:1ZH8}. FT NP_BIND 100 101 NADP. {ECO:0000213|PDB:1ZH8}. FT NP_BIND 173 174 NADP. {ECO:0000213|PDB:1ZH8}. FT BINDING 78 78 NADP; via carbonyl oxygen. FT {ECO:0000213|PDB:1ZH8}. FT BINDING 129 129 NADP. {ECO:0000213|PDB:1ZH8}. FT BINDING 279 279 NADP. {ECO:0000213|PDB:1ZH8}. SQ SEQUENCE 328 AA; 36539 MW; 93E2B37D4518544B CRC64; MKPLRKIRLG IVGCGIAARE LHLPALKNLS HLFEITAVTS RTRSHAEEFA KMVGNPAVFD SYEELLESGL VDAVDLTLPV ELNLPFIEKA LRKGVHVICE KPISTDVETG KKVVELSEKS EKTVYIAENF RHVPAFWKAK ELVESGAIGD PVFMNWQIWV GMDENNKYVH TDWRKKPKHV GGFLSDGGVH HAAAMRLILG EIEWISAVAK DLSPLLGGMD FLSSIFEFEN GTVGNYTISY SLKGNERFEI TGTKGKISIS WDKIVLNEEE MKVPQENSYQ KEFEDFYQVV AEGKPNDLGS PVQALKDLAF IEACVRSAGN KVFVSSLL // ID Q9X155_THEMA Unreviewed; 522 AA. AC Q9X155; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36404.1}; GN OrderedLocusNames=TM_1332 {ECO:0000313|EMBL:AAD36404.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36404.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36404.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36404.1; -; Genomic_DNA. DR PIR; H72267; H72267. DR RefSeq; NP_229134.1; NC_000853.1. DR RefSeq; WP_010865317.1; NC_000853.1. DR EnsemblBacteria; AAD36404; AAD36404; TM_1332. DR GeneID; 898150; -. DR KEGG; tma:TM1332; -. DR PATRIC; 23937599; VBITheMar51294_1345. DR eggNOG; ENOG41090JT; Bacteria. DR eggNOG; ENOG4111TFJ; LUCA. DR InParanoid; Q9X155; -. DR OMA; ESDENME; -. DR OrthoDB; EOG6F81KM; -. DR BioCyc; TMAR243274:GC6P-1363-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 522 AA; 61057 MW; 40F9CFF7B02B82DC CRC64; MKMKGIESLK EIFKYGAFSL PVANYLLCEG NIPGDCKRIL DVLKLAWKGN FKEAIRRADK AVENSRSETA KYFLLANKLV FLKYTGKVDM NLYRYLKRNL PKMSKSIRDT VIVTLINFEA SGVKPLRKMR VWKNNYRKST LSFLYLSLAR READSGDLSE AVHGYIQAYK LSREIPHPTC MVSSLNDLAW DIKEKHPKLA YDLSKGAVFW LGYYREEPGN LFGALDTLFV VEKDMDSPSI HSTAHIIVSL PVPEDYLSLL KKAKKFVLDY TGSTYPNTSQ LRRYVEKVAW KGKTLSSKGI SDILKGKTKM IRADTIRKLL TSGVDTGAPF PVWNEWIKME IERKYRESSE KLKELPFHQR QILFLTTYMA LLDREFLSRK EKLKKAYTLL EDIESFADFM AKDHRTMEFV VSMVKAHPFV EGRKEAVKRA LARMKRKRLE RFVLRYIEMK ESDRKLLDRF LRNYGRYDGV RFGIRLKGPE VVREFAKKYS LKVQPLFAAF WCEEDGRVRR RLERILKYMF LN // ID Q9WYE7_THEMA Unreviewed; 163 AA. AC Q9WYE7; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35399.1}; GN OrderedLocusNames=TM_0311 {ECO:0000313|EMBL:AAD35399.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35399.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35399.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35399.1; -; Genomic_DNA. DR PIR; F72391; F72391. DR RefSeq; NP_228123.1; NC_000853.1. DR RefSeq; WP_010865092.1; NC_000853.1. DR STRING; 243274.TM0311; -. DR EnsemblBacteria; AAD35399; AAD35399; TM_0311. DR GeneID; 897247; -. DR KEGG; tma:TM0311; -. DR PATRIC; 23935501; VBITheMar51294_0316. DR eggNOG; ENOG4106GVR; Bacteria. DR eggNOG; ENOG410XWZ8; LUCA. DR OMA; NESVFEH; -. DR BioCyc; TMAR243274:GC6P-324-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 44 60 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 72 92 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 131 150 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 163 AA; 19176 MW; 66806602503367A1 CRC64; MMLWKALIFL GIYAVLHFGY ELSGWELLKP ICGVDESVFE HLKIGFWAYF FTNIIEYFFA KKKHGFWYPR ILSTVLLPWF IVLIWYMLPV FFGHVESLAV DLSWAFVVTF LAAILSEILE KDLERNSLGT ALKIVIVVLF IISIIFYTAF SYEKPWIDVF TKH // ID Q9WXW9_THEMA Unreviewed; 335 AA. AC Q9WXW9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 78. DE SubName: Full=Sugar ABC transporter, periplasmic sugar-binding protein {ECO:0000313|EMBL:AAD35208.1}; GN OrderedLocusNames=TM_0114 {ECO:0000313|EMBL:AAD35208.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35208.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35208.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:2H3H} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 32-335. RX PubMed=17766373; DOI=10.1110/ps.072969407; RA Tian Y., Cuneo M.J., Changela A., Hocker B., Beese L.S., RA Hellinga H.W.; RT "Structure-based design of robust glucose biosensors using a RT Thermotoga maritima periplasmic glucose-binding protein."; RL Protein Sci. 16:2240-2250(2007). RN [3] {ECO:0000213|PDB:3C6Q} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 32-335. RA Cuneo M.J., Hellinga H.W.; RT "Open to closed transition of a thermophilic glucose binding RT protein."; RL Submitted (FEB-2008) to the PDB data bank. RN [4] {ECO:0000213|PDB:2QVC} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 33-334. RX PubMed=23192024; DOI=10.1107/S1744309112045241; RA Palani K., Kumaran D., Burley S.K., Swaminathan S.; RT "Structure of a periplasmic glucose-binding protein from Thermotoga RT maritima."; RL Acta Crystallogr. F 68:1460-1464(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35208.1; -; Genomic_DNA. DR PIR; A72417; A72417. DR RefSeq; NP_227930.1; NC_000853.1. DR RefSeq; WP_010865054.1; NC_000853.1. DR PDB; 2H3H; X-ray; 1.70 A; A/B=32-335. DR PDB; 2QVC; X-ray; 2.40 A; A/B/C/D=33-334. DR PDB; 3C6Q; X-ray; 2.30 A; A/B/C/D=32-335. DR PDBsum; 2H3H; -. DR PDBsum; 2QVC; -. DR PDBsum; 3C6Q; -. DR ProteinModelPortal; Q9WXW9; -. DR SMR; Q9WXW9; 32-335. DR STRING; 243274.TM0114; -. DR EnsemblBacteria; AAD35208; AAD35208; TM_0114. DR GeneID; 896941; -. DR KEGG; tma:TM0114; -. DR PATRIC; 23935068; VBITheMar51294_0112. DR eggNOG; ENOG4105E20; Bacteria. DR eggNOG; COG1879; LUCA. DR InParanoid; Q9WXW9; -. DR KO; K10439; -. DR OMA; IGPRQAN; -. DR OrthoDB; EOG6JMMRD; -. DR BioCyc; TMAR243274:GC6P-114-MONOMER; -. DR EvolutionaryTrace; Q9WXW9; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015749; P:monosaccharide transport; IBA:GOC. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR025997; SBP_2_dom. DR Pfam; PF13407; Peripla_BP_4; 1. DR SUPFAM; SSF53822; SSF53822; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2H3H, ECO:0000213|PDB:2QVC, KW ECO:0000213|PDB:3C6Q}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 40 282 Peripla_BP_4. {ECO:0000259|Pfam:PF13407}. SQ SEQUENCE 335 AA; 36110 MW; 03D6CA3300D8184E CRC64; MWNKTSLQGG VIMRKLLVFL SVLLVAGLSL ALTIGVIGKS VHPYWSQVEQ GVKAAGKALG VDTKFFVPQK EDINAQLQML ESFIAEGVNG IAIAPSDPTA VIPTIKKALE MGIPVVTLDT DSPDSGRYVY IGTDNYQAGY TAGLIMKELL GGKGKVVIGT GSLTAMNSLQ RIQGFKDAIK DSEIEIVDIL NDEEDGARAV SLAEAALNAH PDLDAFFGVY AYNGPAQALV VKNAGKVGKV KIVCFDTTPD ILQYVKEGVI QATMGQRPYM MGYLSVTVLY LMNKIGVQNT LMMLPKVKVD GKVDYVIDTG VDVVTPENLD EYLKKMEELG IPIKF // ID Q9WY84_THEMA Unreviewed; 40 AA. AC Q9WY84; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35333.1}; GN OrderedLocusNames=TM_0242 {ECO:0000313|EMBL:AAD35333.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35333.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35333.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35333.1; -; Genomic_DNA. DR PIR; C72398; C72398. DR RefSeq; NP_228056.1; NC_000853.1. DR RefSeq; WP_010865077.1; NC_000853.1. DR STRING; 243274.TM0242; -. DR EnsemblBacteria; AAD35333; AAD35333; TM_0242. DR GeneID; 897143; -. DR KEGG; tma:TM0242; -. DR KEGG; tmi:THEMA_03515; -. DR PATRIC; 23935359; VBITheMar51294_0245. DR OrthoDB; EOG6CGCJN; -. DR BioCyc; TMAR243274:GC6P-255-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 40 AA; 4859 MW; 1FCCD2A4628965C0 CRC64; MRLEAKQSIP EFLNGFEISV EGSRVRLRKQ EREYEFEVEK // ID Q9X1L5_THEMA Unreviewed; 208 AA. AC Q9X1L5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36596.1}; GN OrderedLocusNames=TM_1529 {ECO:0000313|EMBL:AAD36596.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36596.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36596.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36596.1; -; Genomic_DNA. DR PIR; E72241; E72241. DR RefSeq; NP_229329.1; NC_000853.1. DR RefSeq; WP_010865355.1; NC_000853.1. DR STRING; 243274.TM1529; -. DR EnsemblBacteria; AAD36596; AAD36596; TM_1529. DR GeneID; 897345; -. DR KEGG; tma:TM1529; -. DR KEGG; tmi:THEMA_06645; -. DR PATRIC; 23938018; VBITheMar51294_1547. DR eggNOG; ENOG4105S6P; Bacteria. DR eggNOG; COG1266; LUCA. DR KO; K07052; -. DR OMA; QRMDVVP; -. DR OrthoDB; EOG6GTZFT; -. DR BioCyc; TMAR243274:GC6P-1569-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003675; CAAX_protease. DR Pfam; PF02517; Abi; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 67 89 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 126 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 138 157 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 163 181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 188 206 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 208 AA; 23420 MW; 9F6632BE67219592 CRC64; MPMVKRISEI SFLSVLIGLF LGWYFVFQVN MLDFWWRMFM TTLIFSVISI FLGGKRNIKP NKYEAPLAIY SAVAAYLLFV VGYLISLLIP PFHRDVVSVY GLAEGQNALK VIILLVFIAF FEEIIWRGFV TEFLLQRLDV VPSILISSLL YSVVHVFTGN MALIVGAFVL GIILSLLYVI TGKVSTPAFA HALWSLLIFV VLPLKGGF // ID Q9X0A1_THEMA Unreviewed; 333 AA. AC Q9X0A1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=Oxidoreductase, aldo/keto reductase family {ECO:0000313|EMBL:AAD36088.1}; GN OrderedLocusNames=TM_1006 {ECO:0000313|EMBL:AAD36088.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36088.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36088.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36088.1; -; Genomic_DNA. DR PIR; H72307; H72307. DR RefSeq; NP_228814.1; NC_000853.1. DR RefSeq; WP_010865241.1; NC_000853.1. DR ProteinModelPortal; Q9X0A1; -. DR STRING; 243274.TM1006; -. DR EnsemblBacteria; AAD36088; AAD36088; TM_1006. DR GeneID; 898707; -. DR KEGG; tma:TM1006; -. DR PATRIC; 23936943; VBITheMar51294_1020. DR eggNOG; ENOG4105CPC; Bacteria. DR eggNOG; COG0667; LUCA. DR InParanoid; Q9X0A1; -. DR OMA; FGFKDGD; -. DR OrthoDB; EOG69WFJ0; -. DR BioCyc; TMAR243274:GC6P-1036-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR001395; Aldo/ket_red/Kv-b. DR InterPro; IPR023210; NADP_OxRdtase_dom. DR PANTHER; PTHR11732; PTHR11732; 1. DR Pfam; PF00248; Aldo_ket_red; 1. DR SUPFAM; SSF51430; SSF51430; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 18 312 Aldo_ket_red. {ECO:0000259|Pfam:PF00248}. SQ SEQUENCE 333 AA; 37538 MW; 3ECC2FD6A503444E CRC64; MGIPKRKLGE RGPEVSAIGL GCMRMSFGQK KLPDRKEMIK LIRTAVELGI NFFDTAEVYG PYTNEELVGE ALEPFKGEVV IATKFGFELY EDGRPGWKGL NSNPEHIKKA VEGSLRRLRV EAIDILYQHR VDPNVPIEEV AGAVKELIEE GKVKHFGLCE ASAETIRRAH KVCPVDVVQY EYSMWWRKPE EELLPTCEEL GIGFVAYSPL GKGFLTGAIG ENSKFDEEDS RSRIPRFQKE NLRENLALVE LRKTIAERKG ATPSQIALAW LLAQKPWIVP IPGTTKLSHL LENIGGAFVE LTPEELQEIN DALSRIEIKG SRYPEDMEKM TYL // ID Q9X296_THEMA Unreviewed; 421 AA. AC Q9X296; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36838.1}; GN OrderedLocusNames=TM_1775 {ECO:0000313|EMBL:AAD36838.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36838.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36838.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36838.1; -; Genomic_DNA. DR PIR; F72213; F72213. DR RefSeq; NP_229572.1; NC_000853.1. DR RefSeq; WP_010865400.1; NC_000853.1. DR STRING; 243274.TM1775; -. DR DNASU; 897848; -. DR EnsemblBacteria; AAD36838; AAD36838; TM_1775. DR GeneID; 897848; -. DR KEGG; tma:TM1775; -. DR eggNOG; ENOG410852W; Bacteria. DR eggNOG; COG0658; LUCA. DR InParanoid; Q9X296; -. DR KO; K02238; -. DR OMA; ALFRFPW; -. DR OrthoDB; EOG6Z3KJ4; -. DR BioCyc; TMAR243274:GC6P-1824-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR004477; ComEC_N. DR Pfam; PF03772; Competence; 1. DR TIGRFAMs; TIGR00360; ComEC_N-term; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 63 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 211 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 223 250 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 270 295 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 307 329 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 335 353 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 365 384 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 390 408 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 180 391 Competence. {ECO:0000259|Pfam:PF03772}. SQ SEQUENCE 421 AA; 47473 MW; E27C57C6C718C9AC CRC64; MCEGHTRNDP CERRHDPGAR VRRKAGKIRS MILVFFSLCL GALIGALFRF PWYMLFLLAA IFWKRNKDIS VVIFFTLLSA SLYQIGTLPA GNYELVGYAE RGRLKQVKVF QEEWKRIHPV RIETSEEGYV YAIGYFDGKA FHPSYLKKVE KPSLKTLKES FSGMANGTVL SVLFGEKNGD IYRSGLGHFF AVSGLHVGIA FSLYTTLLSF LTWRRTYQEL TALLLLVPYV IAVGTPSVIR AYLTIFLWVA FKIFGFRTTP LHTTATVGSF MMIVDPTVVF TPSFLLSFFV TLCILESKNI FELTVKAYLS ALPFLCLFFG GTNMSALVLS IPVSLLMIPV TWLAHLSFLL FLLGLKTSAL IAAKITNIVS LPLNGFIKLA NLLPEVPLPQ YLYFILIFFP LLFLSPDIRD IFRKISGRAI L // ID Q9WYW6_THEMA Unreviewed; 189 AA. AC Q9WYW6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 103. DE SubName: Full=DNA polymerase III, epsilon subunit, putative {ECO:0000313|EMBL:AAD35581.1}; GN OrderedLocusNames=TM_0496 {ECO:0000313|EMBL:AAD35581.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35581.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35581.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35581.1; -; Genomic_DNA. DR PIR; G72370; G72370. DR RefSeq; NP_228306.1; NC_000853.1. DR RefSeq; WP_010865135.1; NC_000853.1. DR ProteinModelPortal; Q9WYW6; -. DR STRING; 243274.TM0496; -. DR DNASU; 897537; -. DR EnsemblBacteria; AAD35581; AAD35581; TM_0496. DR GeneID; 897537; -. DR KEGG; tma:TM0496; -. DR PATRIC; 23935897; VBITheMar51294_0503. DR eggNOG; ENOG4108JDX; Bacteria. DR eggNOG; COG0847; LUCA. DR InParanoid; Q9WYW6; -. DR KO; K02342; -. DR OMA; NRVNEFI; -. DR OrthoDB; EOG6MSS4T; -. DR BioCyc; TMAR243274:GC6P-520-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR006054; DnaQ. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR00573; dnaq; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 10 177 Exonuclease. {ECO:0000259|SMART:SM00479}. SQ SEQUENCE 189 AA; 21514 MW; 620EFB4153B15252 CRC64; MLAMIWNDTV FCVVDTETTG TDPFAGDRIV EIAAVPVFKG KIYRNKAFHS LVNPRIRIPA LIQKVHGISN MDIVEAPDMD TVYDLFRDYV KGTVLVFHNA NFDLTFLDMM AKETGNFPIT NPYIDTLDLS EEIFGRPHSL KWLSERLGIK TTIRHRALPD ALVTARVFVK LVEFLGENRV NEFIRGKRG // ID Q9WXL8_THEMA Unreviewed; 40 AA. AC Q9WXL8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35097.1}; GN OrderedLocusNames=TM_0003 {ECO:0000313|EMBL:AAD35097.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35097.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35097.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35097.1; -; Genomic_DNA. DR PIR; E72429; E72429. DR RefSeq; NP_227819.1; NC_000853.1. DR RefSeq; WP_010865022.1; NC_000853.1. DR EnsemblBacteria; AAD35097; AAD35097; TM_0003. DR GeneID; 896811; -. DR KEGG; tma:TM0003; -. DR BioCyc; TMAR243274:GC6P-3-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 40 AA; 4454 MW; B4E30037DF4467E1 CRC64; METVKAYEVE DIPAIGFNNS LEVWKLFPAS SSRSTSSSFQ // ID Q9X2C8_THEMA Unreviewed; 292 AA. AC Q9X2C8; G4FGJ6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36871.1}; GN OrderedLocusNames=TM_1808 {ECO:0000313|EMBL:AAD36871.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36871.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36871.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36871.1; -; Genomic_DNA. DR PIR; E72208; E72208. DR RefSeq; NP_229605.1; NC_000853.1. DR RefSeq; WP_004082355.1; NZ_CP011107.1. DR STRING; 243274.TM1808; -. DR EnsemblBacteria; AAD36871; AAD36871; TM_1808. DR GeneID; 897723; -. DR KEGG; tma:TM1808; -. DR KEGG; tmi:THEMA_05150; -. DR KEGG; tmw:THMA_1854; -. DR PATRIC; 23938605; VBITheMar51294_1829. DR eggNOG; ENOG4108T47; Bacteria. DR eggNOG; COG1567; LUCA. DR KO; K19139; -. DR OMA; KRDEMKV; -. DR OrthoDB; EOG6JX7GC; -. DR BioCyc; TMAR243274:GC6P-1859-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR005510; DUF314. DR InterPro; IPR005537; RAMP_III_fam. DR Pfam; PF03787; RAMPs; 1. DR TIGRFAMs; TIGR01903; cas5_csm4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 292 AA; 32936 MW; 93272B8DA111C022 CRC64; MIGVRLLVKM SFRSGFRVGR GNETDSTLPT IHSDTIYGAV VYHAFKWSEK AEDFAKKLKV SSLLFVRGDR LLVPKPFLYN TYSLEEDDEE SPKELKKASY VFLDKLADYR SIKEASGAVC KENPVEIVRI PRNSLDRITS SSNLYFVEVA FVKEGFTPAF LAEFPDEYEG LFKTAVKSLG DSGIGADSTY GYGLFNAEFE SAPDFPEEGE YYLTLSLFVP SAEERSKMNE GYYRVVKRRG VKRDEMKVKK EISYVQEGSV FPFKPEGRGV LKIEDYFVQT SPLCVAFGGD GK // ID Q9WZ85_THEMA Unreviewed; 463 AA. AC Q9WZ85; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 96. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35701.1}; GN OrderedLocusNames=TM_0616 {ECO:0000313|EMBL:AAD35701.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35701.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35701.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35701.1; -; Genomic_DNA. DR PIR; D72356; D72356. DR RefSeq; NP_228426.1; NC_000853.1. DR RefSeq; WP_010865165.1; NC_000853.1. DR ProteinModelPortal; Q9WZ85; -. DR STRING; 243274.TM0616; -. DR EnsemblBacteria; AAD35701; AAD35701; TM_0616. DR GeneID; 897699; -. DR KEGG; tma:TM0616; -. DR PATRIC; 23936145; VBITheMar51294_0626. DR eggNOG; ENOG4108175; Bacteria. DR eggNOG; COG1373; LUCA. DR InParanoid; Q9WZ85; -. DR KO; K07133; -. DR OMA; KEFLHAK; -. DR OrthoDB; EOG6DRPCX; -. DR BioCyc; TMAR243274:GC6P-641-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 46 159 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 463 AA; 54028 MW; F88EDEE3971BDD5B CRC64; MDELYIMNPW WRDPEIINTD RHISMFENST FKYFPENLFK KIPLNKPGIY TIRGPRQVGK TTFLKLYIRK LLRDGVKPSN IFFFTCDAVK DRFELIETMK AYFQIFERKA GETRYLFIDE ITAVEDWQKS IKYLVDIGLL ENSLLILTGS SAFDLKRSSE RLPGRKGYGE DLVYLPLTFG EFLESLGISV ERMSVDDIFL KSEEELRILY LKNSFLKEYF VKYLNTGGFP KVIDVFLKEG KIDEITKGVF RDFILGDAEK YLGSRIKVIE IFKKLPDIVG QRFSWNSLVD IFSGAIESVD TIQKYFEYLG YSFILMNVFF VDISRKTVRL KKQKKTYPID RVVVDIIEEI SGKQIKLPQI VEMLTLRHLM GNGKTLPNGM NLYDGPFFWY SDRGNEVDFV FEHGDSLIPV EINFQNNIHR SDYAGMKKVF KKGIVITQDA IFRDENIVAV PAWLFFAVFE GNE // ID Q9X171_THEMA Unreviewed; 259 AA. AC Q9X171; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 86. DE SubName: Full=Lipase, putative {ECO:0000313|EMBL:AAD36421.1}; GN OrderedLocusNames=TM_1350 {ECO:0000313|EMBL:AAD36421.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36421.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36421.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36421.1; -; Genomic_DNA. DR PIR; F72264; F72264. DR RefSeq; NP_229151.1; NC_000853.1. DR RefSeq; WP_010865324.1; NC_000853.1. DR ProteinModelPortal; Q9X171; -. DR STRING; 243274.TM1350; -. DR ESTHER; thema-TM1350; Monoglyceridelipase_lysophospholip. DR EnsemblBacteria; AAD36421; AAD36421; TM_1350. DR GeneID; 898130; -. DR KEGG; tma:TM1350; -. DR KEGG; tmi:THEMA_07590; -. DR PATRIC; 23937638; VBITheMar51294_1362. DR eggNOG; ENOG41080RX; Bacteria. DR eggNOG; COG2267; LUCA. DR OMA; WRRKMAW; -. DR OrthoDB; EOG6S52PZ; -. DR BioCyc; TMAR243274:GC6P-1383-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0016298; F:lipase activity; IBA:GO_Central. DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR022742; Hydrolase_4. DR Pfam; PF12146; Hydrolase_4; 1. DR PRINTS; PR00111; ABHYDROLASE. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 13 239 Hydrolase_4. {ECO:0000259|Pfam:PF12146}. SQ SEQUENCE 259 AA; 29603 MW; 426CCE1F16A9EC97 CRC64; MRMNIQKHGE DWKGTVVIVH GLGEHSGRYR RLVREFVSEG VQVVTFDLPG HGKSPGRRGH LRFDDVFKIL NEITKDLERF VLFGHSLGGL IAIRFTQIFQ PENQKGLVVS APAILLPDTH SPVLEFMVRF LSFFVPFLTM SNGINPSDLS RNREAVEAYI RDPLVHDRIS FKLASDMLSH MKKVLKDAER IKVPVLIFHG TDDRVVSFEG SKKFFEALST EKKLVSFPGG YHELFEDPEH QKEFFKTIVE WSLEKLGGK // ID Q9X070_THEMA Unreviewed; 452 AA. AC Q9X070; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36054.1}; GN OrderedLocusNames=TM_0975 {ECO:0000313|EMBL:AAD36054.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36054.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36054.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36054.1; -; Genomic_DNA. DR PIR; D72309; D72309. DR RefSeq; NP_228783.1; NC_000853.1. DR RefSeq; WP_010865231.1; NC_000853.1. DR EnsemblBacteria; AAD36054; AAD36054; TM_0975. DR GeneID; 898721; -. DR KEGG; tma:TM0975; -. DR KEGG; tmi:THEMA_09470; -. DR PATRIC; 23936879; VBITheMar51294_0988. DR OMA; ESIERQC; -. DR OrthoDB; EOG6CS011; -. DR BioCyc; TMAR243274:GC6P-1005-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 28 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 383 424 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 452 AA; 52391 MW; 6A7A34E68C042995 CRC64; MCRVVTGFQF ILVAIAFLAL GVSVGLFVST MRMRRKRTVD PKKSAAEESS MGMSNTTEKT LSSSKEPEKV EKVIIEDEFN SPVLQIEPYT GDYVGRWEKV ELPQKVLSKL SAAFSSMPLL LFSVPLSSPR VYLVRFSQPF DHLMRSNGVY KAVALRPDGT ITGLPNVLSP GFYRFLGSAA TVWAILAVIT RQKYLHDIEQ RLKKIEEGVA DIKEFLEKER DTGIQGNLLY LKQVYEALKN GDLSEYDINS FNSQLESIER QCQQAVLHYQ IDMENCFKKL EEFEIGAWIG KGLKKQGEEF RKVLNSFFHY SKYLLLVFQE RLVTIYLKTF LPVGKSILRV RINDLKESLR FLERTRKIEE FIEQSLDRIE EFWALFTSEK TENQIKRSLR QDVRRNLREL EEMRERLYES LANFEERLNQ LEAEKQVNLV VFMDQDHKQI KEVRMIPAGG SA // ID Q9X277_THEMA Unreviewed; 364 AA. AC Q9X277; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Phosphate butyryltransferase {ECO:0000313|EMBL:AAD36820.1}; GN OrderedLocusNames=TM_1755 {ECO:0000313|EMBL:AAD36820.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36820.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36820.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36820.1; -; Genomic_DNA. DR PIR; D72214; D72214. DR RefSeq; NP_229553.1; NC_000853.1. DR RefSeq; WP_010865395.1; NC_000853.1. DR ProteinModelPortal; Q9X277; -. DR STRING; 243274.TM1755; -. DR EnsemblBacteria; AAD36820; AAD36820; TM_1755. DR GeneID; 897861; -. DR KEGG; tma:TM1755; -. DR PATRIC; 23938486; VBITheMar51294_1773. DR eggNOG; ENOG4108IJ2; Bacteria. DR eggNOG; COG0280; LUCA. DR InParanoid; Q9X277; -. DR KO; K00634; -. DR OMA; GVIMGAK; -. DR OrthoDB; EOG60GRZ3; -. DR BioCyc; TMAR243274:GC6P-1803-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:InterPro. DR InterPro; IPR002505; PTA_PTB. DR Pfam; PF01515; PTA_PTB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD36820.1}. FT DOMAIN 138 355 PTA_PTB. {ECO:0000259|Pfam:PF01515}. SQ SEQUENCE 364 AA; 40168 MW; DFD6EF97C7EFA8B9 CRC64; MRCPWRKTRR HSDNGWYGPR NQIRPDDHRL HRKVRKSRGD SRRAGNGSPR ARCFEGAQRR GKSDGLSECG RMKNLLEMVE LVRGKRMKIA VGAAEDEEVL KAVARAKEEE IVDPVLFGKR KDIETLVERM NLELEAEIVH VEDPFEAVRK AVESVSRNET QILMKGKIKT SDLFSVFLKK EYGLRTGRTL SAVSVHEVPG YHKILIISDG GLVISPNLQQ RMDIVENSIL VARALGIEKP KIALLGTGDL KSPLTLEIAA LSKIFQQRND CIVDGPLTLD LAISEELASK AGNSPVAGDA DILIVPSIET GNILSKSLVY MARGRAAIVV VGGRVPVVLT SRADDEETRF LSIALSVLVA QKKG // ID Q9X1Y6_THEMA Unreviewed; 222 AA. AC Q9X1Y6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36723.1}; GN OrderedLocusNames=TM_1656 {ECO:0000313|EMBL:AAD36723.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36723.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36723.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36723.1; -; Genomic_DNA. DR PIR; E72228; E72228. DR RefSeq; NP_229456.1; NC_000853.1. DR RefSeq; WP_010865377.1; NC_000853.1. DR ProteinModelPortal; Q9X1Y6; -. DR STRING; 243274.TM1656; -. DR EnsemblBacteria; AAD36723; AAD36723; TM_1656. DR GeneID; 897912; -. DR KEGG; tma:TM1656; -. DR PATRIC; 23938286; VBITheMar51294_1675. DR eggNOG; ENOG41071ZC; Bacteria. DR eggNOG; ENOG410Z04C; LUCA. DR OMA; WYYSLIA; -. DR OrthoDB; EOG625JZ4; -. DR BioCyc; TMAR243274:GC6P-1702-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 13 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 97 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 125 146 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 153 173 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 193 212 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 222 AA; 25363 MW; 63646E49938D893F CRC64; MCVEGLIGDF FRLIIKNWYF SLPAALFLMF AARYVEHIAF AVIGFVIGIN FVFPLLSNIE FLKSYLTNEN VKVVVLVATG VLTAVVLYVL YRYLVFLAAL VTVTFVAYYV INFLVSSFNL QSVQYMNWIT FGLSVFIGLL AGLTAYRKEK EFARILSVVV GAAIFSVLVL FYLSGLFGVE FKPESLFANK MMIFFYVSLF LLFLFLSAWF TFRKRSYQKT SS // ID Q9X1S4_THEMA Unreviewed; 240 AA. AC Q9X1S4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36655.1}; GN OrderedLocusNames=TM_1588 {ECO:0000313|EMBL:AAD36655.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36655.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36655.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Contains GGDEF domain. CC {ECO:0000256|SAAS:SAAS00496774}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36655.1; -; Genomic_DNA. DR PIR; D72236; D72236. DR RefSeq; NP_229388.1; NC_000853.1. DR RefSeq; WP_010865367.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X1S4; -. DR STRING; 243274.TM1588; -. DR EnsemblBacteria; AAD36655; AAD36655; TM_1588. DR GeneID; 897691; -. DR KEGG; tma:TM1588; -. DR KEGG; tmi:THEMA_06340; -. DR KEGG; tmw:THMA_1623; -. DR PATRIC; 23938140; VBITheMar51294_1607. DR eggNOG; COG2199; LUCA. DR OMA; SYGIETW; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; TMAR243274:GC6P-1629-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR Pfam; PF00990; GGDEF; 1. DR SMART; SM00267; GGDEF; 1. DR SUPFAM; SSF55073; SSF55073; 1. DR TIGRFAMs; TIGR00254; GGDEF; 1. DR PROSITE; PS50887; GGDEF; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 25 44 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 50 70 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 109 236 GGDEF. {ECO:0000259|PROSITE:PS50887}. SQ SEQUENCE 240 AA; 27593 MW; F7B69227CCE10D8C CRC64; MITHLTAAVP LFFFVVIVRK YARSLGSYFL ELGVSIITGG LLLTEINGTF GYNIILVGIV VTFFGVTKIF KRLKEIAIKD YLTGLYTRYY FFEEWLPREM ERQKRKSGKG ISFLIIDLDD FKTINDKYSH RIGDKLLKYV ASEIIKNIRK TDCAVRFGGD EILVAFPDTD KKTVENIVKR LEKKLIFNPV GLPVEFSYGI ETWKPGENVE GIVQNADLQM YALKNLKKQK RVLTEEPEVD // ID Q9X2I6_THEMA Unreviewed; 388 AA. AC Q9X2I6; G4FGR5; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=Ornithine decarboxylase {ECO:0000313|EMBL:AAD36935.1}; GN OrderedLocusNames=TM_1873 {ECO:0000313|EMBL:AAD36935.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36935.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36935.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II CC family. {ECO:0000256|RuleBase:RU003737}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36935.1; -; Genomic_DNA. DR PIR; D72200; D72200. DR RefSeq; NP_229669.1; NC_000853.1. DR RefSeq; WP_004082424.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2I6; -. DR STRING; 243274.TM1873; -. DR EnsemblBacteria; AAD36935; AAD36935; TM_1873. DR GeneID; 897797; -. DR KEGG; tma:TM1873; -. DR KEGG; tmw:THMA_1923; -. DR PATRIC; 23938735; VBITheMar51294_1894. DR eggNOG; ENOG4105CU5; Bacteria. DR eggNOG; COG0019; LUCA. DR InParanoid; Q9X2I6; -. DR KO; K01581; -. DR OMA; VFCRILC; -. DR OrthoDB; EOG6Z9B18; -. DR BioCyc; TMAR243274:GC6P-1924-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004586; F:ornithine decarboxylase activity; IBA:GO_Central. DR GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central. DR Gene3D; 2.40.37.10; -; 1. DR Gene3D; 3.20.20.10; -; 1. DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C. DR InterPro; IPR022643; De-COase2_C. DR InterPro; IPR022644; De-COase2_N. DR InterPro; IPR022653; De-COase2_pyr-phos_BS. DR InterPro; IPR000183; Orn/DAP/Arg_de-COase. DR InterPro; IPR002433; Orn_de-COase. DR InterPro; IPR029066; PLP-binding_barrel. DR Pfam; PF02784; Orn_Arg_deC_N; 1. DR Pfam; PF00278; Orn_DAP_Arg_deC; 1. DR PRINTS; PR01179; ODADCRBXLASE. DR PRINTS; PR01182; ORNDCRBXLASE. DR SUPFAM; SSF50621; SSF50621; 1. DR SUPFAM; SSF51419; SSF51419; 1. DR PROSITE; PS00878; ODR_DC_2_1; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Pyridoxal phosphate {ECO:0000256|SAAS:SAAS00418093}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 25 259 Orn_Arg_deC_N. FT {ECO:0000259|Pfam:PF02784}. FT DOMAIN 264 368 Orn_DAP_Arg_deC. FT {ECO:0000259|Pfam:PF00278}. SQ SEQUENCE 388 AA; 43791 MW; 5FFEC9ED33ED2C72 CRC64; MMEYWIRRAL EVVKTPFLLF DLSVVEKKYL EMKAALKKAD IYYAVKANSH PRIISLLARL GSNFDVASKG EIEKLLALGV DGKRMSFGNT IKREEDIAFA YKNGIRLFAV DSEMEVEKVA INAPGSFVFV RVETDGADAD WPLSRKFGTN PEHALQLLSY ASKMKLIPAG LSFHVGSQNL NPESWKKAIE IAGRVFKKAM RSGLNLFLLN VGGGFPVQHT KPIPSMEEIG KAIEEAIDEN LWFVHNLKVI AEPGRYMVGE AGWLVTKVLL KSERSGEKWV YIDAGVFHGL AETIQNFEYE IRVLGKEREE LEEYHLAGPT CDSVDVIYDR IFLPKSITLN DLVCFINAGA YTVEYNTRFN GIEPPKMVFI EELTEISIEE KIKTRVLD // ID Q9X1R6_THEMA Unreviewed; 311 AA. AC Q9X1R6; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 91. DE SubName: Full=Transcriptional regulator, putative {ECO:0000313|EMBL:AAD36647.1}; GN OrderedLocusNames=TM_1580 {ECO:0000313|EMBL:AAD36647.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36647.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36647.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36647.1; -; Genomic_DNA. DR PIR; E72238; E72238. DR RefSeq; NP_229380.1; NC_000853.1. DR RefSeq; WP_010865365.1; NC_000853.1. DR ProteinModelPortal; Q9X1R6; -. DR STRING; 243274.TM1580; -. DR EnsemblBacteria; AAD36647; AAD36647; TM_1580. DR GeneID; 897650; -. DR KEGG; tma:TM1580; -. DR PATRIC; 23938124; VBITheMar51294_1599. DR eggNOG; ENOG4107HIC; Bacteria. DR eggNOG; COG1221; LUCA. DR OMA; SLTYHED; -. DR OrthoDB; EOG6WHNMG; -. DR BioCyc; TMAR243274:GC6P-1621-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR002197; HTH_Fis. DR InterPro; IPR002078; Sigma_54_int. DR Pfam; PF02954; HTH_8; 1. DR PRINTS; PR01590; HTHFIS. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 172 237 Sigma-54 factor interaction. FT {ECO:0000259|PROSITE:PS50045}. SQ SEQUENCE 311 AA; 35881 MW; 8C6529592FB7A88D CRC64; MISEISHDVI WDLYEGEDYR DKILAEKWDV VFGEKILEME DTLFVQSLRE LELALKYAAA RKDLETIKAR FNLLLYTPEL QGAKIKEILF QVLKFYNSFS IFALVSEKGV HRHAYVDFVT GGNYLSLIYH EDLPLNINSH TVFIDDVPPD FSPAGLGGRK IILGMDSTPK NNIPFVEIPP LRERKMDIPY MLDGVIKSLQ FQGKTVKIDD DLTKLLIEYH WPGNTQEFLE KVYEIITLEN PVDQAMKIAS GIDEIKGLNL KEFVDSLVEF VEKKVIKKAL EENEGNRKKV CEVLNMNYKT LSYKMKKYGL T // ID Q9WZ76_THEMA Unreviewed; 282 AA. AC Q9WZ76; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35692.1}; GN OrderedLocusNames=TM_0607 {ECO:0000313|EMBL:AAD35692.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35692.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35692.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35692.1; -; Genomic_DNA. DR PIR; C72355; C72355. DR RefSeq; NP_228417.1; NC_000853.1. DR RefSeq; WP_010865159.1; NC_000853.1. DR ProteinModelPortal; Q9WZ76; -. DR STRING; 243274.TM0607; -. DR EnsemblBacteria; AAD35692; AAD35692; TM_0607. DR GeneID; 897688; -. DR KEGG; tma:TM0607; -. DR PATRIC; 23936129; VBITheMar51294_0618. DR eggNOG; ENOG4108KIZ; Bacteria. DR eggNOG; COG0491; LUCA. DR InParanoid; Q9WZ76; -. DR OMA; RNKFLMA; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; TMAR243274:GC6P-632-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001018; Beta-lactamase_class-B_CS. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR PROSITE; PS00743; BETA_LACTAMASE_B_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 7 192 Lactamase_B. {ECO:0000259|SMART:SM00849}. SQ SEQUENCE 282 AA; 32373 MW; 008A3049F490FF46 CRC64; MAYVPNPVNI GVVYTENAAV LVDSGLDESV PRKISRLLQK PPLYLINTHS HADHCGGNAF LKKRFSTRVF APKMEKEIIE NTVFEPFYLY GAYPPNELRN KFLMAEPSAV DEVIEEGTIT IESVDLEIVP LSGHSTNQIG VAVDGVLFCA DAVFSEETLR KHRIFVIYNV EKFLETLDFL EKTSYSYYVP SHGEVTRDIG ELVEKNRKAV ENIINAVLEI TVNPLSTDEL MKQLFDRFEI TLENLTQYIL YRSTVHAYLS FLLDRKEIER EFRNNVLVWR RC // ID Q9WZK2_THEMA Unreviewed; 217 AA. AC Q9WZK2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD35824.1}; GN OrderedLocusNames=TM_0743 {ECO:0000313|EMBL:AAD35824.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35824.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35824.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35824.1; -; Genomic_DNA. DR PIR; B72340; B72340. DR RefSeq; NP_228552.1; NC_000853.1. DR RefSeq; WP_010865196.1; NC_000853.1. DR STRING; 243274.TM0743; -. DR DNASU; 898410; -. DR EnsemblBacteria; AAD35824; AAD35824; TM_0743. DR GeneID; 898410; -. DR KEGG; tma:TM0743; -. DR KEGG; tmi:THEMA_00940; -. DR PATRIC; 23936406; VBITheMar51294_0756. DR eggNOG; ENOG410644E; Bacteria. DR eggNOG; ENOG41121IH; LUCA. DR OMA; HTWWISP; -. DR OrthoDB; EOG632D2H; -. DR BioCyc; TMAR243274:GC6P-769-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 76 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 88 108 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 120 138 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 182 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 213 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 217 AA; 25058 MW; C1530ACFBD739AD6 CRC64; MIFLFPFHLF LGHVVADHGF TNNAKIREYR GWKLIGHMIW SVFAILAFTF DVIFQSTTGV VVFLVSVVVH LTGDLLRVYL HRKGKKRLIN LLEVALLVIF LVLNAAVKDL FKGSYLTAEF VFYLLGMNAV SVAVTYVFRN FVPGDPKISD IEGISERLAF FVFLLAGKDL FAFLSLALGF LYRLWKFRKP DVRWWMSPVF GVLISVLWNW MMYGRIF // ID Q9X0B0_THEMA Unreviewed; 333 AA. AC Q9X0B0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36095.1}; GN OrderedLocusNames=TM_1018 {ECO:0000313|EMBL:AAD36095.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36095.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36095.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36095.1; -; Genomic_DNA. DR PIR; B72306; B72306. DR RefSeq; NP_228824.1; NC_000853.1. DR RefSeq; WP_010865243.1; NC_000853.1. DR STRING; 243274.TM1018; -. DR EnsemblBacteria; AAD36095; AAD36095; TM_1018. DR GeneID; 897106; -. DR KEGG; tma:TM1018; -. DR PATRIC; 23936965; VBITheMar51294_1031. DR OMA; YLMRIDR; -. DR OrthoDB; EOG6BGNX1; -. DR BioCyc; TMAR243274:GC6P-1047-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 333 AA; 38107 MW; 23E99C4B4E9CD793 CRC64; MKRGILILFV LFSAVLFAQS IDKVRFDSGK FLVFVGSVSK EAVSFEGVDL CYLGNNYNYV EDAIIDGENV LEIYAYRQAS GDGFILRYRK LNSNVWDYRE PTYNNIWNIP YEDVSFYHGE LYKLDNDFLF LGSVGLDGEN FLYLMRIDRE GNILDEKELD FENFLVNEAS ESGVEFLAYK ITGSGHSSAY LCQVFSYSGS LSEKGKQFKL DYLPDFFADG KYYRVEGWMN RELTVYEFGK KKKKRTVKIP FSIPSGGGGY PVLGHTDDSF FTLGLDYSTF HTVVIEIGLD GKLKKTFDLT KAIMEKYGLE SLDYFEIGEK RIFPGPLEHK SDT // ID Q9WZY9_THEMA Unreviewed; 139 AA. AC Q9WZY9; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 94. DE SubName: Full=Methylated-DNA-protein-cysteine methyltransferase {ECO:0000313|EMBL:AAD35968.1}; GN OrderedLocusNames=TM_0887 {ECO:0000313|EMBL:AAD35968.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35968.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35968.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35968.1; -; Genomic_DNA. DR PIR; H72320; H72320. DR RefSeq; NP_228695.1; NC_000853.1. DR RefSeq; WP_010865217.1; NC_000853.1. DR ProteinModelPortal; Q9WZY9; -. DR STRING; 243274.TM0887; -. DR EnsemblBacteria; AAD35968; AAD35968; TM_0887. DR GeneID; 898561; -. DR KEGG; tma:TM0887; -. DR KEGG; tmi:THEMA_00200; -. DR PATRIC; 23936705; VBITheMar51294_0901. DR eggNOG; ENOG4105K85; Bacteria. DR eggNOG; COG0350; LUCA. DR KO; K00567; -. DR OMA; QEYLIVE; -. DR OrthoDB; EOG6DJZ5C; -. DR BioCyc; TMAR243274:GC6P-917-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central. DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_00772; OGT; 1. DR InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS. DR InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd. DR InterPro; IPR008332; MethylG_MeTrfase_N. DR InterPro; IPR023546; MGMT. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01035; DNA_binding_1; 1. DR SUPFAM; SSF46767; SSF46767; 1. DR SUPFAM; SSF53155; SSF53155; 1. DR TIGRFAMs; TIGR00589; ogt; 1. DR PROSITE; PS00374; MGMT; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Methyltransferase {ECO:0000313|EMBL:AAD35968.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000313|EMBL:AAD35968.1}. FT DOMAIN 60 136 DNA_binding_1. FT {ECO:0000259|Pfam:PF01035}. SQ SEQUENCE 139 AA; 15822 MW; 9C174D9F8FB0CF8C CRC64; MFSMRVPGNI SVQTENGKVV KIILGSNETE GSEEILREIE EYLSGQRKSF SFQVEIRGTP FQKRVWEEVR KIPYGETKTY SEIAKKLGTS PRAVGQALSK NPLPLYIPCH RVVSKKGLGG FSAGLEWKKY LIDLERFRK // ID Q9X055_THEMA Unreviewed; 299 AA. AC Q9X055; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 99. DE SubName: Full=Ribokinase {ECO:0000313|EMBL:AAD36039.1}; GN OrderedLocusNames=TM_0960 {ECO:0000313|EMBL:AAD36039.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36039.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36039.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:1VM7} RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of Ribokinase (TM0960) from Thermotoga maritima at RT 2.15 A resolution."; RL Submitted (SEP-2004) to the PDB data bank. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. CC {ECO:0000256|RuleBase:RU003704}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36039.1; -; Genomic_DNA. DR PIR; E72311; E72311. DR RefSeq; NP_228768.1; NC_000853.1. DR RefSeq; WP_010865225.1; NC_000853.1. DR PDB; 1VM7; X-ray; 2.15 A; A/B=1-299. DR PDBsum; 1VM7; -. DR ProteinModelPortal; Q9X055; -. DR SMR; Q9X055; 1-299. DR STRING; 243274.TM0960; -. DR EnsemblBacteria; AAD36039; AAD36039; TM_0960. DR GeneID; 898697; -. DR KEGG; tma:TM0960; -. DR PATRIC; 23936851; VBITheMar51294_0974. DR eggNOG; ENOG4108RVA; Bacteria. DR eggNOG; COG0524; LUCA. DR InParanoid; Q9X055; -. DR KO; K00852; -. DR OMA; GDARHYP; -. DR OrthoDB; EOG64JFMD; -. DR BioCyc; TMAR243274:GC6P-990-MONOMER; -. DR EvolutionaryTrace; Q9X055; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004747; F:ribokinase activity; IEA:InterPro. DR GO; GO:0006014; P:D-ribose metabolic process; IEA:InterPro. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS. DR InterPro; IPR011877; D_ribokin_bac. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR002139; Ribokinase. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF00294; PfkB; 1. DR PRINTS; PR00990; RIBOKINASE. DR SUPFAM; SSF53613; SSF53613; 1. DR TIGRFAMs; TIGR02152; D_ribokin_bact; 1. DR PROSITE; PS00584; PFKB_KINASES_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1VM7}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Kinase {ECO:0000256|RuleBase:RU003704, ECO:0000256|SAAS:SAAS00446051, KW ECO:0000313|EMBL:AAD36039.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Transferase {ECO:0000256|RuleBase:RU003704, KW ECO:0000256|SAAS:SAAS00446051, ECO:0000313|EMBL:AAD36039.1}. FT DOMAIN 5 288 PfkB. {ECO:0000259|Pfam:PF00294}. SQ SEQUENCE 299 AA; 32654 MW; 0EBC29B191AE57FC CRC64; MFLVISVVGS SNIDIVLKVD HFTKPGETQK AIEMNVFPGG KGANQAVTVA KIGEKGCRFV TCIGNDDYSD LLIENYEKLG ITGYIRVSLP TGRAFIEVDK TGQNRIIIFP GANAELKKEL IDWNTLSESD ILLLQNEIPF ETTLECAKRF NGIVIFDPAP AQGINEEIFQ YLDYLTPNEK EIEALSKDFF GEFLTVEKAA EKFLELGVKN VIVKLGDKGV LLVNKNEKKH FPTFKVKAVD TTAAGDVFNG AFAVALSEGK NPEEAVIFGT AAAAISVTRL GAQSSIPARE EVEAFLKNL // ID Q9X2C3_THEMA Unreviewed; 116 AA. AC Q9X2C3; G4FGJ1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=DnaJ-related protein {ECO:0000313|EMBL:AAD36866.1}; GN OrderedLocusNames=TM_1803 {ECO:0000313|EMBL:AAD36866.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36866.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36866.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36866.1; -; Genomic_DNA. DR PIR; H72207; H72207. DR RefSeq; NP_229600.1; NC_000853.1. DR RefSeq; WP_004082350.1; NZ_CP011107.1. DR ProteinModelPortal; Q9X2C3; -. DR STRING; 243274.TM1803; -. DR EnsemblBacteria; AAD36866; AAD36866; TM_1803. DR GeneID; 897833; -. DR KEGG; tma:TM1803; -. DR KEGG; tmi:THEMA_05175; -. DR KEGG; tmw:THMA_1849; -. DR PATRIC; 23938595; VBITheMar51294_1824. DR eggNOG; ENOG4108J3M; Bacteria. DR eggNOG; COG2214; LUCA. DR OMA; INEAYQM; -. DR OrthoDB; EOG6BPDKP; -. DR BioCyc; TMAR243274:GC6P-1854-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR Gene3D; 1.10.287.110; -; 1. DR InterPro; IPR001623; DnaJ_domain. DR Pfam; PF00226; DnaJ; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR PROSITE; PS50076; DNAJ_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 2 76 J. {ECO:0000259|PROSITE:PS50076}. SQ SEQUENCE 116 AA; 13100 MW; 5796A78E60FA2D2C CRC64; MNPYEVLGVP PGASKEEIEK AYRELVKKYH PDRYKDHPLK DLAEEKMKQI NEAYAVLMSG EFSETPGQEN VHNTFYSMGY RYRGNDGCRD ILACLGCAWC TDTCCEACGG DCIPCM // ID Q9X0K0_THEMA Unreviewed; 543 AA. AC Q9X0K0; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36192.1}; GN OrderedLocusNames=TM_1116 {ECO:0000313|EMBL:AAD36192.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36192.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36192.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36192.1; -; Genomic_DNA. DR PIR; A72292; A72292. DR RefSeq; NP_228922.1; NC_000853.1. DR RefSeq; WP_010865266.1; NZ_CP011107.1. DR STRING; 243274.TM1116; -. DR EnsemblBacteria; AAD36192; AAD36192; TM_1116. DR GeneID; 898649; -. DR KEGG; tma:TM1116; -. DR KEGG; tmw:THMA_1139; -. DR PATRIC; 23937167; VBITheMar51294_1132. DR eggNOG; ENOG4106H0X; Bacteria. DR eggNOG; ENOG410Y7X9; LUCA. DR OMA; TITRRFF; -. DR OrthoDB; EOG628F23; -. DR BioCyc; TMAR243274:GC6P-1145-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR InterPro; IPR010317; DUF916. DR Pfam; PF06030; DUF916; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 543 AA; 60133 MW; 179F6FE29D9A5219 CRC64; MGMRRISLMV LILMSGVFLA QGISVRMDPI VVSKTVNPGT SFNYEIFLEN DSEFESITLK AMVMDITETE DGAYDLKQPG STKYSIARWV KVEPDTITVP PKETKTVIVT VNIPRGVSGG LYGAVTFEIQ TPQSQETQRP AEEGAYGEIE FKYRMASFLE IVVSGTRKRI EAFPAYFKVE RSDDIPSIRM QIGDGALVFT LGVLNKSNVH IVTKGTLTIK TKEGRTIAKM PLGAGRGVVL PDITVNMRTI TRRFFPPGEY VARAVVDYGG RRPIVAETTF TVTSEKVETK EEKEEANPVM ITVDPADIEI KAIPGSYRSA IVKVSNLGEE TLQVEGKILP LVYDLYGEIL PEEERGTPPE WIKLTPASFS LRPGQSRNVR VAVRIPKDFT GGYYADVIFK TEGGLQTEVG ANLLVFAGKD EDITKEASAD LVYTVKEDGI YADIVFENTG NYHLLPKITF GLNRITPQQV TDEGLIIPEK VESLIQEEIS STNPVLPGTK RIFSIFIPVV LEEGQYELLA RCDYGKSPIV LRKSFQMEGR NGE // ID Q9WXR2_THEMA Unreviewed; 660 AA. AC Q9WXR2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein, putative {ECO:0000313|EMBL:AAD35150.1}; GN OrderedLocusNames=TM_0056 {ECO:0000313|EMBL:AAD35150.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35150.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35150.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35150.1; -; Genomic_DNA. DR PIR; A72424; A72424. DR RefSeq; NP_227872.1; NC_000853.1. DR RefSeq; WP_010865040.1; NC_000853.1. DR ProteinModelPortal; Q9WXR2; -. DR STRING; 243274.TM0056; -. DR TCDB; 3.A.1.5.29; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAD35150; AAD35150; TM_0056. DR GeneID; 896880; -. DR KEGG; tma:TM0056; -. DR KEGG; tmi:THEMA_04525; -. DR PATRIC; 23934952; VBITheMar51294_0054. DR eggNOG; ENOG4105EN8; Bacteria. DR eggNOG; ENOG410XRAT; LUCA. DR KO; K02035; -. DR OMA; WIAANGS; -. DR OrthoDB; EOG6PP9H6; -. DR BioCyc; TMAR243274:GC6P-56-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GOC. DR InterPro; IPR023765; SBP_5_CS. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PROSITE; PS01040; SBP_BACTERIAL_5; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 660 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004336077. FT DOMAIN 119 530 SBP_bac_5. {ECO:0000259|Pfam:PF00496}. SQ SEQUENCE 660 AA; 76186 MW; 015FF72145D57093 CRC64; MLVVRRLFVL LSLVFMVVLA LAANDTWVFY ATPEEYYKAT GKKITEYHES PMLTKLVEEG KLPPVEQRLP EEPLVVQPVE KVGQFGGTWR RVWKGPSDRW GISKLIEVKL AFWDKEGGKL VPGLAKSWEV LENGRVYIFH LRKGVKWSDG APYTAHDIVF WVNDIVGNDD ITPSKPDWYN IGVKVEALDD YTVKFEFSKP YGLFLLKVPY GGFTGAPAHY LKQFHPKYTP MEEIEKKMVE GVHNTWVDLF NDKNDFLENT ELPTLSPWKP ITDPTEQFYI LERNPYFWAV DIEGNQLPYI DYVRHEYVKN DEVILLKAIS GEIDMQWRHI GGLGAGAGNF TLLMENSQSG GYRVLKWIAA NGSASRISLN YAHSDEVLRK VFNDVRFRQA LSLAINREEI NEILFNGLAE PRQASLVSGS PYFDPEWEKA YAEYDPDRAN KLLDEMGLKW DDKHEYRLLP DGRPLRFTIT VTGQFHVDVW TMVKEYWKQI GVWVEIENLE RSLFYERADA GDFDAMVWNM DRAAQPLSSP MVIFPGSENI ADFWYIGWSG WISYYIDKNI RGVEPEEVPE GPEPPEVVYR LVDLYYQIAS TPDPDKIKEL MAEATKIHRE NLWMIGTVGE DLSPAIAKNN FRNVPEFLVT DDVLRTPLNA MPMQFFIEQK // ID Q9X0W3_THEMA Unreviewed; 62 AA. AC Q9X0W3; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36311.1}; GN OrderedLocusNames=TM_1236 {ECO:0000313|EMBL:AAD36311.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36311.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36311.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36311.1; -; Genomic_DNA. DR PIR; E72279; E72279. DR RefSeq; NP_229041.1; NC_000853.1. DR RefSeq; WP_010865287.1; NC_000853.1. DR STRING; 243274.TM1236; -. DR EnsemblBacteria; AAD36311; AAD36311; TM_1236. DR GeneID; 898248; -. DR KEGG; tma:TM1236; -. DR BioCyc; TMAR243274:GC6P-1266-MONOMER; -. DR Proteomes; UP000008183; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 62 AA; 7366 MW; 809F037252C3C6A9 CRC64; MNTPLKRFFK IGYVIENFLH PYHNKKLLPL SRGVNIKGIF VLLNTLWRVF QDGSLQDLWS FT // ID Q9WYP4_THEMA Unreviewed; 311 AA. AC Q9WYP4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 16-MAR-2016, entry version 68. DE SubName: Full=Creatinine amidohydrolase, putative {ECO:0000313|EMBL:AAD35498.1}; GN OrderedLocusNames=TM_0413 {ECO:0000313|EMBL:AAD35498.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35498.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35498.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35498.1; -; Genomic_DNA. DR PIR; C72381; C72381. DR RefSeq; NP_228223.1; NC_000853.1. DR RefSeq; WP_010865114.1; NC_000853.1. DR ProteinModelPortal; Q9WYP4; -. DR STRING; 243274.TM0413; -. DR EnsemblBacteria; AAD35498; AAD35498; TM_0413. DR GeneID; 897414; -. DR KEGG; tma:TM0413; -. DR PATRIC; 23935709; VBITheMar51294_0418. DR eggNOG; ENOG4107W9I; Bacteria. DR eggNOG; COG1402; LUCA. DR InParanoid; Q9WYP4; -. DR KO; K01470; -. DR OMA; YYGKSNE; -. DR OrthoDB; EOG64V2CK; -. DR BioCyc; MetaCyc:MONOMER-17950; -. DR BioCyc; TMAR243274:GC6P-428-MONOMER; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.10310; -; 1. DR InterPro; IPR024087; Creatininase-like_dom. DR InterPro; IPR003785; Creatininase/forma_Hydrolase. DR Pfam; PF02633; Creatininase; 1. DR SUPFAM; SSF102215; SSF102215; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Hydrolase {ECO:0000313|EMBL:AAD35498.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. SQ SEQUENCE 311 AA; 34947 MW; D81586D6B096CBBA CRC64; MERPTGVYFQ TMTMKQIRER LKQCDLIIIP VGSTENHGPN APTGEDTFLV TRMAEQVALK TGCTVAEPIW YGYHPYHHIG MPGTVPVKDE AFIDYLVSVI AGFWNTGFRK QILLNGHGQE FVIPIAIHKF AKIFQVPAII INLNWYHAIQ DKFKTKEEGG PYETPFIHAD EVETSWSLAL FPEFMHQEWA VDTEPKGFLP EGHIDKAGNL LHRPIAWYGH VGGGPIEVVA YPEGVVGKAT LASAEKAKEG VEALLDYLEK LVRDIMERFP AGKLPPAEML SQRPKEELEA LTKEPLTEGW RNLYTAGNLW G // ID Q9X247_THEMA Unreviewed; 386 AA. AC Q9X247; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 13-APR-2016, entry version 90. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAD36789.1}; GN OrderedLocusNames=TM_1723 {ECO:0000313|EMBL:AAD36789.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36789.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD36789.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] {ECO:0000213|PDB:3OOQ} RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 2-386. RA Malashkevich V.N., Toro R., Sauder J.M., Burley S.K., Almo S.C.; RT "CRYSTAL STRUCTURE OF amidohydrolase from Thermotoga maritima MSB8."; RL Submitted (AUG-2010) to the PDB data bank. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD36789.1; -; Genomic_DNA. DR PIR; G72219; G72219. DR RefSeq; NP_229522.1; NC_000853.1. DR RefSeq; WP_010865390.1; NZ_CP011107.1. DR PDB; 3OOQ; X-ray; 2.06 A; A/B/C/D/E/F/G/H/I/J=2-386. DR PDBsum; 3OOQ; -. DR ProteinModelPortal; Q9X247; -. DR STRING; 243274.TM1723; -. DR DNASU; 897877; -. DR EnsemblBacteria; AAD36789; AAD36789; TM_1723. DR GeneID; 897877; -. DR KEGG; tma:TM1723; -. DR KEGG; tmw:THMA_1765; -. DR PATRIC; 23938422; VBITheMar51294_1741. DR eggNOG; ENOG4105CU1; Bacteria. DR eggNOG; COG1228; LUCA. DR InParanoid; Q9X247; -. DR OMA; KMPMTRM; -. DR OrthoDB; EOG6WHNMD; -. DR BioCyc; TMAR243274:GC6P-1771-MONOMER; -. DR EvolutionaryTrace; Q9X247; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR Gene3D; 2.30.40.10; -; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51338; SSF51338; 2. DR SUPFAM; SSF51556; SSF51556; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3OOQ}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 52 382 Amidohydro-rel. FT {ECO:0000259|Pfam:PF01979}. SQ SEQUENCE 386 AA; 42543 MW; 02F48F6F6B0BD5BA CRC64; MSVKILFKNA TVFPITSRPF KGDVLVSNGK VEKVGENIED PDAEIVDLTG KFLFPGFVDA HSHIGLFEEG VGYYYSDGNE ATDPVTPHVK ALDGFNPQDP AIERALAGGV TSVMIVPGSA NPVGGQGSVI KFRSIIVEEC IVKDPAGLKM AFGENPKRVY GERKQTPSTR MGTAGVIRDY FTKVKNYMKK KELAQKEGKE FTETDLKMEV GEMVLRKKIP ARMHAHRADD ILTAIRIAEE FGFNLVIEHG TEAYKISKVL AEKKIPVVVG PLLTFRTKLE LKDLTMETIA KLLKDGVLIA LMCDHPVIPL EFATVQAATA MRYGAKEEDL LKILTVNPAK ILGLEDRIGS IEPGKDADLV VWSGHPFDMK SVVERVYIDG VEVFRR //